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Conserved domains on  [gi|767934614|ref|XP_011512412|]
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triple functional domain protein isoform X5 [Homo sapiens]

Protein Classification

triple functional domain protein( domain architecture ID 12213613)

triple functional domain protein (Trio) is a large serine/threonine-protein kinase and Rho guanine nucleotide exchange factor that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates and functions as a GEF for Rac1, RhoG, and RhoA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2729-2991 0e+00

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 589.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd14113     1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTY 2888
Cdd:cd14113    81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFV 2968
Cdd:cd14113   161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                         250       260
                  ....*....|....*....|...
gi 767934614 2969 CFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14113   241 CFLLQMDPAKRPSAALCLQEQWL 263
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
1656-1913 2.32e-162

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


:

Pssm-ID: 465196  Cd Length: 261  Bit Score: 501.64  E-value: 2.32e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1656 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 1734
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1735 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETVEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1812
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1813 PMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLS 1892
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSVDQGDSSSPSFNPSDNSLLS 240
                          250       260
                   ....*....|....*....|.
gi 767934614  1893 SSSPIDEMEERKSSSLKRRHY 1913
Cdd:pfam16609  241 SSSPISEMDERRSSFLKKRHY 261
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
2089-2227 6.20e-79

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270061  Cd Length: 140  Bit Score: 257.19  E-value: 6.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2089 VGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEE 2168
Cdd:cd13241     1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2169 NVENDPCKFALTSRTG-DVVETFILHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEY 2227
Cdd:cd13241    81 NVDGDPLRFALKSRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
1413-1535 3.46e-72

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


:

Pssm-ID: 270060  Cd Length: 123  Bit Score: 237.28  E-value: 3.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1413 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1492
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767934614 1493 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1535
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1911-2084 1.22e-51

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 180.96  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1911 RHYVLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDmKGKDKIVFGNIHQIYDWHRDFFLGELEKCLED---PEKLGS 1987
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-PEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1988 LFVKHERRLHMYIAYCQNKPKSEHIVSEYI--DTFFEDLKQRLG---HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKA 2062
Cdd:cd00160    80 VFLKLAPFFKIYSEYCSNHPDALELLKKLKkfNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159
                         170       180
                  ....*....|....*....|..
gi 767934614 2063 SLDTSELERAVEVMCIVPRRCN 2084
Cdd:cd00160   160 HEDREDLKKALEAIKEVASQVN 181
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1236-1406 7.85e-45

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 161.31  E-value: 7.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1236 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1311
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1312 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1386
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                         170       180
                  ....*....|....*....|...
gi 767934614 1387 G---KGEIKDGLEVMLSVPKRAN 1406
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
2496-2554 2.30e-35

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212787  Cd Length: 59  Bit Score: 129.48  E-value: 2.30e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2496 TMLVTHDYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGH 2554
Cdd:cd11853     1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1600-1659 7.50e-32

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212786  Cd Length: 62  Bit Score: 119.81  E-value: 7.50e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767934614 1600 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1659
Cdd:cd11852     1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
508-724 1.82e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 106.76  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  508 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 587
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  588 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 664
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  665 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 724
Cdd:cd00176   151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
10-145 2.53e-22

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


:

Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.83  E-value: 2.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614     10 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 77
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614     78 SIKPLLKILQESFPCCIHVALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 145
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
I-set pfam07679
Immunoglobulin I-set domain;
2626-2717 1.13e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.55  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHnTLNNDGHYSISYSDlGEATLKIVGVTTEDDGIYTCIAVND 2705
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQ-PLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 767934614  2706 MGSASSSASLRV 2717
Cdd:pfam07679   79 AGEAEASAELTV 90
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
849-1078 6.66e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.89  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  849 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 928
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  929 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1008
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1009 EAFLKACTlarrNADVFLKYLHRNSVNMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1078
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
282-507 7.69e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.80  E-value: 7.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  282 QLRLFEQDAEKMFDWITHnKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIR 361
Cdd:cd00176     1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  362 QIASQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 437
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  438 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 507
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
728-955 9.37e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 81.72  E-value: 9.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  728 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 806
Cdd:cd00176     1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  807 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 886
Cdd:cd00176    65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  887 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 955
Cdd:cd00176   144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
171-386 1.85e-15

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.87  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  171 MLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssesfpkknSGSGNADlqnl 248
Cdd:cd00176    12 LEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------EGHPDAE---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  249 lpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHF 328
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614  329 AMNCMNVYVNINRIMSVANRLVESGHYASQ-QIRQIASQLEQEWKAFAAALDERSTLLD 386
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
1084-1184 5.57e-14

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.05  E-value: 5.57e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1084 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1163
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 767934614   1164 AVDKRYRDFSLRMEKYRTSLE 1184
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PHA03247 super family cl33720
large tegument protein UL36; Provisional
2271-2481 3.97e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.58  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRP---SRIPQPvRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAAP--EAGPSAPSRRP----PGADAE 2341
Cdd:PHA03247 2693 GSLTSLADPpppPPTPEP-APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatPGGPARPARPPttagPPAPAP 2771
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2342 GSEREAEPIPKMKVLESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSS--AVPSLGKEPFPPSSP 2419
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAqpTAPPPPPGPPPPSLP 2851
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2420 LQ----KGGSFWSSIPA-SPASRPGSFTFPGDSD----SLQRQTPRHAAPGKDTDRMSTCSSASEQSVQST 2481
Cdd:PHA03247 2852 LGgsvaPGGDVRRRPPSrSPAAKPAAPARPPVRRlarpAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQ 2922
 
Name Accession Description Interval E-value
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2729-2991 0e+00

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 589.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd14113     1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTY 2888
Cdd:cd14113    81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFV 2968
Cdd:cd14113   161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                         250       260
                  ....*....|....*....|...
gi 767934614 2969 CFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14113   241 CFLLQMDPAKRPSAALCLQEQWL 263
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
1656-1913 2.32e-162

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 501.64  E-value: 2.32e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1656 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 1734
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1735 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETVEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1812
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1813 PMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLS 1892
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSVDQGDSSSPSFNPSDNSLLS 240
                          250       260
                   ....*....|....*....|.
gi 767934614  1893 SSSPIDEMEERKSSSLKRRHY 1913
Cdd:pfam16609  241 SSSPISEMDERRSSFLKKRHY 261
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
2089-2227 6.20e-79

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 257.19  E-value: 6.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2089 VGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEE 2168
Cdd:cd13241     1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2169 NVENDPCKFALTSRTG-DVVETFILHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEY 2227
Cdd:cd13241    81 NVDGDPLRFALKSRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
2737-2991 6.30e-76

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 253.61  E-value: 6.30e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKkdRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQLL 2894
Cdd:smart00220   81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQE 2974
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVK 237
                           250
                    ....*....|....*..
gi 767934614   2975 DPAKRPSAALALQEQWL 2991
Cdd:smart00220  238 DPEKRLTAEEALQHPFF 254
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
1413-1535 3.46e-72

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 237.28  E-value: 3.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1413 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1492
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767934614 1493 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1535
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1911-2084 1.22e-51

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 180.96  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1911 RHYVLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDmKGKDKIVFGNIHQIYDWHRDFFLGELEKCLED---PEKLGS 1987
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-PEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1988 LFVKHERRLHMYIAYCQNKPKSEHIVSEYI--DTFFEDLKQRLG---HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKA 2062
Cdd:cd00160    80 VFLKLAPFFKIYSEYCSNHPDALELLKKLKkfNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159
                         170       180
                  ....*....|....*....|..
gi 767934614 2063 SLDTSELERAVEVMCIVPRRCN 2084
Cdd:cd00160   160 HEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1914-2084 1.42e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 169.02  E-value: 1.42e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1914 VLQELVETERDYVRDLGYVVEGYMALMKE--DGVPDDMKgkdkIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVK 1991
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEIK----TIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1992 HERRLHMYIAYCQNKPKSEHIVSEY------IDTFFEDLKQRLG-HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASL 2064
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLKKLlkknpkFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHP 156
                          170       180
                   ....*....|....*....|
gi 767934614  2065 DTSELERAVEVMCIVPRRCN 2084
Cdd:pfam00621  157 DYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1914-2085 1.42e-47

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 169.02  E-value: 1.42e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1914 VLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDMKGKDKIvFGNIHQIYDWHRDFfLGELEKCLED----PEKLGSLF 1989
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL-FGNIEEIYEFHRDF-LDELEERIEEwddsVERIGDVF 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1990 VKHERRLHMYIAYCQNKPKSEHIVSE--YIDTFFEDLKQRLGH----RLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKAS 2063
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALELLKKlkKNPRFQKFLKEIESSpqcrRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                           170       180
                    ....*....|....*....|..
gi 767934614   2064 LDTSELERAVEVMCIVPRRCND 2085
Cdd:smart00325  159 EDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1236-1406 7.85e-45

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 161.31  E-value: 7.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1236 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1311
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1312 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1386
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                         170       180
                  ....*....|....*....|...
gi 767934614 1387 G---KGEIKDGLEVMLSVPKRAN 1406
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1237-1407 1.72e-42

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 154.38  E-value: 1.72e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1237 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPgivNKELIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVGH 1312
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1313 CFVTWADKFQMYVTYCKNKPDSTQLI--LEHAGSYFDEIQQRHGLAN----SISSYLIKPVQRITKYQLLLKELLTCCEE 1386
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156
                           170       180
                    ....*....|....*....|....
gi 767934614   1387 G---KGEIKDGLEVMLSVPKRAND 1407
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1237-1406 4.04e-41

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 150.53  E-value: 4.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1237 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPpgivnKEL-IIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFV 1315
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESE-----EEIkTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1316 TWADKFQMYVTYCKNKPDSTQLI------LEHAGSYFDEIQQR---HGLanSISSYLIKPVQRITKYQLLLKELLTCCEE 1386
Cdd:pfam00621   76 KFAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPP 153
                          170       180
                   ....*....|....*....|...
gi 767934614  1387 G---KGEIKDGLEVMLSVPKRAN 1406
Cdd:pfam00621  154 DhpdYEDLKKALEAIKEVAKQIN 176
Pkinase pfam00069
Protein kinase domain;
2737-2991 4.43e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 152.01  E-value: 4.43e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKekiKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVrylhncriahldlkpenilvdeslaKPTIKLADFgdavqlnttyyihql 2893
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------ESGSSLTTF--------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRlDFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID-QPYAFPELPSNLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 767934614  2974 EDPAKRPSAALALQEQWL 2991
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2740-3025 5.27e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 157.10  E-value: 5.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK----RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:COG0515    12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAAdpeaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIH--QL 2893
Cdd:COG0515    92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD---GRVKLIDFGIARALGGATLTQtgTV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:COG0515   169 VGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALA 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2974 EDPAKRPSAALALQEQWLQAGNGRSTGVLDTSRLTSFIERRKHQNDVRPIRS 3025
Cdd:COG0515   249 KDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAA 300
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
2496-2554 2.30e-35

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 129.48  E-value: 2.30e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2496 TMLVTHDYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGH 2554
Cdd:cd11853     1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
2743-2979 6.99e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 138.03  E-value: 6.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:PTZ00263   26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKReILKMKQVQHvaqEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYihQLLGNPE 2898
Cdd:PTZ00263  106 FTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLD---NKGHVKVTDFGFAKKVPDRTF--TLCGTPE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQEDPAK 2978
Cdd:PTZ00263  181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFP----NWFDGRARDLVKGLLQTDHTK 256

                  .
gi 767934614 2979 R 2979
Cdd:PTZ00263  257 R 257
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1600-1659 7.50e-32

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 119.81  E-value: 7.50e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767934614 1600 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1659
Cdd:cd11852     1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
508-724 1.82e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 106.76  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  508 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 587
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  588 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 664
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  665 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 724
Cdd:cd00176   151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
10-145 2.53e-22

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.83  E-value: 2.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614     10 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 77
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614     78 SIKPLLKILQESFPCCIHVALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 145
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
I-set pfam07679
Immunoglobulin I-set domain;
2626-2717 1.13e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.55  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHnTLNNDGHYSISYSDlGEATLKIVGVTTEDDGIYTCIAVND 2705
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQ-PLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 767934614  2706 MGSASSSASLRV 2717
Cdd:pfam07679   79 AGEAEASAELTV 90
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
849-1078 6.66e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.89  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  849 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 928
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  929 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1008
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1009 EAFLKACTlarrNADVFLKYLHRNSVNMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1078
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
282-507 7.69e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.80  E-value: 7.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  282 QLRLFEQDAEKMFDWITHnKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIR 361
Cdd:cd00176     1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  362 QIASQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 437
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  438 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 507
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
728-955 9.37e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 81.72  E-value: 9.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  728 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 806
Cdd:cd00176     1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  807 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 886
Cdd:cd00176    65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  887 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 955
Cdd:cd00176   144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2633-2717 2.03e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 76.39  E-value: 2.03e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2633 SEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYSDlGEATLKIVGVTTEDDGIYTCIAVNDMGSASSS 2712
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 767934614   2713 ASLRV 2717
Cdd:smart00410   81 TTLTV 85
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
15-145 1.50e-15

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 76.60  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   15 AYLSGGRDKRGGPILTFPAR-SNHDRIRQEDLRRLISYL--ACIPSEEVCKRGFTVIVDMRGSKW------DSIKPLLKI 85
Cdd:cd00170    11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   86 LQESFPCCIHVALIIKPDNF----WQ------KQRTnfgSSKFEFETNmvSLEGLTKVVDPSQLTPEFDG 145
Cdd:cd00170    91 LQDHYPERLKKIYIVNAPWIfsalWKivkpflSEKT---RKKIVFLGS--DLEELLEYIDPDQLPKELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
171-386 1.85e-15

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.87  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  171 MLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssesfpkknSGSGNADlqnl 248
Cdd:cd00176    12 LEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------EGHPDAE---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  249 lpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHF 328
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614  329 AMNCMNVYVNINRIMSVANRLVESGHYASQ-QIRQIASQLEQEWKAFAAALDERSTLLD 386
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
2759-2929 6.09e-15

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 81.81  E-value: 6.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2759 TKRAVATKFVN----KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIL-VLEMADQGRLLDCVVRWGSLTEGKI 2833
Cdd:TIGR03903    2 TGHEVAIKLLRtdapEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2834 RAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFG-----------DAVQLNTTyyiHQLLGNPEFAAP 2902
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGigtllpgvrdaDVATLTRT---TEVLGTPTYCAP 158
                          170       180
                   ....*....|....*....|....*..
gi 767934614  2903 EIILGNPVSLTSDTWSVGVLTYVLLSG 2929
Cdd:TIGR03903  159 EQLRGEPVTPNSDLYAWGLIFLECLTG 185
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2640-2717 3.58e-14

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 70.12  E-value: 3.58e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2640 GETVVLRCRVCGRPKASITWKgpehntlNNDGHYSIS-YSDLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRV 2717
Cdd:cd05725    12 DDSAEFQCEVGGDPVPTVRWR-------KEDGELPKGrYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
SPEC smart00150
Spectrin repeats;
1084-1184 5.57e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.05  E-value: 5.57e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1084 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1163
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 767934614   1164 AVDKRYRDFSLRMEKYRTSLE 1184
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
512-612 8.07e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 8.07e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    512 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 591
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 767934614    592 QLEDRIQDFVRRVEQRKILLD 612
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1080-1187 3.64e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 71.32  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1080 QYVVFERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIK 1159
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100
                  ....*....|....*....|....*...
gi 767934614 1160 KCVTAVDKRYRDFSLRMEKYRTSLEKAL 1187
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEAL 106
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
2787-2937 8.46e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 70.98  E-value: 8.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2787 SLQHPLLVGLLDTFETPTSYILVLEMADqGRLLDCVVRwgslTEGKIRAH-----LGEVLEAVRYLHNCRIAHLDLKPEN 2861
Cdd:NF033483   63 SLSHPNIVSVYDVGEDGGIPYIVMEYVD-GRTLKDYIR----EHGPLSPEeaveiMIQILSALEHAHRNGIVHRDIKPQN 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2862 ILVDESlakPTIKLADFGDAVQLN--TTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDS 2937
Cdd:NF033483  138 ILITKD---GRVKVTDFGIARALSstTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
SPEC smart00150
Spectrin repeats;
851-949 9.88e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.50  E-value: 9.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    851 RHLQAEVKQVLGWIRNGESMLNAgLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCA 930
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
                            90
                    ....*....|....*....
gi 767934614    931 EKVASHWQQLMLKMEDRLK 949
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
SPEC smart00150
Spectrin repeats;
286-386 2.35e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.73  E-value: 2.35e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    286 FEQDAEKMFDWITHNKGLFlnSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIRQIAS 365
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL--ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 767934614    366 QLEQEWKAFAAALDERSTLLD 386
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
2271-2481 3.97e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.58  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRP---SRIPQPvRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAAP--EAGPSAPSRRP----PGADAE 2341
Cdd:PHA03247 2693 GSLTSLADPpppPPTPEP-APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatPGGPARPARPPttagPPAPAP 2771
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2342 GSEREAEPIPKMKVLESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSS--AVPSLGKEPFPPSSP 2419
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAqpTAPPPPPGPPPPSLP 2851
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2420 LQ----KGGSFWSSIPA-SPASRPGSFTFPGDSD----SLQRQTPRHAAPGKDTDRMSTCSSASEQSVQST 2481
Cdd:PHA03247 2852 LGgsvaPGGDVRRRPPSrSPAAKPAAPARPPVRRlarpAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQ 2922
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
25-152 9.81e-11

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 61.96  E-value: 9.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    25 GGPILTFPARS-NHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDS------IKPLLKILQESFPCCIHVA 97
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    98 LIIKPDNFWQKQ----RTNFGSSKFEFETNMVS-LEGLTKVVDPSQLTPEFDGCLEYNHE 152
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1899-2076 1.72e-08

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 60.68  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1899 EMEERKSSSLKRRHYVLQELVETERDYVRDLGYVVEGYMALMKE-DGVPDDMKGK-DKIVFGNIHQIYDWHRDFfLGELE 1976
Cdd:COG5422   473 EVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEEsNIIPENARRNfIKHVFANINEIYAVNSKL-LKALT 551
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1977 K--CLED-PEKLGSLFVKHERRLHMYIAYCQNKP------KSEHIVSEYIDTFFED-LKQRLGHRLQLTDLLIKPVQRIM 2046
Cdd:COG5422   552 NrqCLSPiVNGIADIFLDYVPKFEPFIKYGASQPyakyefEREKSVNPNFARFDHEvERLDESRKLELDGYLTKPTTRLA 631
                         170       180       190
                  ....*....|....*....|....*....|
gi 767934614 2047 KYQLLLKDFLKYSKKASLDTSELERAVEVM 2076
Cdd:COG5422   632 RYPLLLEEVLKFTDPDNPDTEDIPKVIDML 661
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
849-940 5.43e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.09  E-value: 5.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   849 QLRHLQAEVKQVLGWIRNGESMLNAGLItASSLQEAEQLQREHEQFQHAIEkTHQSALQ-VQQKAEAMLQANHYDMDMIR 927
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEIQ 79
                           90
                   ....*....|...
gi 767934614   928 DCAEKVASHWQQL 940
Cdd:pfam00435   80 ERLEELNERWEQL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1446-1531 9.15e-08

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 52.56  E-value: 9.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1446 RERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALWVGrTPTSDNKIVLKASSIENKQ 1521
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94
                           90
                   ....*....|
gi 767934614  1522 DWIKHIREVI 1531
Cdd:pfam00169   95 DWIKAIQSAI 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1424-1532 1.31e-07

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 52.17  E-value: 1.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1424 QGELILQEsfqvwdpKTLIRKGRERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALW 1499
Cdd:smart00233    4 EGWLYKKS-------GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIK 73
                            90       100       110
                    ....*....|....*....|....*....|...
gi 767934614   1500 VGRTPTsdnkIVLKASSIENKQDWIKHIREVIQ 1532
Cdd:smart00233   74 TSDRKT----LLLQAESEEEREKWVEALRKAIA 102
SPEC smart00150
Spectrin repeats;
162-278 1.58e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 1.58e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    162 EDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKKKV--IKAPIEDLDLEGQKLLQriqssesfpkknSG 239
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE------------EG 68
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 767934614    240 SGNAdlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLD 278
Cdd:smart00150   69 HPDA------EEIEERLEELNERWEELKELAEERRQKLE 101
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1603-1654 2.54e-07

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 49.46  E-value: 2.54e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767934614   1603 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRspaAEGLVPC 1654
Cdd:smart00326    6 RALYDYTAQDPDELSFKKGDIITVLEKSDD--GWWKGRLGRG---KEGLFPS 52
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1084-1184 4.62e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 50.39  E-value: 4.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1084 FERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1163
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSE--DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 767934614  1164 AVDKRYRDFSLRMEKYRTSLE 1184
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1221-1398 1.08e-06

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1221 HELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTY---LWEMTsgveeIPPGIVNKELI--IFGNMQEIYEFhNNI 1295
Cdd:COG5422   472 KEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWikpLEESN-----IIPENARRNFIkhVFANINEIYAV-NSK 545
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1296 FLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLIlEHAGS-------YFDEIQ-----QRHGlansIS 1360
Cdd:COG5422   546 LLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEF-EREKSvnpnfarFDHEVErldesRKLE----LD 620
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767934614 1361 SYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVM 1398
Cdd:COG5422   621 GYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
282-385 1.97e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 48.85  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   282 QLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNcMNVY-VNINRIMSVANRLVESGHYASQQI 360
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKALEAE-LAAHqDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 767934614   361 RQIASQLEQEWKAFAAALDERSTLL 385
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
512-611 7.61e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.93  E-value: 7.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   512 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 591
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|
gi 767934614   592 QLEDRIQDFVRRVEQRKILL 611
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2116-2211 2.00e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 45.62  E-value: 2.00e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2116 QDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSClCLEENVENDPCKFALTSRTGdvvETFILHSS 2195
Cdd:smart00233   10 KSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVRE-APDPDSSKKPHCFEIKTSDR---KTLLLQAE 85
                            90
                    ....*....|....*.
gi 767934614   2196 SPSVRQTWIHEINQIL 2211
Cdd:smart00233   86 SEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2116-2212 2.13e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 45.63  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2116 QDAGLLPRCRERRIFLFEQIVIFSepldkKKGFSMPGFLFKNSIKVSCLCLEENVEND----PCKFALTSRTGDVVETFI 2191
Cdd:pfam00169   10 KGGGKKKSWKKRYFVLFDGSLLYY-----KDDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTGERTGKRTYL 84
                           90       100
                   ....*....|....*....|.
gi 767934614  2192 LHSSSPSVRQTWIHEINQILE 2212
Cdd:pfam00169   85 LQAESEEERKDWIKAIQSAIR 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
161-279 8.02e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.15  E-value: 8.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   161 FEDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKK--KVIKAPIEDLDLEGQKLLQRIQSSEsfpkkns 238
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLIDEGHYAS------- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 767934614   239 gsgnadlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQ 279
Cdd:pfam00435   76 -----------EEIQERLEELNERWEQLLELAAERKQKLEE 105
 
Name Accession Description Interval E-value
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2729-2991 0e+00

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 589.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd14113     1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTY 2888
Cdd:cd14113    81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFV 2968
Cdd:cd14113   161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                         250       260
                  ....*....|....*....|...
gi 767934614 2969 CFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14113   241 CFLLQMDPAKRPSAALCLQEQWL 263
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
1656-1913 2.32e-162

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 501.64  E-value: 2.32e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1656 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 1734
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1735 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETVEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1812
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1813 PMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLS 1892
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSVDQGDSSSPSFNPSDNSLLS 240
                          250       260
                   ....*....|....*....|.
gi 767934614  1893 SSSPIDEMEERKSSSLKRRHY 1913
Cdd:pfam16609  241 SSSPISEMDERRSSFLKKRHY 261
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
2743-2990 7.30e-119

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 376.22  E-value: 7.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCV 2822
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2823 VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAP 2902
Cdd:cd14006    81 AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADR-PSPQIKIIDFGLARKLNPGEELKEIFGTPEFVAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2903 EIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSFPddYFKGVSQKAKEFVCFLLQEDPAKRP 2980
Cdd:cd14006   160 EIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANIsaCRVDFSEE--YFSSVSQEAKDFIRKLLVKEPRKRP 237
                         250
                  ....*....|
gi 767934614 2981 SAALALQEQW 2990
Cdd:cd14006   238 TAQEALQHPW 247
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2743-2990 2.81e-112

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 357.35  E-value: 2.81e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCV 2822
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2823 VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAP 2902
Cdd:cd14115    81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEFAAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2903 EIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd14115   161 EVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRPTA 240

                  ....*...
gi 767934614 2983 ALALQEQW 2990
Cdd:cd14115   241 ATCLQHPW 248
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
2089-2227 6.20e-79

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 257.19  E-value: 6.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2089 VGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEE 2168
Cdd:cd13241     1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2169 NVENDPCKFALTSRTG-DVVETFILHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEY 2227
Cdd:cd13241    81 NVDGDPLRFALKSRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
2742-2990 5.49e-76

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 253.94  E-value: 5.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05117     7 VLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMlrrEIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNPE 2898
Cdd:cd05117    87 FDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLKTVCGTPY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAK 2978
Cdd:cd05117   167 YVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLLVVDPKK 246
                         250
                  ....*....|..
gi 767934614 2979 RPSAALALQEQW 2990
Cdd:cd05117   247 RLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
2737-2991 6.30e-76

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 253.61  E-value: 6.30e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKkdRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQLL 2894
Cdd:smart00220   81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQE 2974
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVK 237
                           250
                    ....*....|....*..
gi 767934614   2975 DPAKRPSAALALQEQWL 2991
Cdd:smart00220  238 DPEKRLTAEEALQHPFF 254
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
2743-2991 7.37e-73

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 244.44  E-value: 7.37e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKcRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKptIKLADFGDAVQLNTTYYIHQLLGNPEF 2899
Cdd:cd14103    81 VVDDDFeLTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQ--IKIIDFGLARKYDPDKKLKVLFGTPEF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:cd14103   159 VAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPRKR 238
                         250
                  ....*....|..
gi 767934614 2980 PSAALALQEQWL 2991
Cdd:cd14103   239 MSAAQCLQHPWL 250
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
1413-1535 3.46e-72

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 237.28  E-value: 3.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1413 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1492
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767934614 1493 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1535
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
2731-2991 6.55e-71

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 239.70  E-value: 6.55e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQSLQHPLLVGLLDTFETP 2803
Cdd:cd14105     1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasrrgvsREDIEREVSILRQVLHPNIITLHDVFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2804 TSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDESLAKPTIKLADFGDAV 2882
Cdd:cd14105    81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNVPIPRIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQ 2962
Cdd:cd14105   161 KIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14105   241 LAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
2731-2991 1.34e-70

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 238.77  E-value: 1.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQSLQHPLLVGLLDTFETP 2803
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKssrrgvsREDIEREVSILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2804 TSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDESLAKPTIKLADFGDAV 2882
Cdd:cd14194    81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVPKPRIKIIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQ 2962
Cdd:cd14194   161 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 240
                         250       260
                  ....*....|....*....|....*....
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14194   241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2730-2991 2.06e-69

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 235.32  E-value: 2.06e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2730 KDNFDSFYS-EVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ---VTHELGIL-QSLQHPLLVGLLDTFETPT 2804
Cdd:cd14106     2 TENINEVYTvESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCrneILHEIAVLeLCKDCPRVVNLHEVYETRS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQL 2884
Cdd:cd14106    82 ELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKA 2964
Cdd:cd14106   162 GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLA 241
                         250       260
                  ....*....|....*....|....*..
gi 767934614 2965 KEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14106   242 IDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
2731-2993 2.47e-67

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 229.50  E-value: 2.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQSLQHPLLVGLLDTFETP 2803
Cdd:cd14195     1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSssrrgvsREEIEREVNILREIQHPNIITLHDIFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2804 TSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDESLAKPTIKLADFGDAV 2882
Cdd:cd14195    81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVPNPRIKLIDFGIAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQ 2962
Cdd:cd14195   161 KIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSE 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQEQWLQA 2993
Cdd:cd14195   241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWIKA 271
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
2732-2991 4.70e-64

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 220.21  E-value: 4.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2732 NFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKL-------MKRDQVTHELGILQSLQHPLLVGLLDTFETPT 2804
Cdd:cd14196     2 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHPNIITLHDVYENRT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDESLAKPTIKLADFGDAVQ 2883
Cdd:cd14196    82 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLAHE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQK 2963
Cdd:cd14196   162 IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSEL 241
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14196   242 AKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2742-2991 1.93e-60

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 209.79  E-value: 1.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd14197    16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcrmEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLD-CVV-RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLG 2895
Cdd:cd14197    96 IFNqCVAdREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELREIMG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd14197   176 TPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKTLLIKK 255
                         250
                  ....*....|....*.
gi 767934614 2976 PAKRPSAALALQEQWL 2991
Cdd:cd14197   256 PENRATAEDCLKHPWL 271
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2731-2991 2.08e-59

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 206.70  E-value: 2.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYS-EVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQSLQ-HPLLVGLLDTFETPTS 2805
Cdd:cd14198     3 DNFNNFYIlTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDcraEILHEIAVLELAKsNPRVVNLHEVYETTSE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2806 YILVLEMADQGRLLD-CVVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQ 2883
Cdd:cd14198    83 IILILEYAAGGEIFNlCVPDLAEmVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQK 2963
Cdd:cd14198   163 IGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQL 242
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14198   243 ATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
2735-2991 1.27e-57

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 200.89  E-value: 1.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd14107     2 SVYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdESLAKPTIKLADFGDAVQLNTTYYIHQLL 2894
Cdd:cd14107    82 SEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM-VSPTREDIKICDFGFAQEITPSEHQFSKY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQE 2974
Cdd:cd14107   161 GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQP 240
                         250
                  ....*....|....*..
gi 767934614 2975 DPAKRPSAALALQEQWL 2991
Cdd:cd14107   241 DPEKRPSASECLSHEWF 257
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
2736-2991 2.55e-55

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 194.34  E-value: 2.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd14114     3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHeSDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWG-SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdESLAKPTIKLADFGDAVQLNTTYYIHQL 2893
Cdd:cd14114    83 GGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMC-TTKRSNEVKLIDFGLATHLDPKESVKVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:cd14114   162 TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLLL 241
                         250
                  ....*....|....*...
gi 767934614 2974 EDPAKRPSAALALQEQWL 2991
Cdd:cd14114   242 ADPNKRMTIHQALEHPWL 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2733-3015 8.49e-54

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 191.58  E-value: 8.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKL-KKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQ 2892
Cdd:cd14085    80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVTMKT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLN-ICRLDFSFPDDYFKGVSQKAKEFVCFL 2971
Cdd:cd14085   160 VCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKrILNCDYDFVSPWWDDVSLNAKDLVKKL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 2972 LQEDPAKRPSAALALQEQWLQAGNGRSTgVLDTSR--LTSFIERRK 3015
Cdd:cd14085   240 IVLDPKKRLTTQQALQHPWVTGKAANFA-HMDTAQkkLQEFNARRK 284
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
2743-2990 1.18e-53

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 189.27  E-value: 1.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd14003     8 LGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKikrEIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGELF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGdavqLNTTYYIHQLL----G 2895
Cdd:cd14003    88 DYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDK---NGNLKIIDFG----LSNEFRGGSLLktfcG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPV-SLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQE 2974
Cdd:cd14003   161 TPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIP----SHLSPDARDLIRRMLVV 236
                         250
                  ....*....|....*.
gi 767934614 2975 DPAKRPSAALALQEQW 2990
Cdd:cd14003   237 DPSKRITIEEILNHPW 252
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
2737-2991 2.29e-53

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 188.90  E-value: 2.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTT--YYIHQLL 2894
Cdd:cd14087    83 ELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKKGpnCLMKTTC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQE 2974
Cdd:cd14087   163 GTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLLTV 242
                         250
                  ....*....|....*..
gi 767934614 2975 DPAKRPSAALALQEQWL 2991
Cdd:cd14087   243 NPGERLSATQALKHPWI 259
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
2743-2992 7.27e-53

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 187.30  E-value: 7.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14007     8 LGKGKFGNVYLAREKKSGFIVALKVISKSQLQKsgleHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLN----TTyyihqLL 2894
Cdd:cd14007    88 YKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGS---NGELKLADFGWSVHAPsnrrKT-----FC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFVCFLLQE 2974
Cdd:cd14007   160 GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSS----VSPEAKDLISKLLQK 235
                         250
                  ....*....|....*...
gi 767934614 2975 DPAKRPSAALALQEQWLQ 2992
Cdd:cd14007   236 DPSKRLSLEQVLNHPWIK 253
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1911-2084 1.22e-51

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 180.96  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1911 RHYVLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDmKGKDKIVFGNIHQIYDWHRDFFLGELEKCLED---PEKLGS 1987
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-PEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1988 LFVKHERRLHMYIAYCQNKPKSEHIVSEYI--DTFFEDLKQRLG---HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKA 2062
Cdd:cd00160    80 VFLKLAPFFKIYSEYCSNHPDALELLKKLKkfNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159
                         170       180
                  ....*....|....*....|..
gi 767934614 2063 SLDTSELERAVEVMCIVPRRCN 2084
Cdd:cd00160   160 HEDREDLKKALEAIKEVASQVN 181
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
2736-2991 1.56e-51

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 183.67  E-value: 1.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd14191     3 FYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKeKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWG-SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKptIKLADFGDAVQLNTTYYIHQ 2892
Cdd:cd14191    83 GGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTK--IKLIDFGLARRLENAGSLKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLL 2972
Cdd:cd14191   161 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 240
                         250
                  ....*....|....*....
gi 767934614 2973 QEDPAKRPSAALALQEQWL 2991
Cdd:cd14191   241 KKDMKARLTCTQCLQHPWL 259
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2743-2990 1.76e-51

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 183.34  E-value: 1.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR--DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd14083    11 LGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGkeDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGELFD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFG-----DAVQLNTTyyihqlLG 2895
Cdd:cd14083    91 RIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGlskmeDSGVMSTA------CG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd14083   165 TPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFIRHLMEKD 244
                         250
                  ....*....|....*
gi 767934614 2976 PAKRPSAALALQEQW 2990
Cdd:cd14083   245 PNKRYTCEQALEHPW 259
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
2743-2991 2.40e-51

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 183.24  E-value: 2.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14192    12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKeREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFDR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWG-SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKpTIKLADFGDAVQLNTTYYIHQLLGNPEFA 2900
Cdd:cd14192    92 ITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGN-QIKIIDFGLARRYKPREKLKVNFGTPEFL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2901 APEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRP 2980
Cdd:cd14192   171 APEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCRM 250
                         250
                  ....*....|.
gi 767934614 2981 SAALALQEQWL 2991
Cdd:cd14192   251 SATQCLKHEWL 261
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2743-2985 9.40e-51

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 180.79  E-value: 9.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIiKRKEVEHtlnERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQL-NTTYYIHQLLGNP 2897
Cdd:cd05123    81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSD---GHIKLTDFGLAKELsSDGDRTYTFCGTP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDdyfkGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd05123   158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPE----YVSPEAKSLISGLLQKDPT 233

                  ....*...
gi 767934614 2978 KRPSAALA 2985
Cdd:cd05123   234 KRLGSGGA 241
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
2737-2990 1.42e-50

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 181.13  E-value: 1.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK---KLMKR--DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKrkvAGNDKnlQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKpTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd14098    82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPV-IVKISDFGLAKVIHTGTFLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPEIILGNPVSLTS------DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAK 2965
Cdd:cd14098   161 TFCGTMAYLAPEILMSKEQNLQGgysnlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISEEAI 240
                         250       260
                  ....*....|....*....|....*
gi 767934614 2966 EFVCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd14098   241 DFILRLLDVDPEKRMTAAQALDHPW 265
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
2734-2991 5.05e-50

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 179.34  E-value: 5.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFY--SEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVL 2810
Cdd:cd14193     1 NSYYnvNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKeKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGRLLDCVVRWG-SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKpTIKLADFGDAVQLNTTYY 2889
Cdd:cd14193    81 EYVDGGELFDRIIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAN-QVKIIDFGLARRYKPREK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVC 2969
Cdd:cd14193   160 LRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFIS 239
                         250       260
                  ....*....|....*....|..
gi 767934614 2970 FLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14193   240 KLLIKEKSWRMSASEALKHPWL 261
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2734-2994 8.03e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 179.32  E-value: 8.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14169     2 NSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALrgKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAvQLNTTYYIH 2891
Cdd:cd14169    82 LVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLS-KIEAQGMLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFL 2971
Cdd:cd14169   161 TACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRHL 240
                         250       260
                  ....*....|....*....|...
gi 767934614 2972 LQEDPAKRPSAALALQEQWLQAG 2994
Cdd:cd14169   241 LERDPEKRFTCEQALQHPWISGD 263
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
2743-2991 8.79e-50

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 178.57  E-value: 8.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14190    12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKdKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKpTIKLADFGDAVQLNTTYYIHQLLGNPEFA 2900
Cdd:cd14190    92 IVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGH-QVKIIDFGLARRYNPREKLKVNFGTPEFL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2901 APEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRP 2980
Cdd:cd14190   171 SPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSARM 250
                         250
                  ....*....|.
gi 767934614 2981 SAALALQEQWL 2991
Cdd:cd14190   251 SATQCLKHPWL 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
2737-2990 1.43e-49

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 177.90  E-value: 1.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLM-KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKaKCKgKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DESLAKPTIKLADFGDAVQLntTYYIHQL 2893
Cdd:cd14095    82 GGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVvEHEDGSKSLKLADFGLATEV--KEPLFTV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL--DDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFL 2971
Cdd:cd14095   160 CGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLISRM 239
                         250
                  ....*....|....*....
gi 767934614 2972 LQEDPAKRPSAALALQEQW 2990
Cdd:cd14095   240 LVVDPEKRYSAGQVLDHPW 258
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
2737-2991 3.21e-48

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 173.89  E-value: 3.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK----RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTkpkqREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLN------T 2886
Cdd:cd14099    83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENM---NVKIGDFGLAARLEydgerkK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TyyihqLLGNPEFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfKGVSQKAK 2965
Cdd:cd14099   160 T-----LCGTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAK 232
                         250       260
                  ....*....|....*....|....*.
gi 767934614 2966 EFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14099   233 DLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2730-2991 6.85e-48

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 173.29  E-value: 6.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2730 KDNFDsfYSEVaeLGRGRFSVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYI 2807
Cdd:cd14167     2 RDIYD--FREV--LGTGAFSEVVLAEEKRTQKLVAIKCIAKKALegKETSIENEIAVLHKIKHPNIVALDDIYESGGHLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTT 2887
Cdd:cd14167    78 LIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEF 2967
Cdd:cd14167   158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDF 237
                         250       260
                  ....*....|....*....|....
gi 767934614 2968 VCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14167   238 IQHLMEKDPEKRFTCEQALQHPWI 261
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1914-2084 1.42e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 169.02  E-value: 1.42e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1914 VLQELVETERDYVRDLGYVVEGYMALMKE--DGVPDDMKgkdkIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVK 1991
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEIK----TIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1992 HERRLHMYIAYCQNKPKSEHIVSEY------IDTFFEDLKQRLG-HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASL 2064
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLKKLlkknpkFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHP 156
                          170       180
                   ....*....|....*....|
gi 767934614  2065 DTSELERAVEVMCIVPRRCN 2084
Cdd:pfam00621  157 DYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1914-2085 1.42e-47

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 169.02  E-value: 1.42e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1914 VLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDMKGKDKIvFGNIHQIYDWHRDFfLGELEKCLED----PEKLGSLF 1989
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL-FGNIEEIYEFHRDF-LDELEERIEEwddsVERIGDVF 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1990 VKHERRLHMYIAYCQNKPKSEHIVSE--YIDTFFEDLKQRLGH----RLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKAS 2063
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALELLKKlkKNPRFQKFLKEIESSpqcrRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                           170       180
                    ....*....|....*....|..
gi 767934614   2064 LDTSELERAVEVMCIVPRRCND 2085
Cdd:smart00325  159 EDREDLKKALKAIKELANQVNE 180
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2736-2991 2.10e-47

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 171.62  E-value: 2.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd14108     3 YYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlAKPTIKLADFGDAVQLNTTYYIHQLLG 2895
Cdd:cd14108    83 ELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQ-KTDQVRICDFGNAQELTPNEPQYCKYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd14108   161 TPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVLVSD 240
                         250
                  ....*....|....*.
gi 767934614 2976 PAkRPSAALALQEQWL 2991
Cdd:cd14108   241 RL-RPDAEETLEHPWF 255
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
2742-2982 1.49e-45

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 167.01  E-value: 1.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKL----MKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05581     8 PLGEGSYSTVVLAKEKETGKEYAIKVLDKRHiikeKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPNGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQLL--- 2894
Cdd:cd05581    88 LLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDE---DMHIKITDFGTAKVLGPDSSPESTKgda 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 ---------------GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDdyfkG 2959
Cdd:cd05581   165 dsqiaynqaraasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPE----N 240
                         250       260
                  ....*....|....*....|...
gi 767934614 2960 VSQKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd05581   241 FPPDAKDLIQKLLVLDPSKRLGV 263
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2743-2995 4.01e-45

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 165.94  E-value: 4.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ-VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14166    11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSsLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAvQLNTTYYIHQLLGNPEFAA 2901
Cdd:cd14166    91 ILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLS-KMEQNGIMSTACGTPGYVA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2902 PEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPS 2981
Cdd:cd14166   170 PEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHLLEKNPSKRYT 249
                         250
                  ....*....|....
gi 767934614 2982 AALALQEQWLqAGN 2995
Cdd:cd14166   250 CEKALSHPWI-IGN 262
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1236-1406 7.85e-45

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 161.31  E-value: 7.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1236 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1311
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1312 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1386
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                         170       180
                  ....*....|....*....|...
gi 767934614 1387 G---KGEIKDGLEVMLSVPKRAN 1406
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
2745-2982 2.52e-44

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 163.16  E-value: 2.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2745 RGRFSVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA---DQGR 2817
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRknqvDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLpggDLYS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVvrwGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG----------------DA 2881
Cdd:cd05579    83 LLENV---GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAN---GHLKLTDFGlskvglvrrqiklsiqKK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 VQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfKGVS 2961
Cdd:cd05579   157 SNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPED--PEVS 234
                         250       260
                  ....*....|....*....|.
gi 767934614 2962 QKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd05579   235 DEAKDLISKLLTPDPEKRLGA 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
2743-2990 3.03e-44

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 162.42  E-value: 3.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd14185     8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKLkgKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKP-TIKLADFGDAVQLntTYYIHQLLGNPEF 2899
Cdd:cd14185    88 AIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKStTLKLADFGLAKYV--TGPIFTVCGTPTY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICRL-DFSFPDDYFKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14185   166 VAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQLgHYEFLPPYWDNISEAAKDLISRLLVVDPE 245
                         250
                  ....*....|...
gi 767934614 2978 KRPSAALALQEQW 2990
Cdd:cd14185   246 KRYTAKQVLQHPW 258
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
2742-3006 5.67e-44

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 162.34  E-value: 5.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14104     7 ELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWG-SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKpTIKLADFGDAVQLNTTYYIHQLLGNPEFA 2900
Cdd:cd14104    87 ITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGS-YIKIIEFGQSRQLKPGDKFRLQYTSAEFY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2901 APEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRP 2980
Cdd:cd14104   166 APEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRM 245
                         250       260
                  ....*....|....*....|....*..
gi 767934614 2981 SAALALQEQWLQAGNGR-STGVLDTSR 3006
Cdd:cd14104   246 TAQEALNHPWLKQGMETvSSKDIKTTR 272
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
2742-2995 6.12e-44

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 162.80  E-value: 6.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDqVTHELGILQSL-QHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd14091     7 EIGKGSYSVCKRCIHKATGKEYAVKIIDKS--KRD-PSEEIEILLRYgQHPNIITLRDVYDDGNSVYLVTELLRGGELLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKPTIKLADFGDAVQLNTTyyiHQLLGNP-- 2897
Cdd:cd14091    84 RILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILyADESGDPESLRICDFGFAKQLRAE---NGLLMTPcy 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 --EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLL 2972
Cdd:cd14091   161 taNFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgpNDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKML 240
                         250       260
                  ....*....|....*....|...
gi 767934614 2973 QEDPAKRPSAALALQEQWLQAGN 2995
Cdd:cd14091   241 HVDPSQRPTAAQVLQHPWIRNRD 263
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
2743-2991 6.15e-44

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 162.14  E-value: 6.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD--------QVTH-ELGILQSLQ-HPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14093    11 LGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSeneaeelrEATRrEIEILRQVSgHPNIIELHDVFESPTFIFLVFEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQ 2892
Cdd:cd14093    91 CRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNL---NVKISDFGFATRLDEGEKLRE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEII-----LGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKE 2966
Cdd:cd14093   168 LCGTPGYLAPEVLkcsmyDNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPEWDDISDTAKD 247
                         250       260
                  ....*....|....*....|....*
gi 767934614 2967 FVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14093   248 LISKLLVVDPKKRLTAEEALEHPFF 272
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
2737-2986 1.71e-43

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 160.44  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRerflREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG--DAVQLNTTYYI 2890
Cdd:cd14014    82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED---GRVKLTDFGiaRALGDSGLTQT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCF 2970
Cdd:cd14014   159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILR 238
                         250
                  ....*....|....*.
gi 767934614 2971 LLQEDPAKRPSAALAL 2986
Cdd:cd14014   239 ALAKDPEERPQSAAEL 254
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2742-2991 1.73e-43

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 161.44  E-value: 1.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRD--QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14086     8 ELGKGAFSVVRRCVQKSTGQEFAAKIINtKKLSARDhqKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQL---NTTYYihQLLG 2895
Cdd:cd14086    88 FEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVqgdQQAWF--GFAG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd14086   166 TPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQMLTVN 245
                         250
                  ....*....|....*.
gi 767934614 2976 PAKRPSAALALQEQWL 2991
Cdd:cd14086   246 PAKRITAAEALKHPWI 261
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
2743-2991 1.99e-43

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 160.11  E-value: 1.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQ---VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14081     9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKeKLSKESVlmkVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA-VQLNTTyYIHQLLGNP 2897
Cdd:cd14081    89 FDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKN---NIKIADFGMAsLQPEGS-LLETSCGSP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPV-SLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFVCFLLQEDP 2976
Cdd:cd14081   165 HYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHF----ISPDAQDLLRRMLEVNP 240
                         250
                  ....*....|....*
gi 767934614 2977 AKRPSAALALQEQWL 2991
Cdd:cd14081   241 EKRITIEEIKKHPWF 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
2743-2991 2.56e-43

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 160.04  E-value: 2.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKC--DQKGTKRAVATKFVNKKLMKRDQVT----HELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14080     8 IGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEkflpRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFG--------DAVQLNTTY 2888
Cdd:cd14080    88 DLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNN---NVKLSDFGfarlcpddDGDVLSKTF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 yihqlLGNPEFAAPEIILGNPVS-LTSDTWSVGVLTYVLLSGVSPFlDDSveetclNICRL-------DFSFPDDYfKGV 2960
Cdd:cd14080   165 -----CGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPF-DDS------NIKKMlkdqqnrKVRFPSSV-KKL 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767934614 2961 SQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14080   232 SPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
2743-2987 2.58e-43

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 158.20  E-value: 2.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKklLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRW-GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQL---NTTYYIHQLLGN 2896
Cdd:cd00180    81 LLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSD---GTVKLADFGLAKDLdsdDSLLKTTGGTTP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLlsgvspflddsveetclnicrldfsfpddyfkgvsQKAKEFVCFLLQEDP 2976
Cdd:cd00180   158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYDP 202
                         250
                  ....*....|.
gi 767934614 2977 AKRPSAALALQ 2987
Cdd:cd00180   203 KKRPSAKELLE 213
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
2743-2991 3.18e-43

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 160.25  E-value: 3.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR---------DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14084    14 LGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIgsrreinkpRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLELM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQL 2893
Cdd:cd14084    94 EGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLSKILGETSLMKTL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIIL---GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLN-ICRLDFSFPDDYFKGVSQKAKEFVC 2969
Cdd:cd14084   174 CGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEqILSGKYTFIPKAWKNVSEEAKDLVK 253
                         250       260
                  ....*....|....*....|..
gi 767934614 2970 FLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14084   254 KMLVVDPSRRPSIEEALEHPWL 275
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
2743-2979 6.39e-43

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 158.54  E-value: 6.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFV-----NKKLmkRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkklNKKL--QENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNP 2897
Cdd:cd14009    79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAETLCGSP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14009   159 LYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPA 238

                  ..
gi 767934614 2978 KR 2979
Cdd:cd14009   239 ER 240
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1237-1407 1.72e-42

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 154.38  E-value: 1.72e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1237 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPgivNKELIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVGH 1312
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1313 CFVTWADKFQMYVTYCKNKPDSTQLI--LEHAGSYFDEIQQRHGLAN----SISSYLIKPVQRITKYQLLLKELLTCCEE 1386
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156
                           170       180
                    ....*....|....*....|....
gi 767934614   1387 G---KGEIKDGLEVMLSVPKRAND 1407
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
2743-2991 2.65e-42

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 157.04  E-value: 2.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14079    10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSldmeEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGGEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFG------DAVQLNTTyyihq 2892
Cdd:cd14079    90 FDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNM---NVKIADFGlsnimrDGEFLKTS----- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 lLGNPEFAAPEIILGN----PvslTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFV 2968
Cdd:cd14079   162 -CGSPNYAAPEVISGKlyagP---EVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSH----LSPGARDLI 233
                         250       260
                  ....*....|....*....|...
gi 767934614 2969 CFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14079   234 KRMLVVDPLKRITIPEIRQHPWF 256
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
2743-2991 5.17e-42

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 156.14  E-value: 5.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATK---FVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd06606     8 LGKGSFGSVYLALNLDTGELMAVKeveLSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYI---HQLLGN 2896
Cdd:cd06606    88 SLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG---VVKLADFGCAKRLAEIATGegtKSLRGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF--LDDSVEetclNICRLDFS-----FPDDyfkgVSQKAKEFV- 2968
Cdd:cd06606   165 PYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWseLGNPVA----ALFKIGSSgepppIPEH----LSEEAKDFLr 236
                         250       260
                  ....*....|....*....|....
gi 767934614 2969 -CFllQEDPAKRPSAALALQEQWL 2991
Cdd:cd06606   237 kCL--QRDPKKRPTADELLQHPFL 258
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2738-3015 1.72e-41

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 156.31  E-value: 1.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2738 SEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLmkrdQVTHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14092     9 LREEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL----DTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFG------DAVQLNTTYYI 2890
Cdd:cd14092    85 ELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGfarlkpENQPLKTPCFT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQllgnpeFAAPEIILGNPVSLT----SDTWSVGVLTYVLLSGVSPF----LDDSVEETCLNICRLDFSFPDDYFKGVSQ 2962
Cdd:cd14092   165 LP------YAAPEVLKQALSTQGydesCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSFDGEEWKNVSS 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGRS------TGVLDTSRLTSFIERRK 3015
Cdd:cd14092   239 EAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSstplmtPGVLSSSAAAVSTALRA 297
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2737-2991 1.87e-41

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 155.67  E-value: 1.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFS-VVKKCDQKGTKRAVATKFVNK--------KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYI 2807
Cdd:cd14096     3 YRLINKIGEGAFSnVYKAVPLRNTGKPVAIKVVRKadlssdnlKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL----------------------VD 2865
Cdd:cd14096    83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkadddetkVD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2866 ESLAKP--------TIKLADFGDAVQL--NTTyyiHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLD 2935
Cdd:cd14096   163 EGEFIPgvggggigIVKLADFGLSKQVwdSNT---KTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYD 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2936 DSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14096   240 ESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
2743-2991 3.29e-41

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 154.38  E-value: 3.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd14183    14 IGDGNFAVVKECVERSTGREYALKIINKSKCrgKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDLFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESL-AKPTIKLADFGDAVQLNTTYYihQLLGNPEF 2899
Cdd:cd14183    94 AITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdGSKSLKLGDFGLATVVDGPLY--TVCGTPTY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCL--NICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14183   172 VAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLfdQILMGQVDFPSPYWDNVSDSAKELITMMLQVDVD 251
                         250
                  ....*....|....
gi 767934614 2978 KRPSAALALQEQWL 2991
Cdd:cd14183   252 QRYSALQVLEHPWV 265
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1237-1406 4.04e-41

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 150.53  E-value: 4.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1237 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPpgivnKEL-IIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFV 1315
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESE-----EEIkTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1316 TWADKFQMYVTYCKNKPDSTQLI------LEHAGSYFDEIQQR---HGLanSISSYLIKPVQRITKYQLLLKELLTCCEE 1386
Cdd:pfam00621   76 KFAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPP 153
                          170       180
                   ....*....|....*....|...
gi 767934614  1387 G---KGEIKDGLEVMLSVPKRAN 1406
Cdd:pfam00621  154 DhpdYEDLKKALEAIKEVAKQIN 176
Pkinase pfam00069
Protein kinase domain;
2737-2991 4.43e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 152.01  E-value: 4.43e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKekiKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVrylhncriahldlkpenilvdeslaKPTIKLADFgdavqlnttyyihql 2893
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------ESGSSLTTF--------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRlDFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID-QPYAFPELPSNLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 767934614  2974 EDPAKRPSAALALQEQWL 2991
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2729-3033 7.99e-41

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 154.44  E-value: 7.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WK---DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETP 2803
Cdd:cd14168     1 WKkqvEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKgkESSIENEIAVLRKIKHENIVALEDIYESP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2804 TSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQ 2883
Cdd:cd14168    81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQK 2963
Cdd:cd14168   161 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWLQAgngrstgvlDTSrltsfIERRKHQNDVRPIRsiKNFLQSR 3033
Cdd:cd14168   241 AKDFIRNLMEKDPNKRYTCEQALRHPWIAG---------DTA-----LCKNIHESVSAQIR--KNFAKSK 294
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
2743-2990 2.75e-40

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 151.34  E-value: 2.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd14184     9 IGDGNFAVVKECVERSTGKEFALKIIDKAKCcgKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAK-PTIKLADFGDAVQLNTTYYihQLLGNPEF 2899
Cdd:cd14184    89 AITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGtKSLKLGDFGLATVVEGPLY--TVCGTPTY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL-DDSVEETCLN-ICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14184   167 VAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRsENNLQEDLFDqILLGKLEFPSPYWDNITDSAKELISHMLQVNVE 246
                         250
                  ....*....|...
gi 767934614 2978 KRPSAALALQEQW 2990
Cdd:cd14184   247 ARYTAEQILSHPW 259
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2740-3025 5.27e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 157.10  E-value: 5.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK----RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:COG0515    12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAAdpeaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIH--QL 2893
Cdd:COG0515    92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD---GRVKLIDFGIARALGGATLTQtgTV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:COG0515   169 VGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALA 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2974 EDPAKRPSAALALQEQWLQAGNGRSTGVLDTSRLTSFIERRKHQNDVRPIRS 3025
Cdd:COG0515   249 KDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAA 300
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
2733-2991 9.66e-40

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 152.48  E-value: 9.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQSL-QHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14176    17 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDP-TEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKPTIKLADFGDAVQLNTTyyi 2890
Cdd:cd14176    94 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLRAE--- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNP----EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPDDYFKGVSQK 2963
Cdd:cd14176   171 NGLLMTPcytaNFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDT 250
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14176   251 AKDLVSKMLHVDPHQRLTAALVLRHPWI 278
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
2737-2991 1.39e-39

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 148.89  E-value: 1.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINlESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCV-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlAKptIKLADFGDAVQLNTTYYIHQLL 2894
Cdd:cd05122    82 GSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD-GE--VKLIDFGLSAQLSDGKTRNTFV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPDDYFkgVSQKAKEFVCFLLQ 2973
Cdd:cd05122   159 GTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPpGLRNPKK--WSKEFKDFLKKCLQ 236
                         250
                  ....*....|....*...
gi 767934614 2974 EDPAKRPSAALALQEQWL 2991
Cdd:cd05122   237 KDPEKRPTAEQLLKHPFI 254
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
2740-2979 1.57e-39

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 150.04  E-value: 1.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd05580     6 LKTLGTGSFGRVRLVKHKDSGKYYALKILKKaKIIKLKQVEHvlnEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL-NTTYyihQLL 2894
Cdd:cd05580    86 GELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLD---SDGHIKITDFGFAKRVkDRTY---TLC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQE 2974
Cdd:cd05580   160 GTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFP----SFFDPDAKDLIKRLLVV 235

                  ....*
gi 767934614 2975 DPAKR 2979
Cdd:cd05580   236 DLTKR 240
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
2743-2990 1.85e-39

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 148.71  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADqGRLL 2819
Cdd:cd14082    11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFptkQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH-GDML 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVV--RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNP 2897
Cdd:cd14082    90 EMILssEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFRRSVVGTP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDsvEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14082   170 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDINDQIQNAAFMYPPNPWKEISPDAIDLINNLLQVKMR 247
                         250
                  ....*....|...
gi 767934614 2978 KRPSAALALQEQW 2990
Cdd:cd14082   248 KRYSVDKSLSHPW 260
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
2759-2991 3.21e-39

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 148.04  E-value: 3.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2759 TKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL--DCVVRW-GSLTEGKIRA 2835
Cdd:cd14109    24 TERSTGRNFLAQLRYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELvrDNLLPGkDYYTERQVAV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2836 HLGEVLEAVRYLHNCRIAHLDLKPENILvdesLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSD 2915
Cdd:cd14109   104 FVRQLLLALKHMHDLGIAHLDLRPEDIL----LQDDKLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATD 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2916 TWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14109   180 MWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2737-2991 1.32e-38

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 146.12  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTyYIHQL--- 2893
Cdd:cd14111    85 ELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNL---NAIKIVDFGSAQSFNPL-SLRQLgrr 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSfPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:cd14111   161 TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSASLFLKKVLS 239
                         250
                  ....*....|....*...
gi 767934614 2974 EDPAKRPSAALALQEQWL 2991
Cdd:cd14111   240 SYPWSRPTTKDCFAHAWL 257
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
2737-2991 1.84e-38

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 145.83  E-value: 1.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNT---------T 2887
Cdd:cd14110    85 ELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITE---KNLLKIVDLGNAQPFNQgkvlmtdkkG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIhqllgnpEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYfKGVSQKAKEF 2967
Cdd:cd14110   162 DYV-------ETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCY-AGLSGGAVNF 233
                         250       260
                  ....*....|....*....|....
gi 767934614 2968 VCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14110   234 LKSTLCAKPWGRPTASECLQNPWL 257
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
2737-2991 4.02e-38

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 144.83  E-value: 4.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAE-LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14078     4 YYELHEtIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDlpRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV--QLNTTYYIH 2891
Cdd:cd14078    84 PGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQ---NLKLIDFGLCAkpKGGMDHHLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCF 2970
Cdd:cd14078   161 TCCGSPAYAAPELIQGKPyIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEP----EWLSPSSKLLLDQ 236
                         250       260
                  ....*....|....*....|.
gi 767934614 2971 LLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14078   237 MLQVDPKKRITVKELLNHPWV 257
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
2737-2991 5.35e-38

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 145.00  E-value: 5.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK---LMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREkagSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPT----IKLADFGDAVQLN--TT 2887
Cdd:cd14097    83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNdklnIKVTDFGLSVQKYglGE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEF 2967
Cdd:cd14097   163 DMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNV 242
                         250       260
                  ....*....|....*....|....
gi 767934614 2968 VCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14097   243 LQQLLKVDPAHRMTASELLDNPWI 266
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
2731-2979 9.40e-38

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 144.85  E-value: 9.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSfyseVAELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSY 2806
Cdd:cd14209     1 DDFDR----IKTLGTGSFGRVMLVRHKETGNYYAMKILDKqKVVKLKQVEHtlnEKRILQAINFPFLVKLEYSFKDNSNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNT 2886
Cdd:cd14209    77 YMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQ---QGYIKVTDFGFAKRVKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TYYihQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPdDYFKGvsqKAKE 2966
Cdd:cd14209   154 RTW--TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP-SHFSS---DLKD 227
                         250
                  ....*....|...
gi 767934614 2967 FVCFLLQEDPAKR 2979
Cdd:cd14209   228 LLRNLLQVDLTKR 240
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
2743-2979 1.45e-37

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 143.52  E-value: 1.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhIVQTRQQEHifsEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQLLGNPE 2898
Cdd:cd05572    81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSN---GYVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF--LDDSVEETCLNIcrLDFSFPDDYFKGVSQKAKEFVCFLLQEDP 2976
Cdd:cd05572   158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFggDDEDPMKIYNII--LKGIDKIEFPKYIDKNAKNLIKQLLRRNP 235

                  ...
gi 767934614 2977 AKR 2979
Cdd:cd05572   236 EER 238
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
2743-2991 3.55e-37

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 143.24  E-value: 3.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQSL-QHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14175     9 IGVGSYSVCKRCVHKATNMEYAVKVIDKS--KRDP-SEEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGELLDK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKPTIKLADFGDAVQLNTTyyiHQLLGNP--- 2897
Cdd:cd14175    86 ILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNPESLRICDFGFAKQLRAE---NGLLMTPcyt 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 -EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF---LDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:cd14175   163 aNFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSKMLH 242
                         250
                  ....*....|....*...
gi 767934614 2974 EDPAKRPSAALALQEQWL 2991
Cdd:cd14175   243 VDPHQRLTAKQVLQHPWI 260
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
2739-2979 3.65e-37

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 142.01  E-value: 3.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAEL-GRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEMAd 2814
Cdd:cd14002     4 HVLELiGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRnlrQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT-TYYIHQL 2893
Cdd:cd14002    83 QGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG---KGGVVKLCDFGFARAMSCnTLVLTSI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDdyfkGVSQKAKEFVCFLLQ 2973
Cdd:cd14002   160 KGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPS----NMSPEFKSFLQGLLN 235

                  ....*.
gi 767934614 2974 EDPAKR 2979
Cdd:cd14002   236 KDPSKR 241
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
2743-2991 4.05e-37

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 142.17  E-value: 4.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK-KL--MKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd14074    11 LGRGHFAVVKLARHVFTGEKVAVKVIDKtKLddVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkpTIKLADFGDAVQLNTTYYIHQLLGNPE 2898
Cdd:cd14074    91 DYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQG--LVKLTDFGFSNKFQPGEKLETSCGSLA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14074   169 YSAPEILLGDEYDAPAvDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAH----VSPECKDLIRRMLIRDPK 244
                         250
                  ....*....|....
gi 767934614 2978 KRPSAALALQEQWL 2991
Cdd:cd14074   245 KRASLEEIENHPWL 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
2743-2990 1.66e-36

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 140.23  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14663     8 LGEGTFAKVKFARNTKTGESVAIKIIDKEQVARegmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAV---QLNTTYYIHQLLG 2895
Cdd:cd14663    88 FSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDE---DGNLKISDFGLSAlseQFRQDGLLHTTCG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPdDYFkgvSQKAKEFVCFLLQE 2974
Cdd:cd14663   165 TPNYVAPEVLARRGyDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYP-RWF---SPGAKSLIKRILDP 240
                         250
                  ....*....|....*.
gi 767934614 2975 DPAKRPSAALALQEQW 2990
Cdd:cd14663   241 NPSTRITVEQIMASPW 256
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
2735-2991 3.90e-36

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 139.01  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDQVTH-----ELGILQSLQHPLLVGLLDTFETPTSYILV 2809
Cdd:cd14075     2 GFYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKT--KLDQKTQrllsrEISSMEKLHHPNIIRLYEVVETLSKLHLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFGDAVQLNTTYY 2889
Cdd:cd14075    80 MEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFY---ASNNCVKVGDFGFSTHAKRGET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQLLGNPEFAAPEII-----LGNPVsltsDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKA 2964
Cdd:cd14075   157 LNTFCGSPPYAAPELFkdehyIGIYV----DIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSY----VSEPC 228
                         250       260
                  ....*....|....*....|....*..
gi 767934614 2965 KEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14075   229 QELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
2733-2991 4.07e-36

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 140.15  E-value: 4.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQSL-QHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14178     1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKS--KRDP-SEEIEILLRYgQHPNIITLKDVYDDGKFVYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKPTIKLADFGDAVQLNTTyyi 2890
Cdd:cd14178    78 LMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNPESIRICDFGFAKQLRAE--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNP----EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPDDYFKGVSQK 2963
Cdd:cd14178   155 NGLLMTPcytaNFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSISDA 234
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14178   235 AKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
2743-2933 4.84e-36

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 138.68  E-value: 4.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14073     9 LGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQdmvrIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGdavqLNTTYYIHQLL---- 2894
Cdd:cd14073    89 YDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNG---NAKIADFG----LSNLYSKDKLLqtfc 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14073   162 GSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPF 201
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
2733-3035 5.41e-36

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 140.37  E-value: 5.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR------DQVTHELGILQSLQHPLLVGLLDTFETPTSY 2806
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSspglstEDLKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ILVLEMADQGRLLDCVVRWGS----LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAV 2882
Cdd:cd14094    81 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QL-NTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLdDSVEETCLNICRLDFSFPDDYFKGVS 2961
Cdd:cd14094   161 QLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMNPRQWSHIS 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2962 QKAKEFVCFLLQEDPAKRPSAALALQEQWLQagngrstgvlDTSRLTSfierRKHQNDVrpIRSIKNFLQSRLL 3035
Cdd:cd14094   240 ESAKDLVRRMLMLDPAERITVYEALNHPWIK----------ERDRYAY----RIHLPET--VEQLRKFNARRKL 297
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
2736-2992 1.08e-35

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 137.73  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDcVVRW--GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT-TYYIHQ 2892
Cdd:cd06614    81 GSLTD-IITQnpVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLS---KDGSVKLADFGFAAQLTKeKSKRNS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKgVSQKAKEFVCFLL 2972
Cdd:cd06614   157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEK-WSPEFKDFLNKCL 235
                         250       260
                  ....*....|....*....|
gi 767934614 2973 QEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06614   236 VKDPEKRPSAEELLQHPFLK 255
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
2733-2991 2.17e-35

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 138.22  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQSL-QHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14177     2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKS--KRDP-SEEIEILMRYgQHPNIITLKDVYDDGRYVYLVTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKPTIKLADFGDAVQLNTTyyi 2890
Cdd:cd14177    79 LMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANADSIRICDFGFAKQLRGE--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNP----EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPDDYFKGVSQK 2963
Cdd:cd14177   156 NGLLLTPcytaNFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVSDA 235
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14177   236 AKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
2496-2554 2.30e-35

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 129.48  E-value: 2.30e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2496 TMLVTHDYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGH 2554
Cdd:cd11853     1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2743-3004 2.33e-35

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 138.63  E-value: 2.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQvtHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQ--REIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGGELLER 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAvQLNTTYyiHQLLGNP---- 2897
Cdd:cd14179    93 IKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFA-RLKPPD--NQPLKTPcftl 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF-------LDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCF 2970
Cdd:cd14179   170 HYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFqchdkslTCTSAEEIMKKIKQGDFSFEGEAWKNVSQEAKDLIQG 249
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767934614 2971 LLQEDPAKRPSAALALQEQWLQAGNGRSTGVLDT 3004
Cdd:cd14179   250 LLTVDPNKRIKMSGLRYNEWLQDGSQLSSNPLMT 283
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
2743-2991 2.77e-35

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 136.66  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14162     8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQkflpREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA----------VQLNTTY 2888
Cdd:cd14162    88 LDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNN---NLKITDFGFArgvmktkdgkPKLSETY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 yihqlLGNPEFAAPEIILGNPVSLT-SDTWSVGVLTYVLLSGVSPFlDDSVEETCLNICRLDFSFPDDyfKGVSQKAKEF 2967
Cdd:cd14162   165 -----CGSYAYASPEILRGIPYDPFlSDIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVQRRVVFPKN--PTVSEECKDL 236
                         250       260
                  ....*....|....*....|....
gi 767934614 2968 VCFLLQEDPaKRPSAALALQEQWL 2991
Cdd:cd14162   237 ILRMLSPVK-KRITIEEIKRDPWF 259
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
2740-2992 2.78e-35

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 136.95  E-value: 2.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKF--VNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd06623     6 VKVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCR-IAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ-LLG 2895
Cdd:cd06623    86 LADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLIN---SKGEVKIADFGISKVLENTLDQCNtFVG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDD---SVEETCLNICRLDFSFPDDyfKGVSQKAKEFVCFLL 2972
Cdd:cd06623   163 TVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPgqpSFFELMQAICDGPPPSLPA--EEFSPEFRDFISACL 240
                         250       260
                  ....*....|....*....|
gi 767934614 2973 QEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06623   241 QKDPKKRPSAAELLQHPFIK 260
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
2743-2987 3.07e-35

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 137.41  E-value: 3.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK---------RDQVTHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14181    18 IGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERlspeqleevRSSTLKEIHILRQVSgHPSIITLIDSYESSTFIFLVFDL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQ 2892
Cdd:cd14181    98 MRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQL---HIKLSDFGFSCHLEPGEKLRE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEII----------LGNPVsltsDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQ 2962
Cdd:cd14181   175 LCGTPGYLAPEILkcsmdethpgYGKEV----DLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEWDDRSS 250
                         250       260
                  ....*....|....*....|....*
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd14181   251 TVKDLISRLLVVDPEIRLTAEQALQ 275
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
2742-2991 4.52e-35

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 135.82  E-value: 4.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ---VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd06627     7 LIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlksVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILvdesLAKP-TIKLADFGDAVQLN-TTYYIHQLLGN 2896
Cdd:cd06627    87 ASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL----TTKDgLVKLADFGVATKLNeVEKDENSVVGT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPddyfKGVSQKAKEFV--CFllQ 2973
Cdd:cd06627   163 PYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPpLP----ENISPELRDFLlqCF--Q 236
                         250
                  ....*....|....*...
gi 767934614 2974 EDPAKRPSAALALQEQWL 2991
Cdd:cd06627   237 KDPTLRPSAKELLKHPWL 254
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
2770-2991 5.54e-35

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 136.31  E-value: 5.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2770 KKLMKRD------QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEA 2843
Cdd:cd14088    32 KKFLKRDgrkvrkAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2844 VRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTtyYIHQLLGNPEFAAPEII----LGNPVsltsDTWSV 2919
Cdd:cd14088   112 VAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKLENG--LIKEPCGTPEYLAPEVVgrqrYGRPV----DCWAI 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2920 GVLTYVLLSGVSPFLDDSVEETCLN--------ICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14088   186 GVIMYILLSGNPPFYDEAEEDDYENhdknlfrkILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
2743-2979 6.99e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 138.03  E-value: 6.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:PTZ00263   26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKReILKMKQVQHvaqEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYihQLLGNPE 2898
Cdd:PTZ00263  106 FTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLD---NKGHVKVTDFGFAKKVPDRTF--TLCGTPE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQEDPAK 2978
Cdd:PTZ00263  181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFP----NWFDGRARDLVKGLLQTDHTK 256

                  .
gi 767934614 2979 R 2979
Cdd:PTZ00263  257 R 257
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
2737-2991 9.10e-35

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 135.21  E-value: 9.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-----LMKRDQ----VTHELGILQSLQ---HPLLVGLLDTFETPT 2804
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKErilvdTWVRDRklgtVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEMADQG-RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQ 2883
Cdd:cd14004    82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNG---TIKLIDFGSAAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 LNT----TYYihqllGNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDdsVEEtclnICRLDFSFPddyfK 2958
Cdd:cd14004   159 IKSgpfdTFV-----GTIDYAAPEVLRGNPyGGKEQDIWALGVLLYTLVFKENPFYN--IEE----ILEADLRIP----Y 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767934614 2959 GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14004   224 AVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
2743-2991 1.50e-34

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 134.99  E-value: 1.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR---------------DQVTHELGILQSLQHPLLVGLLDTFETPTS-- 2805
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKrregkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIDDPESdk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2806 -YiLVLEMADQGrlldCVVRWGS------LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADF 2878
Cdd:cd14008    81 lY-LVLEYCEGG----PVMELDSgdrvppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTAD---GTVKISDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2879 GDAVQL-NTTYYIHQLLGNPEFAAPEIILGNPVSLT---SDTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSF 2952
Cdd:cd14008   153 GVSEMFeDGNDTLQKTAGTPAFLAPELCDGDSKTYSgkaADIWALGVTLYCLVFGRLPFNGDNILELYEAIqnQNDEFPI 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767934614 2953 PDDyfkgVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14008   233 PPE----LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
2736-2991 1.62e-34

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 134.44  E-value: 1.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14071     1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEEnlkKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQ 2892
Cdd:cd14071    81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANM---NIKIADFGFSNFFKPGELLKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddYFkgVSQKAKEFVCFL 2971
Cdd:cd14071   158 WCGSPPYAAPEVFEGKEYEGPQlDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIP--FF--MSTDCEHLIRRM 233
                         250       260
                  ....*....|....*....|
gi 767934614 2972 LQEDPAKRPSAALALQEQWL 2991
Cdd:cd14071   234 LVLDPSKRLTIEQIKKHKWM 253
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2737-2991 1.96e-34

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 133.90  E-value: 1.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFV-NKKLMKRdQVTHELGILQSL----QHPLLVGLLDTFETPTS--YILV 2809
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIkNDFRHPK-AALREIKLLKHLndveGHPNIVKLLDVFEHRGGnhLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGrLLDcVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakPTIKLADFGDAVQLNTT 2887
Cdd:cd05118    80 FELMGMN-LYE-LIKDYPrgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLEL--GQLKLADFGLARSFTSP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQlLGNPEFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLdfsfpddyfKGVSQkAKE 2966
Cdd:cd05118   156 PYTPY-VATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRL---------LGTPE-ALD 224
                         250       260
                  ....*....|....*....|....*
gi 767934614 2967 FVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd05118   225 LLSKMLKYDPAKRITASQALAHPYF 249
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2743-2972 4.75e-34

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 135.88  E-value: 4.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05573     9 IGRGAFGEVWLVRDKDTGQVYAMKILRKSDMlKREQIAHvraERDILADADSPWIVRLHYAFQDEDHLYLVMEYMPGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLN----TTYYIHQLL 2894
Cdd:cd05573    89 MNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLD---ADGHIKLADFGLCTKMNksgdRESYLNDSV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 --------------------------GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--C 2946
Cdd:cd05573   166 ntlfqdnvlarrrphkqrrvraysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKImnW 245
                         250       260
                  ....*....|....*....|....*.
gi 767934614 2947 RLDFSFPDDyfKGVSQKAKEFVCFLL 2972
Cdd:cd05573   246 KESLVFPDD--PDVSPEAIDLIRRLL 269
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
2737-2933 1.04e-33

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 132.00  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKC-DQKGtkRAVATKFVNKKLMKRDQ-VTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14161     5 YEFLETLGKGTYGRVKKArDSSG--RLVAIKSIRKDRIKDEQdLLHirrEIEIMSSLNHPHIISVYEVFENSSKIVIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd14161    83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDAN---GNIKIADFGLSNLYNQDKFLQ 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767934614 2892 QLLGNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14161   160 TYCGSPLYASPEIVNGRPyIGPEVDSWSLGVLLYILVHGTMPF 202
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
2737-2987 2.37e-33

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 131.05  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK---RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSekeREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGS----LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTY- 2888
Cdd:cd08215    82 DGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLT---KDGVVKLGDFGISKVLESTTd 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPDDYfkgvSQKAKEF 2967
Cdd:cd08215   159 LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQY----SSELRDL 234
                         250       260
                  ....*....|....*....|
gi 767934614 2968 VCFLLQEDPAKRPSAALALQ 2987
Cdd:cd08215   235 VNSMLQKDPEKRPSANEILS 254
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
2742-2979 2.45e-33

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 131.26  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14010     7 EIGRGKHSVVYKGRRKGTIEFVAIKCVDKS--KRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG-----------------DAVQL 2884
Cdd:cd14010    85 LRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGN---GTLKLSDFGlarregeilkelfgqfsDEGNV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFP-DDYFKGVSQK 2963
Cdd:cd14010   162 NKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPpPKVSSKPSPD 241
                         250
                  ....*....|....*.
gi 767934614 2964 AKEFVCFLLQEDPAKR 2979
Cdd:cd14010   242 FKSLLKGLLEKDPAKR 257
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
2737-2991 4.64e-33

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 130.33  E-value: 4.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK---RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNpssLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQL 2893
Cdd:cd14072    82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADM---NIKIADFGFSNEFTPGNKLDTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddYFkgVSQKAKEFVCFLL 2972
Cdd:cd14072   159 CGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP--FY--MSTDCENLLKKFL 234
                         250
                  ....*....|....*....
gi 767934614 2973 QEDPAKRPSAALALQEQWL 2991
Cdd:cd14072   235 VLNPSKRGTLEQIMKDRWM 253
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
2743-2992 5.37e-33

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 130.81  E-value: 5.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVN---KKLMKRDQVTH-------ELGILQSLQ-HPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14182    11 LGRGVSSVVRRCIHKPTRQEYAVKIIDitgGGSFSPEEVQElreatlkEIDILRKVSgHPNIIQLKDTYETNTFFFLVFD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd14182    91 LMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM---NIKLTDFGFSCQLDPGEKLR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPEII----------LGNPVsltsDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVS 2961
Cdd:cd14182   168 EVCGTPGYLAPEIIecsmddnhpgYGKEV----DMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDRS 243
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767934614 2962 QKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd14182   244 DTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
2740-2979 7.77e-33

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 131.59  E-value: 7.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd05574     6 IKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMiKRNKVKRvltEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 G---RLLDcvVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTT---- 2887
Cdd:cd05574    86 GelfRLLQ--KQPGKrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHES---GHIMLTDFDLSKQSSVTpppv 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 ----------YYIHQLL----------------GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEET 2941
Cdd:cd05574   161 rkslrkgsrrSSVKSIEketfvaepsarsnsfvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDET 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767934614 2942 CLNICRLDFSFPDDyfKGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:cd05574   241 FSNILKKELTFPES--PPVSSEAKDLIRKLLVKDPSKR 276
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
2734-2940 8.90e-33

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 130.13  E-value: 8.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVV-KKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQSLQHPLLVGLLDTFETPTSYILVL 2810
Cdd:cd14201     5 DFEYSRKDLVGHGAFAVVfKGRHRKKTDWEVAIKSINKKNLSKSQILlgKEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVD------ESLAKPTIKLADFGDAVQL 2884
Cdd:cd14201    85 EYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkSSVSGIRIKIADFGFARYL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2885 NTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEE 2940
Cdd:cd14201   165 QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQD 220
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
2743-2991 1.18e-32

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 128.95  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQSLQHPLLVGLLDTFETPTSYI-LVLEMADQGR 2817
Cdd:cd14163     8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQrflpRELQIVERLDHKNIIHVYEMLESADGKIyLVMELAEDGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILvdesLAKPTIKLADFGDAVQL--NTTYYIHQLLG 2895
Cdd:cd14163    88 VFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENAL----LQGFTLKLTDFGFAKQLpkGGRELSQTFCG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPV-SLTSDTWSVGVLTYVLLSGVSPFLDDSVEETclnICRLD--FSFPDDYfkGVSQKAKEFVCFLL 2972
Cdd:cd14163   164 STAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKM---LCQQQkgVSLPGHL--GVSRTCQDLLKRLL 238
                         250
                  ....*....|....*....
gi 767934614 2973 QEDPAKRPSAALALQEQWL 2991
Cdd:cd14163   239 EPDMVLRPSIEEVSWHPWL 257
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
2737-2990 1.47e-32

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 129.84  E-value: 1.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAE-LGRGRFSVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14090     3 YKLTGElLGEGAYASVQTCINLYTGKEYAVKIIEKHPgHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADF--GDAVQLNTTY--- 2888
Cdd:cd14090    83 RGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFdlGSGIKLSSTSmtp 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 -YIHQLL---GNPEFAAPEII---LGNPVSLTS--DTWSVGVLTYVLLSGVSPFLDDSVEE----------TCLN----- 2944
Cdd:cd14090   163 vTTPELLtpvGSAEYMAPEVVdafVGEALSYDKrcDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeacqDCQEllfhs 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 2945 ICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd14090   243 IQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
2743-2991 5.01e-32

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 127.38  E-value: 5.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHEL----GILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14116    13 LGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLrrevEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYiHQLLGNPE 2898
Cdd:cd14116    93 YRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG---SAGELKIADFGWSVHAPSSRR-TTLCGTLD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFVCFLLQEDPAK 2978
Cdd:cd14116   169 YLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDF----VTEGARDLISRLLKHNPSQ 244
                         250
                  ....*....|...
gi 767934614 2979 RPSAALALQEQWL 2991
Cdd:cd14116   245 RPMLREVLEHPWI 257
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1600-1659 7.50e-32

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 119.81  E-value: 7.50e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767934614 1600 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1659
Cdd:cd11852     1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
2743-2991 1.06e-31

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 126.43  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQSLQHPLLVGLLDTFETPTSYI-LVLEMADQGR 2817
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEkflpRELEILARLNHKSIIKTYEIFETSDGKVyIVMELGVQGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLL--- 2894
Cdd:cd14165    89 LLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDF---NIKLTDFGFSKRCLRDENGRIVLskt 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 --GNPEFAAPEIILGNPVS-LTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfKGVSQKAKEFVCFL 2971
Cdd:cd14165   166 fcGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRS--KNLTSECKDLIYRL 243
                         250       260
                  ....*....|....*....|
gi 767934614 2972 LQEDPAKRPSAALALQEQWL 2991
Cdd:cd14165   244 LQPDVSQRLCIDEVLSHPWL 263
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
2737-2991 1.53e-31

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 125.91  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDcpeNIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkptIKLADFGDAVQL---NTTYYI 2890
Cdd:cd14069    83 SGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN---LKISDFGLATVFrykGKERLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNPEFAAPEIIL-----GNPVsltsDTWSVGVLTYVLLSGVSPFldDSVEETCLNIC--RLDFSFPDDYFKGVSQK 2963
Cdd:cd14069   160 NKMCGTLPYVAPELLAkkkyrAEPV----DVWSCGIVLFAMLAGELPW--DQPSDSCQEYSdwKENKKTYLTPWKKIDTA 233
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14069   234 ALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
2743-2981 1.58e-31

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 125.48  E-value: 1.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQK-GTKRAVATKFVNKKLMKR---DQVTHELGILQSLQHPLLVGLLDtFETPTSYI-LVLEMADQGR 2817
Cdd:cd14121     3 LGSGTYATVYKAYRKsGAREVVAVKCVSKSSLNKastENLLTEIELLKKLKHPHIVELKD-FQWDEEHIyLIMEYCSGGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdESLAKPTIKLADFGDAVQLNTTYYIHQLLGNP 2897
Cdd:cd14121    82 LSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLL-SSRYNPVLKLADFGFAQHLKPNDEAHSLRGSP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD-FSFPDdyFKGVSQKAKEFVCFLLQEDP 2976
Cdd:cd14121   161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPT--RPELSADCRDLLLRLLQRDP 238

                  ....*
gi 767934614 2977 AKRPS 2981
Cdd:cd14121   239 DRRIS 243
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
2743-2994 1.80e-31

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 125.82  E-value: 1.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM----KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLlkphQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLL-GNP 2897
Cdd:cd14187    95 LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDM---EVKIGDFGLATKVEYDGERKKTLcGTP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14187   172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPT 247
                         250
                  ....*....|....*..
gi 767934614 2978 KRPSAALALQEQWLQAG 2994
Cdd:cd14187   248 ARPTINELLNDEFFTSG 264
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
2744-2979 2.16e-31

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 125.45  E-value: 2.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2744 GRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05578     9 GKGSFGKVCIVQKKDTKKMFAMKYMNKqKCIEKDSVRNvlnELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDLR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQLLGNPEF 2899
Cdd:cd05578    89 YHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDE---QGHVHITDFNIATKLTDGTLATSTSGTKPY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLnICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:cd05578   166 MAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEE-IRAKFETASVLYPAGWSEEAIDLINKLLERDPQKR 244
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
2743-2991 2.48e-31

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 125.31  E-value: 2.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD-----QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd14070    10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDsyvtkNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLL--- 2894
Cdd:cd14070    90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEND---NIKLIDFGLSNCAGILGYSDPFStqc 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFlddSVEEtcLNICRLDFSFPDDYFK----GVSQKAKEFVCF 2970
Cdd:cd14070   167 GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPF---TVEP--FSLRALHQKMVDKEMNplptDLSPGAISFLRS 241
                         250       260
                  ....*....|....*....|.
gi 767934614 2971 LLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14070   242 LLEPDPLKRPNIKQALANRWL 262
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
2743-2979 3.23e-31

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 126.53  E-value: 3.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAhIVSRSEVTHTLAertVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGdAVQLN--TTYYIHQLLGN 2896
Cdd:cd05585    82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYT---GHIALCDFG-LCKLNmkDDDKTNTFCGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDdyfkGVSQKAKEFVCFLLQEDP 2976
Cdd:cd05585   158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPD----GFDRDAKDLLIGLLNRDP 233

                  ...
gi 767934614 2977 AKR 2979
Cdd:cd05585   234 TKR 236
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
2743-2979 4.49e-31

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 124.40  E-value: 4.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVV-KKCDQKGTKRAVATKFVNKKLMKRDQ--VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd14120     1 IGHGAFAVVfKGRHRKKPDLPVAIKCITKKNLSKSQnlLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILV------DESLAKPTIKLADFGDAVQLNTTYYIHQL 2893
Cdd:cd14120    81 DYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsgrKPSPNDIRLKIADFGFARFLQDGMMAATL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCL----NICrLDFSFPddyfKGVSQKAKEFVC 2969
Cdd:cd14120   161 CGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAfyekNAN-LRPNIP----SGTSPALKDLLL 235
                         250
                  ....*....|
gi 767934614 2970 FLLQEDPAKR 2979
Cdd:cd14120   236 GLLKRNPKDR 245
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
2743-2986 4.52e-31

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 124.59  E-value: 4.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG-- 2816
Cdd:cd14186     9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKagmvQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGem 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 -RLLDCVVRwgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIH-QLL 2894
Cdd:cd14186    89 sRYLKNRKK--PFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNM---NIKIADFGLATQLKMPHEKHfTMC 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFVCFLLQE 2974
Cdd:cd14186   164 GTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAF----LSREAQDLIHQLLRK 239
                         250
                  ....*....|..
gi 767934614 2975 DPAKRPSAALAL 2986
Cdd:cd14186   240 NPADRLSLSSVL 251
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
2742-2987 5.61e-31

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 124.31  E-value: 5.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM----KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG- 2816
Cdd:cd08224     7 KIGKGQFSVVYRARCLLDGRLVALKKVQIFEMmdakARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGd 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 --RLLDCVVRWGSL-TEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT-TYYIHQ 2892
Cdd:cd08224    87 lsRLIKHFKKQKRLiPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFIT---ANGVVKLGDLGLGRFFSSkTTAAHS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDD--SVEETCLNICRLDFS-FPDDYFkgvSQKAKEFVC 2969
Cdd:cd08224   164 LVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEkmNLYSLCKKIEKCEYPpLPADLY---SQELRDLVA 240
                         250
                  ....*....|....*...
gi 767934614 2970 FLLQEDPAKRPSAALALQ 2987
Cdd:cd08224   241 ACIQPDPEKRPDISYVLD 258
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
2737-2991 6.89e-31

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 124.48  E-value: 6.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN---------------KKLMKRDQ-VTHELGILQSLQHPLLVGLLDTF 2800
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglkkerekrlEKEISRDIrTIREAALSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2801 ETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGD 2880
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKS---GNIKIIDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2881 AVQLNTTYYIHQLLGNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKG 2959
Cdd:cd14077   160 SNLYDPRRLLRTFCGSLYFAAPELLQAQPyTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYP----SY 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767934614 2960 VSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14077   236 LSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
2743-2989 6.89e-31

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 125.79  E-value: 6.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKL-MKRDQV----THELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLKKEViIEDDDVectmTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG----DAVQLNTTyyiHQL 2893
Cdd:cd05570    83 LMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLD---AEGHIKIADFGmckeGIWGGNTT---STF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQ 2973
Cdd:cd05570   157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYP----RWLSREAVSILKGLLT 232
                         250       260
                  ....*....|....*....|
gi 767934614 2974 EDPAKR----PSAALALQEQ 2989
Cdd:cd05570   233 KDPARRlgcgPKGEADIKAH 252
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2743-3004 1.34e-30

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 124.60  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQvtHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQ--REVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGGELLDR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDA-VQLNTTYYIHQLLGNPEFA 2900
Cdd:cd14180    92 IKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFArLRPQGSRPLQTPCFTLQYA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2901 APEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDS-------VEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:cd14180   172 APELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfhnhAADIMHKIKEGDFSLEGEAWKGVSEEAKDLVRGLLT 251
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767934614 2974 EDPAKRPSAALALQEQWLQAGNGRSTGVLDT 3004
Cdd:cd14180   252 VDPAKRLKLSELRESDWLQGGSALSSTPLMT 282
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
2743-2940 2.90e-30

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 122.43  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKR-AVATKFVNKKLMKRDQ--VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQtlLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPT------IKLADFGDAVQLNTTYYIHQL 2893
Cdd:cd14202    90 DYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGRKSnpnnirIKIADFGFARYLQNNMMAATL 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEE 2940
Cdd:cd14202   170 CGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD 216
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
2737-2990 3.11e-30

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 122.02  E-value: 3.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd14665    82 ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPA-PRLKICDFGYSKSSVLHSQPKSTVGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVS-LTSDTWSVGVLTYVLLSGVSPFLD----DSVEETCLNICRLDFSFPDDYFkgVSQKAKEFVCFL 2971
Cdd:cd14665   161 PAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDYVH--ISPECRHLISRI 238
                         250
                  ....*....|....*....
gi 767934614 2972 LQEDPAKRPSAALALQEQW 2990
Cdd:cd14665   239 FVADPATRITIPEIRNHEW 257
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
2737-2991 4.00e-30

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 122.59  E-value: 4.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKfvnkkLMKRDQ------VT--HELGILQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK-----KIRLDNeeegipSTalREISLLKELKHPNIVKLLDVIHTENKLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQ--GRLLDcvVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDA--VQL 2884
Cdd:cd07829    76 VFEYCDQdlKKYLD--KRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRD---GVLKLADFGLAraFGI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NTTYYIHQLLgNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSV---------------EETCLNICRL 2948
Cdd:cd07829   151 PLRTYTHEVV-TLWYRAPEILLGSKHYSTAvDIWSVGCIFAELITGKPLFPGDSEidqlfkifqilgtptEESWPGVTKL 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2949 ---DFSFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07829   230 pdyKPTFPkwpkndlEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
2743-2979 1.68e-29

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 122.08  E-value: 1.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKKEvIIAKDEVAHTLTenrVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG----DAVQLNTTyyiHQLL 2894
Cdd:cd05571    83 FFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLD---KDGHIKITDFGlckeEISYGATT---KTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQE 2974
Cdd:cd05571   157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFP----STLSPEAKSLLAGLLKK 232

                  ....*
gi 767934614 2975 DPAKR 2979
Cdd:cd05571   233 DPKKR 237
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
2737-2989 2.95e-29

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 119.03  E-value: 2.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLsqkEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGS----LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFGDAVQLNTTYY 2889
Cdd:cd08530    82 PFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILL---SAGDLVKIGDLGISKVLKKNLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQLlGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFkgvSQKAKEFVC 2969
Cdd:cd08530   159 KTQI-GTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVY---SQDLQQIIR 234
                         250       260
                  ....*....|....*....|
gi 767934614 2970 FLLQEDPAKRPSAALALQEQ 2989
Cdd:cd08530   235 SLLQVNPKKRPSCDKLLQSP 254
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
2743-2979 3.69e-29

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 120.88  E-value: 3.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKaILKRNEVKHIMAernvLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG----DAVQLNTTyyiHQL 2893
Cdd:cd05575    83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLD---SQGHVVLTDFGlckeGIEPSDTT---STF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDdyfkGVSQKAKEFVCFLLQ 2973
Cdd:cd05575   157 CGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRT----NVSPSARDLLEGLLQ 232

                  ....*.
gi 767934614 2974 EDPAKR 2979
Cdd:cd05575   233 KDRTKR 238
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
2742-2979 4.44e-29

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 119.12  E-value: 4.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQSLQH-PLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd05611     3 PISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMiAKNQVTNvkaERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLNGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGdavqLNTTYYIHQ---- 2892
Cdd:cd05611    83 DCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQT---GHLKLTDFG----LSRNGLEKRhnkk 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLL 2972
Cdd:cd05611   156 FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLL 235

                  ....*..
gi 767934614 2973 QEDPAKR 2979
Cdd:cd05611   236 CMDPAKR 242
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
2737-2991 8.11e-29

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 118.02  E-value: 8.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTK--RAVATKfVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAd 2814
Cdd:cd14112     5 FSFGSEIFRGRFSVIVKAVDSTTEtdAHCAVK-IFEVSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKL- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdESLAKPTIKLADFGDAVQLNTTYYIhQLL 2894
Cdd:cd14112    83 QEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMF-QSVRSWQVKLVDFGRAQKVSKLGKV-PVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGN-PVSLTSDTWSVGVLTYVLLSGVSPFL--DDSVEETCLNICRLDFSfPDDYFKGVSQKAKEFVCFL 2971
Cdd:cd14112   161 GDTDWASPEFHNPEtPITVQSDIWGLGVLTFCLLSGFHPFTseYDDEEETKENVIFVKCR-PNLIFVEATQEALRFATWA 239
                         250       260
                  ....*....|....*....|
gi 767934614 2972 LQEDPAKRPSAALALQEQWL 2991
Cdd:cd14112   240 LKKSPTRRMRTDEALEHRWL 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
2743-2982 1.01e-28

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 117.75  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNkklMKRD--QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd06612    11 LGEGSYGSVYKAIHKETGQVVAIKVVP---VEEDlqEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGSVSD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CV-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTY-YIHQLLGNPE 2898
Cdd:cd06612    88 IMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNE---EGQAKLADFGVSGQLTDTMaKRNTVIGTPF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPDD---YFKGVSQKAKEFVCFL---L 2972
Cdd:cd06612   165 WMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSD-------IHPMRAIFMIPNKpppTLSDPEKWSPEFNDFVkkcL 237
                         250
                  ....*....|
gi 767934614 2973 QEDPAKRPSA 2982
Cdd:cd06612   238 VKDPEERPSA 247
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
2735-3016 1.62e-28

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 117.73  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN--KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDleEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQL-NTTYYIH 2891
Cdd:cd06609    81 CGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEE---GDVKLADFGVSGQLtSTMSKRN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPDDYFkgvSQKAKEFVCF 2970
Cdd:cd06609   157 TFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPpSLEGNKF---SKPFKDFVEL 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 2971 LLQEDPAKRPSAALALQEQWLqagngRSTGVldTSRLTSFIERRKH 3016
Cdd:cd06609   234 CLNKDPKERPSAKELLKHKFI-----KKAKK--TSYLTLLIERIKK 272
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
2745-2987 3.31e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 116.74  E-value: 3.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2745 RGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGrllD 2820
Cdd:cd05609    10 NGAYGAVYLVRHRETRQRFAMKKINKQnLILRNQIQQvfvERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGG---D 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 C---VVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdESLAKptIKLADFGDA----VQLNTTYYIH-- 2891
Cdd:cd05609    87 CatlLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLI-TSMGH--IKLTDFGLSkiglMSLTTNLYEGhi 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 ----------QLLGNPEFAAPEIIL----GNPVsltsDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYf 2957
Cdd:cd05609   164 ekdtrefldkQVCGTPEYIAPEVILrqgyGKPV----DWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGD- 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 767934614 2958 KGVSQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd05609   239 DALPDDAQDLITRLLQQNPLERLGTGGAEE 268
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
2743-2991 3.33e-28

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 116.11  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14164     8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQkflpRELSILRRVNHPNIVQMFECIEVANGRLYIVMEAAATDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdeSLAKPTIKLADFG------DAVQLNTTYyihq 2892
Cdd:cd14164    88 LQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILL--SADDRKIKIADFGfarfveDYPELSTTF---- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 lLGNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVeetclNICRLDfSFPDDYFKGVS--QKAKEFVC 2969
Cdd:cd14164   162 -CGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVTGTMPFDETNV-----RRLRLQ-QRGVLYPSGVAleEPCRALIR 234
                         250       260
                  ....*....|....*....|..
gi 767934614 2970 FLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14164   235 TLLQFNPSTRPSIQQVAGNSWL 256
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
2743-2982 3.99e-28

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 118.06  E-value: 3.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTHELG---ILQ---SLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIvAKKEVAHTIGernILVrtaLDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG-DAVQLNTTYYIHQLL 2894
Cdd:cd05586    81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLD---ANGHIALCDFGlSKADLTDNKTTNTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYfkgVSQKAKEFVCFLLQ 2973
Cdd:cd05586   158 GTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDV---LSDEGRSFVKGLLN 234

                  ....*....
gi 767934614 2974 EDPAKRPSA 2982
Cdd:cd05586   235 RNPKHRLGA 243
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
2743-2979 5.00e-28

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 116.47  E-value: 5.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKgetmALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd05577    81 KYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDH---GHVRISDLGLAVEFKGGKKIKGRVGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGN-PVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd05577   158 HGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKD 237

                  ....
gi 767934614 2976 PAKR 2979
Cdd:cd05577   238 PERR 241
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
2743-2979 5.06e-28

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 117.80  E-value: 5.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEvIIAKDEVAHtvtESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG---DAVQLNTTyyIHQLLG 2895
Cdd:cd05595    83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKD---GHIKITDFGlckEGITDGAT--MKTFCG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQED 2975
Cdd:cd05595   158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFP----RTLSPEAKSLLAGLLKKD 233

                  ....
gi 767934614 2976 PAKR 2979
Cdd:cd05595   234 PKQR 237
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
2743-2991 6.49e-28

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 116.28  E-value: 6.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd14173    10 LGEGAYARVQTCINLITNKEYAVKIIEKRPgHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGSILS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADF--GDAVQLN------TTYYIHQ 2892
Cdd:cd14173    90 HIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFdlGSGIKLNsdcspiSTPELLT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEII--LGNPVSLTS---DTWSVGVLTYVLLSGVSPFLD--------DSVE--ETCLN-----ICRLDFSF 2952
Cdd:cd14173   170 PCGSAEYMAPEVVeaFNEEASIYDkrcDLWSLGVILYIMLSGYPPFVGrcgsdcgwDRGEacPACQNmlfesIQEGKYEF 249
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767934614 2953 PDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14173   250 PEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
1411-1546 7.88e-28

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 111.20  E-value: 7.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1411 LSMLEGFDENIESQGELILQESFQVWDPK-TLIRKGRERHLFLFEMSLVFSKEVKDSSGRSK--YLYKSKLFTSELGVTE 1487
Cdd:cd13241     1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSaGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNpgYIYKNHIKVNKMSLEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1488 HVEGDPCKFALWvGRTP-TSDNKIVLKASSIENKQDWIKHIREVIQERTIHLKgALKEPI 1546
Cdd:cd13241    81 NVDGDPLRFALK-SRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLK-ALQSPI 138
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
2743-2991 8.39e-28

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 115.10  E-value: 8.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQK--GTKRAVATKFVNKKLMK------RDQVTHELGILQSLQHPLLVGLLDTFETPTS-YILVLEMA 2813
Cdd:cd13994     1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDEskrkdyVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGkWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQL-----NTTY 2888
Cdd:cd13994    81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG---VLKLTDFGTAEVFgmpaeKESP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YIHQLLGNPEFAAPEIILGNPVS-LTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrldFSFPDDYFKGVSQKAKEF 2967
Cdd:cd13994   158 MSAGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKA----YEKSGDFTNGPYEPIENL 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767934614 2968 -------VCF-LLQEDPAKRPSAALALQEQWL 2991
Cdd:cd13994   234 lpsecrrLIYrMLHPDPEKRITIDEALNDPWV 265
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
2739-2991 1.20e-27

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 114.67  E-value: 1.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAE-LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQ------HPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14133     2 EVLEvLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCIVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGrLLDCV--VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdESLAKPTIKLADFGDAVQLN--TT 2887
Cdd:cd14133    82 LLSQN-LYEFLkqNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILL-ASYSRCQIKIIDFGSSCFLTqrLY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLgnpeFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEF 2967
Cdd:cd14133   160 SYIQSRY----YRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKADDELF 235
                         250       260
                  ....*....|....*....|....*..
gi 767934614 2968 VCFL---LQEDPAKRPSAALALQEQWL 2991
Cdd:cd14133   236 VDFLkklLEIDPKERPTASQALSHPWL 262
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
2743-2997 1.31e-27

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 114.96  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH----ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHqlrrEIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQlNTTYYIHQLLGNPE 2898
Cdd:cd14117    94 YKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMG---YKGELKIADFGWSVH-APSLRRRTMCGTLD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQEDPAK 2978
Cdd:cd14117   170 YLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP----PFLSDGSRDLISKLLRYHPSE 245
                         250
                  ....*....|....*....
gi 767934614 2979 RPSAALALQEQWLQAGNGR 2997
Cdd:cd14117   246 RLPLKGVMEHPWVKANSRR 264
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
2744-2988 1.40e-27

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 116.35  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2744 GRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ--VTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05584     8 GYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQkdTAHtkaERNILEAVKHPFIVDLHYAFQTGGKLYLILEYLSGGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG---DAVQLNTTyyIHQLLG 2895
Cdd:cd05584    88 FMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLD---AQGHVKLTDFGlckESIHDGTV--THTFCG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPdDYfkgVSQKAKEFVCFLLQED 2975
Cdd:cd05584   163 TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLP-PY---LTNEARDLLKKLLKRN 238
                         250
                  ....*....|....*..
gi 767934614 2976 PAKR----PSAALALQE 2988
Cdd:cd05584   239 VSSRlgsgPGDAEEIKA 255
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
2737-2979 1.91e-27

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 114.10  E-value: 1.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkPTIKLADFGdavqLNTTYYIHQ---- 2892
Cdd:cd14662    82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPA-PRLKICDFG----YSKSSVLHSqpks 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVS-LTSDTWSVGVLTYVLLSGVSPFLDDS----VEETCLNICRLDFSFPDdyFKGVSQKAKEF 2967
Cdd:cd14662   157 TVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDdpknFRKTIQRIMSVQYKIPD--YVRVSQDCRHL 234
                         250
                  ....*....|..
gi 767934614 2968 VCFLLQEDPAKR 2979
Cdd:cd14662   235 LSRIFVANPAKR 246
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
2743-2990 2.39e-27

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 113.99  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFV-----NKKLMKR-DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQVeidpiNTEASKEvKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNT---TYYIHQL 2893
Cdd:cd06625    88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSN---GNVKLGDFGASKRLQTicsSTGMKSV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPDDyfkgVSQKAKEFVCFL 2971
Cdd:cd06625   165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAtqPTNPQLPPH----VSEDARDFLSLI 240
                         250
                  ....*....|....*....
gi 767934614 2972 LQEDPAKRPSAALALQEQW 2990
Cdd:cd06625   241 FVRNKKQRPSAEELLSHSF 259
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
2743-2992 3.09e-27

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 114.36  E-value: 3.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd14174    10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAgHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGSILA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADF--GDAVQLN------TTYYIHQ 2892
Cdd:cd14174    90 HIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFdlGSGVKLNsactpiTTPELTT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEI--ILGNPVSLTS---DTWSVGVLTYVLLSGVSPFLDD----------SVEETCLN-----ICRLDFSF 2952
Cdd:cd14174   170 PCGSAEYMAPEVveVFTDEATFYDkrcDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgEVCRVCQNklfesIQEGKYEF 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767934614 2953 PDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd14174   250 PDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
2743-2988 3.19e-27

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 113.27  E-value: 3.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKK--CDQKGTKRAVA-TKFVNKKLMKRD---QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd06632     8 LGSGSFGSVYEgfNGDTGDFFAVKeVSLVDDDKKSREsvkQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkptIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd06632    88 SIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV---VKLADFGMAKHVEAFSFAKSFKGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIIL--GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF--SFPDDyfkgVSQKAKEFVCFLL 2972
Cdd:cd06632   165 PYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDH----LSPDAKDFIRLCL 240
                         250
                  ....*....|....*.
gi 767934614 2973 QEDPAKRPSAALALQE 2988
Cdd:cd06632   241 QRDPEDRPTASQLLEH 256
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
2743-2979 3.58e-27

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 115.10  E-value: 3.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05601     9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSeTLAQEEVSffeEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRW-GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQLL--G 2895
Cdd:cd05601    89 LSLLSRYdDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRT---GHIKLADFGSAAKLSSDKTVTSKMpvG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIIL---GNPVS---LTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrLDF----SFPDDyfKGVSQKAK 2965
Cdd:cd05601   166 TPDYIAPEVLTsmnGGSKGtygVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI--MNFkkflKFPED--PKVSESAV 241
                         250
                  ....*....|....
gi 767934614 2966 EFVCFLLqEDPAKR 2979
Cdd:cd05601   242 DLIKGLL-TDAKER 254
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2737-2991 6.63e-27

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 112.33  E-value: 6.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVV----KKCDQkgtkRAVATKFVNKKLMKR-------DQVTHELGIL---QSLQHPLLVGLLDTFET 2802
Cdd:cd14005     2 YEVGDLLGKGGFGTVysgvRIRDG----LPVAVKFVPKSRVTEwamingpVPVPLEIALLlkaSKPGVPGVIRLLDWYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PTSYILVLEMA----DqgrLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslaKPT--IKLA 2876
Cdd:cd14005    78 PDGFLLIMERPepcqD---LFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLIN----LRTgeVKLI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2877 DFGDAVQLNTTYYiHQLLGNPEFAAPEIIL-----GNPVSLtsdtWSVGVLTYVLLSGVSPFLDDsveetcLNICRLDFS 2951
Cdd:cd14005   151 DFGCGALLKDSVY-TDFDGTRVYSPPEWIRhgryhGRPATV----WSLGILLYDMLCGDIPFEND------EQILRGNVL 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767934614 2952 FPddyfKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14005   220 FR----PRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
2743-2988 8.61e-27

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 113.91  E-value: 8.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtILKKKEQNHIMAernvLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG---DAVQLNTTyyIHQLL 2894
Cdd:cd05603    83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLD---CQGHVVLTDFGlckEGMEPEET--TSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDdyfkGVSQKAKEFVCFLLQE 2974
Cdd:cd05603   158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPG----GKTVAACDLLQGLLHK 233
                         250
                  ....*....|....
gi 767934614 2975 DPAKRPSAALALQE 2988
Cdd:cd05603   234 DQRRRLGAKADFLE 247
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
2742-2979 1.28e-26

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 112.07  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKR-----------------------DQVTHELGILQSLQHPLLVGLL 2797
Cdd:cd14118     1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKkKLLKQagffrrppprrkpgalgkpldplDRVYREIAILKKLDHPNVVKLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2798 DTFETPT--SYILVLEMADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKL 2875
Cdd:cd14118    81 EVLDDPNedNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDD---GHVKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2876 ADFG--------DAVQLNTTyyihqllGNPEFAAPEIILGNPVSLTS---DTWSVGVLTYVLLSGVSPFLDDSVEETCLN 2944
Cdd:cd14118   157 ADFGvsnefegdDALLSSTA-------GTPAFMAPEALSESRKKFSGkalDIWAMGVTLYCFVFGRCPFEDDHILGLHEK 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767934614 2945 ICRLDFSFPDDYFkgVSQKAKEFVCFLLQEDPAKR 2979
Cdd:cd14118   230 IKTDPVVFPDDPV--VSEQLKDLILRMLDKNPSER 262
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
2740-2945 1.91e-26

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 114.36  E-value: 1.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd05600    16 LTQVGQGGYGSVFLARKKDTGEICALKIMKKKvLFKLNEVNHvltERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 G--RLLDCVVrwGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDA------------ 2881
Cdd:cd05600    96 GdfRTLLNNS--GILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLID---SSGHIKLTDFGLAsgtlspkkiesm 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 -VQLN-------------------------TTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLD 2935
Cdd:cd05600   171 kIRLEevkntafleltakerrniyramrkeDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG 250
                         250
                  ....*....|
gi 767934614 2936 DSVEETCLNI 2945
Cdd:cd05600   251 STPNETWANL 260
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2743-2992 2.06e-26

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 111.09  E-value: 2.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK-------KLMKRDQVTHELGILQSL----QHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd14101     8 LGKGGFGTVYAGHRISDGLQVAIKQISRnrvqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGR-LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDesLAKPTIKLADFGDAVQLNTTYYI 2890
Cdd:cd14101    88 RPQHCQdLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVD--LRTGDIKLIDFGSGATLKDSMYT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 hQLLGNPEFAAPEIILGNPV-SLTSDTWSVGVLTYVLLSGVSPFLDDSveetclNICRLDFSFPddyfKGVSQKAKEFVC 2969
Cdd:cd14101   166 -DFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERDT------DILKAKPSFN----KRVSNDCRSLIR 234
                         250       260
                  ....*....|....*....|...
gi 767934614 2970 FLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd14101   235 SCLAYNPSDRPSLEQILLHPWMM 257
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2742-2987 2.20e-26

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 111.27  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM----KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd08228     9 KIGRGQFSEVYRATCLLDRKPVALKKVQIFEMmdakARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGS----LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT-TYYIHQ 2892
Cdd:cd08228    89 LSQMIKYFKKqkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFIT---ATGVVKLGDLGLGRFFSSkTTAAHS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVE--ETCLNICRLDF-SFPDDYFkgvSQKAKEFVC 2969
Cdd:cd08228   166 LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYpPLPTEHY---SEKLRELVS 242
                         250
                  ....*....|....*...
gi 767934614 2970 FLLQEDPAKRPSAALALQ 2987
Cdd:cd08228   243 MCIYPDPDQRPDIGYVHQ 260
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
2743-2979 4.57e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 112.42  E-value: 4.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05602    15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKaILKKKEEKHIMSernvLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG---DAVQLNTTyyIHQLL 2894
Cdd:cd05602    95 LFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLD---SQGHIVLTDFGlckENIEPNGT--TSTFC 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrldFSFPDDYFKGVSQKAKEFVCFLLQE 2974
Cdd:cd05602   170 GTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNI----LNKPLQLKPNITNSARHLLEGLLQK 245

                  ....*
gi 767934614 2975 DPAKR 2979
Cdd:cd05602   246 DRTKR 250
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
2732-2992 5.16e-26

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 110.60  E-value: 5.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2732 NFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKlmKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd06611     2 NPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE--SEEELEDfmvEIDILSECKHPNIVGLYEAYFYENKLWI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCVVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG-DAVQLNT 2886
Cdd:cd06611    80 LIEFCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD---GDVKLADFGvSAKNKST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TYYIHQLLGNPEFAAPEIIL-----GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD---FSFPddyfK 2958
Cdd:cd06611   157 LQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQP----S 232
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767934614 2959 GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06611   233 KWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
2737-2990 8.53e-26

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 110.35  E-value: 8.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK--FVNKKLMKRDQVT----HELGILQSLQHPLLVGLLDTFETPTSYILVL 2810
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKkiKLGERKEAKDGINftalREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGrlLDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT-- 2886
Cdd:cd07841    82 EFMETD--LEKVIKDKSivLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA---SDGVLKLADFGLARSFGSpn 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TYYIHQLLgNPEFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVsPFLDDSVEETCLN-ICRL---------------- 2948
Cdd:cd07841   157 RKMTHQVV-TRWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRV-PFLPGDSDIDQLGkIFEAlgtpteenwpgvtslp 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767934614 2949 ---DFS-FP----DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd07841   235 dyvEFKpFPptplKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
2744-2972 9.28e-26

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 110.78  E-value: 9.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2744 GRGRFSVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05599    10 GRGAFGEVRLVRKKDTGHVYAMKKLRKSEMlEKEQVAHvraERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGGDMM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQLLGNPEF 2899
Cdd:cd05599    90 TLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLD---ARGHIKLSDFGLCTGLKKSHLAYSTVGTPDY 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSFPDDYfkGVSQKAKEFVCFLL 2972
Cdd:cd05599   167 IAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKImnWRETLVFPPEV--PISPEAKDLIERLL 239
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
2743-2979 1.06e-25

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 110.55  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH----ELGILQ-SLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVEctmiERRVLAlASQHPFLTHLFCTFQTESHLFFVMEYLNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAV-QLNTTYYIHQLLGN 2896
Cdd:cd05592    83 LMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDR---EGHIKIADFGMCKeNIYGENKASTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQEDP 2976
Cdd:cd05592   160 PDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYP----RWLTKEAASCLSLLLERNP 235

                  ...
gi 767934614 2977 AKR 2979
Cdd:cd05592   236 EKR 238
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
2743-2979 1.19e-25

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 111.33  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05593    23 LGKGTFGKVILVREKASGKYYAMKILKKEvIIAKDEVAHTLTesrVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG-------DAVQLNTtyyih 2891
Cdd:cd05593   103 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD---GHIKITDFGlckegitDAATMKT----- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 qLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFL 2971
Cdd:cd05593   175 -FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSADAKSLLSGL 249

                  ....*...
gi 767934614 2972 LQEDPAKR 2979
Cdd:cd05593   250 LIKDPNKR 257
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
2743-2980 1.63e-25

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 108.95  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKF--VN------KKLMKRDQVTHELGILQSLQHPLLVGLLDTFET-PTSYILVLEMA 2813
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVACKIhqLNkdwseeKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEIdTDSFCTVLEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DqGRLLDCVV-RWGSLTEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYI 2890
Cdd:cd13990    88 D-GNDLDFYLkQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVSGEIKITDFGLSKIMDDESYN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 H-------QLLGNPEFAAPEIIL--GNPVSLTS--DTWSVGVLTYVLLSGVSPFLDDSVEETCL--NICR--LDFSFPDD 2955
Cdd:cd13990   167 SdgmeltsQGAGTYWYLPPECFVvgKTPPKISSkvDVWSVGVIFYQMLYGRKPFGHNQSQEAILeeNTILkaTEVEFPSK 246
                         250       260
                  ....*....|....*....|....*
gi 767934614 2956 yfKGVSQKAKEFVCFLLQEDPAKRP 2980
Cdd:cd13990   247 --PVVSSEAKDFIRRCLTYRKEDRP 269
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
2743-2979 1.79e-25

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 110.05  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKvILNRKEQKHIMAernvLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG----DAVQLNTTYyihQL 2893
Cdd:cd05604    84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLD---SQGHIVLTDFGlckeGISNSDTTT---TF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrldFSFPDDYFKGVSQKAKEFVCFLLQ 2973
Cdd:cd05604   158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENI----LHKPLVLRPGISLTAWSILEELLE 233

                  ....*.
gi 767934614 2974 EDPAKR 2979
Cdd:cd05604   234 KDRQLR 239
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
508-724 1.82e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 106.76  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  508 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 587
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  588 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 664
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  665 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 724
Cdd:cd00176   151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
2742-2991 2.33e-25

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 107.88  E-value: 2.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd08529     7 KLGKGSFGVVYKVVRKVDGRVYALKQIDISRMsrkMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLN-TTYYIHQLLG 2895
Cdd:cd08529    87 HSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGD---NVKIGDLGVAKILSdTTNFAQTIVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPDDYfkgvSQKAKEFVCFLLQE 2974
Cdd:cd08529   164 TPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASY----SQDLSQLIDSCLTK 239
                         250
                  ....*....|....*..
gi 767934614 2975 DPAKRPSAALALQEQWL 2991
Cdd:cd08529   240 DYRQRPDTTELLRNPSL 256
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2746-2979 2.73e-25

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 108.25  E-value: 2.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2746 GRFSVVKKCDQKGTKRAVATKFVNKK--LMKRDQVTH---ELGILQSL-QHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05583     8 GKVFLVRKVGGHDAGKLYAMKVLKKAtiVQKAKTAEHtmtERQVLEAVrQSPFLVTLHYAFQTDAKLHLILDYVNGGELF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQL--NTTYYIHQLLGNP 2897
Cdd:cd05583    88 THLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDS---EGHVVLTDFGLSKEFlpGENDRAYSFCGTI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPV--SLTSDTWSVGVLTYVLLSGVSPFLDD----SVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFL 2971
Cdd:cd05583   165 EYMAPEVVRGGSDghDKAVDWWSLGVLTYELLTGASPFTVDgernSQSEISKRILKSHPPIP----KTFSAEAKDFILKL 240

                  ....*...
gi 767934614 2972 LQEDPAKR 2979
Cdd:cd05583   241 LEKDPKKR 248
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
2743-2990 5.55e-25

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 106.99  E-value: 5.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVthELGILQSlQHPLLVGLLDTFET---PTSYIL-VLEMADQGRL 2818
Cdd:cd14089     9 LGLGINGKVLECFHKKTGEKFALKVLRDNPKARREV--ELHWRAS-GCPHIVRIIDVYENtyqGRKCLLvVMECMEGGEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd14089    86 FSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQTPCYT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEiILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDsveeTCLNIC-----RL---DFSFPDDYFKGVSQKAKEF 2967
Cdd:cd14089   166 PYYVAPE-VLGPEKYDKScDMWSLGVIMYILLCGYPPFYSN----HGLAISpgmkkRIrngQYEFPNPEWSNVSEEAKDL 240
                         250       260
                  ....*....|....*....|...
gi 767934614 2968 VCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd14089   241 IRGLLKTDPSERLTIEEVMNHPW 263
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2743-2991 6.38e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 107.55  E-value: 6.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCdqkgTKRAVATKFVNKKLMKRDQVTHELGI-LQSLQHPLLVGLLDTF---------ETPTSYIL-VLE 2811
Cdd:cd14171    14 LGTGISGPVRVC----VKKSTGERFALKILLDRPKARTEVRLhMMCSGHPNIVQIYDVYansvqfpgeSSPRARLLiVME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFG----DAVQLNTT 2887
Cdd:cd14171    90 LMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGfakvDQGDLMTP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYihqllgNPEFAAPEII----------LGNPVSLTS-------DTWSVGVLTYVLLSGVSPFLDDSVEETCLN-----I 2945
Cdd:cd14171   170 QF------TPYYVAPQVLeaqrrhrkerSGIPTSPTPytydkscDMWSLGVIIYIMLCGYPPFYSEHPSRTITKdmkrkI 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 2946 CRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14171   244 MTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2737-2987 7.42e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 106.86  E-value: 7.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEM- 2812
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMsekEKQQLVSEVNILRELKHPNIVRYYDRIVDRANTTLYIVMe 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ----ADQGRLL-DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNC-----RIAHLDLKPENILVDEslaKPTIKLADFGDAV 2882
Cdd:cd08217    82 ycegGDLAQLIkKCKKENQYIPEEFIWKIFTQLLLALYECHNRsvgggKILHRDLKPANIFLDS---DNNVKLGDFGLAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLNT-TYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSF-PDDYfkgv 2960
Cdd:cd08217   159 VLSHdSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRiPSRY---- 234
                         250       260
                  ....*....|....*....|....*..
gi 767934614 2961 SQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd08217   235 SSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
2737-2991 1.08e-24

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 107.02  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVA---------TKFVNKKLMKrdqvthELGILQSLQHPLLVGLLDTFETPTSYI 2807
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAikkfkesedDEDVKKTALR------EVKVLRQLRHENIVNLKEAFRRKGRLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQL--N 2885
Cdd:cd07833    77 LVFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG---VLKLCDFGFARALtaR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 TTYYIHQLLGNPEFAAPEIILGN-----PVsltsDTWSVGVLTYVLLSGVSPF------------------LDDSVEETC 2942
Cdd:cd07833   154 PASPLTDYVATRWYRAPELLVGDtnygkPV----DVWAIGCIMAELLDGEPLFpgdsdidqlyliqkclgpLPPSHQELF 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2943 LNICRLD-FSFPD---------DYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07833   230 SSNPRFAgVAFPEpsqpeslerRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
2743-2979 1.18e-24

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 108.58  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05594    33 LGKGTFGKVILVKEKATGRYYAMKILKKEvIVAKDEVAHTLTenrVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCR-IAHLDLKPENILVDESlakPTIKLADFG---DAVQLNTTyyIHQLL 2894
Cdd:cd05594   113 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKD---GHIKITDFGlckEGIKDGAT--MKTFC 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQE 2974
Cdd:cd05594   188 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLSPEAKSLLSGLLKK 263

                  ....*
gi 767934614 2975 DPAKR 2979
Cdd:cd05594   264 DPKQR 268
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2737-2980 2.75e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 104.81  E-value: 2.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQaalNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd08220    82 PGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKK--RTVVKIGDFGISKILSSKSKAY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFkgvSQKAKEFVCFL 2971
Cdd:cd08220   160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRY---SEELRHLILSM 236

                  ....*....
gi 767934614 2972 LQEDPAKRP 2980
Cdd:cd08220   237 LHLDPNKRP 245
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
2743-2981 2.98e-24

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 104.62  E-value: 2.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK----KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHsrvaKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkptIKLADFGDAVQLNTTYYIHQLL-GNP 2897
Cdd:cd14189    89 AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENME---LKVGDFGLAARLEPPEQRKKTIcGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14189   166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP----ASLSLPARHLLAGILKRNPG 241

                  ....
gi 767934614 2978 KRPS 2981
Cdd:cd14189   242 DRLT 245
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
2743-2981 3.58e-24

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 104.26  E-value: 3.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR-----DQVTHELGILQSLQHPLLVGLLDTFETPTS---YIlVLEMAD 2814
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRipngeANVKREIQILRRLNHRNVIKLVDVLYNEEKqklYM-VMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QG--RLLDCVVRwGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILV--DEslakpTIKLADFGDAVQLN---TT 2887
Cdd:cd14119    80 GGlqEMLDSAPD-KRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLttDG-----TLKISDFGVAEALDlfaED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPEFAAPEIILGNPV--SLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAK 2965
Cdd:cd14119   154 DTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDD----VDPDLQ 229
                         250
                  ....*....|....*.
gi 767934614 2966 EFVCFLLQEDPAKRPS 2981
Cdd:cd14119   230 DLLRGMLEKDPEKRFT 245
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
2743-2981 6.85e-24

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 103.39  E-value: 6.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVatkfvnkKLMKRDQVTH--------ELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd13999     1 IGSGSFGEVYKGKWRGTDVAI-------KKLKVEDDNDellkefrrEVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCvvrwgsLTEGKIRAHLGEVL-------EAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTT 2887
Cdd:cd13999    74 GGSLYDL------LHKKKIPLSWSLRLkialdiaRGMNYLHSPPIIHRDLKSLNILLDENF---TVKIADFGLSRIKNST 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIH-QLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICR-----LDFSFPDDYFKGV 2960
Cdd:cd13999   145 TEKMtGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKElSPIQIAAAVVQKglrppIPPDCPPELSKLI 224
                         250       260
                  ....*....|....*....|.
gi 767934614 2961 SQkakefvCflLQEDPAKRPS 2981
Cdd:cd13999   225 KR------C--WNEDPEKRPS 237
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
2743-2983 7.38e-24

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 103.56  E-value: 7.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQ-HPLLVGLLD-TFETPTSYILVLEMADQGRLLD 2820
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSvHPHIIKTYDvAFETEDYYVFAQEYAPYGDLFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DESLAKptIKLADFGDAVQLNTTyyIHQLLGNPEF 2899
Cdd:cd13987    81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDCRR--VKLCDFGLTRRVGST--VKRVSGTIPY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEI--------ILGNPVsltSDTWSVGVLTYVLLSGVSPF-----LDDSVEETCLNICRLDFSFPDDyFKGVSQKAKE 2966
Cdd:cd13987   157 TAPEVceakknegFVVDPS---IDVWAFGVLLFCCLTGNFPWekadsDDQFYEEFVRWQKRKNTAVPSQ-WRRFTPKALR 232
                         250
                  ....*....|....*..
gi 767934614 2967 FVCFLLQEDPAKRPSAA 2983
Cdd:cd13987   233 MFKKLLAPEPERRCSIK 249
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
2735-2945 8.41e-24

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 105.48  E-value: 8.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVL 2810
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKdVLKRNQVAHvkaERDILAEADNEWVVKLYYSFQDKENLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL----NT 2886
Cdd:cd05598    81 DYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILID---RDGHIKLTDFGLCTGFrwthDS 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TYYI-HQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNI 2945
Cdd:cd05598   158 KYYLaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKV 217
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
2743-2979 9.33e-24

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 103.95  E-value: 9.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05630     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd05630    88 KFHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDH---GHIRISDLGLAVHVPEGQTIKGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDP 2976
Cdd:cd05630   165 VGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDP 244

                  ...
gi 767934614 2977 AKR 2979
Cdd:cd05630   245 AER 247
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
2737-2979 9.69e-24

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 104.05  E-value: 9.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAiPEVIRLKQEQHvhnEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYihQ 2892
Cdd:cd05612    83 VPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDK---EGHIKLTDFGFAKKLRDRTW--T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLL 2972
Cdd:cd05612   158 LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFP----RHLDLYAKDLIKKLL 233

                  ....*..
gi 767934614 2973 QEDPAKR 2979
Cdd:cd05612   234 VVDRTRR 240
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
2740-2993 1.35e-23

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 103.19  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd06605     6 LGELGEGNGGVVSKVRHRPSGQIMAVKVIrlEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTE---GKI-RAhlgeVLEAVRYLHNCR-IAHLDLKPENILVDeslAKPTIKLADFGDAVQL-------- 2884
Cdd:cd06605    86 LDKILKEVGRIPErilGKIaVA----VVKGLIYLHEKHkIIHRDVKPSNILVN---SRGQVKLCDFGVSGQLvdslaktf 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 -NTTYYIhqllgnpefaAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFlDDSVEETCLNI-----CRLDFS---FPDD 2955
Cdd:cd06605   159 vGTRSYM----------APERISGGKYTVKSDIWSLGLSLVELATGRFPY-PPPNAKPSMMIfellsYIVDEPpplLPSG 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767934614 2956 YFkgvSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQA 2993
Cdd:cd06605   228 KF---SPDFQDFVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
2743-2991 1.88e-23

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 102.95  E-value: 1.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD---------QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14076     9 LGEGEFGKVKLGWPLPKANHRSGVQVAIKLIRRDtqqencqtsKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQ--LNTTYYIH 2891
Cdd:cd14076    89 SGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKN---RNLVITDFGFANTfdHFNGDLMS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPEIILGNPVSLTS--DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL-------DFSFPDDyfkgVSQ 2962
Cdd:cd14076   166 TSCGSPCYAAPELVVSDSMYAGRkaDIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLyryicntPLIFPEY----VTP 241
                         250       260
                  ....*....|....*....|....*....
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14076   242 KARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
2742-2992 3.69e-23

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 102.35  E-value: 3.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR---------------------------DQVTHELGILQSLQHPLLV 2794
Cdd:cd14199     9 EIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqprgpiERVYQEIAILKKLDHPNVV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2795 GLLDTFETPTS--YILVLEMADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPT 2872
Cdd:cd14199    89 KLVEVLDDPSEdhLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGED---GH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2873 IKLADFG--------DAVQLNTtyyihqlLGNPEFAAPEIILGNPVSLTS---DTWSVGVLTYVLLSGVSPFLDDSVEET 2941
Cdd:cd14199   165 IKIADFGvsnefegsDALLTNT-------VGTPAFMAPETLSETRKIFSGkalDVWAMGVTLYCFVFGQCPFMDERILSL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2942 CLNICRLDFSFPDDYfkGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd14199   238 HSKIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2743-2991 5.21e-23

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 101.60  E-value: 5.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELgilQSLQHPLLVGLLDTFET----PTSYILVLEMADQGRL 2818
Cdd:cd14172    12 LGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHW---RASGGPHIVHILDVYENmhhgKRCLLIIMECMEGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWG--SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd14172    89 FSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQNALQTPCYT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL----DFSFPDDYFKGVSQKAKEFVCFLL 2972
Cdd:cd14172   169 PYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRirmgQYGFPNPEWAEVSEEAKQLIRHLL 248
                         250
                  ....*....|....*....
gi 767934614 2973 QEDPAKRPSAALALQEQWL 2991
Cdd:cd14172   249 KTDPTERMTITQFMNHPWI 267
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2746-2979 5.77e-23

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 102.00  E-value: 5.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2746 GRFSVVKKCDQKGTKRAVATKFVNKK--LMKRDQVTHELGILQSLQH----PLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05613    14 GKVFLVRKVSGHDAGKLYAMKVLKKAtiVQKAKTAEHTRTERQVLEHirqsPFLVTLHYAFQTDTKLHLILDYINGGELF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQ--LNTTYYIHQLLGNP 2897
Cdd:cd05613    94 THLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSS---GHVVLTDFGLSKEflLDENERAYSFCGTI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTS--DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd05613   171 EYMAPEIVRGGDSGHDKavDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDIIQRLLMKD 250

                  ....
gi 767934614 2976 PAKR 2979
Cdd:cd05613   251 PKKR 254
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
2743-2979 8.54e-23

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 102.09  E-value: 8.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFS---VVKKCDQKGTKRAVATKFVNKKLMK-RDQV--THELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd05582     3 LGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKvRDRVrtKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG---DAV-QLNTTYyihQ 2892
Cdd:cd05582    83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDED---GHIKLTDFGlskESIdHEKKAY---S 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLL 2972
Cdd:cd05582   157 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLLRALF 232

                  ....*..
gi 767934614 2973 QEDPAKR 2979
Cdd:cd05582   233 KRNPANR 239
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
2737-2983 1.13e-22

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 100.51  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNkkLMKR----DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd06610     3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRID--LEKCqtsmDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCV---VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQL----- 2884
Cdd:cd06610    81 LSGGSLLDIMkssYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGED---GSVKIADFGVSASLatggd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NTTYYIHQLLGNPEFAAPEII-LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPDDYFKGVSQ 2962
Cdd:cd06610   158 RTRKVRKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPpSLETGADYKKYS 237
                         250       260
                  ....*....|....*....|..
gi 767934614 2963 KA-KEFVCFLLQEDPAKRPSAA 2983
Cdd:cd06610   238 KSfRKMISLCLQKDPSKRPTAE 259
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2743-2991 1.19e-22

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 100.04  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK-------KLMKRDQVTHELGILQSLQHPL--LVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14100     8 LGSGGFGSVYSGIRVADGAPVAIKHVEKdrvsewgELPNGTRVPMEIVLLKKVGSGFrgVIRLLDWFERPDSFVLVLERP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGR-LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDesLAKPTIKLADFGDAVQLNTTYYIhQ 2892
Cdd:cd14100    88 EPVQdLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILID--LNTGELKLIDFGSGALLKDTVYT-D 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDT-WSVGVLTYVLLSGVSPFLDDsvEEtclnICRLDFSFPddyfKGVSQKAKEFVCFL 2971
Cdd:cd14100   165 FDGTRVYSPPEWIRFHRYHGRSAAvWSLGILLYDMVCGDIPFEHD--EE----IIRGQVFFR----QRVSSECQHLIKWC 234
                         250       260
                  ....*....|....*....|
gi 767934614 2972 LQEDPAKRPSAALALQEQWL 2991
Cdd:cd14100   235 LALRPSDRPSFEDIQNHPWM 254
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
2776-2983 1.96e-22

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 99.53  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2776 DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHL 2855
Cdd:cd06628    51 DALQREIALLRELQHENIVQYLGSSSDANHLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHR 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2856 DLKPENILVDEslaKPTIKLADFG-----DAVQLNTTYYIHQ--LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLS 2928
Cdd:cd06628   131 DIKGANILVDN---KGGIKISDFGiskklEANSLSTKNNGARpsLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2929 GVSPFLDDSVEETCLNICRLDF-SFPDDyfkgVSQKAKEFVCFLLQEDPAKRPSAA 2983
Cdd:cd06628   208 GTHPFPDCTQMQAIFKIGENASpTIPSN----ISSEARDFLEKTFEIDHNKRPTAD 259
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
2735-2993 2.04e-22

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 99.86  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQSLQH---PLLVGLLDTFETPTSYILV 2809
Cdd:cd06917     1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRLlDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYY 2889
Cdd:cd06917    81 MDYCEGGSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNT---GNVKLCDFGVAASLNQNSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQ-LLGNPEFAAPEIIL-GNPVSLTSDTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICRLDFSFPDDYFkgvSQKAKE 2966
Cdd:cd06917   157 KRStFVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSDvDALRAVMLIPKSKPPRLEGNGY---SPLLKE 233
                         250       260
                  ....*....|....*....|....*..
gi 767934614 2967 FVCFLLQEDPAKRPSAALALQEQWLQA 2993
Cdd:cd06917   234 FVAACLDEEPKDRLSADELLKSKWIKQ 260
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
10-145 2.53e-22

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.83  E-value: 2.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614     10 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 77
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614     78 SIKPLLKILQESFPCCIHVALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 145
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2737-2991 2.93e-22

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 98.87  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKklmkrDQVThELGILQSLQHPL--------------LVGLLDTFET 2802
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVK-----ERVT-EWGTLNGVMVPLeivllkkvgsgfrgVIKLLDWYER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PTSYILVLEMADQGR-LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDesLAKPTIKLADFGDA 2881
Cdd:cd14102    76 PDGFLIVMERPEPVKdLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVD--LRTGELKLIDFGSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 VQLNTTYYIhQLLGNPEFAAPEIILGNPVSLTSDT-WSVGVLTYVLLSGVSPFLDDsvEEtclnICRLDFSFPddyfKGV 2960
Cdd:cd14102   154 ALLKDTVYT-DFDGTRVYSPPEWIRYHRYHGRSATvWSLGVLLYDMVCGDIPFEQD--EE----ILRGRLYFR----RRV 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767934614 2961 SQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14102   223 SPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2739-2993 3.42e-22

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 99.42  E-value: 3.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAELGRGRFSVVKKCDQKGTKRAVATKFV----NKKLMKrdQVTHELGILQSLQHPLLVGLLDTF--ETPTSYILVLEM 2812
Cdd:cd06621     5 ELSSLGEGAGGSVTKCRLRNTKTIFALKTIttdpNPDVQK--QILRELEINKSCASPYIVKYYGAFldEQDSSIGIAMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQG---RLLDCVVRWGSLTEGKIRAHLGE-VLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQL---- 2884
Cdd:cd06621    83 CEGGsldSIYKKVKKKGGRIGEKVLGKIAEsVLKGLSYLHSRKIIHRDIKPSNILLTR---KGQVKLCDFGVSGELvnsl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 -----NTTYYIhqllgnpefaAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVE-----ETCLNICRL-DFSFP 2953
Cdd:cd06621   160 agtftGTSYYM----------APERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVNMpNPELK 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2954 DDYFKGV--SQKAKEFVCFLLQEDPAKRPSAALALQEQWLQA 2993
Cdd:cd06621   230 DEPENGIkwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKA 271
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
2081-2214 4.53e-22

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 94.28  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2081 RRCNDMMNVGRLQGFDGKIVAQGKLLLQDTFLVTDQDagllpRCRERRIFLFEQIVIFSEPLDKKKGFSMpgFLFKNSIK 2160
Cdd:cd13242     5 RHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGR-----KKCLRHVFLFEDLILFSKPKKTPGGKDV--YIYKHSIK 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2161 VSCLCLEENVENDPCKFALTSRTGDVVETFILHSSSPSVRQTWIHEINQILENQ 2214
Cdd:cd13242    78 TSDIGLTENVGDSGLKFEIWFRRRKARDTYILQATSPEIKQAWTSDIAKLLWKQ 131
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
2734-3015 5.50e-22

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 98.59  E-value: 5.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd06642     3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEieDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQL-NTTYYI 2890
Cdd:cd06642    83 YLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSE---QGDVKLADFGVAGQLtDTQIKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPDDYFKGV----SQKAKE 2966
Cdd:cd06642   159 NTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSD-------LHPMRVLFLIPKNSPPTLegqhSKPFKE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2967 FVCFLLQEDPAKRPSAALALQEQWLQagngRSTGvlDTSRLTSFIERRK 3015
Cdd:cd06642   232 FVEACLNKDPRFRPTAKELLKHKFIT----RYTK--KTSFLTELIDRYK 274
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
2743-2979 5.94e-22

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 98.58  E-value: 5.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd05605    88 KFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDH---GHVRISDLGLAVEIPEGETIRGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF-----------LDDSVEETclnicrldfsfPDDYFKGVSQKAK 2965
Cdd:cd05605   165 VGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFrarkekvkreeVDRRVKED-----------QEEYSEKFSEEAK 233
                         250
                  ....*....|....
gi 767934614 2966 EFVCFLLQEDPAKR 2979
Cdd:cd05605   234 SICSQLLQKDPKTR 247
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
2737-2991 7.54e-22

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 98.56  E-value: 7.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKfvnKKLMKR------DQVTHELGILQSLQ-HPLLVGLLDTFETPTSYILV 2809
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALK---KVALRKleggipNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQG--RLLDCVVRwgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLN-- 2885
Cdd:cd07832    79 FEYMLSSlsEVLRDEER--PLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS---STGVLKIADFGLARLFSee 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 -TTYYIHQlLGNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGvSPFLD--DSVEETCLNICRL------------- 2948
Cdd:cd07832   154 dPRLYSHQ-VATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNG-SPLFPgeNDIEQLAIVLRTLgtpnektwpelts 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2949 --DFS---FP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07832   232 lpDYNkitFPeskgirlEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
1403-1539 9.37e-22

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 93.51  E-value: 9.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1403 KRANDAMHLSMLEGFDENIESQGELILQESFQVWDPktliRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSE 1482
Cdd:cd13242     5 RHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQG----RKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 1483 LGVTEHVEGDPCKFALWVgRTPTSDNKIVLKASSIENKQDWIKHIREVIQERTIHLK 1539
Cdd:cd13242    81 IGLTENVGDSGLKFEIWF-RRRKARDTYILQATSPEIKQAWTSDIAKLLWKQAIRNR 136
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
2743-2979 9.88e-22

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 98.14  E-value: 9.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRA--HLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd05631    88 KFHIYNMGNPGFDEQRAifYAAELCCGLEDLQRERIVYRDLKPENILLDD---RGHIRISDLGLAVQIPEGETVRGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDP 2976
Cdd:cd05631   165 VGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNP 244

                  ...
gi 767934614 2977 AKR 2979
Cdd:cd05631   245 KER 247
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
2732-2932 1.02e-21

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 98.18  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2732 NFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR-DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVL 2810
Cdd:cd06643     2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEElEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMAdQGRLLDCVV----RwgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG-DAVQLN 2885
Cdd:cd06643    82 EFC-AGGAVDAVMleleR--PLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFT---LDGDIKLADFGvSAKNTR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2886 TTYYIHQLLGNPEFAAPEIIL-----GNPVSLTSDTWSVGVlTYVLLSGVSP 2932
Cdd:cd06643   156 TLQRRDSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGV-TLIEMAQIEP 206
I-set pfam07679
Immunoglobulin I-set domain;
2626-2717 1.13e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.55  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHnTLNNDGHYSISYSDlGEATLKIVGVTTEDDGIYTCIAVND 2705
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQ-PLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 767934614  2706 MGSASSSASLRV 2717
Cdd:pfam07679   79 AGEAEASAELTV 90
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
2737-2987 1.27e-21

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 97.73  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKL--------MKRdqvthELGILQSLQ---HPLLVGLLDTFETP-- 2803
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLseegiplsTIR-----EIALLKQLEsfeHPNVVRLLDVCHGPrt 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2804 ---TSYILVLEMADQ--GRLLDCVVRWGsLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADF 2878
Cdd:cd07838    76 dreLKLTLVFEHVDQdlATYLDKCPKPG-LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDG---QVKLADF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2879 GdavqLNTTYYIHQLLgNPE-----FAAPEIILGNPVSLTSDTWSVGVLTYVLLS------GVS--------------PF 2933
Cdd:cd07838   152 G----LARIYSFEMAL-TSVvvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNrrplfrGSSeadqlgkifdviglPS 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 2934 LDDSVEETCLNICRLDFSFP---DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd07838   227 EEEWPRNSALPRSSFPSYTPrpfKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQ 283
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
2743-2981 2.32e-21

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 96.97  E-value: 2.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVV--KKCDQKGTKRAVATKFVNKK----LMKRdqvthELGILQSLQ-HPLLVGLLDTFETPTS------YILv 2809
Cdd:cd14037    11 LAEGGFAHVylVKTSNGGNRAALKRVYVNDEhdlnVCKR-----EIEIMKRLSgHKNIVGYIDSSANRSGngvyevLLL- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRLLDCV---VRWGsLTEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDESlakPTIKLADFGDA--- 2881
Cdd:cd14037    85 MEYCKGGGVIDLMnqrLQTG-LTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDS---GNYKLCDFGSAttk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 ----------------VQLNTTyyihqllgnPEFAAPEII---LGNPVSLTSDTWSVGVLTYVLLSGVSPFlddsvEETC 2942
Cdd:cd14037   161 ilppqtkqgvtyveedIKKYTT---------LQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPF-----EESG 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767934614 2943 -LNICRLDFSFPDdyFKGVSQKAKEFVCFLLQEDPAKRPS 2981
Cdd:cd14037   227 qLAILNGNFTFPD--NSRYSKRLHKLIRYMLEEDPEKRPN 264
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
2737-2983 2.33e-21

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 96.30  E-value: 2.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKL---MKRDQVTHELGILQSL-QHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd13997     2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFrgpKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWG---SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYY 2889
Cdd:cd13997    82 CENGSLQDALEELSpisKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFIS---NKGTCKIGDFGLATRLETSGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQllGNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGvSPFLDDSVEETCLNICRLdfsfPDDYFKGVSQKAKEFV 2968
Cdd:cd13997   159 VEE--GDSRYLAPELLNENYTHLPKaDIFSLGVTVYEAATG-EPLPRNGQQWQQLRQGKL----PLPPGLVLSQELTRLL 231
                         250
                  ....*....|....*
gi 767934614 2969 CFLLQEDPAKRPSAA 2983
Cdd:cd13997   232 KVMLDPDPTRRPTAD 246
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
1416-1531 2.55e-21

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 91.88  E-value: 2.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1416 GFDENIESQGELILQESFQVW------DPKTLIR-KGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEH 1488
Cdd:cd01227     4 GYDGNLGDLGKLLMQGSFNVWtehkkgHTKKLARfKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYKNSLNTTAVGLTEN 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767934614 1489 VEGDPCKFALWV-GRTPTsdnkIVLKASSIENKQDWIKHIREVI 1531
Cdd:cd01227    84 VKGDTKKFEIWLnGREEV----FIIQAPTPEIKAAWVKAIRQVL 123
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
2730-2991 2.59e-21

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 96.36  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2730 KDNFDSFysevAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd06648     6 RSDLDNF----VKIGEGSTGIVCIATDKSTGRQVAVKKMDlRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNT-T 2887
Cdd:cd06648    82 VMEFLEGGALTD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSD---GRVKLSDFGFCAQVSKeV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKgVSQKAKEF 2967
Cdd:cd06648   158 PRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHK-VSPRLRSF 236
                         250       260
                  ....*....|....*....|....
gi 767934614 2968 VCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd06648   237 LDRMLVRDPAQRATAAELLNHPFL 260
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
2776-2991 2.78e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 96.22  E-value: 2.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2776 DQVTHELGILQSLQHPLLVGL---------LDTFETPTSYILVLEMADQGRLLDCVVrwgsltegkIRAHLGEVLEAVRY 2846
Cdd:cd06626    44 KEIADEMKVLEGLDHPNLVRYygvevhreeVYIFMEYCQEGTLEELLRHGRILDEAV---------IRVYTLQLLEGLAY 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2847 LHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQL--NTTYYIH----QLLGNPEFAAPEIILGNPVS---LTSDTW 2917
Cdd:cd06626   115 LHENGIVHRDIKPANIFLDSN---GLIKLGDFGSAVKLknNTTTMAPgevnSLVGTPAYMAPEVITGNKGEghgRAADIW 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2918 SVGVLTYVLLSGVSP--FLDdsveetclNICRLDF--------SFPDDyfKGVSQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd06626   192 SLGCVVLEMATGKRPwsELD--------NEWAIMYhvgmghkpPIPDS--LQLSPEGKDFLSRCLESDPKKRPTASELLD 261

                  ....
gi 767934614 2988 EQWL 2991
Cdd:cd06626   262 HPFI 265
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
2743-2979 3.13e-21

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 97.46  E-value: 3.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQ-SLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDdvecTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG----DAVQLNTTyyiHQL 2893
Cdd:cd05587    84 LMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLD---AEGHIKIADFGmckeGIFGGKTT---RTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQ 2973
Cdd:cd05587   158 CGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAVSICKGLLT 233

                  ....*.
gi 767934614 2974 EDPAKR 2979
Cdd:cd05587   234 KHPAKR 239
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
2743-2934 4.42e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 96.36  E-value: 4.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATK---FVNKKLMK-RDQVTHELGILQSLQHPLLVGLLD----TFETPTSYILVLEM-- 2812
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrQELSPSDKnRERWCLEVQIMKKLNHPNVVSARDvppeLEKLSPNDLPLLAMey 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ---ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYY 2889
Cdd:cd13989    81 csgGDLRKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYAKELDQGSL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767934614 2890 IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL 2934
Cdd:cd13989   161 CTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFL 205
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2789-3007 5.47e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 96.26  E-value: 5.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2789 QHPLLVGLLDTFE----TPTSYILVLEMADQGRLLDCVVRWG--SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENI 2862
Cdd:cd14170    53 QCPHIVRIVDVYEnlyaGRKCLLIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2863 LVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDD---SVE 2939
Cdd:cd14170   133 LYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglAIS 212
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2940 ETCLNICRL-DFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGRSTGVLDTSRL 3007
Cdd:cd14170   213 PGMKTRIRMgQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRV 281
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
2737-2990 6.47e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 95.65  E-value: 6.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR---DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEgvpSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQG--RLLDCVVRWGsLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkptIKLADFGDA----VQLNTt 2887
Cdd:cd07860    82 HQDlkKFMDASALTG-IPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA---IKLADFGLArafgVPVRT- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 yYIHQLLgNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL----------------DF 2950
Cdd:cd07860   157 -YTHEVV-TLWYRAPEILLGCKYYSTAvDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTlgtpdevvwpgvtsmpDY 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2951 --SFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd07860   235 kpSFPkwarqdfSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
2743-2991 6.98e-21

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 94.69  E-value: 6.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVN----KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIPhsrvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLL-GNP 2897
Cdd:cd14188    89 AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENM---ELKVGDFGLAARLEPLEHRRRTIcGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd14188   166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLP----SSLLAPAKHLIASMLSKNPE 241
                         250
                  ....*....|....
gi 767934614 2978 KRPSAALALQEQWL 2991
Cdd:cd14188   242 DRPSLDEIIRHDFF 255
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
2743-2991 7.33e-21

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 95.20  E-value: 7.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKkCDQKGTKRAVATKFV-------NKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd06631     9 LGKGAYGTVY-CGLTSTGQLIAVKQVeldtsdkEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFGDAVQL--NTTYYIH-Q 2892
Cdd:cd06631    88 GSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIML---MPNGVIKLIDFGCAKRLciNLSSGSQsQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LL----GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNI---CRLDFSFPDDYfkgvSQKAK 2965
Cdd:cd06631   165 LLksmrGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgsgRKPVPRLPDKF----SPEAR 240
                         250       260
                  ....*....|....*....|....*.
gi 767934614 2966 EFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd06631   241 DFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
2737-2979 8.99e-21

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 95.40  E-value: 8.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKR--------------------------DQVTHELGILQSLQ 2789
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKkLLKQygfprrppprgskaaqgeqakplaplERVYQEIAILKKLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2790 HPLLVGLLDTFETPT--SYILVLEMADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDES 2867
Cdd:cd14200    82 HVNIVKLIEVLDDPAedNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2868 lakPTIKLADFGDAVQLN-TTYYIHQLLGNPEFAAPEIILGNPVSLTS---DTWSVGVLTYVLLSGVSPFLDDSVEETCL 2943
Cdd:cd14200   161 ---GHVKIADFGVSNQFEgNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGVTLYCFVYGKCPFIDEFILALHN 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767934614 2944 NICRLDFSFPDDyfKGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:cd14200   238 KIKNKPVEFPEE--PEISEELKDLILKMLDKNPETR 271
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
2737-2986 9.28e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 95.18  E-value: 9.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI--RLESEEEgvpstAIREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 M--ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG--DAVQLNTT 2887
Cdd:cd07861    80 FlsMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDN---KGVIKLADFGlaRAFGIPVR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLgNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL----------------DF 2950
Cdd:cd07861   157 VYTHEVV-TLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRIlgtptediwpgvtslpDY 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767934614 2951 --SFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALAL 2986
Cdd:cd07861   236 knTFPkwkkgslRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKAL 280
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
2737-2979 1.01e-20

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 94.72  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK--------LMKRDQVTHELGILQSL-QHPLLVGLLDTFETPTSYI 2807
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskdgnDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMADQGRLLDCVV--RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdeSLAKPTIKLADFGDAVQLN 2885
Cdd:cd13993    82 IVLEYCPNGDLFEAITenRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILL--SQDEGTVKLCDFGLATTEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 TTYYIHqlLGNPEFAAPEIILGNPVSLTS------DTWSVGVLTYVLLSGVSPFLDDSVEEtclNICRLDFSFPDDYFKG 2959
Cdd:cd13993   160 ISMDFG--VGSEFYMAPECFDEVGRSLKGypcaagDIWSLGIILLNLTFGRNPWKIASESD---PIFYDYYLNSPNLFDV 234
                         250       260
                  ....*....|....*....|...
gi 767934614 2960 VSQKAKEFVCFL---LQEDPAKR 2979
Cdd:cd13993   235 ILPMSDDFYNLLrqiFTVNPNNR 257
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
2737-2929 1.13e-20

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 95.75  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFS-VVKKCDQKGTKRAVATKFV-NKKLMKRDQVThELGILQSL--------QHplLVGLLDTFETPTSY 2806
Cdd:cd14135     2 YRVYGYLGKGVFSnVVRARDLARGNQEVAIKIIrNNELMHKAGLK-ELEILKKLndadpddkKH--CIRLLRHFEHKNHL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ILVLEMADqGRLLDCVVRWGS---LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFGDAVQ 2883
Cdd:cd14135    79 CLVFESLS-MNLREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEK--KNTLKLCDFGSASD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 LN----TTYYIHQLlgnpeFAAPEIILGNPVSLTSDTWSVGVLTYVLLSG 2929
Cdd:cd14135   156 IGeneiTPYLVSRF-----YRAPEIILGLPYDYPIDMWSVGCTLYELYTG 200
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2737-2987 1.20e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 94.41  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKfVNKKL----MKRD---QVTHELGILQSLQHPLLVGLLDTFETPTSYILV 2809
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELK-VLKEIsvgeLQPDetvDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMAdQGRLLDCVVRW-----GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakptIKLADFGDA-VQ 2883
Cdd:cd08222    81 TEYC-EGGDLDDKISEykksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV----IKVGDFGISrIL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPDDYfkgvSQ 2962
Cdd:cd08222   156 MGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKY----SK 231
                         250       260
                  ....*....|....*....|....*
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd08222   232 ELNAIYSRMLNKDPALRPSAAEILK 256
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
2740-2995 1.25e-20

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 95.10  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR-DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd06644    17 IGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEElEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWG-SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG-DAVQLNTTYYIHQLLGN 2896
Cdd:cd06644    97 DAIMLELDrGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD---GDIKLADFGvSAKNVKTLQRRDSFIGT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIIL-----GNPVSLTSDTWSVGVlTYVLLSGVSPFLDDsveetcLNICRLDFSFPDDYFKGVSQKAK---EFV 2968
Cdd:cd06644   174 PYWMAPEVVMcetmkDTPYDYKADIWSLGI-TLIEMAQIEPPHHE------LNPMRVLLKIAKSEPPTLSQPSKwsmEFR 246
                         250       260       270
                  ....*....|....*....|....*....|
gi 767934614 2969 CFL---LQEDPAKRPSAALALQEQWLQAGN 2995
Cdd:cd06644   247 DFLktaLDKHPETRPSAAQLLEHPFVSSVT 276
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
2743-2979 1.70e-20

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 95.49  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05597     9 IGRGAFGEVAVVKLKSTEKVYAMKILNKwEMLKRAETAcfrEERDVLVNGDRRWITKLHYAFQDENYLYLVMDYYCGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQL--LG 2895
Cdd:cd05597    89 LTLLSKFEDrLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRN---GHIRLADFGSCLKLREDGTVQSSvaVG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNP-----VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD--FSFPDDYfKGVSQKAKEFV 2968
Cdd:cd05597   166 TPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKehFSFPDDE-DDVSEEAKDLI 244
                         250
                  ....*....|.
gi 767934614 2969 CFLLQeDPAKR 2979
Cdd:cd05597   245 RRLIC-SRERR 254
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
2743-2933 2.34e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 95.18  E-value: 2.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGIL-QSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEdidwVQTEKHVFeTASNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG---DAVQLNTTyyIHQLL 2894
Cdd:cd05588    83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLD---SEGHIKLTDYGmckEGLRPGDT--TSTFC 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd05588   158 GTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
2721-2979 2.51e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 95.47  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2721 GMDGIMVTWKDNFDSFySEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGIL-QSLQHPLLVG 2795
Cdd:cd05617     2 GMDGIKISQGLGLQDF-DLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEdidwVQTEKHVFeQASSNPFLVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2796 LLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKL 2875
Cdd:cd05617    81 LHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLD---ADGHIKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2876 ADFGDAVQ-LNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF---LDDSVEETCLNICRLDFS 2951
Cdd:cd05617   158 TDYGMCKEgLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVILE 237
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2952 FPDDYFKGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:cd05617   238 KPIRIPRFLSVKASHVLKGFLNKDPKER 265
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
2737-2992 2.80e-20

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 93.45  E-value: 2.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd06647     9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ-LL 2894
Cdd:cd06647    89 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFCAQITPEQSKRStMV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC---RLDFSFPDDyfkgVSQKAKEFVCFL 2971
Cdd:cd06647   165 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFLNRC 240
                         250       260
                  ....*....|....*....|.
gi 767934614 2972 LQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06647   241 LEMDVEKRGSAKELLQHPFLK 261
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
2743-2979 2.87e-20

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 94.68  E-value: 2.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDdvectMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG-------DAVQLNTtyyi 2890
Cdd:cd05616    88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLD---SEGHIKIADFGmckeniwDGVTTKT---- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 hqLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCF 2970
Cdd:cd05616   161 --FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYP----KSMSKEAVAICKG 234

                  ....*....
gi 767934614 2971 LLQEDPAKR 2979
Cdd:cd05616   235 LMTKHPGKR 243
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2737-2974 2.88e-20

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 95.84  E-value: 2.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05621    54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfEMIKRSDSAffwEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIH- 2891
Cdd:cd05621   134 MPGGDLVNLMSNY-DVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKY---GHLKLADFGTCMKMDETGMVHc 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 -QLLGNPEFAAPEIILGNP----VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPDDYfkGVSQKA 2964
Cdd:cd05621   210 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhKNSLNFPDDV--EISKHA 287
                         250
                  ....*....|
gi 767934614 2965 KEFVCFLLQE 2974
Cdd:cd05621   288 KNLICAFLTD 297
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
2737-2991 2.94e-20

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 93.89  E-value: 2.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKI--RLETEDEgvpstAIREISLLKELNHPNIVRLLDVVHSENKLYLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQG--RLLDCVvRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDA----VQLN 2885
Cdd:cd07835    79 FLDLDlkKYMDSS-PLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDT---EGALKLADFGLArafgVPVR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 TtyYIHQLLgNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL---------------- 2948
Cdd:cd07835   155 T--YTHEVV-TLWYRAPEILLGSKHYSTPvDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTlgtpdedvwpgvtslp 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2949 DF--SFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07835   232 DYkpTFPkwarqdlSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2737-2974 3.07e-20

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 96.23  E-value: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05622    75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIH- 2891
Cdd:cd05622   155 MPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS---GHLKLADFGTCMKMNKEGMVRc 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 -QLLGNPEFAAPEIILGNP----VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPDDyfKGVSQKA 2964
Cdd:cd05622   231 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDD--NDISKEA 308
                         250
                  ....*....|
gi 767934614 2965 KEFVCFLLQE 2974
Cdd:cd05622   309 KNLICAFLTD 318
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
2743-2934 3.50e-20

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 93.87  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKL--MKRDQVTHELGILQSLQHPLLVGLLDTFE-----TPTSY-ILVLEMAD 2814
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELspKNRERWCLEIQIMKRLNHPNVVAARDVPEglqklAPNDLpLLAMEYCQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRL---LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd14038    82 GGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767934614 2892 QLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL 2934
Cdd:cd14038   162 SFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
2737-2983 4.04e-20

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 93.17  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH-ELGILQSL-QHPLLVGLLDT---FETPTSYILVLE 2811
Cdd:cd13985     2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIkEIEIMKRLcGHPNIVQYYDSailSSEGRKEVLLLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNC--RIAHLDLKPENILVDESlakPTIKLADFGDA------ 2881
Cdd:cd13985    82 EYCPGSLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFSNT---GRFKLCDFGSAttehyp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 -------------VQLNTTyyihqllgnPEFAAPEII---LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVeetcLNI 2945
Cdd:cd13985   159 leraeevniieeeIQKNTT---------PMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSK----LAI 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767934614 2946 CRLDFSFPDdyFKGVSQKAKEFVCFLLQEDPAKRPSAA 2983
Cdd:cd13985   226 VAGKYSIPE--QPRYSPELHDLIRHMLTPDPAERPDIF 261
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2737-2971 4.19e-20

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 94.75  E-value: 4.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05596    28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKfEMIKRSDSAffwEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIH- 2891
Cdd:cd05596   108 MPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLD---ASGHLKLADFGTCMKMDKDGLVRs 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 -QLLGNPEFAAPEIILG----NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrLD----FSFPDDyfKGVSQ 2962
Cdd:cd05596   184 dTAVGTPDYISPEVLKSqggdGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKI--MNhknsLQFPDD--VEISK 259
                         250
                  ....*....|
gi 767934614 2963 KAKEFVC-FL 2971
Cdd:cd05596   260 DAKSLICaFL 269
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
2740-2979 4.26e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 94.29  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQ---SLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05589     4 IAVLGRGHFGKVLLAEYKPTGELFAIKALKKGdIIARDEVESlmcEKRIFEtvnSARHPFLVNLFACFQTPEHVCFVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLL-----DCvvrwgsLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG------DA 2881
Cdd:cd05589    84 AAGGDLMmhiheDV------FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLD---TEGYVKIADFGlckegmGF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 VQLNTTYyihqlLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddYFkgVS 2961
Cdd:cd05589   155 GDRTSTF-----CGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYP--RF--LS 225
                         250
                  ....*....|....*...
gi 767934614 2962 QKAKEFVCFLLQEDPAKR 2979
Cdd:cd05589   226 TEAISIMRRLLRKNPERR 243
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
2734-3015 4.48e-20

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 93.21  E-value: 4.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd06641     3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEieDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQL-NTTYYI 2890
Cdd:cd06641    83 YLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSE---HGEVKLADFGVAGQLtDTQIKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPD--------DYFKGVsq 2962
Cdd:cd06641   159 N*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSE-------LHPMKVLFLIPKnnpptlegNYSKPL-- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2963 kaKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGRstgvldTSRLTSFIERRK 3015
Cdd:cd06641   230 --KEFVEACLNKEPSFRPTAKELLKHKFILRNAKK------TSYLTELIDRYK 274
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
2790-2979 4.87e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 92.61  E-value: 4.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2790 HPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslA 2869
Cdd:PHA03390   68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDR--A 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2870 KPTIKLADFGDAVQLNT--TYYihqllGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFlDDSVEEtCLNICR 2947
Cdd:PHA03390  146 KDRIYLCDYGLCKIIGTpsCYD-----GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF-KEDEDE-ELDLES 218
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767934614 2948 L------DFSFPddyfKGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:PHA03390  219 LlkrqqkKLPFI----KNVSKNANDFVQSMLKYNINYR 252
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
2743-2979 6.44e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 93.02  E-value: 6.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKgyegAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS----LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQL-----NTTYY 2889
Cdd:cd05608    89 RYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDD---GNVRISDLGLAVELkdgqtKTKGY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IhqllGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF--LDDSVE--ETCLNICRLDFSFPDDYfkgvSQKAK 2965
Cdd:cd05608   166 A----GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFraRGEKVEnkELKQRILNDSVTYSEKF----SPASK 237
                         250
                  ....*....|....
gi 767934614 2966 EFVCFLLQEDPAKR 2979
Cdd:cd05608   238 SICEALLAKDPEKR 251
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2743-2968 7.09e-20

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 95.08  E-value: 7.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05624    80 IGRGAFGEVAVVKMKNTERIYAMKILNKwEMLKRAETAcfrEERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRW-GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ--LLG 2895
Cdd:cd05624   160 LTLLSKFeDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLD---MNGHIRLADFGSCLKMNDDGTVQSsvAVG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPVSL-----TSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD--FSFPdDYFKGVSQKAKEFV 2968
Cdd:cd05624   237 TPDYISPEILQAMEDGMgkygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerFQFP-SHVTDVSEEAKDLI 315
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
2743-2933 8.64e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 93.94  E-value: 8.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGIL-QSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05618    28 IGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEdidwVQTEKHVFeQASNHPFLVGLHSCFQTESRLFFVIEYVNGGD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQ-LNTTYYIHQLLGN 2896
Cdd:cd05618   108 LMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLD---SEGHIKLTDYGMCKEgLRPGDTTSTFCGT 184
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd05618   185 PNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2746-3029 1.01e-19

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 93.45  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2746 GRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH----ELGILQSL-QHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05614    14 GKVFLVRKVSGHDANKLYAMKVLRKaALVQKAKTVEhtrtERNVLEHVrQSPFLVTLHYAFQTDAKLHLILDYVSGGELF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT-----TYyihQLL 2894
Cdd:cd05614    94 THLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLD---SEGHVVLTDFGLSKEFLTeekerTY---SFC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFL----DDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFVC 2969
Cdd:cd05614   168 GTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFPSF----IGPVARDLLQ 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2970 FLLQEDPAKR----PSAALALQEQWLQAGngrstgvLDTSRLTSfierRKHQNDVRP-IRS---IKNF 3029
Cdd:cd05614   244 KLLCKDPKKRlgagPQGAQEIKEHPFFKG-------LDWEALAL----RKVNPPFRPsIRSeldVGNF 300
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2737-2991 1.10e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 91.56  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMpvkEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRW-GSL-TEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFGDAVQLN-TTYYI 2890
Cdd:cd08225    82 DGGDLMKRINRQrGVLfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKN--GMVAKLGDFGIARQLNdSMELA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFkgvSQKAKEFVCF 2970
Cdd:cd08225   160 YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNF---SRDLRSLISQ 236
                         250       260
                  ....*....|....*....|.
gi 767934614 2971 LLQEDPAKRPSAALALQEQWL 2991
Cdd:cd08225   237 LFKVSPRDRPSITSILKRPFL 257
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
2734-3015 1.16e-19

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 92.04  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd06640     3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEieDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd06640    83 YLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSE---QGDVKLADFGVAGQLTDTQIKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 Q-LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRldfsFPDDYFKG-VSQKAKEFVC 2969
Cdd:cd06640   159 NtFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPK----NNPPTLVGdFSKPFKEFID 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 2970 FLLQEDPAKRPSAALALQEQWLQAGNGRstgvldTSRLTSFIERRK 3015
Cdd:cd06640   235 ACLNKDPSFRPTAKELLKHKFIVKNAKK------TSYLTELIDRFK 274
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
2737-2955 1.83e-19

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 93.38  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05629     3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMfKKDQLAHvkaERDVLAESDSPWVVSLYYSFQDAQYLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTY---Y 2889
Cdd:cd05629    83 LPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILID---RGGHIKLSDFGLSTGFHKQHdsaY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQLL---------------------------------------------GNPEFAAPEIILGNPVSLTSDTWSVGVLTY 2924
Cdd:cd05629   160 YQKLLqgksnknridnrnsvavdsinltmsskdqiatwkknrrlmaystvGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767934614 2925 VLLSGVSPFLDDSVEETCLNIC--RLDFSFPDD 2955
Cdd:cd05629   240 ECLIGWPPFCSENSHETYRKIInwRETLYFPDD 272
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
2743-2979 2.32e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 91.78  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDdvdctMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQ------LNTTYyih 2891
Cdd:cd05591    83 LMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLD---AEGHCKLADFGMCKEgilngkTTTTF--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 qlLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFL 2971
Cdd:cd05591   157 --CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAF 230

                  ....*...
gi 767934614 2972 LQEDPAKR 2979
Cdd:cd05591   231 MTKNPAKR 238
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
2743-2979 2.50e-19

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 92.37  E-value: 2.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDdvectMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG----DAVQLNTTyyiHQL 2893
Cdd:cd05615    98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLD---SEGHIKIADFGmckeHMVEGVTT---RTF 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddyfKGVSQKAKEFVCFLLQ 2973
Cdd:cd05615   172 CGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAVSICKGLMT 247

                  ....*.
gi 767934614 2974 EDPAKR 2979
Cdd:cd05615   248 KHPAKR 253
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
2743-2979 3.01e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 91.91  E-value: 3.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH----ELGILQ-SLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVEctmvEKRVLSlAWEHPFLTHLFCTFQTKENLFFVMEYLNGGD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG--------DAvQLNTtyy 2889
Cdd:cd05619    93 LMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDK---DGHIKIADFGmckenmlgDA-KTST--- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 ihqLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcRLDFSFpddYFKGVSQKAKEFVC 2969
Cdd:cd05619   166 ---FCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI-RMDNPF---YPRWLEKEAKDILV 238
                         250
                  ....*....|
gi 767934614 2970 FLLQEDPAKR 2979
Cdd:cd05619   239 KLFVREPERR 248
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2775-2986 3.32e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 89.80  E-value: 3.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2775 RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRI 2852
Cdd:cd08221    43 RRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2853 AHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQ-LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVS 2931
Cdd:cd08221   123 LHRDIKTLNIFLTKA---DLVKLGDFGISKVLDSESSMAEsIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKR 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2932 PFLDDSVEETCLNICRLDFSFPDDYFkgvSQKAKEFVCFLLQEDPAKRPSAALAL 2986
Cdd:cd08221   200 TFDATNPLRLAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQDPEDRPTAEELL 251
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
2731-2991 3.37e-19

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 91.86  E-value: 3.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnKKLMK-RDQVTHELGILQSLQH------PLLVGLLDTFETP 2803
Cdd:cd14134     8 DLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKII-RNVEKyREAAKIEIDVLETLAEkdpngkSHCVQLRDWFDYR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2804 TSYILVLEMADQGrLLD--CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDES------------- 2867
Cdd:cd14134    87 GHMCIVFELLGPS-LYDflKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlVDSDyvkvynpkkkrqi 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2868 --LAKPTIKLADFGDAV--------QLNTTYYihqllgnpefAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVS------ 2931
Cdd:cd14134   166 rvPKSTDIKLIDFGSATfddeyhssIVSTRHY----------RAPEVILGLGWSYPCDVWSIGCILVELYTGELlfqthd 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2932 -------------PFLDDSVEETCLNICRLDFS-----FPDD----------------YFKGVSQKAKEFVCF---LLQE 2974
Cdd:cd14134   236 nlehlammerilgPLPKRMIRRAKKGAKYFYFYhgrldWPEGsssgrsikrvckplkrLMLLVDPEHRLLFDLirkMLEY 315
                         330
                  ....*....|....*..
gi 767934614 2975 DPAKRPSAALALQEQWL 2991
Cdd:cd14134   316 DPSKRITAKEALKHPFF 332
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
2742-2994 5.36e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 90.43  E-value: 5.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd06659    28 KIGEGSTGVVCIAREKHSGRQVAVKMMDlRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 cVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQ-LLGNPEF 2899
Cdd:cd06659   108 -IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG---RVKLSDFGFCAQISKDVPKRKsLVGTPYW 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETclnICRLDFSFPDDY--FKGVSQKAKEFVCFLLQEDPA 2977
Cdd:cd06659   184 MAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQA---MKRLRDSPPPKLknSHKASPVLRDFLERMLVRDPQ 260
                         250
                  ....*....|....*...
gi 767934614 2978 KRPSAALALQEQW-LQAG 2994
Cdd:cd06659   261 ERATAQELLDHPFlLQTG 278
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
2737-2987 5.83e-19

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 89.29  E-value: 5.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVI--KLEPGDDFEiiqQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQ- 2892
Cdd:cd06613    80 GGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTED---GDVKLADFGVSAQLTATIAKRKs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGN---PVSLTSDTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPDDYFKGVSQKAKE--- 2966
Cdd:cd06613   157 FIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMFD-------LHPMRALFLIPKSNFDPPKLKDKEkws 229
                         250       260
                  ....*....|....*....|....*.
gi 767934614 2967 -----FVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd06613   230 pdfhdFIKKCLTKNPKKRPTATKLLQ 255
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
849-1078 6.66e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.89  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  849 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 928
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  929 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1008
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1009 EAFLKACTlarrNADVFLKYLHRNSVNMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1078
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
2743-2979 7.80e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 90.35  E-value: 7.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDdvectMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG-------DAVQLNTtyyi 2890
Cdd:cd05590    83 LMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDH---EGHCKLADFGmckegifNGKTTST---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 hqLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF---LDDSVEETCLNicrldfsfpDD--YFKGVSQKAK 2965
Cdd:cd05590   156 --FCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFeaeNEDDLFEAILN---------DEvvYPTWLSQDAV 224
                         250
                  ....*....|....
gi 767934614 2966 EFVCFLLQEDPAKR 2979
Cdd:cd05590   225 DILKAFMTKNPTMR 238
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
2092-2212 7.96e-19

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 84.74  E-value: 7.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2092 LQGFDGKIVAQGKLLLQDTFLVTDQDAgLLPRCRERRIFLFEQIVIFSEPLDKKKGFSmpGFLFKNSIKVSCLCLEENVE 2171
Cdd:cd13240     2 LEGCDEDLDSLGEVILQDSFQVWDPKQ-LIRKGRERHVFLFELCLVFSKEVKDSNGKS--KYIYKSRLMTSEIGVTEHIE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2172 NDPCKFALTSRTGDVVET-FILHSSSPSVRQTWIHEINQILE 2212
Cdd:cd13240    79 GDPCKFALWTGRVPTSDNkIVLKASSLEVKQTWVKKLREVIQ 120
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
2743-2979 8.64e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 90.03  E-value: 8.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05632    10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesmALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd05632    90 KFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDY---GHIRISDLGLAVKIPEGESIRGRVGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDP 2976
Cdd:cd05632   167 VGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDP 246

                  ...
gi 767934614 2977 AKR 2979
Cdd:cd05632   247 KQR 249
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
2743-2986 9.23e-19

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 88.87  E-value: 9.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCD-QKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd14066     1 IGSGGFGTVYKGVlENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 --------VVRWGSLTegKIRAHlgeVLEAVRYLHN---CRIAHLDLKPENILVDESlakPTIKLADFGDAVQLN---TT 2887
Cdd:cd14066    81 lhchkgspPLPWPQRL--KIAKG---IARGLEYLHEecpPPIIHGDIKSSNILLDED---FEPKLTDFGLARLIPpseSV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICrldfsfpdDYFKgvSQKAKEF 2967
Cdd:cd14066   153 SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLV--------EWVE--SKGKEEL 222
                         250       260
                  ....*....|....*....|..
gi 767934614 2968 VCFL---LQEDPAKRPSAALAL 2986
Cdd:cd14066   223 EDILdkrLVDDDGVEEEEVEAL 244
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2733-2988 9.45e-19

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 88.89  E-value: 9.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQSLQHPLLVGLLDTF-ETPTSYILv 2809
Cdd:cd13996     4 YLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIrlTEKSSASEKVLREVKALAKLNHPNIVRYYTAWvEEPPLYIQ- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRLLDCVVRWGSLTEGKIRAHLG---EVLEAVRYLHNCRIAHLDLKPENILVDESLAkpTIKLADFGDAV---- 2882
Cdd:cd13996    83 MELCEGGTLRDWIDRRNSSSKNDRKLALElfkQILKGVSYIHSKGIVHRDLKPSNIFLDNDDL--QVKIGDFGLATsign 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLNTTYYIHQLL-----------GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSveeTCLNICRlDFS 2951
Cdd:cd13996   161 QKRELNNLNNNNngntsnnsvgiGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTAMERS---TILTDLR-NGI 236
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767934614 2952 FPdDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQE 2988
Cdd:cd13996   237 LP-ESFKAKHPKEADLIQSLLSKNPEERPSAEQLLRS 272
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
2743-2979 9.69e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 90.00  E-value: 9.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDdvectMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG----DAVQLN--TTYyih 2891
Cdd:cd05620    83 LMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRD---GHIKIADFGmckeNVFGDNraSTF--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 qlLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcRLDfsfPDDYFKGVSQKAKEFVCFL 2971
Cdd:cd05620   157 --CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI-RVD---TPHYPRWITKESKDILEKL 230

                  ....*...
gi 767934614 2972 LQEDPAKR 2979
Cdd:cd05620   231 FERDPTRR 238
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2742-2980 1.01e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 89.32  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMK---RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd08229    31 KIGRGQFSEVYRATCLLDGVPVALKKVQIfDLMDakaRADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGS----LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT-TYYIHQ 2892
Cdd:cd08229   111 LSRMIKHFKKqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFIT---ATGVVKLGDLGLGRFFSSkTTAAHS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVE--ETCLNICRLDF-SFPDDYFkgvSQKAKEFVC 2969
Cdd:cd08229   188 LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYpPLPSDHY---SEELRQLVN 264
                         250
                  ....*....|.
gi 767934614 2970 FLLQEDPAKRP 2980
Cdd:cd08229   265 MCINPDPEKRP 275
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
2734-2979 1.19e-18

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 89.19  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRD----QVTHELGILQSLQHPLLVGLLDTFETPTSYILV 2809
Cdd:cd05607     1 DKYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKsgekMALLEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRLLDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTT 2887
Cdd:cd05607    81 MSLMNGGDLKYHIYNVGErgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDD---NGNCRLSDLGLAVEVKEG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDD----SVEETCLNICRLDFSFPDDYFkgvSQK 2963
Cdd:cd05607   158 KPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEDEVKFEHQNF---TEE 234
                         250
                  ....*....|....*.
gi 767934614 2964 AKEFVCFLLQEDPAKR 2979
Cdd:cd05607   235 AKDICRLFLAKKPENR 250
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
2743-2994 1.19e-18

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 90.09  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHP-----LLVGLLDTFETPTSYILVLEMADQGr 2817
Cdd:cd14229     8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNEnadefNFVRAYECFQHRNHTCLVFEMLEQN- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVV--RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKP-TIKLADFGDAVQLNTTyYIHQLL 2894
Cdd:cd14229    87 LYDFLKqnKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHVSKT-VCSTYL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGvSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCfllQE 2974
Cdd:cd14229   166 QSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKTSRFFC---RE 241
                         250       260
                  ....*....|....*....|.
gi 767934614 2975 DPAKRPSAAL-ALQEQWLQAG 2994
Cdd:cd14229   242 TDAPYSSWRLkTLEEHEAETG 262
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
2737-2982 1.23e-18

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 90.32  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH----ELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05610     6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHqvqaERDALALSKSPFIVHLYYSLQSANNVYLVMEY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG-DAVQLN------ 2885
Cdd:cd05610    86 LIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISN---EGHIKLTDFGlSKVTLNrelnmm 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 ----------------------------------TTYYI-------------HQLLGNPEFAAPEIILGNPVSLTSDTWS 2918
Cdd:cd05610   163 dilttpsmakpkndysrtpgqvlslisslgfntpTPYRTpksvrrgaarvegERILGTPDYLAPELLLGKPHGPAVDWWA 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2919 VGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKgVSQKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd05610   243 LGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEE-LSVNAQNAIEILLTMDPTKRAGL 305
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
2742-2981 1.36e-18

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 88.36  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKC---DQKGTKRAVATKFVNKKLMKRDQV--THELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd00192     2 KLGEGAFGEVYKGklkGGDGKTVDVAVKTLKEDASESERKdfLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLG---------EVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTT 2887
Cdd:cd00192    82 DLLDFLRKSRPVFPSPEPSTLSlkdllsfaiQIAKGMEYLASKKFVHRDLAARNCLVGE---DLVVKISDFGLSRDIYDD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPE---FAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETCLNIC---RLDF--SFPDDYFK 2958
Cdd:cd00192   159 DYYRKKTGGKLpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRkgyRLPKpeNCPDELYE 238
                         250       260
                  ....*....|....*....|...
gi 767934614 2959 GVSQkakefvCFllQEDPAKRPS 2981
Cdd:cd00192   239 LMLS------CW--QLDPEDRPT 253
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
2737-2937 1.54e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 88.63  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK---------FVNKKLMKrdqvthELGILQSLQHPLLVGLLDTFETPTSYI 2807
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKkfleseddkMVKKIAMR------EIKMLKQLRHENLVNLIEVFRRKKRWY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLN-- 2885
Cdd:cd07846    77 LVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQS---GVVKLCDFGFARTLAap 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2886 ----TTYYIHQLLGNPEFAAPEIILGNPVsltsDTWSVGVLTYVLLSGVSPFLDDS 2937
Cdd:cd07846   154 gevyTDYVATRWYRAPELLVGDTKYGKAV----DVWAVGCLVTEMLTGEPLFPGDS 205
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
2737-2987 1.95e-18

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 88.71  E-value: 1.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK--FVNKKLMKRdqvthELGILQSLQHPLLVGLLDTFETPTS------YIL 2808
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDKRYKNR-----ELQIMRRLKHPNIVKLKYFFYSSGEkkdevyLNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLE-MAD--QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFGDAVQL- 2884
Cdd:cd14137    81 VMEyMPEtlYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPE--TGVLKLCDFGSAKRLv 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 ----NTTY-----YihqllgnpefAAPEIILGNPVSLTS-DTWSVG------VLTYVLLSGvspflDDSVE--------- 2939
Cdd:cd14137   159 pgepNVSYicsryY----------RAPELIFGATDYTTAiDIWSAGcvlaelLLGQPLFPG-----ESSVDqlveiikvl 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2940 -----ETCLNIC--RLDFSFP-------DDYF-KGVSQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd14137   224 gtptrEQIKAMNpnYTEFKFPqikphpwEKVFpKRTPPDAIDLLSKILVYNPSKRLTALEALA 286
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2742-2993 1.96e-18

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 88.37  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKL--MKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG--- 2816
Cdd:cd06622     8 ELGKGNYGSVYKVLHRPTGVTMAMKEIRLELdeSKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGsld 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYL---HNcrIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQL 2893
Cdd:cd06622    88 KLYAGGVATEGIPEDVLRRITYAVVKGLKFLkeeHN--IIHRDVKPTNVLVN---GNGQVKLCDFGVSGNLVASLAKTNI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 lGNPEFAAPE-IILGNPV-----SLTSDTWSVGVLTYVLLSGVSPF---LDDSVEETCLNICRLDF-SFPDDYfkgvSQK 2963
Cdd:cd06622   163 -GCQSYMAPErIKSGGPNqnptyTVQSDVWSLGLSILEMALGRYPYppeTYANIFAQLSAIVDGDPpTLPSGY----SDD 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 767934614 2964 AKEFVCFLLQEDPAKRPSAALALQEQWLQA 2993
Cdd:cd06622   238 AQDFVAKCLNKIPNRRPTYAQLLEHPWLVK 267
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
2737-2990 1.96e-18

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 88.39  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKfvnKKLMKRDQ----VT--HELGILQSLQHPLLVGLLD------TFETPT 2804
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALK---KIRMENEKegfpITaiREIKLLQKLDHPNVVRLKEivtskgSAKYKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEMAD---QGRLLDCVVRwgsLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDA 2881
Cdd:cd07840    78 SIYMVFEYMDhdlTGLLDNPEVK---FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILIN---NDGVLKLADFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 VQLNTTyyihqllGNPEFA---------APEIILGnpvsLTS-----DTWSVGVLTYVLLSGvSPFLDDSVEETCLN-IC 2946
Cdd:cd07840   152 RPYTKE-------NNADYTnrvitlwyrPPELLLG----ATRygpevDMWSVGCILAELFTG-KPIFQGKTELEQLEkIF 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2947 RL-------------------DFSFP-------DDYFKGV-SQKAKEFVCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd07840   220 ELcgspteenwpgvsdlpwfeNLKPKkpykrrlREVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
2743-2987 2.22e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 87.87  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVvkkCDQ-----KGTKRAVA-TKFVNKKLMKRDQV----THELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd06630     8 LGTGAFSS---CYQardvkTGTLMAVKqVSFCRNSSSEQEEVveaiREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKptIKLADFGDAVQLNTTY---- 2888
Cdd:cd06630    85 MAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQR--LRIADFGAAARLASKGtgag 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 -YIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSF-PDDYFKGVSQKAKE 2966
Cdd:cd06630   163 eFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATtPPPIPEHLSPGLRD 242
                         250       260
                  ....*....|....*....|.
gi 767934614 2967 FVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd06630   243 VTLRCLELQPEDRPPARELLK 263
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
2741-2936 3.19e-18

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 87.44  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2741 AELGRGRFSVVKKCDQKGtkRAVATKFVN---KKLMKRDQVTHELGILqSLQHPLLVGLL--DTFETPTSYILVL-EMAD 2814
Cdd:cd13979     9 EPLGSGGFGSVYKATYKG--ETVAVKIVRrrrKNRASRQSFWAELNAA-RLRHENIVRVLaaETGTDFASLGLIImEYCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVR-WGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLN----TTYY 2889
Cdd:cd13979    86 NGTLQQLIYEgSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQ---GVCKLCDFGCSVKLGegneVGTP 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2890 IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDD 2936
Cdd:cd13979   163 RSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGL 209
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
2737-3000 3.38e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 89.11  E-value: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSE---VAELGRGRFSVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:PLN00034   73 LSElerVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLldcvvrwgsltEGKIRAHLG-------EVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL 2884
Cdd:PLN00034  153 FMDGGSL-----------EGTHIADEQfladvarQILSGIAYLHRRHIVHRDIKPSNLLIN---SAKNVKIADFGVSRIL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NTTY-YIHQLLGNPEFAAPEII-----LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFK 2958
Cdd:PLN00034  219 AQTMdPCNSSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPA 298
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767934614 2959 GVSQKAKEFVCFLLQEDPAKRPSAALALQEQW-LQAGNGRSTG 3000
Cdd:PLN00034  299 TASREFRHFISCCLQREPAKRWSAMQLLQHPFiLRAQPGQGQG 341
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
2737-2991 3.47e-18

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 88.89  E-value: 3.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKfvnkKLMKRDQVTH-------ELGILQSLQHPLLVGLLDTFeTPTSYI-- 2807
Cdd:cd07851    17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIK----KLSRPFQSAIhakrtyrELRLLKHMKHENVIGLLDVF-TPASSLed 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 -----LVLEMADQGrlLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV 2882
Cdd:cd07851    92 fqdvyLVTHLMGAD--LNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDC---ELKILDFGLAR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLN---TTYyihqlLGNPEFAAPEIILgNPVSL--TSDTWSVGVLTYVLLSGVSPFL-DDSVEE-TC-LNIC-------- 2946
Cdd:cd07851   167 HTDdemTGY-----VATRWYRAPEIML-NWMHYnqTVDIWSVGCIMAELLTGKTLFPgSDHIDQlKRiMNLVgtpdeell 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2947 -------------------RLDFSfpdDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07851   241 kkissesarnyiqslpqmpKKDFK---EVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
2743-2934 3.59e-18

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 87.67  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKL--MKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYI-----LVLEMADQ 2815
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELsvKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEYCSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 G---RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQ 2892
Cdd:cd14039    81 GdlrKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAKDLDQGSLCTS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL 2934
Cdd:cd14039   161 FVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFL 202
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
2740-2993 4.32e-18

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 87.49  E-value: 4.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATK--FVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTF--ETPTsYILVLEMADQ 2815
Cdd:cd06620    10 LKDLGAGNGGSVSKVLHIPTGTIMAKKviHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFlnENNN-IIICMEYMDC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLlDCVVR-WGSLTE---GKIRAhlgEVLEAVRYLHNC-RIAHLDLKPENILVDeslAKPTIKLADFGDAVQLnTTYYI 2890
Cdd:cd06620    89 GSL-DKILKkKGPFPEevlGKIAV---AVLEGLTYLYNVhRIIHRDIKPSNILVN---SKGQIKLCDFGVSGEL-INSIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF----LDDSVEETCLNIcrLDF----------SFPDDy 2956
Cdd:cd06620   161 DTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFagsnDDDDGYNGPMGI--LDLlqrivnepppRLPKD- 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767934614 2957 fKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQ-WLQA 2993
Cdd:cd06620   238 -RIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDpFIQA 274
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
2737-2930 4.57e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 87.43  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK-FVN-------KKLMKRdqvthELGILQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd07847     3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVEseddpviKKIALR-----EIRMLKQLKHPNLVNLIEVFRRKRKLHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRL--LDCVVRwgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNT 2886
Cdd:cd07847    78 VFEYCDHTVLneLEKNPR--GVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQ---GQIKLCDFGFARILTG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2887 T--YYIhQLLGNPEFAAPEIILGN-----PVsltsDTWSVGVLTYVLLSGV 2930
Cdd:cd07847   153 PgdDYT-DYVATRWYRAPELLVGDtqygpPV----DVWAIGCVFAELLTGQ 198
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2781-2986 5.23e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 86.57  E-value: 5.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2781 ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCV-VRWGSL-TEGKIRAHLGEVLEAVRYLHNCRIAHLDLK 2858
Cdd:cd08219    48 EAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQKIkLQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIK 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2859 PENILVDESlakPTIKLADFGDAVQL-NTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDS 2937
Cdd:cd08219   128 SKNIFLTQN---GKVKLGDFGSARLLtSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANS 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767934614 2938 VEETCLNICRLDFS-FPDDYfkgvSQKAKEFVCFLLQEDPAKRPSAALAL 2986
Cdd:cd08219   205 WKNLILKVCQGSYKpLPSHY----SYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
2731-2991 6.76e-18

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 87.63  E-value: 6.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSL-----QHPL---LVGLLDTFET 2802
Cdd:cd14136     6 EVYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVreadpKDPGrehVVQLLDDFKH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 P----TSYILVLE-MAD-----------QGRLLDCVvrwgslteGKIRAHlgeVLEAVRYLHN-CRIAHLDLKPENILVD 2865
Cdd:cd14136    86 TgpngTHVCMVFEvLGPnllklikrynyRGIPLPLV--------KKIARQ---VLQGLDYLHTkCGIIHTDIKPENVLLC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2866 ESlaKPTIKLADFGDAVQLNTTYY--IHQLlgnpEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF---------L 2934
Cdd:cd14136   155 IS--KIEVKIADLGNACWTDKHFTedIQTR----QYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphsgedysR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2935 DDS----VEETCLNICR---LDFSFPDDYF-------------------------KGVSQKAKEFVCFL---LQEDPAKR 2979
Cdd:cd14136   229 DEDhlalIIELLGRIPRsiiLSGKYSREFFnrkgelrhisklkpwpledvlvekyKWSKEEAKEFASFLlpmLEYDPEKR 308
                         330
                  ....*....|..
gi 767934614 2980 PSAALALQEQWL 2991
Cdd:cd14136   309 ATAAQCLQHPWL 320
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
2737-2992 6.88e-18

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 87.09  E-value: 6.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd06655    21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINlQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ-LL 2894
Cdd:cd06655   101 GSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLG---MDGSVKLTDFGFCAQITPEQSKRStMV 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC---RLDFSFPDDyfkgVSQKAKEFVCFL 2971
Cdd:cd06655   177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSPIFRDFLNRC 252
                         250       260
                  ....*....|....*....|.
gi 767934614 2972 LQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06655   253 LEMDVEKRGSAKELLQHPFLK 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
2737-2992 7.01e-18

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 87.09  E-value: 7.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd06654    22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ-LL 2894
Cdd:cd06654   102 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFCAQITPEQSKRStMV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC---RLDFSFPDDyfkgVSQKAKEFVCFL 2971
Cdd:cd06654   178 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFLNRC 253
                         250       260
                  ....*....|....*....|.
gi 767934614 2972 LQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06654   254 LEMDVEKRGSAKELLQHQFLK 274
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
282-507 7.69e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.80  E-value: 7.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  282 QLRLFEQDAEKMFDWITHnKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIR 361
Cdd:cd00176     1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  362 QIASQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 437
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  438 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 507
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
2743-2992 7.86e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 87.04  E-value: 7.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVnKKLMKRDQVT----HELGILQSLQHPLLVGLLD--TFETPTSYILVLEMADQ- 2815
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKV-RMDNERDGIPisslREITLLLNLRHPNIVELKEvvVGKHLDSIFLVMEYCEQd 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 -GRLLDCVVRwgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGdavqLNTTYYIHQLL 2894
Cdd:cd07845    94 lASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTD---KGCLKIADFG----LARTYGLPAKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPE-----FAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGvSPFLDDSVEETCLN-ICRL------------------- 2948
Cdd:cd07845   165 MTPKvvtlwYRAPELLLGCTTYTTAiDMWAVGCILAELLAH-KPLLPGKSEIEQLDlIIQLlgtpnesiwpgfsdlplvg 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2949 DFSFPDD-Y------FKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd07845   244 KFTLPKQpYnnlkhkFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFK 294
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
2743-2934 1.06e-17

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 86.13  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGtkRAVATKFVNKK------------LMKRDQVTH----------ELGILQSLQHPLLVGLLDTF 2800
Cdd:cd14000     2 LGDGGFGSVYRASYKG--EPVAVKIFNKHtssnfanvpadtMLRHLRATDamknfrllrqELTVLSHLHHPSIVYLLGIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2801 ETPTsyILVLEMADQGRLlDCVVRWGSLTEGKIRAHLGE-----VLEAVRYLHNCRIAHLDLKPENILVdESLAKPT--- 2872
Cdd:cd14000    80 IHPL--MLVLELAPLGSL-DHLLQQDSRSFASLGRTLQQrialqVADGLRYLHSAMIIYRDLKSHNVLV-WTLYPNSaii 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2873 IKLADFGDAVQlNTTYYIHQLLGNPEFAAPEIILGNPV-SLTSDTWSVGVLTYVLLSGVSPFL 2934
Cdd:cd14000   156 IKIADYGISRQ-CCRMGAKGSEGTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAPMV 217
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
2737-2991 1.09e-17

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 86.05  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH--ELGILQSLQ-HPLLVGLLDTF-ETPTSYiLVLE- 2811
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMNlrEVKSLRKLNeHPNIVKLKEVFrENDELY-FVFEy 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 ---------MADQGRLLdcvvrwgslTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV 2882
Cdd:cd07830    80 megnlyqlmKDRKGKPF---------SESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE---VVKIADFGLAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLN-----TTY-----YihqllgnpefAAPEIIL-----GNPVsltsDTWSVGVLTYVLLSgVSPFLDDSVEETCLN-IC 2946
Cdd:cd07830   148 EIRsrppyTDYvstrwY----------RAPEILLrstsySSPV----DIWALGCIMAELYT-LRPLFPGSSEIDQLYkIC 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2947 -------------------RLDFSFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07830   213 svlgtptkqdwpegyklasKLGFRFPqfaptslHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2734-2989 1.11e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 87.03  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd06650     4 DDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPaiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTE---GKIRAHLGEVLEAVRYLHncRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTY 2888
Cdd:cd06650    84 HMDGGSLDQVLKKAGRIPEqilGKVSIAVIKGLTYLREKH--KIMHRDVKPSNILVN---SRGEIKLCDFGVSGQLIDSM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 yIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF-LDDSVEETCLNICRLDF------SFPDDYFKGVS 2961
Cdd:cd06650   159 -ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpPPDAKELELMFGCQVEGdaaetpPRPRTPGRPLS 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767934614 2962 QKAK---------EFVCFLLQEDPAKRPSAALALQEQ 2989
Cdd:cd06650   238 SYGMdsrppmaifELLDYIVNEPPPKLPSGVFSLEFQ 274
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
2731-2968 1.15e-17

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 87.81  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSfyseVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSY 2806
Cdd:cd05627     2 DDFES----LKVIGRGAFGEVRLVQKKDTGHIYAMKILRKAdMLEKEQVAHiraERDILVEADGAWVVKMFYSFQDKRNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLN- 2885
Cdd:cd05627    78 YLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLD---AKGHVKLSDFGLCTGLKk 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 ---TTYY--------------------------------IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGV 2930
Cdd:cd05627   155 ahrTEFYrnlthnppsdfsfqnmnskrkaetwkknrrqlAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGY 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767934614 2931 SPFLDDSVEETCLNIC--RLDFSFPDDYfkGVSQKAKEFV 2968
Cdd:cd05627   235 PPFCSETPQETYRKVMnwKETLVFPPEV--PISEKAKDLI 272
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2737-2981 1.24e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 85.25  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK---RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSpkeREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCV--VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd08218    82 DGGDLYKRInaQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKD---GIIKLGDFGIARVLNSTVELA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 Q-LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPDDYfkgvSQKAKEFVC 2969
Cdd:cd08218   159 RtCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRY----SYDLRSLVS 234
                         250
                  ....*....|..
gi 767934614 2970 FLLQEDPAKRPS 2981
Cdd:cd08218   235 QLFKRNPRDRPS 246
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
2743-2933 1.37e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 85.48  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATK---FVNKKLMKRDQVTH---ELGILQSLQHPLLVG----LLDTFETPTSyiLVLEM 2812
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGRELAVKqvqFDPESPETSKEVNAlecEIQLLKNLLHERIVQyygcLRDPQERTLS--IFMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYY--- 2889
Cdd:cd06652    88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSV---GNVKLGDFGASKRLQTICLsgt 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767934614 2890 -IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd06652   165 gMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
2743-2933 1.88e-17

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 85.08  E-value: 1.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFV-----NKKLMKR-DQVTHELGILQSLQHPLLV---GLLDTFETPTSYILVLEMA 2813
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVpfdpdSQETSKEvNALECEIQLLKNLRHDRIVqyyGCLRDPEEKKLSIFVEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DqGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYY---- 2889
Cdd:cd06653    90 G-GSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRIQTICMsgtg 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2890 IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd06653   166 IKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
2733-2992 2.15e-17

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 86.27  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqvTH-ELGILQSLQHPLLVGLLDTFETPTSY 2806
Cdd:cd07855     3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKkipnaFDVVTTAKR---TLrELKILRHFKHDNIIAIRDILRPKVPY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ------ILVLEMAdQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGD 2880
Cdd:cd07855    80 adfkdvYVVLDLM-ESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENC---ELKIGDFGM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2881 AVQLNT-----TYYIHQLLGNPEFAAPEIILGNP-VSLTSDTWSVGVL--------------TYV--------LLSGVSP 2932
Cdd:cd07855   156 ARGLCTspeehKYFMTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIfaemlgrrqlfpgkNYVhqlqliltVLGTPSQ 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 2933 FLDDSVEetCLNICRLDFSFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd07855   236 AVINAIG--ADRVRRYIQNLPnkqpvpwETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLA 300
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
2737-2968 2.24e-17

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 87.02  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKaDMLEKEQVGHiraERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLN----TTY 2888
Cdd:cd05628    83 LPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLD---SKGHVKLSDFGLCTGLKkahrTEF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YI---HQL-----------------------------LGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDD 2936
Cdd:cd05628   160 YRnlnHSLpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767934614 2937 SVEETCLNIC--RLDFSFPDDYfkGVSQKAKEFV 2968
Cdd:cd05628   240 TPQETYKKVMnwKETLIFPPEV--PISEKAKDLI 271
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2625-2704 2.36e-17

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 78.76  E-value: 2.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2625 PPEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPehNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVN 2704
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKN--GEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
2737-2989 3.18e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 89.41  E-value: 3.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK---RDQVTHELGILQSLQHPLLVGLLDTFETPTS---YILvL 2810
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKereKSQLVIEVNVMRELKHKNIVRYIDRFLNKANqklYIL-M 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGRL----LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNC-------RIAHLDLKPENILVDESL----------- 2868
Cdd:PTZ00266   94 EFCDAGDLsrniQKCYKMFGKIEEHAIVDITRQLLHALAYCHNLkdgpngeRVLHRDLKPQNIFLSTGIrhigkitaqan 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2869 ---AKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSL--TSDTWSVGVLTYVLLSGVSPFlddsveETCL 2943
Cdd:PTZ00266  174 nlnGRPIAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHETKSYddKSDMWALGCIIYELCSGKTPF------HKAN 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2944 NICRLDFSF---PDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQ 2989
Cdd:PTZ00266  248 NFSQLISELkrgPDLPIKGKSKELNILIKNLLNLSAKERPSALQCLGYQ 296
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
2742-2981 3.60e-17

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 84.12  E-value: 3.60e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2742 ELGRGRFSVVKKCD----QKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:smart00219    6 KLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEqqIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2816 GRLLDCVVRwgslTEGKIraHLGEVL-------EAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTY 2888
Cdd:smart00219   86 GDLLSYLRK----NRPKL--SLSDLLsfalqiaRGMEYLESKNFIHRDLAARNCLVGENL---VVKISDFGLSRDLYDDD 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2889 YIHQLLGN-PEF-AAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETCLNI---CRLDF--SFPDDYFKGV 2960
Cdd:smart00219  157 YYRKRGGKlPIRwMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLkngYRLPQppNCPPELYDLM 236
                           250       260
                    ....*....|....*....|.
gi 767934614   2961 SQkakefvCFllQEDPAKRPS 2981
Cdd:smart00219  237 LQ------CW--AEDPEDRPT 249
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
2742-2981 3.77e-17

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 84.14  E-value: 3.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2742 ELGRGRFSVVKKC----DQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:smart00221    6 KLGEGAFGEVYKGtlkgKGDGKEVEVAVKTLKEDASEqqIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2816 GRLLDCvvrwgsltegkIRAHLGEVL-------------EAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV 2882
Cdd:smart00221   86 GDLLDY-----------LRKNRPKELslsdllsfalqiaRGMEYLESKNFIHRDLAARNCLVGENL---VVKISDFGLSR 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2883 QLNTTYYIHQLLGN-PEF-AAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETCLNIC---RLDF--SFPD 2954
Cdd:smart00221  152 DLYDDDYYKVKGGKlPIRwMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKkgyRLPKppNCPP 231
                           250       260
                    ....*....|....*....|....*..
gi 767934614   2955 DYFKGVSQkakefvCFllQEDPAKRPS 2981
Cdd:smart00221  232 ELYKLMLQ------CW--AEDPEDRPT 250
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
2776-2991 3.91e-17

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 84.36  E-value: 3.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2776 DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHL 2855
Cdd:cd06629    53 DALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2856 DLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ---LLGNPEFAAPEII--LGNPVSLTSDTWSVGVLTYVLLSGV 2930
Cdd:cd06629   133 DLKADNILVD---LEGICKISDFGISKKSDDIYGNNGatsMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGR 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2931 SPFLDDSVEETCLNICRLDFS--FPDDYfkGVSQKAKEFV--CFLLqeDPAKRPSAALALQEQWL 2991
Cdd:cd06629   210 RPWSDDEAIAAMFKLGNKRSAppVPEDV--NLSPEALDFLnaCFAI--DPRDRPTAAELLSHPFL 270
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
2737-2933 6.79e-17

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 85.03  E-value: 6.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFS-VVKKCDQKGTKRAVATK-FVNKKLMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:PTZ00426   32 FNFIRTLGTGSFGrVILATYKNEDFPPVAIKrFEKSKIIKQKQVDHvfsERKILNYINHPFCVNLYGSFKDESYLYLVLE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYih 2891
Cdd:PTZ00426  112 FVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKD---GFIKMTDFGFAKVVDTRTY-- 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2892 QLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:PTZ00426  187 TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
2743-2991 7.21e-17

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 83.23  E-value: 7.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQS-LQHPLLVGLLDTFETPTSYILVLEMADQGRLlDC 2821
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSrLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSL-SA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVR--WGSLT--EGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDesLAKPTIKLADFGDAVQL-----NTTYYIhq 2892
Cdd:cd06624    95 LLRskWGPLKdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVN--TYSGVVKISDFGTSKRLaginpCTETFT-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 llGNPEFAAPEII------LGNPvsltSDTWSVGVLTYVLLSGVSPFLDDSVEETCLnicrldfsFPDDYFK-------G 2959
Cdd:cd06624   171 --GTLQYMAPEVIdkgqrgYGPP----ADIWSLGCTIIEMATGKPPFIELGEPQAAM--------FKVGMFKihpeipeS 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767934614 2960 VSQKAKEFV--CFllQEDPAKRPSAALALQEQWL 2991
Cdd:cd06624   237 LSEEAKSFIlrCF--EPDPDKRATASDLLQDPFL 268
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
2737-2937 8.38e-17

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 84.00  E-value: 8.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd06656    21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ-LL 2894
Cdd:cd06656   101 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFCAQITPEQSKRStMV 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDS 2937
Cdd:cd06656   177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 219
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
2737-2973 8.57e-17

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 83.52  E-value: 8.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQSLQHPLLVGLLDTFETPTSYILVLEM-- 2812
Cdd:cd07871     7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaiREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYld 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVRWGSLTEGKIraHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG--DAVQLNTTYYI 2890
Cdd:cd07871    87 SDLKQYLDNCGNLMSMHNVKI--FMFQLLRGLSYCHKRKILHRDLKPQNLLINE---KGELKLADFGlaRAKSVPTKTYS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLgNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQ----KAK 2965
Cdd:cd07871   162 NEVV-TLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSneefRSY 240

                  ....*...
gi 767934614 2966 EFVCFLLQ 2973
Cdd:cd07871   241 LFPQYRAQ 248
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
728-955 9.37e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 81.72  E-value: 9.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  728 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 806
Cdd:cd00176     1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  807 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 886
Cdd:cd00176    65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  887 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 955
Cdd:cd00176   144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
2737-2990 1.08e-16

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 83.30  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNkklMKRDQVT-----HELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIH---LDAEEGTpstaiREISLMKELKHENIVRLHDVIHTENKLMLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQG--RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDA----VQLN 2885
Cdd:cd07836    79 YMDKDlkKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINK---RGELKLADFGLArafgIPVN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 T------TYYihqllgnpeFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFK 2958
Cdd:cd07836   156 TfsnevvTLW---------YRAPDVLLGSRTYSTSiDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWP 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 2959 GVSQKAK-------------------------EFVCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd07836   227 GISQLPEykptfpryppqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
2740-2922 1.24e-16

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 82.85  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKravATKFVNKKLMK-------RDQVTHELGILQSLQ---HPLLVGLLDTFETPTSYILV 2809
Cdd:cd14052     5 VELIGSGEFSQVYKVSERVPT---GKVYAVKKLKPnyagakdRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRL---LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNT 2886
Cdd:cd14052    82 TELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITF---EGTLKIGDFGMATVWPL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767934614 2887 TYYIhQLLGNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd14052   159 IRGI-EREGDREYIAPEILSEHMYDKPADIFSLGLI 193
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
2743-2920 1.94e-16

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 83.45  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQ-------HPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd14212     7 LGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLNtkydpedKHHIVRLLDHFMHHGHLCIVFELLGV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 G--RLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeSLAKPTIKLADFGDAVQLN-TTY-YI- 2890
Cdd:cd14212    87 NlyELLK-QNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLV-NLDSPEIKLIDFGSACFENyTLYtYIq 164
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767934614 2891 --HqllgnpeFAAPEIILGNPVSLTSDTWSVG 2920
Cdd:cd14212   165 srF-------YRSPEVLLGLPYSTAIDMWSLG 189
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
2737-2991 1.98e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 82.70  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFV----NKKLMKRDQVtHELGILQSLQ---HPLLVGLLDTFET-----PT 2804
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVrvqtNEDGLPLSTV-REVALLKRLEafdHPNIVRLMDVCATsrtdrET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEMADQG--RLLDCVVRWGsLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAv 2882
Cdd:cd07863    81 KVTLVFEHVDQDlrTYLDKVPPPG-LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVT---SGGQVKLADFGLA- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 qlntTYYIHQLLGNPE-----FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL--------- 2948
Cdd:cd07863   156 ----RIYSCQMALTPVvvtlwYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLiglppeddw 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 2949 --DFSFP------------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07863   232 prDVTLPrgafsprgprpvQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
2742-2992 2.02e-16

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 82.78  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd06658    29 KIGEGSTGIVCIATEKHTGKQVAVKKMDlRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 cVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYYIHQ-LLGNPEF 2899
Cdd:cd06658   109 -IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLT---SDGRIKLSDFGFCAQVSKEVPKRKsLVGTPYW 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDdsvEETCLNICRLDFSFP---DDYFKgVSQKAKEFVCFLLQEDP 2976
Cdd:cd06658   185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFN---EPPLQAMRRIRDNLPprvKDSHK-VSSVLRGFLDLMLVREP 260
                         250
                  ....*....|....*.
gi 767934614 2977 AKRPSAALALQEQWLQ 2992
Cdd:cd06658   261 SQRATAQELLQHPFLK 276
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2633-2717 2.03e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 76.39  E-value: 2.03e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2633 SEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYSDlGEATLKIVGVTTEDDGIYTCIAVNDMGSASSS 2712
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 767934614   2713 ASLRV 2717
Cdd:smart00410   81 TTLTV 85
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
2737-2982 2.14e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 82.74  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd07873     4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTaiREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QG---RLLDCvvrWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG--DAVQLNTTYY 2889
Cdd:cd07873    84 KDlkqYLDDC---GNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINE---RGELKLADFGlaRAKSIPTKTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQLLgNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKaKEFV 2968
Cdd:cd07873   158 SNEVV-TLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSN-EEFK 235
                         250
                  ....*....|....
gi 767934614 2969 CFllqEDPAKRPSA 2982
Cdd:cd07873   236 SY---NYPKYRADA 246
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
2737-2991 2.35e-16

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 82.59  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKC-DQKgTKRAVATKFVNKKLMKRDQVTHELGILQSLQH------PLLVGLLDTFETPTSYILV 2809
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKClDHK-TGQLVAIKIIRNKKRFHQQALVEVKILKHLNDndpddkHNIVRYKDSFIFRGHLCIV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQG--RLLdCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLaKPTIKLADFGDAVQLN-T 2886
Cdd:cd14210    94 FELLSINlyELL-KSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPS-KSSIKVIDFGSSCFEGeK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TY-YIHQLLgnpeFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL-DDSVEETCLnICRLdFSFPDDYFKGVSQKA 2964
Cdd:cd14210   172 VYtYIQSRF----YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPgENEEEQLAC-IMEV-LGVPPKSLIDKASRR 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2965 KE------------------------------------FVCFL---LQEDPAKRPSAALALQEQWL 2991
Cdd:cd14210   246 KKffdsngkprpttnskgkkrrpgskslaqvlkcddpsFLDFLkkcLRWDPSERMTPEEALQHPWI 311
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
2739-2920 2.55e-16

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 82.88  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAE-LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHP-----LLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14211     2 EVLEfLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFEM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGrLLDCVV--RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDESLAKPTIKLADFGDAVQLN---- 2885
Cdd:cd14211    82 LEQN-LYDFLKqnKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENImLVDPVRQPYRVKVIDFGSASHVSkavc 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767934614 2886 TTYyihqlLGNPEFAAPEIILGNPVSLTSDTWSVG 2920
Cdd:cd14211   161 STY-----LQSRYYRAPEIILGLPFCEAIDMWSLG 190
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
2743-2988 2.91e-16

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 81.79  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKrdqvTHELGILQSLQHPLLVGLLDTF-ETPTSYILvLEMADQGRLLDC 2821
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFR----AEELMACAGLTSPRVVPLYGAVrEGPWVNIF-MDLKEGGSLGQL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTikLADFGDAVQLNTTYYIHQLLGNPEFA- 2900
Cdd:cd13991    89 IKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAF--LCDFGHAECLDPDGLGKSLFTGDYIPg 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2901 -----APEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD---FSFPDDYFKGVSQKAKEFvcflL 2972
Cdd:cd13991   167 tethmAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPpplREIPPSCAPLTAQAIQAG----L 242
                         250       260
                  ....*....|....*....|...
gi 767934614 2973 QEDPAKRPSA-------ALALQE 2988
Cdd:cd13991   243 RKEPVHRASAaelrrktNRALQE 265
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
2735-2945 3.41e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 83.52  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVL 2810
Cdd:cd05626     1 SMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKdVLNRNQVAHvkaERDILAEADNEWVVKLYYSFQDKDNLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL----NT 2886
Cdd:cd05626    81 DYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILID---LDGHIKLTDFGLCTGFrwthNS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TYY--------------------------------------------IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd05626   158 KYYqkgshirqdsmepsdlwddvsncrcgdrlktleqratkqhqrclAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVI 237
                         250       260
                  ....*....|....*....|...
gi 767934614 2923 TYVLLSGVSPFLDDSVEETCLNI 2945
Cdd:cd05626   238 LFEMLVGQPPFLAPTPTETQLKV 260
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
2743-2979 4.34e-16

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 81.33  E-value: 4.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQSLQH----PLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFILDLMN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTyYIHQLL 2894
Cdd:cd05606    82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEH---GHVRISDLGLACDFSKK-KPHASV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIIL-GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRL----DFSFPDDYfkgvSQKAKEFVC 2969
Cdd:cd05606   158 GTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDK-HEIDRMtltmNVELPDSF----SPELKSLLE 232
                         250
                  ....*....|
gi 767934614 2970 FLLQEDPAKR 2979
Cdd:cd05606   233 GLLQRDVSKR 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
2743-2968 5.01e-16

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 83.14  E-value: 5.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05623    80 IGRGAFGEVAVVKLKNADKVFAMKILNKwEMLKRAETAcfrEERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRW-GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL--NTTYYIHQLLG 2895
Cdd:cd05623   160 LTLLSKFeDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMD---MNGHIRLADFGSCLKLmeDGTVQSSVAVG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILG-----NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPDDyFKGVSQKAKEFV 2968
Cdd:cd05623   237 TPDYISPEILQAmedgkGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKERFQFPTQ-VTDVSENAKDLI 315
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
2743-2993 5.39e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 82.22  E-value: 5.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATK-----FVNKKlmkrD-QVTH-ELGILQSL-QHPLLVGLLDTF--ETPTSYILVLEM 2812
Cdd:cd07852    15 LGKGAYGIVWKAIDKKTGEVVALKkifdaFRNAT----DaQRTFrEIMFLQELnDHPNIIKLLNVIraENDKDIYLVFEY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGrlLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNT------ 2886
Cdd:cd07852    91 METD--LHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLN---SDCRVKLADFGLARSLSQleedde 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 ----TYYIhqllgnpefA-----APEIILGNPvSLTS--DTWSVGVLTYVLLSG-------------------------- 2929
Cdd:cd07852   166 npvlTDYV---------AtrwyrAPEILLGST-RYTKgvDMWSVGCILGEMLLGkplfpgtstlnqlekiievigrpsae 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2930 -----VSPFLDDSVEetclNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQA 2993
Cdd:cd07852   236 diesiQSPFAATMLE----SLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
2763-2937 6.07e-16

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 79.85  E-value: 6.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2763 VATKFVnkklmkRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLE 2842
Cdd:cd14059    19 VAVKKV------RDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIAS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2843 AVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd14059    93 GMNYLHLHKIIHRDLKSPNVLVTYN---DVLKISDFGTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVV 169
                         170
                  ....*....|....*.
gi 767934614 2923 TYVLLSGVSPFLD-DS 2937
Cdd:cd14059   170 LWELLTGEIPYKDvDS 185
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
2743-2997 7.53e-16

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 82.10  E-value: 7.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVV-KKCDQKGTKRAVATKFVN--KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPT----SYILVLEMADQ 2815
Cdd:cd07853     8 IGYGAFGVVwSVTDPRDGKRVALKKMPNvfQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHidpfEEIYVVTELMQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA--VQLNTTYYIHQL 2893
Cdd:cd07853    88 SDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNC---VLKICDFGLArvEEPDESKHMTQE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 LGNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSG--------------------VSPFLDD---SVEETCLNICRLD 2949
Cdd:cd07853   165 VVTQYYRAPEILMGSRHYTSAvDIWSVGCIFAELLGRrilfqaqspiqqldlitdllGTPSLEAmrsACEGARAHILRGP 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2950 FSFPD-----DYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGR 2997
Cdd:cd07853   245 HKPPSlpvlyTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEGRLR 297
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
2743-2983 8.11e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 80.00  E-value: 8.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKraVATKFVNKKLMKRdQVTHELGILQSLQHPLLVGLLDTFETPTsyILVLEMADQGRLlDCV 2822
Cdd:cd14068     2 LGDGGFGSVYRAVYRGED--VAVKIFNKHTSFR-LLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSL-DAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2823 VRW--GSLT---EGKIRAHlgeVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTI--KLADFGDAvQLNTTYYIHQLLG 2895
Cdd:cd14068    76 LQQdnASLTrtlQHRIALH---VADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIA-QYCCRMGIKTSEG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIILGNPV-SLTSDTWSVGVLTYVLLSGVSPFLDdsveetclnicrlDFSFPDDYFKGVSQK-----AKEFVC 2969
Cdd:cd14068   152 TPGFRAPEVARGNVIyNQQADVYSFGLLLYDILTCGERIVE-------------GLKFPNEFDELAIQGklpdpVKEYGC 218
                         250       260
                  ....*....|....*....|....*
gi 767934614 2970 F-----------LLQEDPAKRPSAA 2983
Cdd:cd14068   219 ApwpgvealikdCLKENPQCRPTSA 243
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
2735-2945 9.52e-16

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 82.02  E-value: 9.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVL 2810
Cdd:cd05625     1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQL----NT 2886
Cdd:cd05625    81 DYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD---GHIKLTDFGLCTGFrwthDS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2887 TYY--------------------------------------------IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd05625   158 KYYqsgdhlrqdsmdfsnewgdpencrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 237
                         250       260
                  ....*....|....*....|...
gi 767934614 2923 TYVLLSGVSPFLDDSVEETCLNI 2945
Cdd:cd05625   238 LFEMLVGQPPFLAQTPLETQMKV 260
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
2740-2988 1.22e-15

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 79.61  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKgTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05112     9 VQEIGSGQFGLVHLGYWL-NKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCV-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG-DAVQLNTTYYIHQLLGNP 2897
Cdd:cd05112    88 DYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGEN---QVVKVSDFGmTRFVLDDQYTSSTGTKFP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 -EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETclnICRLDFSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd05112   165 vKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEV---VEDINAGFRLYKPRLASTHVYEIMNHCWKER 241
                         250
                  ....*....|...
gi 767934614 2976 PAKRPSAALALQE 2988
Cdd:cd05112   242 PEDRPSFSLLLRQ 254
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
2742-2981 1.45e-15

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 79.46  E-value: 1.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2742 ELGRGRFSVVKKC----DQKGTKRAVATKFVNKKLMKRDQV--THELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:pfam07714    6 KLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGADEEEREdfLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2816 GRLLDCVVRWGSLTEGKIRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQLL 2894
Cdd:pfam07714   86 GDLLDFLRKHKRKLTLKDLLSMAlQIAKGMEYLESKNFVHRDLAARNCLVSE---NLVVKISDFGLSRDIYDDDYYRKRG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2895 G---NPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETCLNI---CRLDFSF--PDDYFKGVSQkak 2965
Cdd:pfam07714  163 GgklPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLedgYRLPQPEncPDELYDLMKQ--- 239
                          250
                   ....*....|....*.
gi 767934614  2966 efvCflLQEDPAKRPS 2981
Cdd:pfam07714  240 ---C--WAYDPEDRPT 250
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
15-145 1.50e-15

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 76.60  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   15 AYLSGGRDKRGGPILTFPAR-SNHDRIRQEDLRRLISYL--ACIPSEEVCKRGFTVIVDMRGSKW------DSIKPLLKI 85
Cdd:cd00170    11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   86 LQESFPCCIHVALIIKPDNF----WQ------KQRTnfgSSKFEFETNmvSLEGLTKVVDPSQLTPEFDG 145
Cdd:cd00170    91 LQDHYPERLKKIYIVNAPWIfsalWKivkpflSEKT---RKKIVFLGS--DLEELLEYIDPDQLPKELGG 155
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
2737-2983 1.61e-15

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 78.89  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKK--CDQKGTKRAVA---TKFVNKKLMKR--DQV-THElgilQSLQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd14050     3 FTILSKLGEGSFGEVFKvrSREDGKLYAVKrsrSRFRGEKDRKRklEEVeRHE----KLGEHPNCVRFIKAWEEKGILYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGrLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTY 2888
Cdd:cd14050    79 QTELCDTS-LQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKD---GVCKLGDFGLVVELDKED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YIHQLLGNPEFAAPEIILGNPvSLTSDTWSVGVltyvllsgvspflddsveeTCLNI-CRLDFS-------------FPD 2954
Cdd:cd14050   155 IHDAQEGDPRYMAPELLQGSF-TKAADIFSLGI-------------------TILELaCNLELPsggdgwhqlrqgyLPE 214
                         250       260
                  ....*....|....*....|....*....
gi 767934614 2955 DYFKGVSQKAKEFVCFLLQEDPAKRPSAA 2983
Cdd:cd14050   215 EFTAGLSPELRSIIKLMMDPDPERRPTAE 243
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
171-386 1.85e-15

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.87  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  171 MLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssesfpkknSGSGNADlqnl 248
Cdd:cd00176    12 LEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------EGHPDAE---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  249 lpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHF 328
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614  329 AMNCMNVYVNINRIMSVANRLVESGHYASQ-QIRQIASQLEQEWKAFAAALDERSTLLD 386
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
2743-2992 2.46e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 79.88  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFeTPTSY------ILVLE 2811
Cdd:cd07834     8 IGSGAYGVVCSAYDKRTGRKVAIKkisnvFDDLIDAKR--ILREIKILRHLKHENIIGLLDIL-RPPSPeefndvYIVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGrlLDCVVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYI 2890
Cdd:cd07834    85 LMETD--LHKVIKSPQpLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNC---DLKICDFGLARGVDPDEDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLlgnPEFA------APEIILG-----NPVsltsDTWSVG------VLTYVLLSGVS--------------PFLDDSVE 2939
Cdd:cd07834   160 GFL---TEYVvtrwyrAPELLLSskkytKAI----DIWSVGcifaelLTRKPLFPGRDyidqlnlivevlgtPSEEDLKF 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2940 ETCLN----ICRLDFSFPDDY---FKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd07834   233 ISSEKarnyLKSLPKKPKKPLsevFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLA 292
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
2737-2987 3.10e-15

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 78.85  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH--ELGILQSLQ-HPLLVGLLDT-FETPT-SYILVLE 2811
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNlrEIQALRRLSpHPNILRLIEVlFDRKTgRLALVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MAD-------QGRLldcvvrwGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslaKPTIKLADFGDAVQL 2884
Cdd:cd07831    81 LMDmnlyeliKGRK-------RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIK----DDILKLADFGSCRGI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NT----TYYIhqllGNPEFAAPEIILGNPV-SLTSDTWSVGVLTYVLLSGVSPF-----LDD-------------SVEET 2941
Cdd:cd07831   150 YSkppyTEYI----STRWYRAPECLLTDGYyGPKMDIWAVGCVFFEILSLFPLFpgtneLDQiakihdvlgtpdaEVLKK 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2942 CLNICRLDFSFPDDYFKG-------VSQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd07831   226 FRKSRHMNYNFPSKKGTGlrkllpnASAEGLDLLKKLLAYDPDERITAKQALR 278
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
2742-2904 3.78e-15

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 78.04  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVA-TKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETP--TSYILVLEMADQG 2816
Cdd:cd13983     8 VLGRGSFKTVYRAFDTEEGIEVAwNEIKLRKLPKaeRQRFKQEIEILKSLKHPNIIKFYDSWESKskKEVIFITELMTSG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDESLAKptIKLADFGDAVQLNTTYyIHQLL 2894
Cdd:cd13983    88 TLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGE--VKIGDLGLATLLRQSF-AKSVI 164
                         170
                  ....*....|
gi 767934614 2895 GNPEFAAPEI 2904
Cdd:cd13983   165 GTPEFMAPEM 174
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2742-2933 4.34e-15

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 77.77  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKK---CDQKGTKRAVATKFVNKKLMKRDQ--VTHELGILQSLQHPLLVGLLDTFETPtSYILVLEMADQG 2816
Cdd:cd05060     2 ELGHGNFGSVRKgvyLMKSGKEVEVAVKTLKQEHEKAGKkeFLREASVMAQLDHPCIVRLIGVCKGE-PLMLVMELAPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFG--DAVQLNTTYYIHQLL 2894
Cdd:cd05060    81 PLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLL---VNRHQAKISDFGmsRALGAGSDYYRATTA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2895 GN-P-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05060   158 GRwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY 199
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
2735-2991 4.79e-15

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 78.53  E-value: 4.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd06657    20 TYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQ- 2892
Cdd:cd06657   100 EGGALTD-IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQVSKEVPRRKs 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRLDFSFPDDYFKGVSQKAKEFVCFLL 2972
Cdd:cd06657   176 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIRDNLPPKLKNLHKVSPSLKGFLDRLL 254
                         250
                  ....*....|....*....
gi 767934614 2973 QEDPAKRPSAALALQEQWL 2991
Cdd:cd06657   255 VRDPAQRATAAELLKHPFL 273
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
2743-2979 4.88e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 79.34  E-value: 4.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHE---LGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTyYIHQLLG 2895
Cdd:cd05633    93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE---HGHVRISDLGLACDFSKK-KPHASVG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIIL-GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQE 2974
Cdd:cd05633   169 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDSFSPELKSLLEGLLQR 247

                  ....*
gi 767934614 2975 DPAKR 2979
Cdd:cd05633   248 DVSKR 252
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
2723-2922 5.65e-15

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 78.35  E-value: 5.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2723 DGIMVTWKDnfDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKF---VNKKLMKRdqvthELGILQSLQ-HPLLVGLLD 2798
Cdd:cd14132     8 ENLNVEWGS--QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVlkpVKKKKIKR-----EIKILQNLRgGPNIVKLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2799 TFETPTS--YILVLEMADQgrlLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLA 2876
Cdd:cd14132    81 VVKDPQSktPSLIFEYVNN---TDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHE--KRKLRLI 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2877 DFGDAvqlntTYYIHqllgNPE---------FAAPEIILGNPV---SLtsDTWSVGVL 2922
Cdd:cd14132   156 DWGLA-----EFYHP----GQEynvrvasryYKGPELLVDYQYydySL--DMWSLGCM 202
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
2759-2929 6.09e-15

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 81.81  E-value: 6.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2759 TKRAVATKFVN----KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIL-VLEMADQGRLLDCVVRWGSLTEGKI 2833
Cdd:TIGR03903    2 TGHEVAIKLLRtdapEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2834 RAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFG-----------DAVQLNTTyyiHQLLGNPEFAAP 2902
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGigtllpgvrdaDVATLTRT---TEVLGTPTYCAP 158
                          170       180
                   ....*....|....*....|....*..
gi 767934614  2903 EIILGNPVSLTSDTWSVGVLTYVLLSG 2929
Cdd:TIGR03903  159 EQLRGEPVTPNSDLYAWGLIFLECLTG 185
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
2737-2990 6.35e-15

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 78.51  E-value: 6.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKfvnKKLMKRDQ----VT--HELGILQSLQHPLLVGLLDTF--------ET 2802
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALK---KILMHNEKdgfpITalREIKILKKLKHPNVVPLIDMAverpdkskRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PTSYILVLEMADQ---GRLLDCVVRwgsLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG 2879
Cdd:cd07866    87 RGSVYMVTPYMDHdlsGLLENPSVK---LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDN---QGILKIADFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2880 davqLNTTYY--IHQLLGNPE--------------FAAPEIILGNPVSLTS-DTWSVG-VLTYV-----LLSGVS----- 2931
Cdd:cd07866   161 ----LARPYDgpPPNPKGGGGggtrkytnlvvtrwYRPPELLLGERRYTTAvDIWGIGcVFAEMftrrpILQGKSdidql 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2932 ---------PFLDDSVEETCLNICRLDFSFPD------DYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd07866   237 hlifklcgtPTEETWPGWRSLPGCEGVHSFTNyprtleERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
2743-2958 6.74e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 78.11  E-value: 6.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVA-TKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd07848     9 VGEGAYGVVLKCRHKETKEIVAiKKFKDSEENEevKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL------NTTYYIhql 2893
Cdd:cd07848    89 LLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLIS---HNDVLKLCDFGFARNLsegsnaNYTEYV--- 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2894 lGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFK 2958
Cdd:cd07848   163 -ATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMK 226
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
2743-2979 9.54e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 78.17  E-value: 9.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHE---LGILQSLQHPLLVGLLDTFETPTSYILVLEMADQ 2815
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNErimLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTyYIHQLLG 2895
Cdd:cd14223    88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDE---FGHVRISDLGLACDFSKK-KPHASVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 NPEFAAPEIIL-GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQE 2974
Cdd:cd14223   164 THGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTMAVELPDSFSPELRSLLEGLLQR 242

                  ....*
gi 767934614 2975 DPAKR 2979
Cdd:cd14223   243 DVNRR 247
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
2737-2991 9.65e-15

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 78.38  E-value: 9.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFETPTSYI-LVL 2810
Cdd:cd07856    12 YSDLQPVGMGAFGLVCSARDQLTGQNVAVKkimkpFSTPVLAKR--TYRELKLLKHLRHENIISLSDIFISPLEDIyFVT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMadQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA-VQ------ 2883
Cdd:cd07856    90 EL--LGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENC---DLKICDFGLArIQdpqmtg 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 -LNTTYYihqllgnpefAAPEIILG-NPVSLTSDTWSVGVLTYVLLSG---------------VSPFLDDSVEETCLNIC 2946
Cdd:cd07856   165 yVSTRYY----------RAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGkplfpgkdhvnqfsiITELLGTPPDDVINTIC 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 2947 R---LDF--SFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07856   235 SentLRFvqSLPkrervpfSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
2737-2933 9.70e-15

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 78.55  E-value: 9.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTS-------Y 2806
Cdd:cd07878    17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfqSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSienfnevY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ILVLEMadqGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLN- 2885
Cdd:cd07878    97 LVTNLM---GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDC---ELRILDFGLARQADd 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 -TTYYIhqllGNPEFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd07878   171 eMTGYV----ATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALF 216
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
2737-2961 1.19e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 77.72  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd07872     8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaiREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QG---RLLDCvvrwGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG--DAVQLNTTY 2888
Cdd:cd07872    88 KDlkqYMDDC----GNiMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINE---RGELKLADFGlaRAKSVPTKT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2889 YIHQLLgNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVS 2961
Cdd:cd07872   161 YSNEVV-TLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGIS 233
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
2740-2992 1.26e-14

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 77.34  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSL-QHPLLVGLLDTFETPTSYI-----LVLEMA 2813
Cdd:cd06639    27 IETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQYVggqlwLVLELC 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCV---VRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYY 2889
Cdd:cd06639   107 NGGSVTELVkglLKCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT---TEGGVKLVDFGVSAQLTSARL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQL-LGNPEFAAPEII-----LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICR---LDFSFPDDYFKGV 2960
Cdd:cd06639   184 RRNTsVGTPFWMAPEVIaceqqYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRnppPTLLNPEKWCRGF 263
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767934614 2961 SQkakeFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06639   264 SH----FISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
2729-3038 1.29e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 77.77  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQSLQHPllvgllDTFETPT 2804
Cdd:cd06633    15 YKDDPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKkmsYSGKQTNEKWQdIIKEVKFLQQLKHP------NTIEYKG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYI------LVLE--MADQGRLLDcvVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLA 2876
Cdd:cd06633    89 CYLkdhtawLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2877 DFGDAVQLNTTyyiHQLLGNPEFAAPEIILG---NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDfsFP 2953
Cdd:cd06633   164 DFGSASIASPA---NSFVGTPYWMAPEVILAmdeGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQND--SP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2954 DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQagNGRSTGVldtsrLTSFIERRKHQndvrpIRSIKNfLQSR 3033
Cdd:cd06633   239 TLQSNEWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVR--RERPPRV-----LIDLIQRTKDA-----VRELDN-LQYR 305

                  ....*
gi 767934614 3034 LLPRV 3038
Cdd:cd06633   306 KMKKI 310
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
2737-2922 1.30e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 77.38  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKC-DQKGTKRAVATKFVNKKLMKRD---QVTHELGIL---QSLQHPLLVGLLDT-----FETPT 2804
Cdd:cd07862     3 YECVAEIGEGAYGKVFKArDLKNGGRFVALKRVRVQTGEEGmplSTIREVAVLrhlETFEHPNVVRLFDVctvsrTDRET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEMADQG--RLLDCVVRWGSLTEgKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDA- 2881
Cdd:cd07862    83 KLTLVFEHVDQDltTYLDKVPEPGVPTE-TIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSS---GQIKLADFGLAr 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2882 ---VQLNTTYYIHQLLgnpeFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd07862   159 iysFQMALTSVVVTLW----YRAPEVLLQSSYATPVDLWSVGCI 198
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
2764-2983 1.80e-14

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 76.67  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2764 ATKFVNKKLMK------RDQVTHELGILQSLQHPLLVGLlDTFETPTSYILVLEMADQGRLLdcvvrwGSLTEGKIRAHL 2837
Cdd:cd14001    32 AVKKINSKCDKgqrslyQERLKEEAKILKSLNHPNIVGF-RAFTKSEDGSLCLAMEYGGKSL------NDLIEERYEAGL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2838 G------------EVLEAVRYLHN-CRIAHLDLKPENILVDESLAkpTIKLADFGDAVQLNTTYyihQLLGNPEF----- 2899
Cdd:cd14001   105 GpfpaatilkvalSIARALEYLHNeKKILHGDIKSGNVLIKGDFE--SVKLCDFGVSLPLTENL---EVDSDPKAqyvgt 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 ---AAPEIIL-GNPVSLTSDTWSVGVLTYVLLSGVSPFL------DDSVEETCLnicRLDF-------------SFPDDY 2956
Cdd:cd14001   180 epwKAKEALEeGGVITDKADIFAYGLVLWEMMTLSVPHLnlldieDDDEDESFD---EDEEdeeayygtlgtrpALNLGE 256
                         250       260
                  ....*....|....*....|....*..
gi 767934614 2957 FKGVSQKAKEFVCFLLQEDPAKRPSAA 2983
Cdd:cd14001   257 LDDSYQKVIELFYACTQEDPKDRPSAA 283
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
2743-2992 1.84e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 76.27  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVN------KKLMKRDQVTHELGILQSLQHPLLV---GLLDTFETPTSYILvLEMA 2813
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQfdpespETSKEVSALECEIQLLKNLQHERIVqyyGCLRDRAEKTLTIF-MEYM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYY---- 2889
Cdd:cd06651    94 PGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRLQTICMsgtg 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPddYFKGVSQKAKEFVC 2969
Cdd:cd06651   171 IRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQ--LPSHISEHARDFLG 248
                         250       260
                  ....*....|....*....|...
gi 767934614 2970 FLLQEdPAKRPSAALALQEQWLQ 2992
Cdd:cd06651   249 CIFVE-ARHRPSAEELLRHPFAQ 270
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
2743-2920 1.92e-14

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 77.36  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSL-QHP-----LLVGLLDTFETPTSYILVLEMADQG 2816
Cdd:cd14226    21 IGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDtenkyYIVRLKRHFMFRNHLCLVFELLSYN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 rLLDCV--VRWGSLTEGKIRAHLGEVLEAVRYLH--NCRIAHLDLKPENILVDESlAKPTIKLADFGDAVQLNTTyyIHQ 2892
Cdd:cd14226   101 -LYDLLrnTNFRGVSLNLTRKFAQQLCTALLFLStpELSIIHCDLKPENILLCNP-KRSAIKIIDFGSSCQLGQR--IYQ 176
                         170       180
                  ....*....|....*....|....*...
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVG 2920
Cdd:cd14226   177 YIQSRFYRSPEVLLGLPYDLAIDMWSLG 204
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2737-2989 2.09e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 76.39  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRD--QVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14049     8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILiKKVTKRDcmKVLREVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGR-LLDCVV---RWGSLTEGKIRAH-----------LGEVLEAVRYLHNCRIAHLDLKPENILVdeSLAKPTIKLADF 2878
Cdd:cd14049    88 LCELsLWDWIVernKRPCEEEFKSAPYtpvdvdvttkiLQQLLEGVTYIHSMGIVHRDLKPRNIFL--HGSDIHVRIGDF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2879 G----DAVQLNTTYYIHQLL---------GNPEFAAPEIILGNPVSLTSDTWSVGVltyVLLSGVSPFLDDSVEETCLNI 2945
Cdd:cd14049   166 GlacpDILQDGNDSTTMSRLnglthtsgvGTCLYAAPEQLEGSHYDFKSDMYSIGV---ILLELFQPFGTEMERAEVLTQ 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2946 CRlDFSFPDDYFKGVSQKAKeFVCFLLQEDPAKRPSAALALQEQ 2989
Cdd:cd14049   243 LR-NGQIPKSLCKRWPVQAK-YIKLLTSTEPSERPSASQLLESE 284
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
2740-2991 2.54e-14

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 76.19  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSL-QHPLLVGLLDTFETPTSYI------LVLEM 2812
Cdd:cd06608    11 VEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKKDPPGgddqlwLVMEY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCV----VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTY 2888
Cdd:cd06608    91 CGGGSVTDLVkglrKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE---AEVKLVDFGVSAQLDSTL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 YI-HQLLGNPEFAAPEII-----LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD---FSFPDDYfkg 2959
Cdd:cd06608   168 GRrNTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPpptLKSPEKW--- 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767934614 2960 vSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd06608   245 -SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
2740-2980 2.58e-14

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 75.56  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGtKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05059     9 LKELGSGQFGVVHLGKWRG-KIDVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCV-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA-VQLNTTYYIHQLLGNP 2897
Cdd:cd05059    88 NYLrERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQN---VVKVSDFGLArYVLDDEYTSSVGTKFP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 -EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETCLNICRldfSFPDDYFKGVSQKAKEFVCFLLQED 2975
Cdd:cd05059   165 vKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQ---GYRLYRPHLAPTEVYTIMYSCWHEK 241

                  ....*
gi 767934614 2976 PAKRP 2980
Cdd:cd05059   242 PEERP 246
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
1413-1534 2.60e-14

Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; Obscurin-myosin light chain kinase/Obscurin-MLCK) is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270059  Cd Length: 125  Bit Score: 71.81  E-value: 2.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1413 MLEGFDENIESQGELILQESFQVWDPKTLIR---KGRERHLFLFEMSLVFSKEVKDSSGRSK-YLYKSKLFTSELGVTEH 1488
Cdd:cd13239     1 LIENYPAPLQALGEPIRQGHFTVWEEAPEVKtssRGHHRHVFLFKNCVVICKPKRDSRTDTVtYVFKNKMKLSDIDVKDT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 1489 VEGDPCKFALWVGRTpTSDNKIVLKASSIENKQDWIKHIREvIQER 1534
Cdd:cd13239    81 VEGDDRSFGLWHEHR-GSVRKYTLQARSAIIKSSWLKDLRD-LQQR 124
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
2730-2992 2.62e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 77.11  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2730 KDNFDSFYSEV-AELGRGRFSVVKKCDQKGTKRAVATK---------FVNKKLMKRDQV------THELGILQSLQHPLL 2793
Cdd:PTZ00024    3 SFSISERYIQKgAHLGEGTYGKVEKAYDTLTGKIVAIKkvkiieisnDVTKDRQLVGMCgihfttLRELKIMNEIKHENI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2794 VGLLDTFeTPTSYI-LVLE-MA-DQGRLLDCVVRwgsLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaK 2870
Cdd:PTZ00024   83 MGLVDVY-VEGDFInLVMDiMAsDLKKVVDRKIR---LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINS---K 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2871 PTIKLADFG-------------------DAVQLNTTYYIHQLLgnpeFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGV 2930
Cdd:PTZ00024  156 GICKIADFGlarrygyppysdtlskdetMQRREEMTSKVVTLW----YRAPELLMGaEKYHFAVDMWSVGCIFAELLTGK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2931 --------------------SPFLDDSVEETCLNI-CRLDFSFP---DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALAL 2986
Cdd:PTZ00024  232 plfpgeneidqlgrifellgTPNEDNWPQAKKLPLyTEFTPRKPkdlKTIFPNASDDAIDLLQSLLKLNPLERISAKEAL 311

                  ....*.
gi 767934614 2987 QEQWLQ 2992
Cdd:PTZ00024  312 KHEYFK 317
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2737-2992 2.66e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 76.71  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNK--KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd06615     3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLeiKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTE---GKIRAhlgEVLEAVRYLH-NCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL-----N 2885
Cdd:cd06615    83 GGSLDQVLKKAGRIPEnilGKISI---AVLRGLTYLReKHKIMHRDVKPSNILVN---SRGEIKLCDFGVSGQLidsmaN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 TtyyihqLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSP-----------FLDDSVE--ETCLNICRLDFSF 2952
Cdd:cd06615   157 S------FVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeleaMFGRPVSegEAKESHRPVSGHP 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2953 PD-----------DYF----------KGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06615   231 PDsprpmaifellDYIvnepppklpsGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
2737-2973 2.87e-14

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 77.00  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRF-SVVKKCDQKGTKRAVATKFVN--KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSY------I 2807
Cdd:cd07877    19 YQNLSPVGSGAYgSVCAAFDTKTGLRVAVKKLSRpfQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLeefndvY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMadQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAvqLNTT 2887
Cdd:cd07877    99 LVTHL--MGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDC---ELKILDFGLA--RHTD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIHQLLGNPEFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVSPFL-DDSVEETCLnICRLDFSFPDDYFKGV-SQKA 2964
Cdd:cd07877   172 DEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPgTDHIDQLKL-ILRLVGTPGAELLKKIsSESA 250

                  ....*....
gi 767934614 2965 KEFVCFLLQ 2973
Cdd:cd07877   251 RNYIQSLTQ 259
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2737-2980 3.11e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 75.62  E-value: 3.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRF-SVVKKCDQKGTKRAVATKFVN-------KKLMKRDQ----VTHELGIL-QSLQHPLLVGLLDTF-ET 2802
Cdd:cd08528     2 YAVLELLGSGAFgCVYKVRKKSNGQTLLALKEINmtnpafgRTEQERDKsvgdIISEVNIIkEQLRHPNIVRYYKTFlEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PTSYIlVLEMADQGRLLDCVV----RWGSLTEGKIRAHLGEVLEAVRYLHNCR-IAHLDLKPENILVDESlAKPTIklAD 2877
Cdd:cd08528    82 DRLYI-VMELIEGAPLGEHFSslkeKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGED-DKVTI--TD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2878 FGDAVQ-LNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPDD 2955
Cdd:cd08528   158 FGLAKQkGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEpLPEG 237
                         250       260
                  ....*....|....*....|....*
gi 767934614 2956 YFkgvSQKAKEFVCFLLQEDPAKRP 2980
Cdd:cd08528   238 MY---SDDITFVIRSCLTPDPEARP 259
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2640-2717 3.58e-14

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 70.12  E-value: 3.58e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2640 GETVVLRCRVCGRPKASITWKgpehntlNNDGHYSIS-YSDLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRV 2717
Cdd:cd05725    12 DDSAEFQCEVGGDPVPTVRWR-------KEDGELPKGrYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
2743-2935 3.80e-14

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 75.18  E-value: 3.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSspnCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAH-LGEVLEAVRYLHNCR--IAHLDLKPENILVDESLakpTIKLADFGDAV------QLNTTYYI 2890
Cdd:cd13978    81 SLLEREIQDVPWSLRFRiIHEIALGMNFLHNMDppLLHHDLKPENILLDNHF---HVKISDFGLSKlgmksiSANRRRGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2891 HQLLGNPEFAAPEIIlgNPV----SLTSDTWSVGVLTYVLLSGVSPFLD 2935
Cdd:cd13978   158 ENLGGTPIYMAPEAF--DDFnkkpTSKSDVYSFAIVIWAVLTRKEPFEN 204
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2733-2991 3.98e-14

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 75.82  E-value: 3.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYS-----EVAE-LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQ-HPLLVGLLDTF----- 2800
Cdd:cd06638    10 FDSFPDpsdtwEIIEtIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVKFYGMYykkdv 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2801 ETPTSYILVLEMADQGRLLDCVV----RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLA 2876
Cdd:cd06638    90 KNGDQLWLVLELCNGGSVTDLVKgflkRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLT---TEGGVKLV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2877 DFGDAVQL-NTTYYIHQLLGNPEFAAPEII-----LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDF 2950
Cdd:cd06638   167 DFGVSAQLtSTRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPLAD-------LHPMRALF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2951 SFPDDYFKGVSQK---AKEFVCFL---LQEDPAKRPSAALALQEQWL 2991
Cdd:cd06638   240 KIPRNPPPTLHQPelwSNEFNDFIrkcLTKDYEKRPTVSDLLQHVFI 286
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
2094-2214 5.08e-14

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 71.07  E-value: 5.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2094 GFDGKIVAQGKLLLQDTFLV-TDQDAG-----LLPRCRERRIFLFEQIVIFSepldKKKG--FSMPGFLFKNSIKVSCLC 2165
Cdd:cd01227     4 GYDGNLGDLGKLLMQGSFNVwTEHKKGhtkklARFKPMQRHIFLYEKAVLFC----KKRGenGEAPSYSYKNSLNTTAVG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2166 LEENVENDPCKFALTsrTGDVVETFILHSSSPSVRQTWIHEINQILENQ 2214
Cdd:cd01227    80 LTENVKGDTKKFEIW--LNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
SPEC smart00150
Spectrin repeats;
1084-1184 5.57e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.05  E-value: 5.57e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1084 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1163
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 767934614   1164 AVDKRYRDFSLRMEKYRTSLE 1184
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2734-2932 5.65e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 75.86  E-value: 5.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd06649     4 DDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPaiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLlDCVVRWGSLTEGKIRAHLG-EVLEAVRYL-HNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLNTTYy 2889
Cdd:cd06649    84 HMDGGSL-DQVLKEAKRIPEEILGKVSiAVLRGLAYLrEKHQIMHRDVKPSNILVN---SRGEIKLCDFGVSGQLIDSM- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767934614 2890 IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSP 2932
Cdd:cd06649   159 ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
SPEC smart00150
Spectrin repeats;
512-612 8.07e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 8.07e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    512 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 591
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 767934614    592 QLEDRIQDFVRRVEQRKILLD 612
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
2776-2988 9.45e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 73.87  E-value: 9.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2776 DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDcvvrwgSLTEGKIRAHL-----GEVLEAVRYLHN- 2849
Cdd:cd14148    38 ENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNR------ALAGKKVPPHVlvnwaVQIARGMNYLHNe 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2850 --CRIAHLDLKPENILV-----DESLAKPTIKLADFGDAVQLNTTYYIhQLLGNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd14148   112 aiVPIIHRDLKSSNILIlepieNDDLSGKTLKITDFGLAREWHKTTKM-SAAGTYAWMAPEVIRLSLFSKSSDVWSFGVL 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2923 TYVLLSGVSPF--LDDSVEETCLNICRLDFSFPddyfkgvSQKAKEFVCfLLQE----DPAKRPSAALALQE 2988
Cdd:cd14148   191 LWELLTGEVPYreIDALAVAYGVAMNKLTLPIP-------STCPEPFAR-LLEEcwdpDPHGRPDFGSILKR 254
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
2745-2988 9.59e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 74.30  E-value: 9.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2745 RGRFSVVKKCDQKGTKRAVATKfvnkklmkrDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVV- 2823
Cdd:cd14146    16 KGQEVAVKAARQDPDEDIKATA---------ESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLNRALAa 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2824 ---RWGSLTEGKIRAHL-----GEVLEAVRYLHN---CRIAHLDLKPENILVDESL-----AKPTIKLADFGDAVQLNTT 2887
Cdd:cd14146    87 anaAPGPRRARRIPPHIlvnwaVQIARGMLYLHEeavVPILHRDLKSSNILLLEKIehddiCNKTLKITDFGLAREWHRT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2888 YYIhQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF--LDDSVEETCLNICRLDFSFPDDYFKGVSQKAK 2965
Cdd:cd14146   167 TKM-SAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYrgIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMK 245
                         250       260
                  ....*....|....*....|...
gi 767934614 2966 EfvCFllQEDPAKRPSAALALQE 2988
Cdd:cd14146   246 E--CW--EQDPHIRPSFALILEQ 264
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
2743-2968 1.07e-13

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 74.71  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ--------VTHELGILQSLQHPLLVGLLDTFETPT-SYILVLEMA 2813
Cdd:cd14041    14 LGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDTdSFCTVLEYC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 dQGRLLDCVVRWGSL-TEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYY- 2889
Cdd:cd14041    94 -EGNDLDFYLKQHKLmSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYn 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2890 -------IHQLLGNPEFAAPE-IILGN---PVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLN----ICRLDFSFPD 2954
Cdd:cd14041   173 svdgmelTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQentiLKATEVQFPP 252
                         250
                  ....*....|....
gi 767934614 2955 DyfKGVSQKAKEFV 2968
Cdd:cd14041   253 K--PVVTPEAKAFI 264
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
2736-2937 1.15e-13

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 73.79  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKCdqKGTKRAV-ATKFVNkkLMKRDQVT-----HELGILQSLQH-PLLVGLLD---TFETPTS 2805
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKV--LNPKKKIyALKRVD--LEGADEQTlqsykNEIELLKKLKGsDRIIQLYDyevTDEDDYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2806 YIlVLEM--ADQGRLLDcvVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPEN-ILVDESLakptiKLADFG-- 2879
Cdd:cd14131    78 YM-VMECgeIDLATILK--KKRPKpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLVKGRL-----KLIDFGia 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2880 DAVQLNTTyYIH--QLLGNPEFAAPEIILGN----------PVSLTSDTWSVGVLTYVLLSGVSPFLDDS 2937
Cdd:cd14131   150 KAIQNDTT-SIVrdSQVGTLNYMSPEAIKDTsasgegkpksKIGRPSDVWSLGCILYQMVYGKTPFQHIT 218
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
2742-2934 1.80e-13

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 73.07  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKK--CDQKGTKRAVATKFV----NKKLMKrDQVTHELGILQSLQHPLLVGLLDTFETpTSYILVLEMADQ 2815
Cdd:cd05116     2 ELGSGNFGTVKKgyYQMKKVVKTVAVKILkneaNDPALK-DELLREANVMQQLDNPYIVRMIGICEA-ESWMLVMEMAEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2816 GRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFG--DAVQLNTTYYIHQL 2893
Cdd:cd05116    80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLL---VTQHYAKISDFGlsKALRADENYYKAQT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2894 LGN-P-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFL 2934
Cdd:cd05116   157 HGKwPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYK 200
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
2742-2947 2.53e-13

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 72.85  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRaVATKFV-NKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd05148    13 KLGSGYFGEVWEGLWKNRVR-VAIKILkSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLLA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVvrwgSLTEGKIR--AHL----GEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLL 2894
Cdd:cd05148    92 FL----RSPEGQVLpvASLidmaCQVAEGMAYLEEQNSIHRDLAARNILVGEDL---VCKVADFGLARLIKEDVYLSSDK 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2895 GNP-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETCLNICR 2947
Cdd:cd05148   165 KIPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITA 219
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
2737-2961 2.90e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 73.31  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:PLN00009    4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKI--RLEQEDEgvpstAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADqgrlLDCVVRWGSLTEGK-----IRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFG--DAVQL 2884
Cdd:PLN00009   82 YLD----LDLKKHMDSSPDFAknprlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRR--TNALKLADFGlaRAFGI 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2885 NTTYYIHQLLgNPEFAAPEIILGN-PVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVS 2961
Cdd:PLN00009  156 PVRTFTHEVV-TLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGVT 232
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1080-1187 3.64e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 71.32  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1080 QYVVFERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIK 1159
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100
                  ....*....|....*....|....*...
gi 767934614 1160 KCVTAVDKRYRDFSLRMEKYRTSLEKAL 1187
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEAL 106
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
2837-2985 3.84e-13

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 73.30  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2837 LGEVLEAVRYLHNCRIAHLDLKPENILVD-ESLAKPTIKLADFG-----DAVQLNTTYYIHQ--LLGNPEFAAPEIILGN 2908
Cdd:cd14018   144 ILQLLEGVDHLVRHGIAHRDLKSDNILLElDFDGCPWLVIADFGccladDSIGLQLPFSSWYvdRGGNACLMAPEVSTAV 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2909 PVSLT------SDTWSVGVLTYVLLSGVSPF---LDDSVEETCLNICRLDfSFPDdyfkGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:cd14018   224 PGPGVvinyskADAWAVGAIAYEIFGLSNPFyglGDTMLESRSYQESQLP-ALPS----AVPPDVRQVVKDLLQRDPNKR 298

                  ....*.
gi 767934614 2980 PSAALA 2985
Cdd:cd14018   299 VSARVA 304
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
2640-2717 4.14e-13

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 67.10  E-value: 4.14e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2640 GETVVLRCRVCGRPKASITW-KGPEhnTLNNDGHYSIsysdLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRV 2717
Cdd:cd04969    17 GGDVIIECKPKASPKPTISWsKGTE--LLTNSSRICI----LPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
2739-2929 4.28e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 73.59  E-value: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAE-LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPL-----LVGLLDTFETPTSYILVLEM 2812
Cdd:cd14227    18 EVLEfLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESaddynFVRAYECFQHKNHTCLVFEM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGrLLDCVV--RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDESLAKPTIKLADFGDAVQLN---- 2885
Cdd:cd14227    98 LEQN-LYDFLKqnKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENImLVDPSRQPYRVKVIDFGSASHVSkavc 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2886 TTYyihqlLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSG 2929
Cdd:cd14227   177 STY-----LQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 215
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
2737-2987 4.38e-13

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 73.22  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFETPTSY----- 2806
Cdd:cd07850     2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKklsrpFQNVTHAKR--AYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 -ILVLEMADQGRlldCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQLN 2885
Cdd:cd07850    80 vYLVMELMDANL---CQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVK---SDCTLKILDFGLARTAG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 TTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVG------VLTYVLLSGV----------------SPFLDDSVEETCL 2943
Cdd:cd07850   154 TSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGcimgemIRGTVLFPGTdhidqwnkiieqlgtpSDEFMSRLQPTVR 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2944 NICR-------LDFS--FPDDYF--------KGVSQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd07850   234 NYVEnrpkyagYSFEelFPDVLFppdseehnKLKASQARDLLSKMLVIDPEKRISVDDALQ 294
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
2745-2991 5.84e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 71.58  E-value: 5.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2745 RGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVThelgILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVR 2824
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVE----IQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKLES 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2825 WGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkptiKLADFGDAVQL-NTTYYIHQLLGNPEFAAPE 2903
Cdd:cd13995    90 CGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKA----VLVDFGLSVQMtEDVYVPKDLRGTEIYMSPE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2904 IILGNPVSLTSDTWSVGVLTYVLLSGVSPFLD---DSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRP 2980
Cdd:cd13995   166 VILCRGHNTKADIYSLGATIIHMQTGSPPWVRrypRSAYPSYLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRS 245
                         250
                  ....*....|.
gi 767934614 2981 SAALALQEQWL 2991
Cdd:cd13995   246 SAAELLKHEAL 256
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
2743-2985 5.92e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 73.92  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKfvnKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTsyilvLEMADQGRLLDCV 2822
Cdd:PTZ00036   74 IGNGSFGVVYEAICIDTSEKVAIK---KVLQDPQYKNRELLIMKNLNHINIIFLKDYYYTEC-----FKKNEKNIFLNVV 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2823 VRWGSLTEGKIRAHLG----------------EVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFGDAVQL-- 2884
Cdd:PTZ00036  146 MEFIPQTVHKYMKHYArnnhalplflvklysyQLCRALAYIHSKFICHRDLKPQNLLIDPN--THTLKLCDFGSAKNLla 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 --NTTYYIHQLLgnpeFAAPEIILGNPVSLTS-DTWSVG------VLTYVLLSGVSP---------FLDDSVEETC--LN 2944
Cdd:PTZ00036  224 gqRSVSYICSRF----YRAPELMLGATNYTTHiDLWSLGciiaemILGYPIFSGQSSvdqlvriiqVLGTPTEDQLkeMN 299
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2945 ICRLDFSFPD--------DYFKGVSQKAKEFVCFLLQEDPAKR--PSAALA 2985
Cdd:PTZ00036  300 PNYADIKFPDvkpkdlkkVFPKGTPDDAINFISQFLKYEPLKRlnPIEALA 350
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2743-3014 7.12e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 71.83  E-value: 7.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLlD 2820
Cdd:cd06619     9 LGHGNGGTVYKAYHLLTRRILAVKVIplDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL-D 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGSLTEGKIRAhlgEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDAVQL----NTTYyihqlLGN 2896
Cdd:cd06619    88 VYRKIPEHVLGRIAV---AVVKGLTYLWSLKILHRDVKPSNMLVN---TRGQVKLCDFGVSTQLvnsiAKTY-----VGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLD-----DSVEETCLNICRLDFS---FPDDYFkgvSQKAKEFV 2968
Cdd:cd06619   157 NAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQiqknqGSLMPLQLLQCIVDEDppvLPVGQF---SEKFVHFI 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 2969 CFLLQEDPAKRPSAALALQEQWLQAGNGRSTGVLDTSRLTSFIERR 3014
Cdd:cd06619   234 TQCMRKQPKERPAPENLMDHPFIVQYNDGNAEVVSMWVCRALEERR 279
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2741-2988 7.52e-13

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 71.23  E-value: 7.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2741 AELGRGRFSVVKKCDQKGTKraVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd05039    12 ELIGKGEFGDVMLGDYRGQK--VAVKCLKDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGsltegkiRAHLG---------EVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd05039    90 YLRSRG-------RAVITrkdqlgfalDVCEGMEYLESKKFVHRDLAARNVLVSEDN---VAKVSDFGLAKEASSNQDGG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLlgnP-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF----LDDSVE-----------ETClnicrldfsfPD 2954
Cdd:cd05039   160 KL---PiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYpripLKDVVPhvekgyrmeapEGC----------PP 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767934614 2955 DYFKGVSQkakefvCFllQEDPAKRPSAALALQE 2988
Cdd:cd05039   227 EVYKVMKN------CW--ELDPAKRPTFKQLREK 252
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
2737-2992 7.74e-13

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 71.33  E-value: 7.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKkmsYSGKQSTEKWQdIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 AdQGRLLDCV-VRWGSLTEGKIRAHLGEVLEAVRYLHN-CRIaHLDLKPENILVDESlakPTIKLADFGDAVQLNTTyyi 2890
Cdd:cd06607    83 C-LGSASDIVeVHKKPLQEVEIAAICHGALQGLAYLHShNRI-HRDVKAGNILLTEP---GTVKLADFGSASLVCPA--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLGNPEFAAPEIILG---NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDfsFPDDYFKGVSQKAKEF 2967
Cdd:cd06607   155 NSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQND--SPTLSSGEWSDDFRNF 232
                         250       260
                  ....*....|....*....|....*
gi 767934614 2968 VCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06607   233 VDSCLQKIPQDRPSAEDLLKHPFVT 257
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2626-2717 9.22e-13

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 66.29  E-value: 9.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITW--KGPEHNTLNNDGHYSIsYSDLGEATLKIVGVTTEDDGIYTCIAV 2703
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWykNGVPIDPSSIPGKYKI-ESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                          90
                  ....*....|....
gi 767934614 2704 NDMGSASSSASLRV 2717
Cdd:cd20951    80 NIHGEASSSASVVV 93
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
2737-2933 9.31e-13

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 72.29  E-value: 9.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFeTP-------T 2804
Cdd:cd07880    17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKklyrpFQSELFAKR--AYRELRLLKHMKHENVIGLLDVF-TPdlsldrfH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEM--ADQGRLLdcvvRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV 2882
Cdd:cd07880    94 DFYLVMPFmgTDLGKLM----KHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDC---ELKILDFGLAR 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2883 QLN---TTYYIHQLlgnpeFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd07880   167 QTDsemTGYVVTRW-----YRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLF 216
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
2739-2929 1.01e-12

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 72.43  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAE-LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPL-----LVGLLDTFETPTSYILVLEM 2812
Cdd:cd14228    18 EVLEfLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENadeynFVRSYECFQHKNHTCLVFEM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGrLLDCVV--RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKP-TIKLADFGDAVQLN---- 2885
Cdd:cd14228    98 LEQN-LYDFLKqnKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHVSkavc 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2886 TTYyihqlLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSG 2929
Cdd:cd14228   177 STY-----LQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 215
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2740-2992 1.02e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 71.64  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFV----NKKLMKRdqVTHELGI-LQSLQHPLLVGLLDTFETPTSYILVLE-MA 2813
Cdd:cd06618    20 LGEIGSGTCGQVYKMRHKKTGHVMAVKQMrrsgNKEENKR--ILMDLDVvLKSHDCPYIVKCYGYFITDSDVFICMElMS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DqgrlldCVVRWGSLTEGKIRAH-LGE----VLEAVRYL---HNcrIAHLDLKPENILVDESlakPTIKLADFGDAVQLN 2885
Cdd:cd06618    98 T------CLDKLLKRIQGPIPEDiLGKmtvsIVKALHYLkekHG--VIHRDVKPSNILLDES---GNVKLCDFGISGRLV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2886 TTYYIHQLLGNPEFAAPEIILGNPVS---LTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICrLDFSFPD-DYFKGVS 2961
Cdd:cd06618   167 DSKAKTRSAGCAAYMAPERIDPPDNPkydIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKI-LNEEPPSlPPNEGFS 245
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767934614 2962 QKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06618   246 PDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
2737-2987 1.07e-12

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 71.25  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQ----VTHELGILQSLQHPLLVGLLDT-FETPTSYILvLE 2811
Cdd:cd14046     8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKI--KLRSESKnnsrILREVMLLSRLNHQHVVRYYQAwIERANLYIQ-ME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIH 2891
Cdd:cd14046    85 YCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSN---GNVKIGDFGLATSNKLNVELA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2892 QLLGNPEFAAPeiiLGNPVSLTSdtwSVGVLTYV---LLSGVSPFLDDSVE---------ETC------------LNICR 2947
Cdd:cd14046   162 TQDINKSTSAA---LGSSGDLTG---NVGTALYVapeVQSGTKSTYNEKVDmyslgiiffEMCypfstgmervqiLTALR 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767934614 2948 L-DFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd14046   236 SvSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLK 276
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
2781-2982 1.45e-12

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 70.47  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2781 ELGILQSLQHPLLVGLLD--TFETPTSYI----LVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAH 2854
Cdd:cd14012    48 ELESLKKLRHPNLVSYLAfsIERRGRSDGwkvyLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2855 LDLKPENILVDESLAKPTIKLADFGDAVQLN--TTYYIHQLLGNPEFAAPEIILGN-PVSLTSDTWSVGVLTYVLLSGVS 2931
Cdd:cd14012   128 KSLHAGNVLLDRDAGTGIVKLTDYSLGKTLLdmCSRGSLDEFKQTYWLPPELAQGSkSPTRKTDVWDLGLLFLQMLFGLD 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2932 PFLDDSVEETCLNICRLDFSFPDdyfkgvsqkakeFVCFLLQEDPAKRPSA 2982
Cdd:cd14012   208 VLEKYTSPNPVLVSLDLSASLQD------------FLSKCLSLDPKKRPTA 246
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
2844-2987 1.65e-12

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 70.38  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2844 VRYLHNCRIAHLDLKPENILVDESLAKPTIK--LADFGDAVQLNT-TYYIHQLLGNPE---FAAPEIILGNPVSLTS--- 2914
Cdd:cd13982   112 LAHLHSLNIVHRDLKPQNILISTPNAHGNVRamISDFGLCKKLDVgRSSFSRRSGVAGtsgWIAPEMLSGSTKRRQTrav 191
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2915 DTWSVG-VLTYVLLSGVSPFLDDSVEETclNICRLDFSFPDDYFKGV-SQKAKEFVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd13982   192 DIFSLGcVFYYVLSGGSHPFGDKLEREA--NILKGKYSLDKLLSLGEhGPEAQDLIERMIDFDPEKRPSAEEVLN 264
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
2743-2933 1.67e-12

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 70.11  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAV-ATKFVNKKLMKR--DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd14061     2 IGVGGFGKVYRGIWRGEEVAVkAARQDPDEDISVtlENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCvvrwgsLTEGKIRAHL-----GEVLEAVRYLHNCR---IAHLDLKPENILVDE-----SLAKPTIKLADFGDAVQLNT 2886
Cdd:cd14061    82 RV------LAGRKIPPHVlvdwaIQIARGMNYLHNEApvpIIHRDLKSSNILILEaieneDLENKTLKITDFGLAREWHK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2887 TYYIHQLlGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14061   156 TTRMSAA-GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
2764-2992 2.05e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 72.36  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2764 ATKFVNKKLMKRD--QVTH---ELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLldcvvrwGSLTEGKIRAHLG 2838
Cdd:PTZ00267   93 KEKVVAKFVMLNDerQAAYarsELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDL-------NKQIKQRLKEHLP 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2839 -----------EVLEAVRYLHNCRIAHLDLKPENILVdeslaKPT--IKLADFG------DAVQLNTTyyiHQLLGNPEF 2899
Cdd:PTZ00267  166 fqeyevgllfyQIVLALDEVHSRKMMHRDLKSANIFL-----MPTgiIKLGDFGfskqysDSVSLDVA---SSFCGTPYY 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2900 AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFsfpDDYFKGVSQKAKEFVCFLLQEDPAKR 2979
Cdd:PTZ00267  238 LAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKY---DPFPCPVSSGMKALLDPLLSKNPALR 314
                         250
                  ....*....|...
gi 767934614 2980 PSAALALQEQWLQ 2992
Cdd:PTZ00267  315 PTTQQLLHTEFLK 327
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
2742-2921 2.51e-12

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 69.68  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKK---CDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQSLQHPLLVGLLDTFETPtSYILVLEMAD 2814
Cdd:cd05040     2 KLGDGSFGVVRRgewTTPSGKVIQVAVKCLKSDVLSQpnamDDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTELAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCV-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFG--DAVQLNTTYYIH 2891
Cdd:cd05040    81 LGSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILL---ASKDKVKIGDFGlmRALPQNEDHYVM 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767934614 2892 QLLGNPEFA--APEIILGNPVSLTSDTWSVGV 2921
Cdd:cd05040   158 QEHRKVPFAwcAPESLKTRKFSHASDVWMFGV 189
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
617-848 2.69e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 68.63  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  617 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKR---FGQQQQTTLQVTVNVIKEGEDLIQQLRDSAissnktphns 693
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKheaLEAELAAHEERVEALNELGEQLIEEGHPDA---------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  694 siNHIETVLQQLDEAQSQMEELFQERKIKLELFLQLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHH 772
Cdd:cd00176    75 --EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA----DDLEQWLEEKEAALASEDLgKDLESVEELLKKH 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614  773 ADKALTMNNltfdviHQGQdllqyVNEVQASGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCV 848
Cdd:cd00176   149 KELEEELEA------HEPR-----LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
2729-2990 2.95e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 70.48  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKfvnKKLMKRDQ----VT--HELGILQSLQHPLLVGLLDTFET 2802
Cdd:cd07865     6 PFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALK---KVLMENEKegfpITalREIKILQLLKHENVVNLIEICRT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PT--------SYILVLEMADQ---GRLLDCVVRWgslTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakP 2871
Cdd:cd07865    83 KAtpynrykgSIYLVFEFCEHdlaGLLSNKNVKF---TLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKD---G 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2872 TIKLADFGdavqLNTTYYIHQLLGNPEFA---------APEIILGN-----PVsltsDTWSVGVLTYVLLSGvSPFLDDS 2937
Cdd:cd07865   157 VLKLADFG----LARAFSLAKNSQPNRYTnrvvtlwyrPPELLLGErdygpPI----DMWGAGCIMAEMWTR-SPIMQGN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2938 VEETCLN----IC------------RLD----FSFPDDYFKGVSQKAKEFV-----CFLLQE----DPAKRPSAALALQE 2988
Cdd:cd07865   228 TEQHQLTlisqLCgsitpevwpgvdKLElfkkMELPQGQKRKVKERLKPYVkdpyaLDLIDKllvlDPAKRIDADTALNH 307

                  ..
gi 767934614 2989 QW 2990
Cdd:cd07865   308 DF 309
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
2631-2717 3.05e-12

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 64.72  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2631 PLSEVTCETGETVVLRCRVCGRPKASITWKgpeHNTLNNDGHYSISysDLGEATLKIVGVTTEDDGIYTCIAVNDMGSAS 2710
Cdd:cd20978     7 PEKNVVVKGGQDVTLPCQVTGVPQPKITWL---HNGKPLQGPMERA--TVEDGTLTIINVQPEDTGYYGCVATNEIGDIY 81

                  ....*..
gi 767934614 2711 SSASLRV 2717
Cdd:cd20978    82 TETLLHV 88
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
2776-2933 4.50e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 69.30  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2776 DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQG---RLL-------DCVVRWGSltegkirahlgEVLEAVR 2845
Cdd:cd14145    50 ENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGplnRVLsgkrippDILVNWAV-----------QIARGMN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2846 YLHNCRIA---HLDLKPENILV-----DESLAKPTIKLADFGDAVQLNTTYYIhQLLGNPEFAAPEIILGNPVSLTSDTW 2917
Cdd:cd14145   119 YLHCEAIVpviHRDLKSSNILIlekveNGDLSNKILKITDFGLAREWHRTTKM-SAAGTYAWMAPEVIRSSMFSKGSDVW 197
                         170
                  ....*....|....*.
gi 767934614 2918 SVGVLTYVLLSGVSPF 2933
Cdd:cd14145   198 SYGVLLWELLTGEVPF 213
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
2743-2968 4.75e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 69.70  E-value: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQ--------VTHELGILQSLQHPLLVGLLDTFETPT-SYILVLEMA 2813
Cdd:cd14040    14 LGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 dQGRLLDCVVRWGSL-TEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDESLAKPTIKLADFG-------DAVQ 2883
Cdd:cd14040    94 -EGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGlskimddDSYG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 LNTTYYIHQLLGNPEFAAPE-IILGN---PVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLN----ICRLDFSFPDD 2955
Cdd:cd14040   173 VDGMDLTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentiLKATEVQFPVK 252
                         250
                  ....*....|...
gi 767934614 2956 YFkgVSQKAKEFV 2968
Cdd:cd14040   253 PV--VSNEAKAFI 263
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
2742-2904 5.76e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 68.98  E-value: 5.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVA-TKFVNKKLMKRDQ--VTHELGILQSLQHPLLVGLLDTFET----PTSYILVLEMAD 2814
Cdd:cd14031    17 ELGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAEQqrFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVdeslAKPT--IKLADFGDAVQLNTTYyI 2890
Cdd:cd14031    97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI----TGPTgsVKIGDLGLATLMRTSF-A 171
                         170
                  ....*....|....
gi 767934614 2891 HQLLGNPEFAAPEI 2904
Cdd:cd14031   172 KSVIGTPEFMAPEM 185
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
2740-2981 5.80e-12

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 68.76  E-value: 5.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIlVLEMADQGRLL 2819
Cdd:cd05067    12 VERLGAGQFGEVWMGYYNGHTK-VAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYI-ITEYMENGSLV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCV-VRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLLGN- 2896
Cdd:cd05067    90 DFLkTPSGIkLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTL---SCKIADFGLARLIEDNEYTAREGAKf 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2897 P-EFAAPEIILGNPVSLTSDTWSVGV-LTYVLLSGVSPFLDDSVEETCLNICRL-DFSFPDdyfkGVSQKAKEFVCFLLQ 2973
Cdd:cd05067   167 PiKWTAPEAINYGTFTIKSDVWSFGIlLTEIVTHGRIPYPGMTNPEVIQNLERGyRMPRPD----NCPEELYQLMRLCWK 242

                  ....*...
gi 767934614 2974 EDPAKRPS 2981
Cdd:cd05067   243 ERPEDRPT 250
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2740-2991 5.88e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 68.92  E-value: 5.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR-DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd06645    16 IQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDfAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQ-LLGNP 2897
Cdd:cd06645    96 QDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDN---GHVKLADFGVSAQITATIAKRKsFIGTP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2898 EFAAPEIIL---GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFP--DDYFKGvSQKAKEFVCFLL 2972
Cdd:cd06645   173 YWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPklKDKMKW-SNSFHHFVKMAL 251
                         250
                  ....*....|....*....
gi 767934614 2973 QEDPAKRPSAALALQEQWL 2991
Cdd:cd06645   252 TKNPKKRPTAEKLLQHPFV 270
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
2742-2980 5.96e-12

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 69.28  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQSLQHPLLVGLLD--TFETPTSYI----- 2807
Cdd:cd05091    13 ELGEDRFGKVYKGHLFGTAPGEQTQAVAIKTLKdkaegplREEFRHEAMLRSRLQHPNIVCLLGvvTKEQPMSMIfsycs 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 -------LVLEM--ADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADF 2878
Cdd:cd05091    93 hgdlhefLVMRSphSDVGSTDDDKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKL---NVKISDL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2879 GDAVQLNTTYYiHQLLGNPEFA----APEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFL---DDSVEETCLNicRLDF 2950
Cdd:cd05091   170 GLFREVYAADY-YKLMGNSLLPirwmSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCgysNQDVIEMIRN--RQVL 246
                         250       260       270
                  ....*....|....*....|....*....|
gi 767934614 2951 SFPDDYFKGVSQKAKEfvCFllQEDPAKRP 2980
Cdd:cd05091   247 PCPDDCPAWVYTLMLE--CW--NEFPSRRP 272
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
2737-2987 6.41e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 69.00  E-value: 6.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQSLQHPLLVGLLDTFETPTSYILVLE 2811
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRV--RLDDDDEgvpssALREICLLKELKHKNIVRLYDVLHSDKKLTLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQG--RLLDCVVrwGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDA-------- 2881
Cdd:cd07839    80 YCDQDlkKYFDSCN--GDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKN---GELKLADFGLArafgipvr 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 ---VQLNTTYYihqllgnpefAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSP-FLDDSVEETCLNICRLDFSFPDDY 2956
Cdd:cd07839   155 cysAEVVTLWY----------RPPDVLFGAKLYSTSiDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIFRLLGTPTEES 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2957 FKGVSQ--KAKEFVCF-------------------LLQE----DPAKRPSAALALQ 2987
Cdd:cd07839   225 WPGVSKlpDYKPYPMYpattslvnvvpklnstgrdLLQNllvcNPVQRISAEEALQ 280
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2737-2991 7.61e-12

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 68.95  E-value: 7.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkklmkrdQVTHELG----------ILQSLQHPLLVGLLDTFETPTSY 2806
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI--------RLEHEEGapftaireasLLKDLKHANIVTLHDIIHTKKTL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ILVLE---------MADQGRLLDcvvrwgsltEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLAD 2877
Cdd:cd07844    74 TLVFEyldtdlkqyMDDCGGGLS---------MHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISE---RGELKLAD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2878 FG--DAVQLNTTYYIHQ---LLGNPefaaPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPF----------------LD 2935
Cdd:cd07844   142 FGlaRAKSVPSKTYSNEvvtLWYRP----PDVLLGSTEYSTSlDMWGVGCIFYEMATGRPLFpgstdvedqlhkifrvLG 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2936 DSVEETCLNICRL----DFSFPDDYFK---------GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07844   218 TPTEETWPGVSSNpefkPYSFPFYPPRplinhaprlDRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
2787-2937 8.46e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 70.98  E-value: 8.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2787 SLQHPLLVGLLDTFETPTSYILVLEMADqGRLLDCVVRwgslTEGKIRAH-----LGEVLEAVRYLHNCRIAHLDLKPEN 2861
Cdd:NF033483   63 SLSHPNIVSVYDVGEDGGIPYIVMEYVD-GRTLKDYIR----EHGPLSPEeaveiMIQILSALEHAHRNGIVHRDIKPQN 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2862 ILVDESlakPTIKLADFGDAVQLN--TTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDS 2937
Cdd:NF033483  138 ILITKD---GRVKVTDFGIARALSstTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
2729-3038 9.38e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 68.92  E-value: 9.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQSLQHPLLVGLLDTFETPT 2804
Cdd:cd06635    19 FKEDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKkmsYSGKQSNEKWQdIIKEVKFLQRIKHPNSIEYKGCYLREH 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLE--MADQGRLLDcvVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAV 2882
Cdd:cd06635    99 TAWLVMEycLGSASDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLADFGSAS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLNTTyyiHQLLGNPEFAAPEIILG---NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICR-----LDFSFPD 2954
Cdd:cd06635   174 IASPA---NSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQnesptLQSNEWS 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2955 DYFkgvsqkaKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGRSTgvldtsrLTSFIERRKHqndvrPIRSIKNfLQSRL 3034
Cdd:cd06635   251 DYF-------RNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETV-------LIDLIQRTKD-----AVRELDN-LQYRK 310

                  ....
gi 767934614 3035 LPRV 3038
Cdd:cd06635   311 MKKL 314
SPEC smart00150
Spectrin repeats;
851-949 9.88e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.50  E-value: 9.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    851 RHLQAEVKQVLGWIRNGESMLNAgLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCA 930
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
                            90
                    ....*....|....*....
gi 767934614    931 EKVASHWQQLMLKMEDRLK 949
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
2735-2967 1.15e-11

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 68.96  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAE-LGRGRF-SVVKKCDQKgTKRAVATKFV-NKKLMKRdQVTHELGILQSL-------QHPLlVGLLD------ 2798
Cdd:cd14225    42 AYRYEILEvIGKGSFgQVVKALDHK-TNEHVAIKIIrNKKRFHH-QALVEVKILDALrrkdrdnSHNV-IHMKEyfyfrn 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2799 ----TFE--TPTSYILVLEMADQGRLLDCVVRWGSltegkirahlgEVLEAVRYLHNCRIAHLDLKPENILVdESLAKPT 2872
Cdd:cd14225   119 hlciTFEllGMNLYELIKKNNFQGFSLSLIRRFAI-----------SLLQCLRLLYRERIIHCDLKPENILL-RQRGQSS 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2873 IKLADFGdavqlnTTYYIHQ----LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL 2948
Cdd:cd14225   187 IKVIDFG------SSCYEHQrvytYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEV 260
                         250
                  ....*....|....*....
gi 767934614 2949 dFSFPDDYFKGVSQKAKEF 2967
Cdd:cd14225   261 -LGLPPPELIENAQRRRLF 278
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
2742-2904 1.16e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 67.72  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRF-SVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTS----YILVLEMAD 2814
Cdd:cd14033     8 EIGRGSFkTVYRGLDTETTVEVAWCELQTRKLSKgeRQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHN--CRIAHLDLKPENILVDESLAkpTIKLADFGDAVqLNTTYYIHQ 2892
Cdd:cd14033    88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSrcPPILHRDLKCDNIFITGPTG--SVKIGDLGLAT-LKRASFAKS 164
                         170
                  ....*....|..
gi 767934614 2893 LLGNPEFAAPEI 2904
Cdd:cd14033   165 VIGTPEFMAPEM 176
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
2729-2992 1.22e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 68.51  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQSLQHPLLVGLLDTFETPT 2804
Cdd:cd06634     9 FKDDPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKkmsYSGKQSNEKWQdIIKEVKFLQKLRHPNTIEYRGCYLREH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLE--MADQGRLLDcvVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAV 2882
Cdd:cd06634    89 TAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEP---GLVKLGDFGSAS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 QLNTTyyiHQLLGNPEFAAPEIILG---NPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICR-----LDFSFPD 2954
Cdd:cd06634   164 IMAPA---NSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQnespaLQSGHWS 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767934614 2955 DYFkgvsqkaKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06634   241 EYF-------RNFVDSCLQKIPQDRPTSDVLLKHRFLL 271
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2737-2987 1.25e-11

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 68.32  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKfvnKKLMKRDQ------VTHELGILQSLQH-PLLVGLLD---TFETPTSY 2806
Cdd:cd07837     3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEegvpstALREVSLLQMLSQsIYIVRLLDvehVEENGKPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 I-LVLEMADQG--RLLDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFG-- 2879
Cdd:cd07837    80 LyLVFEYLDTDlkKFIDSYGRGPHnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQ--KGLLKIADLGlg 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2880 DAVQLNTTYYIHQLLgNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL---------- 2948
Cdd:cd07837   158 RAFTIPIKSYTHEIV-TLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLlgtpneevwp 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2949 ------DFSF-----PDDYFKGVSQKAKEFVCFL---LQEDPAKRPSAALALQ 2987
Cdd:cd07837   237 gvsklrDWHEypqwkPQDLSRAVPDLEPEGVDLLtkmLAYDPAKRISAKAALQ 289
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
2742-2904 1.30e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 68.15  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRF-SVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTS----YILVLEMAD 2814
Cdd:cd14030    32 EIGRGSFkTVYKGLDTETTVEVAWCELQDRKLSKseRQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDESLAkpTIKLADFGDAVqLNTTYYIHQ 2892
Cdd:cd14030   112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTG--SVKIGDLGLAT-LKRASFAKS 188
                         170
                  ....*....|..
gi 767934614 2893 LLGNPEFAAPEI 2904
Cdd:cd14030   189 VIGTPEFMAPEM 200
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
2743-2879 1.37e-11

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 64.39  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQSLQHPLL--VGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDdVNNEEGEDLESEMDILRRLKGLELniPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DcVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG 2879
Cdd:cd13968    81 A-YTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSE---DGNVKLIDFG 136
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
2839-2986 1.49e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 69.90  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2839 EVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFGDAVQLNTTYYI---HQLLGNPEFAAPEIILGNPVSLTSD 2915
Cdd:PTZ00283  151 QVLLAVHHVHSKHMIHRDIKSANILL---CSNGLVKLGDFGFSKMYAATVSDdvgRTFCGTPYYVAPEIWRRKPYSKKAD 227
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2916 TWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDfSFPDDyfkgVSQKAKEFVCFLLQEDPAKRPSAALAL 2986
Cdd:PTZ00283  228 MFSLGVLLYELLTLKRPFDGENMEEVMHKTLagRYD-PLPPS----ISPEMQEIVTALLSSDPKRRPSSSKLL 295
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2643-2712 1.76e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 61.96  E-value: 1.76e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2643 VVLRCRVCGRPKASITWKGPEHNTLNNDghYSISYSDLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSS 2712
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSS--RDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
2740-2934 1.78e-11

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 67.79  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKC----DQKGTKRAVATKFVN--KKLMKRDQVTHELGILQSLQHPLLVGLLDTFETP--TSYILVLE 2811
Cdd:cd05038     9 IKQLGEGHFGSVELCrydpLGDNTGEQVAVKSLQpsGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrRSLRLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGRLLDcvvrwgSLTEGKIRAHLGEVL-------EAVRYLHNCRIAHLDLKPENILVD-ESLakptIKLADFGDAVQ 2883
Cdd:cd05038    89 YLPSGSLRD------YLQRHRDQIDLKRLLlfasqicKGMEYLGSQRYIHRDLAARNILVEsEDL----VKISDFGLAKV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2884 LNTT---YYIHQLLGNPEF-AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL 2934
Cdd:cd05038   159 LPEDkeyYYVKEPGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
2743-2992 1.79e-11

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 67.31  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVatkfvnkKLMKRDQVTH----ELGILQSLQHPLLVGLLDTF-ETPTSYILVLEMADQGR 2817
Cdd:cd05082    14 IGKGEFGDVMLGDYRGNKVAV-------KCIKNDATAQaflaEASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWG-SLTEGKIRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQLlg 2895
Cdd:cd05082    87 LVDYLRSRGrSVLGGDCLLKFSlDVCEAMEYLEGNNFVHRDLAARNVLVSE---DNVAKVSDFGLTKEASSTQDTGKL-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2896 nP-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETclnICRLDFSFPDDYFKGVSQKAKEFV--CFL 2971
Cdd:cd05082   162 -PvKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDV---VPRVEKGYKMDAPDGCPPAVYDVMknCWH 237
                         250       260
                  ....*....|....*....|.
gi 767934614 2972 LqeDPAKRPSaALALQEqWLQ 2992
Cdd:cd05082   238 L--DAAMRPS-FLQLRE-QLE 254
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
2737-2968 1.86e-11

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 68.20  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRA--VATK-----FVNKKLMKRdqVTHELGILQSLQ-HPLLVGLLDT---FETPTS 2805
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEetVAIKkitnvFSKKILAKR--ALRELKLLRHFRgHKNITCLYDMdivFPGNFN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2806 YILVLEmadqgRLLDC----VVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG- 2879
Cdd:cd07857    80 ELYLYE-----ELMEAdlhqIIRSGQpLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVN---ADCELKICDFGl 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2880 ----DAVQLNTTYYIHQLLGNPEFAAPEIILGN-PVSLTSDTWSVGVLTYVLLsGVSPFL--DDSVEETCLNICRLDFSF 2952
Cdd:cd07857   152 argfSENPGENAGFMTEYVATRWYRAPEIMLSFqSYTKAIDVWSVGCILAELL-GRKPVFkgKDYVDQLNQILQVLGTPD 230
                         250
                  ....*....|....*.
gi 767934614 2953 PDDYFKGVSQKAKEFV 2968
Cdd:cd07857   231 EETLSRIGSPKAQNYI 246
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
391-612 1.98e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 65.93  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  391 FHQKAEKYMSNVDSWCKACGEVDLPSELQDLEDAIHHHQGIYEHITLAYSEVSQdgkslLDKLqrpltpgsSDSLTASAN 470
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEA-----LNEL--------GEQLIEEGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  471 YSKAVHHvlDVIHEVLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKR 550
Cdd:cd00176    72 PDAEEIQ--ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEELLKK 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767934614  551 HEDFEEVAQNTYTNADKLLEAAEQLAQTGECD-PEEIYQAAHQLEDRIQDFVRRVEQRKILLD 612
Cdd:cd00176   148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLE 210
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
2737-2991 2.01e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 68.58  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFeTPTSYI---- 2807
Cdd:cd07874    19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKklsrpFQNQTHAKR--AYRELVLMKCVNHKNIISLLNVF-TPQKSLeefq 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 ---LVLEMADQGRlldCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQL 2884
Cdd:cd07874    96 dvyLVMELMDANL---CQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLARTA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLT------YVLLSGVS----------------PFLDDSVEETC 2942
Cdd:cd07874   170 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgemvrhKILFPGRDyidqwnkvieqlgtpcPEFMKKLQPTV 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2943 LNICR-------LDFS--FPDDYFKGVSQ-------KAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07874   250 RNYVEnrpkyagLTFPklFPDSLFPADSEhnklkasQARDLLSKMLVIDPAKRISVDEALQHPYI 314
SPEC smart00150
Spectrin repeats;
286-386 2.35e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.73  E-value: 2.35e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    286 FEQDAEKMFDWITHNKGLFlnSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIRQIAS 365
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL--ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 767934614    366 QLEQEWKAFAAALDERSTLLD 386
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
2743-2981 2.84e-11

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 66.94  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFV---NKKlmKRDQVTHELGILQSLQHPLLVGLLD------TFETPTSYiLVLEMA 2813
Cdd:cd13986     8 LGEGGFSFVYLVEDLSTGRLYALKKIlchSKE--DVKEAMREIENYRLFNHPNILRLLDsqivkeAGGKKEVY-LLLPYY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLD----CVVRWGSLTEGKIRAHLGEVLEAVRYLHNCR---IAHLDLKPENILVDESlakPTIKLADFGDAVQ--- 2883
Cdd:cd13986    85 KRGSLQDeierRLVKGTFFPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSED---DEPILMDLGSMNPari 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2884 -LNTTyyiHQLLGNPEFA---------APEI-------ILGNPVsltsDTWSVGVLTYVLLSGVSPF-----LDDSVEet 2941
Cdd:cd13986   162 eIEGR---REALALQDWAaehctmpyrAPELfdvkshcTIDEKT----DIWSLGCTLYALMYGESPFerifqKGDSLA-- 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767934614 2942 cLNICRLDFSFPDDyfKGVSQKAKEFVCFLLQEDPAKRPS 2981
Cdd:cd13986   233 -LAVLSGNYSFPDN--SRYSEELHQLVKSMLVVNPAERPS 269
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
2743-2933 3.28e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 66.75  E-value: 3.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVatkfvnKKLMK---------RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd14158    23 LGEGGFGVVFKGYINDKNVAV------KKLAAmvdistedlTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLD---CVVRWGSLT-EGKIRAHLGEVlEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA---VQLNT 2886
Cdd:cd14158    97 PNGSLLDrlaCLNDTPPLSwHMRCKIAQGTA-NGINYLHENNHIHRDIKSANILLDETF---VPKISDFGLArasEKFSQ 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2887 TYYIHQLLGNPEFAAPEIILGNpVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14158   173 TIMTERIVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPV 218
PHA03247 PHA03247
large tegument protein UL36; Provisional
2271-2481 3.97e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.58  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRP---SRIPQPvRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAAP--EAGPSAPSRRP----PGADAE 2341
Cdd:PHA03247 2693 GSLTSLADPpppPPTPEP-APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatPGGPARPARPPttagPPAPAP 2771
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2342 GSEREAEPIPKMKVLESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSS--AVPSLGKEPFPPSSP 2419
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAqpTAPPPPPGPPPPSLP 2851
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2420 LQ----KGGSFWSSIPA-SPASRPGSFTFPGDSD----SLQRQTPRHAAPGKDTDRMSTCSSASEQSVQST 2481
Cdd:PHA03247 2852 LGgsvaPGGDVRRRPPSrSPAAKPAAPARPPVRRlarpAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQ 2922
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
2744-2933 4.55e-11

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 65.75  E-value: 4.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2744 GRGRFSVVKKCDQKGTKRAVATKfvnkKLMKRDQVTHelgILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVV 2823
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVK----KLLKIEKEAE---ILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2824 RWGS--LTEGKIRAHLGEVLEAVRYLHN---CRIAHLDLKPENILVdesLAKPTIKLADFGDAVQLNTTYYIhQLLGNPE 2898
Cdd:cd14060    75 SNESeeMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVI---AADGVLKICDFGASRFHSHTTHM-SLVGTFP 150
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14060   151 WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
2737-2933 4.56e-11

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 66.64  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQSLQHPLLVGLLDTFETPTSYILVLEM-- 2812
Cdd:cd07869     7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTaiREASLLKGLKHANIVLLHDIIHTKETLTLVFEYvh 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDcvVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG--DAVQLNTTYYI 2890
Cdd:cd07869    87 TDLCQYMD--KHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDT---GELKLADFGlaRAKSVPSHTYS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2891 HQLLgNPEFAAPEIILGNP-VSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd07869   162 NEVV-TLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAF 204
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
2742-2933 4.93e-11

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 66.12  E-value: 4.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRA--VATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETpTSYILVLEMADQGR 2817
Cdd:cd05115    11 ELGSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEKavRDEMMREAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMASGGP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVV-RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDESLAKptikLADFG--DAVQLNTTYYIHQL 2893
Cdd:cd05115    90 LNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLlVNQHYAK----ISDFGlsKALGADDSYYKARS 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767934614 2894 LGN-P-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05115   166 AGKwPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
2742-2933 5.17e-11

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 66.04  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd05114    11 ELGSGLFGVVRLGKWRAQYK-VAIKAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 V-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDA-VQLNTTYYIHQLLGNP-E 2898
Cdd:cd05114    90 LrQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDT---GVVKVSDFGMTrYVLDDQYTSSSGAKFPvK 166
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTY-VLLSGVSPF 2933
Cdd:cd05114   167 WSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPF 202
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
2743-2924 5.86e-11

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 65.38  E-value: 5.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLD--TFETPTsYIlVLEMADQGRLLD 2820
Cdd:cd05034     3 LGAGQFGEVWMGVWNGTTK-VAVKTLKPGTMSPEAFLQEAQIMKKLRHDKLVQLYAvcSDEEPI-YI-VTELMSKGSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 cVVRWGS---LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkptIKLADFGDAVQLNTTYYI-HQLLGN 2896
Cdd:cd05034    80 -YLRTGEgraLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNV---CKVADFGLARLIEDDEYTaREGAKF 155
                         170       180
                  ....*....|....*....|....*....
gi 767934614 2897 P-EFAAPEIILGNPVSLTSDTWSVGVLTY 2924
Cdd:cd05034   156 PiKWTAPEAALYGRFTIKSDVWSFGILLY 184
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2737-2991 6.59e-11

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 65.82  E-value: 6.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQ---VTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMA 2813
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKII--KLEPGDDfslIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTYYIHQ- 2892
Cdd:cd06646    89 GGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDN---GDVKLADFGVAAKITATIAKRKs 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGNPEFAAPEIIL---GNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFP--DDYFKGvSQKAKEF 2967
Cdd:cd06646   166 FIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPPklKDKTKW-SSTFHNF 244
                         250       260
                  ....*....|....*....|....
gi 767934614 2968 VCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd06646   245 VKISLTKNPKKRPTAERLLTHLFV 268
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
2742-2933 8.03e-11

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 65.29  E-value: 8.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGtKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC 2821
Cdd:cd05113    11 ELGTGQFGVVKYGKWRG-QYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 VVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLLGN--PE 2898
Cdd:cd05113    90 LREMRKrFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQG---VVKVSDFGLSRYVLDDEYTSSVGSKfpVR 166
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767934614 2899 FAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05113   167 WSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
25-152 9.81e-11

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 61.96  E-value: 9.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    25 GGPILTFPARS-NHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDS------IKPLLKILQESFPCCIHVA 97
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    98 LIIKPDNFWQKQ----RTNFGSSKFEFETNMVS-LEGLTKVVDPSQLTPEFDGCLEYNHE 152
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
2737-2922 1.02e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 66.22  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFeTPTSYI---- 2807
Cdd:cd07875    26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKklsrpFQNQTHAKR--AYRELVLMKCVNHKNIIGLLNVF-TPQKSLeefq 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 ---LVLEMADQGRlldCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQL 2884
Cdd:cd07875   103 dvyIVMELMDANL---CQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLARTA 176
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767934614 2885 NTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd07875   177 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCI 214
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2631-2717 1.20e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 60.28  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2631 PLSEVTCETGETVVLRCRVCGRPKASITWKgPEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVNDMGSAS 2710
Cdd:cd20973     3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWM-KDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                  ....*..
gi 767934614 2711 SSASLRV 2717
Cdd:cd20973    82 CSAELTV 88
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
1390-1533 1.30e-10

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 61.98  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1390 EIKDGLEVMLSVPKRAND-------AMHL----SMLEGFDE-NIESQGELILQESFqvwdpkTLIRKGRERHLFLFEMSL 1457
Cdd:cd13243     3 VVEEALDTMTQVAWHINDmkrkhehAVRVqeiqSLLDGWEGpELTTYGDLVLEGTF------RMAGAKNERLLFLFDKML 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 1458 VFSKEVKDSSgrskYLYKSKLFTSELGVTEHVEGDPCKFalWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQE 1533
Cdd:cd13243    77 LITKKREDGI----LQYKTHIMCSNLMLSESIPKEPLSF--QVLPFDNPKLQYTLQAKNQEQKRLWTQEIKRLILE 146
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
2767-2929 1.45e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 65.82  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2767 FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFeTPTSYI-------LVLEMADQGRlldCVVRWGSLTEGKIRAHLGE 2839
Cdd:cd07876    58 FQNQTHAKR--AYRELVLLKCVNHKNIISLLNVF-TPQKSLeefqdvyLVMELMDANL---CQVIHMELDHERMSYLLYQ 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2840 VLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSV 2919
Cdd:cd07876   132 MLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSV 208
                         170
                  ....*....|
gi 767934614 2920 GVLTYVLLSG 2929
Cdd:cd07876   209 GCIMGELVKG 218
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
2743-2933 1.49e-10

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 64.75  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKK---CDQKGTKRAVATKF--VNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIlVLEMADQGR 2817
Cdd:cd05056    14 IGEGQFGDVYQgvyMSPENEKIAVAVKTckNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPVWI-VMELAPLGE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCV-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdesLAKPTIKLADFGDAVQLNTTYYIHQLLGN 2896
Cdd:cd05056    93 LRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV---SSPDCVKLGDFGLSRYMEDESYYKASKGK 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767934614 2897 -P-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05056   170 lPiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPF 209
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
2771-2986 1.60e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 66.17  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2771 KLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLE---------MADQGRLLDCvvrwgsltegKIRAHLGEVL 2841
Cdd:PHA03212  123 KAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPryktdlycyLAAKRNIAIC----------DILAIERSVL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2842 EAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDA---VQLNTTYYiHQLLGNPEFAAPEIILGNPVSLTSDTWS 2918
Cdd:PHA03212  193 RAIQYLHENRIIHRDIKAENIFINHP---GDVCLGDFGAAcfpVDINANKY-YGWAGTIATNAPELLARDPYGPAVDIWS 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2919 VGVLTYVLLSGV-SPFLDDSVEETCLN------ICRLDFSFPDDY-----------FKGVSQKAKE-------------- 2966
Cdd:PHA03212  269 AGIVLFEMATCHdSLFEKDGLDGDCDSdrqiklIIRRSGTHPNEFpidaqanldeiYIGLAKKSSRkpgsrplwtnlyel 348
                         250       260
                  ....*....|....*....|....*.
gi 767934614 2967 ------FVCFLLQEDPAKRPSAALAL 2986
Cdd:PHA03212  349 pidleyLICKMLAFDAHHRPSAEALL 374
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2626-2717 1.96e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.82  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHySISYSDLGEATLKIVGVTTEDDGIYTCIAVND 2705
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAH-KMLVRENGRHSLIIEPVTKRDAGIYTCIARNR 79
                          90
                  ....*....|..
gi 767934614 2706 MGSASSSASLRV 2717
Cdd:cd05744    80 AGENSFNAELVV 91
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
2737-2933 2.05e-10

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 65.31  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFETPTSY----- 2806
Cdd:cd07879    17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKklsrpFQSEIFAKR--AYRELTLLKHMQHENVIGLLDVFTSAVSGdefqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2807 ---ILVLEMADQGRlldcvVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQ 2883
Cdd:cd07879    95 fylVMPYMQTDLQK-----IMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDC---ELKILDFGLARH 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2884 LN---TTYYIHQLlgnpeFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd07879   167 ADaemTGYVVTRW-----YRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLF 215
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
2731-2940 2.14e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 65.05  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHP--------LLVGLLDTFET 2802
Cdd:cd14216     6 DLFNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSdpndpnreMVVQLLDDFKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 P----TSYILVLEMADQgRLLDCVVR--WGSLTEGKIRAHLGEVLEAVRYLHN-CRIAHLDLKPENILVDES-------- 2867
Cdd:cd14216    86 SgvngTHICMVFEVLGH-HLLKWIIKsnYQGLPLPCVKKIIRQVLQGLDYLHTkCRIIHTDIKPENILLSVNeqyirrla 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2868 ----------LAKP---------TIKLADFGDAVQLNTtyYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLS 2928
Cdd:cd14216   165 aeatewqrnfLVNPlepknaeklKVKIADLGNACWVHK--HFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELAT 242
                         250
                  ....*....|..
gi 767934614 2929 GVSPFLDDSVEE 2940
Cdd:cd14216   243 GDYLFEPHSGED 254
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
2742-2904 2.20e-10

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 63.94  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVA-TKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTS----YILVLEMAD 2814
Cdd:cd14032     8 ELGRGSFKTVYKGLDTETWVEVAwCELQDRKLTKveRQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDESLAkpTIKLADFGDAVqLNTTYYIHQ 2892
Cdd:cd14032    88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTG--SVKIGDLGLAT-LKRASFAKS 164
                         170
                  ....*....|..
gi 767934614 2893 LLGNPEFAAPEI 2904
Cdd:cd14032   165 VIGTPEFMAPEM 176
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
2739-2992 2.20e-10

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 64.74  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAEL-GRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQH----PLLVGLLDTFETP---TSYILVL 2810
Cdd:cd06637     9 ELVELvGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHhrniATYYGAFIKKNPPgmdDQLWLVM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 EMADQGRLLDCV--VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTY 2888
Cdd:cd06637    89 EFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSAQLDRTV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2889 -YIHQLLGNPEFAAPEIIL--GNP---VSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRldFSFPDDYFKGVSQ 2962
Cdd:cd06637   166 gRRNTFIGTPYWMAPEVIAcdENPdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPR--NPAPRLKSKKWSK 243
                         250       260       270
                  ....*....|....*....|....*....|
gi 767934614 2963 KAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd06637   244 KFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
2740-2935 2.27e-10

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 64.26  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPL-LVGLLDTF--ETPTSY----ILVLEM 2812
Cdd:cd06636    21 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRnIATYYGAFikKSPPGHddqlWLVMEF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCV--VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDAVQLNTTY-Y 2889
Cdd:cd06636   101 CGAGSVTDLVknTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSAQLDRTVgR 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2890 IHQLLGNPEFAAPEIIL--GNPVS---LTSDTWSVGVLTYVLLSGVSPFLD 2935
Cdd:cd06636   178 RNTFIGTPYWMAPEVIAcdENPDAtydYRSDIWSLGITAIEMAEGAPPLCD 228
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2737-2982 2.78e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 63.66  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVnkKLMKRdQVTHELGILQSLQHPLLV----------GLLDTFET---- 2802
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV--KLNNE-KAEREVKALAKLDHPNIVryngcwdgfdYDPETSSSnssr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 -PTSYILV-LEMADQGRLLDCVVRWGSLTEGKIRAH--LGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADF 2878
Cdd:cd14047    85 sKTKCLFIqMEFCEKGTLESWIEKRNGEKLDKVLALeiFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTG---KVKIGDF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2879 GDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYfk 2958
Cdd:cd14047   162 GLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWTDLRNGILPDIFDKRY-- 239
                         250       260
                  ....*....|....*....|....
gi 767934614 2959 gvsQKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd14047   240 ---KIEKTIIKKMLSKKPEDRPNA 260
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2625-2717 3.26e-10

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 59.11  E-value: 3.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2625 PPEFVIPLSEVTCETGETVVLRCRVCGRPKASITWK---GPEHNTL--------NNDGHYsISYsdlgeatLKIVGVTTE 2693
Cdd:cd20956     1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTldgFPIPESPrfrvgdyvTSDGDV-VSY-------VNISSVRVE 72
                          90       100
                  ....*....|....*....|....
gi 767934614 2694 DDGIYTCIAVNDMGSASSSASLRV 2717
Cdd:cd20956    73 DGGEYTCTATNDVGSVSHSARINV 96
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
2740-2933 3.36e-10

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 63.52  E-value: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGL--LDTFETPTsYILVLEMAdQGR 2817
Cdd:cd05072    12 VKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLyaVVTKEEPI-YIITEYMA-KGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVV--RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA-VQLNTTYYIHQLL 2894
Cdd:cd05072    89 LLDFLKsdEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESL---MCKIADFGLArVIEDNEYTAREGA 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767934614 2895 GNP-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05072   166 KFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY 206
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
2776-2988 3.75e-10

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 63.51  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2776 DQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDcvvrwgSLTEGKIRAHL-----GEVLEAVRYLHN- 2849
Cdd:cd14147    47 ESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSR------ALAGRRVPPHVlvnwaVQIARGMHYLHCe 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2850 --CRIAHLDLKPENIL-----VDESLAKPTIKLADFGDAVQLNTTYYIhQLLGNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd14147   121 alVPVIHRDLKSNNILllqpiENDDMEHKTLKITDFGLAREWHKTTQM-SAAGTYAWMAPEVIKASTFSKGSDVWSFGVL 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2923 TYVLLSGVSPF--LDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEfvCFllQEDPAKRPSAALALQE 2988
Cdd:cd14147   200 LWELLTGEVPYrgIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMAD--CW--AQDPHRRPDFASILQQ 263
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
2634-2717 4.66e-10

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 58.66  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2634 EVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSIsysdLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSA 2713
Cdd:cd20952     8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITT----LENGSLQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                  ....
gi 767934614 2714 SLRV 2717
Cdd:cd20952    84 VLDV 87
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2737-2982 6.80e-10

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 62.45  E-value: 6.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKC-DQKGTKRAVATKFVNKKLMKRDQ--VTHELGILQSLQHPLLVGLLDTFETPTSYILVL--- 2810
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVrHKRDRKQYVIKKLNLKNASKRERkaAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVmgf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2811 -EMAD--------QGRLLD--CVVRWgsltegkirahLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFG 2879
Cdd:cd08223    82 cEGGDlytrlkeqKGVLLEerQVVEW-----------FVQIAMALQYMHERNILHRDLKTQNIFLTKS---NIIKVGDLG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2880 DAVQLNTTYYI-HQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPDDYf 2957
Cdd:cd08223   148 IARVLESSSDMaTTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQY- 226
                         250       260
                  ....*....|....*....|....*
gi 767934614 2958 kgvSQKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd08223   227 ---SPELGELIKAMLHQDPEKRPSV 248
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
2839-2986 7.07e-10

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 62.81  E-value: 7.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2839 EVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIklADFGDAVQLNTTyyiHQLL----GNPEFAAPEIILGNPVS-LT 2913
Cdd:cd13974   140 DVVRVVEALHKKNIVHRDLKLGNMVLNKRTRKITI--TNFCLGKHLVSE---DDLLkdqrGSPAYISPDVLSGKPYLgKP 214
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2914 SDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfKGVSQKAKEFVCFLLQEDPAKRPSAALAL 2986
Cdd:cd13974   215 SDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPED--GRVSENTVCLIRKLLVLNPQKRLTASEVL 285
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
2640-2717 8.65e-10

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 57.87  E-value: 8.65e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2640 GETVVLRCRVCGRPKASITWKGPEHNTLNNDGHySISYSDlgeATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRV 2717
Cdd:cd05764    15 GQRATLRCKARGDPEPAIHWISPEGKLISNSSR-TLVYDN---GTLDILITTVKDTGAFTCIASNPAGEATARVELHI 88
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
2743-2933 1.27e-09

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 62.51  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKR--DQVTHELGILQSLQHPLLVGLLDTFETPTSY--ILVLEMADQGRL 2818
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRplDVQMREFEVLKKLNHKNIVKLFAIEEELTTRhkVLVMELCPCGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 ---LDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENIL--VDESlAKPTIKLADFGDAVQLNTTYYIHQL 2893
Cdd:cd13988    81 ytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGED-GQSVYKLTDFGAARELEDDEQFVSL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767934614 2894 LGNPEFAAPEI----IL----GNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd13988   160 YGTEEYLHPDMyeraVLrkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
2740-2928 1.35e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 61.83  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGRGRFSVVKKC--DQKG--TKRAVATKFVNKKLMKRDQ-VTHELGILQSLQHPLLVGLLDTFETP--TSYILVLEM 2812
Cdd:cd05081     9 ISQLGKGNFGSVELCryDPLGdnTGALVAVKQLQHSGPDQQRdFQREIQILKALHSDFIVKYRGVSYGPgrRSLRLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDCVVR-WGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFGDA--VQLNTTYY 2889
Cdd:cd05081    89 LPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVE---SEAHVKIADFGLAklLPLDKDYY 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767934614 2890 IHQLLG-NPEF-AAPEIILGNPVSLTSDTWSVGVLTYVLLS 2928
Cdd:cd05081   166 VVREPGqSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
2743-2922 1.44e-09

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 61.35  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKfVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCV 2822
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMK-ELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2823 VRWGSLTEGKIRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIH-------QLL 2894
Cdd:cd14065    80 KSMDEQLPWSQRVSLAkDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMPDEKTKKpdrkkrlTVV 159
                         170       180
                  ....*....|....*....|....*...
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd14065   160 GSPYWMAPEMLRGESYDEKVDVFSFGIV 187
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
2731-2929 1.74e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 62.73  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2731 DNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSL--------QHPLLVGLLDTFET 2802
Cdd:cd14218     6 DLFNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKCVrdsdpsdpKRETIVQLIDDFKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 P----TSYILVLEMADQgRLLDCVVR--WGSLTEGKIRAHLGEVLEAVRYLHN-CRIAHLDLKPENIL--VDES------ 2867
Cdd:cd14218    86 SgvngVHVCMVLEVLGH-QLLKWIIKsnYQGLPLPCVKSILRQVLQGLDYLHTkCKIIHTDIKPENILmcVDEGyvrrla 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2868 --------------------------LAKP---------TIKLADFGDAVQLNTtyYIHQLLGNPEFAAPEIILGNPVSL 2912
Cdd:cd14218   165 aeatiwqqagapppsgssvsfgasdfLVNPlepqnadkiRVKIADLGNACWVHK--HFTEDIQTRQYRALEVLIGAEYGT 242
                         250
                  ....*....|....*..
gi 767934614 2913 TSDTWSVGVLTYVLLSG 2929
Cdd:cd14218   243 PADIWSTACMAFELATG 259
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
2743-2929 2.38e-09

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 62.07  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRF-SVVKKCDQKgTKRAVATKFV-NKKLMKRdQVTHELGILQSLQHP------LLVGLLD----------TFE--T 2802
Cdd:cd14224    73 IGKGSFgQVVKAYDHK-THQHVALKMVrNEKRFHR-QAAEEIRILEHLKKQdkdntmNVIHMLEsftfrnhicmTFEllS 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PTSYILVLEMADQGRLLDCVVRWgsltegkirAHlgEVLEAVRYLHNCRIAHLDLKPENILVDESlAKPTIKLADFGDAV 2882
Cdd:cd14224   151 MNLYELIKKNKFQGFSLQLVRKF---------AH--SILQCLDALHRNKIIHCDLKPENILLKQQ-GRSGIKVIDFGSSC 218
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2883 QLNTTYYIHqlLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSG 2929
Cdd:cd14224   219 YEHQRIYTY--IQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG 263
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2742-2933 2.68e-09

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 60.70  E-value: 2.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIlVLEMADQGRLLDc 2821
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYI-VTEFMSKGSLLD- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 vvrwgSLTEGKIRA--------HLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAkptIKLADFGDAVQL-NTTYYIHQ 2892
Cdd:cd14203    79 -----FLKDGEGKYlklpqlvdMAAQIASGMAYIERMNYIHRDLRAANILVGDNLV---CKIADFGLARLIeDNEYTARQ 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767934614 2893 LLGNP-EFAAPEIILGNPVSLTSDTWSVGVL-TYVLLSGVSPF 2933
Cdd:cd14203   151 GAKFPiKWTAPEAALYGRFTIKSDVWSFGILlTELVTKGRVPY 193
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2625-2717 2.86e-09

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 56.42  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2625 PPeFVIPLSEVTCETGETVVLRCRVCGRPKASITW-KG----PEHntlnndgHYSISYSDlgeATLKIVGVTT-EDDGIY 2698
Cdd:cd20958     1 PP-FIRPMGNLTAVAGQTLRLHCPVAGYPISSITWeKDgrrlPLN-------HRQRVFPN---GTLVIENVQRsSDEGEY 69
                          90       100
                  ....*....|....*....|
gi 767934614 2699 TCIAVNDMG-SASSSASLRV 2717
Cdd:cd20958    70 TCTARNQQGqSASRSVFVKV 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
2274-2477 3.05e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.42  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2274 TSRS-RPSRIPQPVRHHPPVlvssaassqaeadkmsgtstpGPSLPPPGAAPEAG---------PSAPSRRPPGADAEGS 2343
Cdd:PHA03247 2583 TSRArRPDAPPQSARPRAPV---------------------DDRGDPRGPAPPSPlppdthapdPPPPSPSPAANEPDPH 2641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2344 EREAEPIPkmkvlESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSsavpSLGKEPFPPSSPLQKG 2423
Cdd:PHA03247 2642 PPPTVPPP-----ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLT----SLADPPPPPPTPEPAP 2712
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2424 GSFWSSIPASPASRPGSFTFPG-DSDSLQRQTPRHAA-PGKDTDRMSTCSSASEQS 2477
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPAlPAAPAPPAVPAGPAtPGGPARPARPPTTAGPPA 2768
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
2769-2954 3.77e-09

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 60.21  E-value: 3.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2769 NKKLMKrdqvthELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLgEVLEAVRYLH 2848
Cdd:cd14027    35 NEALLE------EGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLH 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2849 NCRIAHLDLKPENILVDESLAkptIKLADFGDAV-----QLNTTYYIHQ--LLGNPEFAAPEIILGNPVSLT-------- 2913
Cdd:cd14027   108 GKGVIHKDLKPENILVDNDFH---IKIADLGLASfkmwsKLTKEEHNEQreVDGTAKKNAGTLYYMAPEHLNdvnakpte 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2914 -SDTWSVGVLTYVLLSGVSPFlDDSVEETCLNICRLDFSFPD 2954
Cdd:cd14027   185 kSDVYSFAIVLWAIFANKEPY-ENAINEDQIIMCIKSGNRPD 225
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
2779-2924 4.58e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.83  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2779 THELGILQSLQHPLLVGLLDTFETPTSYILVLE--MADQGRLLDCVVRwgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLD 2856
Cdd:PHA03211  208 VHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPkyRSDLYTYLGARLR--PLGLAQVTAVARQLLSAIDYIHGEGIIHRD 285
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2857 LKPENILVDeslAKPTIKLADFGDAVQLN---TTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTY 2924
Cdd:PHA03211  286 IKTENVLVN---GPEDICLGDFGAACFARgswSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
2742-2987 4.92e-09

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 59.93  E-value: 4.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATK---FVNKKLM-----KRdqVTHELGILQSLQ-HPLLVGLLDTFETPTSYILVLEM 2812
Cdd:cd14019     8 KIGEGTFSSVYKAEDKLHDLYDRNKgrlVALKHIYptsspSR--ILNELECLERLGgSNNVSGLITAFRNEDQVVAVLPY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2813 ADQGRLLDcVVRWGSLTEgkIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTikLADFGDAvqlNTTYYIHQ 2892
Cdd:cd14019    86 IEHDDFRD-FYRKMSLTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGV--LVDFGLA---QREEDRPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 LLGN----PEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGVSPFLDDSVEETCL-NICRLdfsFPDDyfkgvsqKAKE 2966
Cdd:cd14019   158 QRAPragtRGFRAPEVLFKCPHQTTAiDIWSAGVILLSILSGRFPFFFSSDDIDALaEIATI---FGSD-------EAYD 227
                         250       260
                  ....*....|....*....|.
gi 767934614 2967 FVCFLLQEDPAKRPSAALALQ 2987
Cdd:cd14019   228 LLDKLLELDPSKRITAEEALK 248
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
2846-2933 5.27e-09

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 59.71  E-value: 5.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2846 YLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV---QLNTTYYIHQLLGNPEFAAPEIIL---GNPVSLTSDTWSV 2919
Cdd:cd14062   104 YLHAKNIIHRDLKSNNIFLHEDL---TVKIGDFGLATvktRWSGSQQFEQPTGSILWMAPEVIRmqdENPYSFQSDVYAF 180
                          90
                  ....*....|....
gi 767934614 2920 GVLTYVLLSGVSPF 2933
Cdd:cd14062   181 GIVLYELLTGQLPY 194
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
2625-2717 5.45e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 55.67  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2625 PPEFVIPLSEVTCETGETVVLRCRVCGRPKASITW--KGPE-HNTLNNDGHysiSYSDLgeATLKIVGVTTEDDGIYTCI 2701
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWfcEGKElQNSPDIQIH---QEGDL--HSLIIAEAFEEDTGRYSCL 75
                          90
                  ....*....|....*.
gi 767934614 2702 AVNDMGSASSSASLRV 2717
Cdd:cd20972    76 ATNSVGSDTTSAEIFV 91
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
2735-2992 5.71e-09

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 60.56  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2735 SFYSEVAELGRG-RFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDT-------------- 2799
Cdd:cd07854     5 SRYMDLRPLGCGsNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVYEVlgpsgsdltedvgs 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2800 -FETPTSYIlVLEMADQGrlLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVD-ESLakpTIKLAD 2877
Cdd:cd07854    85 lTELNSVYI-VQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDL---VLKIGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2878 FGDAVQLNTTY----YIHQLLGNPEFAAPEIILgNPVSLTS--DTWSVGVLTYVLLSGVS------------------PF 2933
Cdd:cd07854   159 FGLARIVDPHYshkgYLSEGLVTKWYRSPRLLL-SPNNYTKaiDMWAAGCIFAEMLTGKPlfagaheleqmqlilesvPV 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 2934 LDDSVEETCLNI----CRLDFSFPDDYFK----GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd07854   238 VREEDRNELLNVipsfVRNDGGEPRRPLRdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
2729-2981 6.31e-09

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 60.09  E-value: 6.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVaELGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIl 2808
Cdd:cd05069     7 WEIPRESLRLDV-KLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYI- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDcVVRWGS---LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQL- 2884
Cdd:cd05069    84 VTEFMGKGSLLD-FLKEGDgkyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNL---VCKIADFGLARLIe 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2885 NTTYYIHQLLGNP-EFAAPEIILGNPVSLTSDTWSVGVL-TYVLLSGVSPFlDDSVEETCLNICRLDFSFPDDyfKGVSQ 2962
Cdd:cd05069   160 DNEYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILlTELVTKGRVPY-PGMVNREVLEQVERGYRMPCP--QGCPE 236
                         250
                  ....*....|....*....
gi 767934614 2963 KAKEFVCFLLQEDPAKRPS 2981
Cdd:cd05069   237 SLHELMKLCWKKDPDERPT 255
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
2626-2717 9.93e-09

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 54.77  E-value: 9.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVND 2705
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                          90
                  ....*....|..
gi 767934614 2706 MGSASSSASLRV 2717
Cdd:cd05892    81 AGVVSCNARLDV 92
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
2833-2991 1.03e-08

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 59.76  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2833 IRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlaKPTIKLADFGDAVQLNT--TYYIHQLLGNPEFAAPE-IILGN- 2908
Cdd:cd14013   122 IKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEG--DGQFKIIDLGAAADLRIgiNYIPKEFLLDPRYAPPEqYIMSTq 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2909 -------PVSLT-------------SDTWSVGVltyVLLSGVSPFL--DDSVEETCLNICRLDFSFP-----------DD 2955
Cdd:cd14013   200 tpsappaPVAAAlspvlwqmnlpdrFDMYSAGV---ILLQMAFPNLrsDSNLIAFNRQLKQCDYDLNawrmlveprasAD 276
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2956 YFKGVS------QKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd14013   277 LREGFEildlddGAGWDLVTKLIRYKPRGRLSASAALAHPYF 318
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
2729-2922 1.50e-08

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 58.93  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEVaELGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIl 2808
Cdd:cd05071     4 WEIPRESLRLEV-KLGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYI- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCVVRWGS--LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQL-N 2885
Cdd:cd05071    81 VTEYMSKGSLLDFLKGEMGkyLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENL---VCKVADFGLARLIeD 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767934614 2886 TTYYIHQLLGNP-EFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd05071   158 NEYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGIL 195
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
1420-1533 1.50e-08

unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest isoform is composed of 53 immunoglobulin (Ig) domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains at its N-terminus, and 2 protein kinase domains (PK1 and PK2) at its C-terminus. unc-89 mutants display disorganization of muscle A-bands, and usually lack M-lines. The COOH-terminal region of obscurin, the human homolog of unc89, interacts via two specific Ig-like domains with the NH(2)-terminal Z-disk region of titin, a protein that connects the Z line to the M line in the sarcomere and contributes to the contraction of striated muscle. obscurin is also thought to be involved in Ca2+/calmodulin via its IQ domains, as well as G protein-coupled signal transduction in the sarcomere via its RhoGEF/DH domain. The DH-PH region of OBSCN and unc89, the C. elegans homolog, has exchange activity for RhoA and Rho-1 respectively, but not for the small GTPases homologous to Cdc42 or Rac. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270134  Cd Length: 114  Bit Score: 55.05  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1420 NIESQGELILQESFQVWDPKTlirKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHvEGDPCKFALW 1499
Cdd:cd13325     2 NIHKLGRLLRHDWFTVTDGEG---KAKERYLFLFKSRILITKVRRISEDRSVFILKDIIRLPEVNVKQH-PDDERTFELQ 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767934614 1500 VGRTPTSDNKIVLKASSIENKQDWIKHIREVIQE 1533
Cdd:cd13325    78 PKLPAFGILPIDFKAHKDEIKDYWLNEIEEYAND 111
CRAL_TRIO pfam00650
CRAL/TRIO domain;
20-145 1.52e-08

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 56.11  E-value: 1.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    20 GRDKRGGPILTF-PARSNHDRIRQEDLRRLISYLACI---PSEEVCKRGFTVIVDMRGSK--------WDSIKPLLKILQ 87
Cdd:pfam00650    8 GRDKEGRPVLYLrLGRHDPKKSSEEELVRFLVLVLERallLMPEGQVEGLTVIIDLKGLSlsnmdwwsISLLKKIIKILQ 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934614    88 ESFPCCIHVALIIKPD---NFWQKQRTNFGS----SKFEFeTNMVSLEGLTKVVDPSQLTPEFDG 145
Cdd:pfam00650   88 DNYPERLGKILIVNAPwifNTIWKLIKPFLDpktrEKIVF-LKNSNEEELEKYIPPEQLPKEYGG 151
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
2734-2920 1.56e-08

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 59.31  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2734 DSFYSEVAELGRGRFSVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLDTFETPTS--- 2805
Cdd:cd07858     4 DTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKkianaFDNRIDAKR--TLREIKLLRHLDHENVIAIKDIMPPPHReaf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2806 ---YIlVLEMADQGrlLDCVVRWG-SLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG-- 2879
Cdd:cd07858    82 ndvYI-VYELMDTD--LHQIIRSSqTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLN---ANCDLKICDFGla 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 767934614 2880 ----DAVQLNTTYYIHQLlgnpeFAAPEIILGNPVSLTS-DTWSVG 2920
Cdd:cd07858   156 rttsEKGDFMTEYVVTRW-----YRAPELLLNCSEYTTAiDVWSVG 196
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1899-2076 1.72e-08

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 60.68  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1899 EMEERKSSSLKRRHYVLQELVETERDYVRDLGYVVEGYMALMKE-DGVPDDMKGK-DKIVFGNIHQIYDWHRDFfLGELE 1976
Cdd:COG5422   473 EVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEEsNIIPENARRNfIKHVFANINEIYAVNSKL-LKALT 551
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1977 K--CLED-PEKLGSLFVKHERRLHMYIAYCQNKP------KSEHIVSEYIDTFFED-LKQRLGHRLQLTDLLIKPVQRIM 2046
Cdd:COG5422   552 NrqCLSPiVNGIADIFLDYVPKFEPFIKYGASQPyakyefEREKSVNPNFARFDHEvERLDESRKLELDGYLTKPTTRLA 631
                         170       180       190
                  ....*....|....*....|....*....|
gi 767934614 2047 KYQLLLKDFLKYSKKASLDTSELERAVEVM 2076
Cdd:COG5422   632 RYPLLLEEVLKFTDPDNPDTEDIPKVIDML 661
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
2742-2928 1.73e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 58.49  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCD----QKGTKRAVATKFVNKKLMK--RDqVTHELGILQSLQHPLLVGLLDTFETP--TSYILVLEMA 2813
Cdd:cd14205    11 QLGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTEEhlRD-FEREIEILKSLQHDNIVKYKGVCYSAgrRNLRLIMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2814 DQGRLLDCVVRWGS-LTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFG--DAVQLNTTYYI 2890
Cdd:cd14205    90 PYGSLRDYLQKHKErIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENEN---RVKIGDFGltKVLPQDKEYYK 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767934614 2891 HQLLG-NPEF-AAPEIILGNPVSLTSDTWSVGVLTYVLLS 2928
Cdd:cd14205   167 VKEPGeSPIFwYAPESLTESKFSVASDVWSFGVVLYELFT 206
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
2631-2717 1.92e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 54.05  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2631 PLSEVTCETGETVVLRCRVCGRPKASITWK--------GPEHNTLNNDGhysisysdlgeATLKIVGVTTEDDGIYTCIA 2702
Cdd:cd20970     8 PSFTVTAREGENATFMCRAEGSPEPEISWTrngnliieFNTRYIVRENG-----------TTLTIRNIRRSDMGIYLCIA 76
                          90
                  ....*....|....*.
gi 767934614 2703 VNDM-GSASSSASLRV 2717
Cdd:cd20970    77 SNGVpGSVEKRITLQV 92
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
2743-2933 1.96e-08

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 57.83  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGtkRAVATKFVNKKLMKRDQVThELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDC- 2821
Cdd:cd14058     1 VGRGSFGVVCKARWRN--QIVAVKIIESESEKKAFEV-EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2822 ---VVRWGSLTEGKIRAHLgEVLEAVRYLHNCR---IAHLDLKPENILVdesLAKPT-IKLADFGDAVQLNTtyYIHQLL 2894
Cdd:cd14058    78 hgkEPKPIYTAAHAMSWAL-QCAKGVAYLHSMKpkaLIHRDLKPPNLLL---TNGGTvLKICDFGTACDIST--HMTNNK 151
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767934614 2895 GNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14058   152 GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2270-2478 2.03e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 60.27  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2270 GAPSTSRSRPSRIPQPVRHHPPVlvssaassqaeadkmsgtSTPGPSLPPPGAAPEAGPSAPSRRPPGADAEGSereaep 2349
Cdd:PRK12323  372 AGPATAAAAPVAQPAPAAAAPAA------------------AAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS------ 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2350 iPKMKVLESPRKGAANASGSSPDAPAKDARAslgtlPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKGGSFWSS 2429
Cdd:PRK12323  428 -PAPEALAAARQASARGPGGAPAPAPAPAAA-----PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEE 501
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2430 IPASPASRPGSFTFPGDSDSLQRQTPRHAAPGKDTDRMSTCSSASEQSV 2478
Cdd:PRK12323  502 LPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPA 550
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2743-2928 2.25e-08

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 58.19  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKrAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGL--LDTFETPTsYIlVLEMADQGRLLD 2820
Cdd:cd05068    16 LGSGQFGEVWEGLWNNTT-PVAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLyaVCTLEEPI-YI-ITELMKHGSLLE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVvrwgsltEGKIRA-HL-------GEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA--VQLNTTYYI 2890
Cdd:cd05068    93 YL-------QGKGRSlQLpqlidmaAQVASGMAYLESQNYIHRDLAARNVLVGENN---ICKVADFGLArvIKVEDEYEA 162
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767934614 2891 HQLLGNP-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS 2928
Cdd:cd05068   163 REGAKFPiKWTAPEAANYNRFSIKSDVWSFGILLTEIVT 201
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
2743-2933 2.27e-08

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 57.82  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLD--TFETPtsYILVLEMADQGRLLD 2820
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGvcTREPP--FYIITEFMPYGNLLD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRW--GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESlakPTIKLADFGDA-VQLNTTYYIHQLLGNP 2897
Cdd:cd05052    92 YLRECnrEELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGEN---HLVKVADFGLSrLMTGDTYTAHAGAKFP 168
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767934614 2898 -EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05052   169 iKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPY 206
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
2842-2933 2.28e-08

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 58.10  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2842 EAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV---QLNTTYYIHQLLGNPEFAAPEIIL---GNPVSLTSD 2915
Cdd:cd14150   107 QGMDYLHAKNIIHRDLKSNNIFLHEGL---TVKIGDFGLATvktRWSGSQQVEQPSGSILWMAPEVIRmqdTNPYSFQSD 183
                          90
                  ....*....|....*...
gi 767934614 2916 TWSVGVLTYVLLSGVSPF 2933
Cdd:cd14150   184 VYAYGVVLYELMSGTLPY 201
PHA03247 PHA03247
large tegument protein UL36; Provisional
2271-2437 2.36e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 60.34  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRPSRIPQPVRHHPPvlvssaaSSQAEADKMSGTSTPGPSLPPPGAAPEAGPSAPSRRPPgadaeGSEREAEPI 2350
Cdd:PHA03247 2644 PTVPPPERPRDDPAPGRVSRP-------RRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPP-----PPPPTPEPA 2711
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2351 PKMKVLESPRK-GAANASGSSPDAPAKDARASLGTLPL--GKPRAGAASPLNS-PLSSAVPSLGKEPFPPSSPLQKGGSF 2426
Cdd:PHA03247 2712 PHALVSATPLPpGPAAARQASPALPAAPAPPAVPAGPAtpGGPARPARPPTTAgPPAPAPPAAPAAGPPRRLTRPAVASL 2791
                         170
                  ....*....|.
gi 767934614 2427 WSSIPASPASR 2437
Cdd:PHA03247 2792 SESRESLPSPW 2802
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
2737-2933 2.54e-08

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 58.05  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd07870     2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTaiREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdESLAKptIKLADFG--DAVQLNTTYYIHQ 2892
Cdd:cd07870    82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLI-SYLGE--LKLADFGlaRAKSIPSQTYSSE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2893 LLgNPEFAAPEIILG-NPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd07870   159 VV-TLWYRPPDVLLGaTDYSSALDIWGAGCIFIEMLQGQPAF 199
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
2737-2920 2.85e-08

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 58.32  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKC-DQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHP------LLVGLLDTFETPTSYILV 2809
Cdd:cd14213    14 YEIVDTLGEGAFGKVVECiDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTdpnstfRCVQMLEWFDHHGHVCIV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRLlDCVVRWGSLT--EGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDES----------------LAKP 2871
Cdd:cd14213    94 FELLGLSTY-DFIKENSFLPfpIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSdyvvkynpkmkrdertLKNP 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2872 TIKLADFGDAvqlntTY---YIHQLLGNPEFAAPEIILGNPVSLTSDTWSVG 2920
Cdd:cd14213   173 DIKVVDFGSA-----TYddeHHSTLVSTRHYRAPEVILALGWSQPCDVWSIG 219
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2272-2474 2.97e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 59.80  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2272 PSTSRSRPSRIPQPVRHHPPVLVSSAASSQAEADKMSgTSTPGPSLPPPGAAPeaGPSAPSRRPPGADAEGSEREAEPIP 2351
Cdd:PHA03307   75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGP-SSPDPPPPTPPPASP--PPSPAPDLSEMLRPVGSPGPPPAAS 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2352 KMKVLESPRKGAANASGSSPDAPAKD-----ARAS---LGTLPLGKPRAGAA-------SPLNSPLSSAVPSLGKEP-FP 2415
Cdd:PHA03307  152 PPAAGASPAAVASDAASSRQAALPLSspeetARAPsspPAEPPPSTPPAAASprpprrsSPISASASSPAPAPGRSAaDD 231
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2416 P------SSPLQKGGSFWSSIPASPASRPGSFTFPGdsdslqrqTPRHAAPGKDTDRMSTCSSAS 2474
Cdd:PHA03307  232 AgasssdSSSSESSGCGWGPENECPLPRPAPITLPT--------RIWEASGWNGPSSRPGPASSS 288
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
1410-1534 3.05e-08

Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269931  Cd Length: 138  Bit Score: 54.96  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1410 HLSMLEGFDENIES-QGELILQESFQVWDPKTL--IRKGR--ERHLFLFEMSLVFSKevKDSSGRSKYLYKSKLFTSELG 1484
Cdd:cd01224     3 NLEKLAAWQSTVEGwEGEDLSDRSSELIHSGELtkISAGRaqERTFFLFDHQLVYCK--KDLLRRKNYIYKGRIDTDNME 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 1485 V------TEHVEGDPCKFALWVGRtpTSDNK-IVLKASSIENKQDWIKHIREviqER 1534
Cdd:cd01224    81 IedlpdgKDDESGVTVKNAWKIYN--ASKNKwYVLCAKSAEEKQRWLEAFAE---ER 132
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
2742-2988 3.40e-08

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 57.25  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLL 2819
Cdd:cd05084     3 RIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPdlKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 DCVVRWGSLTEGKIRAHLGE-VLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYY-----IHQL 2893
Cdd:cd05084    83 TFLRTEGPRLKVKELIRMVEnAAAGMEYLESKHCIHRDLAARNCLVTE---KNVLKISDFGMSREEEDGVYaatggMKQI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2894 lgnP-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEET-----------CLNICrldfsfPDDYFKGV 2960
Cdd:cd05084   160 ---PvKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTreaveqgvrlpCPENC------PDEVYRLM 230
                         250       260
                  ....*....|....*....|....*...
gi 767934614 2961 SQkakefvCFllQEDPAKRPSAALALQE 2988
Cdd:cd05084   231 EQ------CW--EYDPRKRPSFSTVHQD 250
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
2818-2982 4.31e-08

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 57.33  E-value: 4.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVRWGsltegkirahLGEVLEAVRYLHN-CRIAHLDLKPENILVDESLAkptIKLADFGDAVQL----NTTYYIHQ 2892
Cdd:cd14011   111 LYDVEIKYG----------LLQISEALSFLHNdVKLVHGNICPESVVINSNGE---WKLAGFDFCISSeqatDQFPYFRE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2893 --------LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDdsveetclniCRLDFSFPDDY-------- 2956
Cdd:cd14011   178 ydpnlpplAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFD----------CVNNLLSYKKNsnqlrqls 247
                         170       180
                  ....*....|....*....|....*....
gi 767934614 2957 ---FKGVSQKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd14011   248 lslLEKVPEELRDHVKTLLNVTPEVRPDA 276
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
2743-2933 4.44e-08

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 57.38  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTkraVATKFVNKKLMKRDQVT---HELGILQSLQHPLLVgLLDTFETPTSYILVLEMADQGRLl 2819
Cdd:cd14151    16 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQafkNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2820 dcvvrWGSLTEGKIRAHLGEVLEAVR-------YLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV---QLNTTYY 2889
Cdd:cd14151    91 -----YHHLHIIETKFEMIKLIDIARqtaqgmdYLHAKSIIHRDLKSNNIFLHEDL---TVKIGDFGLATvksRWSGSHQ 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2890 IHQLLGNPEFAAPEIIL---GNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14151   163 FEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 209
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2739-2981 4.57e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 57.37  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAELGRGRFSVVKKCDQKGTKRAVATK----FVNKKLMKRDQVTHELgILQSLQHPLLV---GLLdtFETPTSYIlVLE 2811
Cdd:cd06616    10 DLGEIGRGAFGTVNKMLHKPSGTIMAVKrirsTVDEKEQKRLLMDLDV-VMRSSDCPYIVkfyGAL--FREGDCWI-CME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2812 MADQGrlLDCVVRwgsLTEGKIRAHLGE---------VLEAVRYLHN-CRIAHLDLKPENILVDESLAkptIKLADFGDA 2881
Cdd:cd06616    86 LMDIS--LDKFYK---YVYEVLDSVIPEeilgkiavaTVKALNYLKEeLKIIHRDVKPSNILLDRNGN---IKLCDFGIS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 VQLNTTYYIHQLLGNPEFAAPEIILGN----PVSLTSDTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICRLDFS-FPDD 2955
Cdd:cd06616   158 GQLVDSIAKTRDAGCRPYMAPERIDPSasrdGYDVRSDVWSLGITLYEVATGKFPYPKwNSVFDQLTQVVKGDPPiLSNS 237
                         250       260
                  ....*....|....*....|....*.
gi 767934614 2956 YFKGVSQKAKEFVCFLLQEDPAKRPS 2981
Cdd:cd06616   238 EEREFSPSFVNFVNLCLIKDESKRPK 263
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
2737-2933 5.15e-08

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 57.71  E-value: 5.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKC-DQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHP------LLVGLLDTFETPTSYILV 2809
Cdd:cd14214    15 YEIVGDLGEGTFGKVVEClDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKdkenkfLCVLMSDWFNFHGHMCIA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGR---LLDCVVRWGSLTEgkIRAHLGEVLEAVRYLHNCRIAHLDLKPENILV----------------DESLAK 2870
Cdd:cd14214    95 FELLGKNTfefLKENNFQPYPLPH--IRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlynesksceEKSVKN 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2871 PTIKLADFGDAV---QLNTTyyihqLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14214   173 TSIRVADFGSATfdhEHHTT-----IVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLF 233
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
849-940 5.43e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.09  E-value: 5.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   849 QLRHLQAEVKQVLGWIRNGESMLNAGLItASSLQEAEQLQREHEQFQHAIEkTHQSALQ-VQQKAEAMLQANHYDMDMIR 927
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEIQ 79
                           90
                   ....*....|...
gi 767934614   928 DCAEKVASHWQQL 940
Cdd:pfam00435   80 ERLEELNERWEQL 92
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
2729-2933 5.50e-08

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 57.00  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2729 WKDNFDSFYSEvAELGRGRFSVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYIl 2808
Cdd:cd05070     4 WEIPRESLQLI-KRLGNGQFGEVWMGTWNGNTK-VAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYI- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCvvrwgsLTEGKIRA--------HLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGD 2880
Cdd:cd05070    81 VTEYMSKGSLLDF------LKDGEGRAlklpnlvdMAAQVAAGMAYIERMNYIHRDLRSANILVGNGL---ICKIADFGL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2881 AVQL-NTTYYIHQLLGNP-EFAAPEIILGNPVSLTSDTWSVGV-LTYVLLSGVSPF 2933
Cdd:cd05070   152 ARLIeDNEYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGIlLTELVTKGRVPY 207
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
2742-2933 5.56e-08

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 56.96  E-value: 5.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCD-QKGTKraVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVlEMADQGRLLD 2820
Cdd:cd05073    18 KLGAGQFGEVWMATyNKHTK--VAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIIT-EFMAKGSLLD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVvrwgSLTEG------KIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQLNTTYYIHQLL 2894
Cdd:cd05073    95 FL----KSDEGskqplpKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASL---VCKIADFGLARVIEDNEYTAREG 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2895 GN-P-EFAAPEIILGNPVSLTSDTWSVGV-LTYVLLSGVSPF 2933
Cdd:cd05073   168 AKfPiKWTAPEAINFGSFTIKSDVWSFGIlLMEIVTYGRIPY 209
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
2625-2717 7.23e-08

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 52.63  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2625 PPEFVIPLSEV--TCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYsDLGEATlkIVGVTTEDDGIYTCIA 2702
Cdd:cd05730     1 PPTIRARQSEVnaTANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNE-DGSEMT--ILDVDKLDEAEYTCIA 77
                          90
                  ....*....|....*
gi 767934614 2703 VNDMGSASSSASLRV 2717
Cdd:cd05730    78 ENKAGEQEAEIHLKV 92
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
2736-2934 7.71e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 56.45  E-value: 7.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRF-SVVKKC---DQKGTKRAVATKFVNKK--LMKRDQVTHELGILQSLQHPLLVGLLDTFETP--TSYI 2807
Cdd:cd05080     5 YLKKIRDLGEGHFgKVSLYCydpTNDGTGEMVAVKALKADcgPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMADQGRLLDCVVRwGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFG--DAVQLN 2885
Cdd:cd05080    85 LIMEYVPLGSLRDYLPK-HSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDN---DRLVKIGDFGlaKAVPEG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2886 TTYY-IHQLLGNPEF-AAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFL 2934
Cdd:cd05080   161 HEYYrVREDGDSPVFwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQ 211
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
2630-2715 7.79e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 52.20  E-value: 7.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2630 IPLSEVTCETGETVVLRCRV-CGRPKASITWKGpEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVNDMGS 2708
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSK-EGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                   ....*..
gi 767934614  2709 ASSSASL 2715
Cdd:pfam00047   80 ATLSTSL 86
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
2739-2983 8.26e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 56.47  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAELGRGRFSVVKKCDQ---------KGTKRAVAtKFVNKKLMKRDQVTHE-LGilqslQHPLLVGLLDTFETPTSYIL 2808
Cdd:cd14139     4 ELEKIGVGEFGSVYKCIKrldgcvyaiKRSMRPFA-GSSNEQLALHEVYAHAvLG-----HHPHVVRYYSAWAEDDHMII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCVVRWGSL----TEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILV------------------DE 2866
Cdd:cd14139    78 QNEYCNGGSLQDAISENTKSgnhfEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIchkmqsssgvgeevsneeDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2867 SLAKPTI-KLADFGDAVQLNTTYYIHqllGNPEFAAPEIILGNPVSL-TSDTWSVGvLTYVLLSGVSPFLDDSVEETCLN 2944
Cdd:cd14139   158 FLSANVVyKIGDLGHVTSINKPQVEE---GDSRFLANEILQEDYRHLpKADIFALG-LTVALAAGAEPLPTNGAAWHHIR 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767934614 2945 icrlDFSFPDDYFKgVSQKAKEFVCFLLQEDPAKRPSAA 2983
Cdd:cd14139   234 ----KGNFPDVPQE-LPESFSSLLKNMIQPDPEQRPSAT 267
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1446-1531 9.15e-08

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 52.56  E-value: 9.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1446 RERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALWVGrTPTSDNKIVLKASSIENKQ 1521
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94
                           90
                   ....*....|
gi 767934614  1522 DWIKHIREVI 1531
Cdd:pfam00169   95 DWIKAIQSAI 104
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
2631-2717 9.18e-08

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 51.64  E-value: 9.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2631 PLSEVTCETGETVVLRCRVCGRPKASITWKgPEHNTLNNDghySISYSDLGEaTLKIVGVTTEDDGIYTCIAVNDMGSAS 2710
Cdd:cd05731     1 SESSTMVLRGGVLLLECIAEGLPTPDIRWI-KLGGELPKG---RTKFENFNK-TLKIENVSEADSGEYQCTASNTMGSAR 75

                  ....*..
gi 767934614 2711 SSASLRV 2717
Cdd:cd05731    76 HTISVTV 82
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
2760-2984 9.91e-08

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 56.24  E-value: 9.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2760 KRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIR-AHLG 2838
Cdd:cd13992    25 GRTVAIKHITFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKsSFIK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2839 EVLEAVRYLHNCRI-AHLDLKPENILVDESLakpTIKLADFG-------DAVQLNTTYYIH-QLLgnpeFAAPEIILGNP 2909
Cdd:cd13992   105 DIVKGMNYLHSSSIgYHGRLKSSNCLVDSRW---VVKLTDFGlrnlleeQTNHQLDEDAQHkKLL----WTAPELLRGSL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2910 V----SLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSFPDDyFKGVSQKAKEFVCFLLQ---EDPAKRP 2980
Cdd:cd13992   178 LevrgTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVisGGNKPFRPEL-AVLLDEFPPRLVLLVKQcwaENPEKRP 256

                  ....
gi 767934614 2981 SAAL 2984
Cdd:cd13992   257 SFKQ 260
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
2839-2933 1.04e-07

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 56.19  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2839 EVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV---QLNTTYYIHQLLGNPEFAAPEIIL---GNPVSL 2912
Cdd:cd14149   116 QTAQGMDYLHAKNIIHRDMKSNNIFLHEGL---TVKIGDFGLATvksRWSGSQQVEQPTGSILWMAPEVIRmqdNNPFSF 192
                          90       100
                  ....*....|....*....|.
gi 767934614 2913 TSDTWSVGVLTYVLLSGVSPF 2933
Cdd:cd14149   193 QSDVYSYGIVLYELMTGELPY 213
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
2740-2936 1.10e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 56.81  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2740 VAELGrgrFSVVKKCdQKGTKRAVatkFVNKKLMKRDQVTHELG----------ILQSLQHPLLVGLLDTFETPTSYILV 2809
Cdd:PHA03209   63 VASLG---YTVIKTL-TPGSEGRV---FVATKPGQPDPVVLKIGqkgttlieamLLQNVNHPSVIRMKDTLVSGAITCMV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2810 LEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGdAVQLNTTY- 2888
Cdd:PHA03209  136 LPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFIND---VDQVCIGDLG-AAQFPVVAp 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767934614 2889 YIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDD 2936
Cdd:PHA03209  212 AFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFED 259
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
2765-2988 1.19e-07

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 55.98  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2765 TKFVNKKLMKRDQ-----VTHELGILQSLQ-HPLLVGLLDTFETP--------TSYILVLEMAdQGRLLDCVVRwgslTE 2830
Cdd:cd14036    26 KEYALKRLLSNEEeknkaIIQEINFMKKLSgHPNIVQFCSAASIGkeesdqgqAEYLLLTELC-KGQLVDFVKK----VE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2831 GKIRAHLGEVLE-------AVRYLHNCR--IAHLDLKPENILVDeslAKPTIKLADFG---------------------- 2879
Cdd:cd14036   101 APGPFSPDTVLKifyqtcrAVQHMHKQSppIIHRDLKIENLLIG---NQGQIKLCDFGsatteahypdyswsaqkrslve 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2880 DAVQLNTTyyihqllgnPEFAAPEII---LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVeetcLNICRLDFSFPddy 2956
Cdd:cd14036   178 DEITRNTT---------PMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEDGAK----LRIINAKYTIP--- 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767934614 2957 fkgvsQKAKEFVCF------LLQEDPAKRPSAALALQE 2988
Cdd:cd14036   242 -----PNDTQYTVFhdlirsTLKVNPEERLSITEIVEQ 274
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1424-1532 1.31e-07

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 52.17  E-value: 1.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   1424 QGELILQEsfqvwdpKTLIRKGRERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALW 1499
Cdd:smart00233    4 EGWLYKKS-------GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIK 73
                            90       100       110
                    ....*....|....*....|....*....|...
gi 767934614   1500 VGRTPTsdnkIVLKASSIENKQDWIKHIREVIQ 1532
Cdd:smart00233   74 TSDRKT----LLLQAESEEEREKWVEALRKAIA 102
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2743-2982 1.33e-07

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 56.04  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATK--FVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTF-ETPTS-----------YIl 2808
Cdd:cd14048    14 LGRGGFGVVFEAKNKVDDCNYAVKriRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWlERPPEgwqekmdevylYI- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2809 VLEMADQGRLLDCVVRWGSLTEGKIRAHLG---EVLEAVRYLHNCRIAHLDLKPENIL--VDEslakpTIKLADFGDAV- 2882
Cdd:cd14048    93 QMQLCRKENLKDWMNRRCTMESRELFVCLNifkQIASAVEYLHSKGLIHRDLKPSNVFfsLDD-----VVKVGDFGLVTa 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2883 -----------QLNTTYYIH-QLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSveETCLNICRLDf 2950
Cdd:cd14048   168 mdqgepeqtvlTPMPAYAKHtGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFSTQMERI--RTLTDVRKLK- 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767934614 2951 sFPDDYFKGVSQKAKeFVCFLLQEDPAKRPSA 2982
Cdd:cd14048   245 -FPALFTNKYPEERD-MVQQMLSPSPSERPEA 274
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
2895-2991 1.34e-07

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 55.44  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEII--LGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDyfkgVSQKAKEFVCFLL 2972
Cdd:cd14023   148 GCPAYVSPEILntTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDH----VSPKARCLIRSLL 223
                          90
                  ....*....|....*....
gi 767934614 2973 QEDPAKRPSAALALQEQWL 2991
Cdd:cd14023   224 RREPSERLTAPEILLHPWF 242
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
2743-2933 1.40e-07

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 55.53  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLD 2820
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPdlKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2821 CVVRWGS-LTEGKIRAHLGEVLEAVRYLH--NCriAHLDLKPENILVDEslaKPTIKLADFGDAVQLNTTYYIHQ--LLG 2895
Cdd:cd05041    83 FLRKKGArLTVKQLLQMCLDAAAGMEYLEskNC--IHRDLAARNCLVGE---NNVLKISDFGMSREEEDGEYTVSdgLKQ 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767934614 2896 NP-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05041   158 IPiKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPY 197
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
2742-2940 1.54e-07

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 55.84  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKKCD-----QKGTKRAVATKFVNKK-LMK-RDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd05048    12 ELGEGAFGKVYKGEllgpsSEESAISVAIKTLKENaSPKtQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLDCVVRWGSLTEGKIRAHLGEVLEAVR----------------YLHNCRIAHLDLKPENILVDESLakpTIKLADF 2878
Cdd:cd05048    92 HGDLHEFLVRHSPHSDVGVSSDDDGTASSLDqsdflhiaiqiaagmeYLSSHHYVHRDLAARNCLVGDGL---TVKISDF 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2879 GDAVQL-NTTYY--IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEE 2940
Cdd:cd05048   169 GLSRDIySSDYYrvQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQE 234
SPEC smart00150
Spectrin repeats;
162-278 1.58e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 1.58e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    162 EDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKKKV--IKAPIEDLDLEGQKLLQriqssesfpkknSG 239
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE------------EG 68
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 767934614    240 SGNAdlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLD 278
Cdd:smart00150   69 HPDA------EEIEERLEELNERWEELKELAEERRQKLE 101
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
2737-2991 1.61e-07

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 55.96  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2737 YSEVAELGRGRFSVVKKCDQKGTKRAVATKFV---NKKLMKRDQVTHELGILQSLQHPLLVGL----------LDTFETP 2803
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldNEKEGFPITAIREIKILRQLNHRSVVNLkeivtdkqdaLDFKKDK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2804 TSYILVLEMADQ---GRLLDCVVrwgSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGD 2880
Cdd:cd07864    89 GAFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNN---KGQIKLADFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2881 AVQLNT------TYYIHQLLGNPefaaPEIILGNPVSLTS-DTWSVGVLTYVLLSGvSPFLDDSVE----ETCLNIC--- 2946
Cdd:cd07864   163 ARLYNSeesrpyTNKVITLWYRP----PELLLGEERYGPAiDVWSCGCILGELFTK-KPIFQANQElaqlELISRLCgsp 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2947 ---------------------------RLDFSFpddyfkgVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd07864   238 cpavwpdviklpyfntmkpkkqyrrrlREEFSF-------IPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2636-2717 1.75e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 51.38  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2636 TCETGETVVLRCRVCGRPKASITW-KGPEHntLNNDGHYSIsysdLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSAS 2714
Cdd:cd20957    12 TVDFGRTAVFNCSVTGNPIHTVLWmKDGKP--LGHSSRVQI----LSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAE 85

                  ...
gi 767934614 2715 LRV 2717
Cdd:cd20957    86 LKL 88
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
1603-1653 1.77e-07

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 49.77  E-value: 1.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767934614 1603 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRSpaaEGLVP 1653
Cdd:cd00174     3 RALYDYEAQDDDELSFKKGDIITVLEKDDD--GWWEGELNGGR---EGLFP 48
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2272-2474 2.40e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.10  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2272 PSTSRSRPSRIPQPVRHHPPVlvssaASSQAEADKMSGTSTPGP--SLPPPGAAPEAGPSAPSRRPPGADAEGS-EREAE 2348
Cdd:PHA03307  110 GPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPPaaSPPAAGASPAAVASDAASSRQAALPLSSpEETAR 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2349 PIPKMKVLESPRKGAANASGSSP--DAPAKDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLG-----KEPFPPSSPLQ 2421
Cdd:PHA03307  185 APSSPPAEPPPSTPPAAASPRPPrrSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGwgpenECPLPRPAPIT 264
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2422 KGGSFWSSIPASPASRPGSFTFPGDSDSlqrqtPRHAAPGKDTDRMSTCSSAS 2474
Cdd:PHA03307  265 LPTRIWEASGWNGPSSRPGPASSSSSPR-----ERSPSPSPSSPGSGPAPSSP 312
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
1442-1527 2.44e-07

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 51.00  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1442 IRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKsklFTSELGVTEHVEGD-PCKFALWVgrtpTSDNKIVLKASSIENK 1520
Cdd:cd00821    13 LKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIP---LSGILEVEEVSPKErPHCFELVT----PDGRTYYLQADSEEER 85

                  ....*..
gi 767934614 1521 QDWIKHI 1527
Cdd:cd00821    86 QEWLKAL 92
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1603-1654 2.54e-07

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 49.46  E-value: 2.54e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767934614   1603 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRspaAEGLVPC 1654
Cdd:smart00326    6 RALYDYTAQDPDELSFKKGDIITVLEKSDD--GWWKGRLGRG---KEGLFPS 52
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
2736-2990 2.67e-07

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 55.37  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKCDQKGTKRavaTKFVNKKLMKRDQVTH---------ELGILQSLQHPLLVGLLDTFETPT-- 2804
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKNGKD---GKEYAIKKFKGDKEQYtgisqsacrEIALLRELKHENVVSLVEVFLEHAdk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2805 SYILVLEMADQGrlLDCVVRW------GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DESLAKPTIKLAD 2877
Cdd:cd07842    78 SVYLLFDYAEHD--LWQIIKFhrqakrVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmGEGPERGVVKIGD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2878 FGDAVQLNTTyyIHQLL-GNPE-----FAAPEIILGNPvSLTS--DTWSVGVLTYVLLSGV-------------SPFLDD 2936
Cdd:cd07842   156 LGLARLFNAP--LKPLAdLDPVvvtiwYRAPELLLGAR-HYTKaiDIWAIGCIFAELLTLEpifkgreakikksNPFQRD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2937 SVEEtclnICRLdFSFPDD--------------------------------YFKGVSQKAKEFVCF--LLQEDPAKRPSA 2982
Cdd:cd07842   233 QLER----IFEV-LGTPTEkdwpdikkmpeydtlksdtkastypnsllakwMHKHKKPDSQGFDLLrkLLEYDPTKRITA 307

                  ....*...
gi 767934614 2983 ALALQEQW 2990
Cdd:cd07842   308 EEALEHPY 315
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
2626-2717 2.87e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 50.87  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVND 2705
Cdd:cd05893     1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                          90
                  ....*....|..
gi 767934614 2706 MGSASSSASLRV 2717
Cdd:cd05893    81 QGRISCTGRLMV 92
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
2634-2717 2.87e-07

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 50.85  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2634 EVTCETGETVVLRCRVCGRPKASITWKGPEHNTLN---NDGHYSISysdlgEATLKIVGVTTEDDGIYTCIAVNDMGSAS 2710
Cdd:cd20969    11 QVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSaksNGRLTVFP-----DGTLEVRYAQVQDNGTYLCIAANAGGNDS 85

                  ....*..
gi 767934614 2711 SSASLRV 2717
Cdd:cd20969    86 MPAHLHV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
2626-2718 2.93e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.81  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITW-KGPEHNTLNNDGHYSISYSDlGEATLKIVGVTTEDDGIYTCIAVN 2704
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWfRDGQVISTSTLPGVQISFSD-GRAKLSIPAVTKANSGRYSLTATN 79
                          90
                  ....*....|....
gi 767934614 2705 DMGSASSSASLRVL 2718
Cdd:cd20974    80 GSGQATSTAELLVL 93
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
2732-2992 3.15e-07

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 55.39  E-value: 3.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2732 NFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATK----FVNKKLMKRdqVTHELGILQSLQHPLLVGLLD-----TFET 2802
Cdd:cd07849     2 DVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKkispFEHQTYCLR--TLREIKILLRFKHENIIGILDiqrppTFES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PTSYILVLEMADQGrlLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA- 2881
Cdd:cd07849    80 FKDVYIVQELMETD--LYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNC---DLKICDFGLAr 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2882 VQLNTTYYIHQLLgnpEFA------APEIILGNPVSLTS-DTWSVGVLTYVLLSGV--------------------SPFL 2934
Cdd:cd07849   155 IADPEHDHTGFLT---EYVatrwyrAPEIMLNSKGYTKAiDIWSVGCILAEMLSNRplfpgkdylhqlnlilgilgTPSQ 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767934614 2935 DDSveETCLNICRLDF--SFP-------DDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 2992
Cdd:cd07849   232 EDL--NCIISLKARNYikSLPfkpkvpwNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLE 296
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
2780-2934 3.17e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 54.59  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2780 HELGILQSLQHPLLVGLLDTFETPTSYilVLEMADQGRLldcvvrwGSLTEGKIRAH----LGEVL---------EAVRY 2846
Cdd:cd14067    59 QEASMLHSLQHPCIVYLIGISIHPLCF--ALELAPLGSL-------NTVLEENHKGSsfmpLGHMLtfkiayqiaAGLAY 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2847 LHNCRIAHLDLKPENILV---DESLAKpTIKLADFGDAVQlnttyYIHQ----LLGNPEFAAPEIILGNPVSLTSDTWSV 2919
Cdd:cd14067   130 LHKKNIIFCDLKSDNILVwslDVQEHI-NIKLSDYGISRQ-----SFHEgalgVEGTPGYQAPEIRPRIVYDEKVDMFSY 203
                         170
                  ....*....|....*
gi 767934614 2920 GVLTYVLLSGVSPFL 2934
Cdd:cd14067   204 GMVLYELLSGQRPSL 218
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
2625-2717 3.86e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 50.33  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2625 PPEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKgPEHNTLNNDGHYSISYSDLGEatLKIVGVTTEDDGIYTCIAVN 2704
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWI-RNAQPLQYAADRSTCEAGVGE--LHIQDVLPEDHGTYTCLAKN 77
                          90
                  ....*....|...
gi 767934614 2705 DMGSASSSASLRV 2717
Cdd:cd20976    78 AAGQVSCSAWVTV 90
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
2746-2990 3.93e-07

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 54.54  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2746 GRFSVVKKCDQKGTKRAVATKFVnkKLMKRDQ---VT--HELGILQSLQHPLLVGLLDTF--ETPTSYILVLEMA--DQG 2816
Cdd:cd07843    16 GTYGVVYRARDKKTGEIVALKKL--KMEKEKEgfpITslREINILLKLQHPNIVTVKEVVvgSNLDKIYMVMEYVehDLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDcvVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDEslaKPTIKLADFGDA--VQLNTTYYIhQLL 2894
Cdd:cd07843    94 SLME--TMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNN---RGILKICDFGLAreYGSPLKPYT-QLV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2895 GNPEFAAPEIILGNPVSLTS-DTWSVGVLTYVLLSGvSPFLDDSVEETCLN-ICRL-----DFSFPdDYFKGVSQKAKEF 2967
Cdd:cd07843   168 VTLWYRAPELLLGAKEYSTAiDMWSVGCIFAELLTK-KPLFPGKSEIDQLNkIFKLlgtptEKIWP-GFSELPGAKKKTF 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2968 V------------------------CFLLQEDPAKRPSAALALQEQW 2990
Cdd:cd07843   246 TkypynqlrkkfpalslsdngfdllNRLLTYDPAKRISAEDALKHPY 292
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
2743-2922 4.00e-07

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 54.06  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQKGTKRAVATKfVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCV 2822
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVK-IYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2823 VRWGSLTEGKIRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQL-----NTTYYIHQLLGN 2896
Cdd:cd14156    80 AREELPLSWREKVELAcDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVgempaNDPERKLSLVGS 159
                         170       180
                  ....*....|....*....|....*.
gi 767934614 2897 PEFAAPEIILGNPVSLTSDTWSVGVL 2922
Cdd:cd14156   160 AFWMAPEMLRGEPYDRKVDVFSFGIV 185
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
2635-2707 4.09e-07

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 50.29  E-value: 4.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2635 VTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDgHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVNDMG 2707
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSE-HYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYG 82
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
2736-2928 4.13e-07

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 54.55  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2736 FYSEVAELGRGRFSVVKKC------DQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGL--LDTFETPTSYI 2807
Cdd:cd05079     5 FLKRIRDLGEGHFGKVELCrydpegDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYkgICTEDGGNGIK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2808 LVLEMADQGRLLDCVVRwgslTEGKIR-----AHLGEVLEAVRYLHNCRIAHLDLKPENILVDeslAKPTIKLADFG--D 2880
Cdd:cd05079    85 LIMEFLPSGSLKEYLPR----NKNKINlkqqlKYAVQICKGMDYLGSRQYVHRDLAARNVLVE---SEHQVKIGDFGltK 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767934614 2881 AVQLNTTYY-IHQLLGNPEF-AAPEIILGNPVSLTSDTWSVGVLTYVLLS 2928
Cdd:cd05079   158 AIETDKEYYtVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLT 207
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
2789-2991 4.51e-07

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 53.59  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2789 QHPLLVGLLDTFeTPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPEN-ILVDEs 2867
Cdd:cd13976    43 SHPNISGVHEVI-AGETKAYVFFERDHGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKfVFADE- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2868 lAKPTIKLADFGDAVQLN-TTYYIHQLLGNPEFAAPEIIlgNPVSLTS----DTWSVGVLTYVLLSGVSPFLDDSVEETC 2942
Cdd:cd13976   121 -ERTKLRLESLEDAVILEgEDDSLSDKHGCPAYVSPEIL--NSGATYSgkaaDVWSLGVILYTMLVGRYPFHDSEPASLF 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2943 LNICRLDFSFPDdyfkGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 2991
Cdd:cd13976   198 AKIRRGQFAIPE----TLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
2743-2933 4.57e-07

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 54.28  E-value: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKCDQK--GTKRAVATKFVNKKLMKRDQ--VTHELGILQSL-QHPLLVGLLDTFETPTSYILVLEMADQGR 2817
Cdd:cd05047     3 IGEGNFGQVLKARIKkdGLRMDAAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2818 LLDCVVR----------------WGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKptiKLADFGda 2881
Cdd:cd05047    83 LLDFLRKsrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA---KIADFG-- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2882 VQLNTTYYIHQLLGN--PEFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05047   158 LSRGQEVYVKKTMGRlpVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1084-1184 4.62e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 50.39  E-value: 4.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  1084 FERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1163
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSE--DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 767934614  1164 AVDKRYRDFSLRMEKYRTSLE 1184
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
2640-2717 4.85e-07

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 50.00  E-value: 4.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767934614 2640 GETVVLRCRVCGRPKASITW-KGPEhnTLNNDGHYSIsysdLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRV 2717
Cdd:cd05852    17 GGRVIIECKPKAAPKPKFSWsKGTE--LLVNNSRISI----WDDGSLEILNITKLDEGSYTCFAENNRGKANSTGVLSV 89
SPEC smart00150
Spectrin repeats;
617-724 5.03e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.41  E-value: 5.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614    617 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKR---FGQQQQTTLQVTVNVIKEGEDLIQQlrdsaissnktpHNS 693
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKheaFEAELEAHEERVEALNELGEQLIEE------------GHP 70
                            90       100       110
                    ....*....|....*....|....*....|.
gi 767934614    694 SINHIETVLQQLDEAQSQMEELFQERKIKLE 724
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQKLE 101
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
2643-2715 5.15e-07

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 49.89  E-value: 5.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767934614 2643 VVLRCRVCGRPKASITWKGPEHNTLNNDgHYSIsysdLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASL 2715
Cdd:cd05723    15 IVFECEVTGKPTPTVKWVKNGDVVIPSD-YFKI----VKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQL 82
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
2739-2953 5.68e-07

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 53.72  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2739 EVAELGRGRFSVVKKcdqKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRL 2818
Cdd:cd05065    16 EFGEVCRGRLKLPGK---REIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENGAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2819 lDCVVRW--GSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDA--VQLNTT--YYIHQ 2892
Cdd:cd05065    93 -DSFLRQndGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNL---VCKVSDFGLSrfLEDDTSdpTYTSS 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2893 LLGN-P-EFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEETcLNICRLDFSFP 2953
Cdd:cd05065   169 LGGKiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDV-INAIEQDYRLP 231
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
2733-2982 6.34e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 53.87  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2733 FDSFYSEVAELGRGRFSVVKKCDQ---------KGTKRAVATKfVNKKLMKRDQVTHE-LGilqslQHPLLVGLLDTFET 2802
Cdd:cd14138     3 YATEFHELEKIGSGEFGSVFKCVKrldgciyaiKRSKKPLAGS-VDEQNALREVYAHAvLG-----QHSHVVRYYSAWAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2803 PTSYILVLEMADQGRLLDCVV----RWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADF 2878
Cdd:cd14138    77 DDHMLIQNEYCNGGSLADAISenyrIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2879 GDAVQLNTTYYIHQLLG------NPE-------FAAPEIILGNPVSL-TSDTWSVGvLTYVLLSGVSPFLDDSVEETCLN 2944
Cdd:cd14138   157 EDEWASNKVIFKIGDLGhvtrvsSPQveegdsrFLANEVLQENYTHLpKADIFALA-LTVVCAAGAEPLPTNGDQWHEIR 235
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767934614 2945 ICRLDfSFPddyfKGVSQKAKEFVCFLLQEDPAKRPSA 2982
Cdd:cd14138   236 QGKLP-RIP----QVLSQEFLDLLKVMIHPDPERRPSA 268
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
2743-2933 6.51e-07

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 53.81  E-value: 6.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2743 LGRGRFSVVKKC----DQKGTKRAVATKFVNKKLMKRD--QVTHELGILQSLQHPLLVGLLDTFETPtSYILVLEMADQG 2816
Cdd:cd05111    15 LGSGVFGTVHKGiwipEGDSIKIPVAIKVIQDRSGRQSfqAVTDHMLAIGSLDHAYIVRLLGICPGA-SLQLVTQLLPLG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2817 RLLDCV-VRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAVQL---NTTYYIHQ 2892
Cdd:cd05111    94 SLLDHVrQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPS---QVQVADFGVADLLypdDKKYFYSE 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767934614 2893 LLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPF 2933
Cdd:cd05111   171 AKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPY 212
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
2626-2717 6.77e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 49.71  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2626 PEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKgPEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVND 2705
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQ-LDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNR 79
                          90
                  ....*....|..
gi 767934614 2706 MGSASSSASLRV 2717
Cdd:cd20990    80 AGQNSFNLELVV 91
SH3_Eps8 cd11764
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ...
1601-1654 7.03e-07

Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212698 [Multi-domain]  Cd Length: 54  Bit Score: 48.41  E-value: 7.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767934614 1601 LTVVIHDFTACNSNELTIRRGQTVEVLErphDKPDWCLVRTtdrSPAAEGLVPC 1654
Cdd:cd11764     1 YVRVLYDFTARNSKELSVLKGEYLEVLD---DSRQWWKVRN---SRGQVGYVPH 48
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
2742-2940 7.09e-07

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 53.50  E-value: 7.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2742 ELGRGRFSVVKK-------CDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMAD 2814
Cdd:cd05032    13 ELGQGSFGMVYEglakgvvKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2815 QGRLLD------------CVVrwGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLakpTIKLADFGDAV 2882
Cdd:cd05032    93 KGDLKSylrsrrpeaennPGL--GPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDL---TVKIGDFGMTR 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767934614 2883 QL-NTTYY--IHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLS-GVSPFLDDSVEE 2940
Cdd:cd05032   168 DIyETDYYrkGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEE 229
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1221-1398 1.08e-06

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1221 HELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTY---LWEMTsgveeIPPGIVNKELI--IFGNMQEIYEFhNNI 1295
Cdd:COG5422   472 KEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWikpLEESN-----IIPENARRNFIkhVFANINEIYAV-NSK 545
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 1296 FLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLIlEHAGS-------YFDEIQ-----QRHGlansIS 1360
Cdd:COG5422   546 LLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEF-EREKSvnpnfarFDHEVErldesRKLE----LD 620
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767934614 1361 SYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVM 1398
Cdd:COG5422   621 GYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2271-2487 1.88e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.02  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRPSRIPQPVRHHPPVlvssaASSQAEADKMSGTSTPGP--SLPPPGAAPEAGPSAPSRRPPGADAEGS-EREA 2347
Cdd:PHA03307  109 PGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPPaaSPPAAGASPAAVASDAASSRQAALPLSSpEETA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2348 EPIPKMKVLESPRKGAANASGSSP--DAPAKDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLG-----KEPFPPSSPL 2420
Cdd:PHA03307  184 RAPSSPPAEPPPSTPPAAASPRPPrrSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGwgpenECPLPRPAPI 263
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2421 QKGGSFWSSIPA-SPASRPGSftfPGDSDSLQRQTPRhAAPGKDTDRMSTCSSASEQSVQSTQSNGSE 2487
Cdd:PHA03307  264 TLPTRIWEASGWnGPSSRPGP---ASSSSSPRERSPS-PSPSSPGSGPAPSSPRASSSSSSSRESSSS 327
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
282-385 1.97e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 48.85  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   282 QLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNcMNVY-VNINRIMSVANRLVESGHYASQQI 360
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKALEAE-LAAHqDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 767934614   361 RQIASQLEQEWKAFAAALDERSTLL 385
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2272-2461 2.16e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.64  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2272 PSTSRSrPSRIPQPVRHHPPvlvssaassqaeadkMSGTSTPGPSLPPPGAAPEAGPSAPSRRPpgadaegsereaepip 2351
Cdd:PHA03307  260 PAPITL-PTRIWEASGWNGP---------------SSRPGPASSSSSPRERSPSPSPSSPGSGP---------------- 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2352 kmkvLESPRKGAANASGSSPDAPAKDARASLGtlplgkPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKGGSfwSSIP 2431
Cdd:PHA03307  308 ----APSSPRASSSSSSSRESSSSSTSSSSES------SRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRP--SRAP 375
                         170       180       190
                  ....*....|....*....|....*....|
gi 767934614 2432 ASPASRPGSFTFPGDSDSLQRQTPRHAAPG 2461
Cdd:PHA03307  376 SSPAASAGRPTRRRARAAVAGRARRRDATG 405
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2271-2478 5.13e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.48  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRPsriPQPVRHHPPVLVSSAASSQ---AEADKMSGTSTPGPSLPPPGAAPEAGPSAPSRRPPGAD----AEGS 2343
Cdd:PHA03307   24 PPATPGDAA---DDLLSGSQGQLVSDSAELAavtVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLstlaPASP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2344 EREAEPIPKMKVLESPRkGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKG 2423
Cdd:PHA03307  101 AREGSPTPPGPSSPDPP-PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSP 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767934614 2424 GSFWSSIPASPASRPGSftfpgdsdslqrqTPRHAAPGKDTDRMSTCSSASEQSV 2478
Cdd:PHA03307  180 EETARAPSSPPAEPPPS-------------TPPAAASPRPPRRSSPISASASSPA 221
PHA03247 PHA03247
large tegument protein UL36; Provisional
2272-2460 6.90e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2272 PSTSRSRPSRIP-----QPVrhHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAAPEAGP-SAPSRRPPGAdaegser 2345
Cdd:PHA03247 2510 PAPSRLAPAILPdepvgEPV--HPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSVPpPRPAPRPSEP------- 2580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2346 eaepipkmkvlesprkgAANASGSSPDAPAKDARASLGTLPLGKPRAGAASplnSPLSSAVPSLGKEPFPPSS-PLQKGG 2424
Cdd:PHA03247 2581 -----------------AVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP---SPLPPDTHAPDPPPPSPSPaANEPDP 2640
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767934614 2425 SfwSSIPASPASRPGSFTFPGDSdSLQRQTPRHAAP 2460
Cdd:PHA03247 2641 H--PPPTVPPPERPRDDPAPGRV-SRPRRARRLGRA 2673
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
512-611 7.61e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.93  E-value: 7.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   512 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 591
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|
gi 767934614   592 QLEDRIQDFVRRVEQRKILL 611
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2271-2449 1.36e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRPSRIPqPVRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAApeAGPSAPSRRPPGADAEGSEREAEPI 2350
Cdd:PHA03307  288 SSSPRERSPSPSP-SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGA--AVSPGPSPSRSPSPSRPPPPADPSS 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2351 PKMKvlESPRKGAANASGSSPDAPAKDARASLGTLPLGK---PRAGAASPLNSPLSSAVPSlgKEPFPPSSPLQKGGSFW 2427
Cdd:PHA03307  365 PRKR--PRPSRAPSSPAASAGRPTRRRARAAVAGRARRRdatGRFPAGRPRPSPLDAGAAS--GAFYARYPLLTPSGEPW 440
                         170       180
                  ....*....|....*....|..
gi 767934614 2428 ssiPASPASRPGSFTFPGDSDS 2449
Cdd:PHA03307  441 ---PGSPPPPPGRVRYGGLGDS 459
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2116-2211 2.00e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 45.62  E-value: 2.00e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   2116 QDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSClCLEENVENDPCKFALTSRTGdvvETFILHSS 2195
Cdd:smart00233   10 KSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVRE-APDPDSSKKPHCFEIKTSDR---KTLLLQAE 85
                            90
                    ....*....|....*.
gi 767934614   2196 SPSVRQTWIHEINQIL 2211
Cdd:smart00233   86 SEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2116-2212 2.13e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 45.63  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  2116 QDAGLLPRCRERRIFLFEQIVIFSepldkKKGFSMPGFLFKNSIKVSCLCLEENVEND----PCKFALTSRTGDVVETFI 2191
Cdd:pfam00169   10 KGGGKKKSWKKRYFVLFDGSLLYY-----KDDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTGERTGKRTYL 84
                           90       100
                   ....*....|....*....|.
gi 767934614  2192 LHSSSPSVRQTWIHEINQILE 2212
Cdd:pfam00169   85 LQAESEEERKDWIKAIQSAIR 105
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2271-2480 3.80e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRPSRIPQPVRHHPPVlvssaassqaeadkMSGTSTPGPSlPPPGAAPEAGPSA---PSRRPPGADAEGSEREA 2347
Cdd:PHA03307  192 EPPPSTPPAAASPRPPRRSSPI--------------SASASSPAPA-PGRSAADDAGASSsdsSSSESSGCGWGPENECP 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2348 EPIPKMKVLESPRKGAANASGSSPDAPAKDARASlgtlplGKPRAGAASPLNS---PLSSAVPSLGKEPFPPSSPLQKGG 2424
Cdd:PHA03307  257 LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS------PRERSPSPSPSSPgsgPAPSSPRASSSSSSSRESSSSSTS 330
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934614 2425 SFwSSIPASPASRPGsftfPGDSDSLQRQTPRHAAPGKDTDRMSTCSSASEQSVQS 2480
Cdd:PHA03307  331 SS-SESSRGAAVSPG----PSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAAS 381
PHA03247 PHA03247
large tegument protein UL36; Provisional
2305-2460 7.66e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2305 DKMSGTSTPGPSLPPPgaaPEAGPSAPSRRPPgADAEGSEREAEPIpkmkVLESPRKGAANASGSSPDAPAKDARASLGT 2384
Cdd:PHA03247  266 DRAPETARGATGPPPP---PEAAAPNGAAAPP-DGVWGAALAGAPL----ALPAPPDPPPPAPAGDAEEEDDEDGAMEVV 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2385 LPLGKPRAGAAS-------PLNSPLSSAVPSLGKEPFPPSSPLQKGGSFWSSIPASPASRPgsftfPGDSDSLQRQTPRH 2457
Cdd:PHA03247  338 SPLPRPRQHYPLgfpkrrrPTWTPPSSLEDLSAGRHHPKRASLPTRKRRSARHAATPFARG-----PGGDDQTRPAAPVP 412

                  ...
gi 767934614 2458 AAP 2460
Cdd:PHA03247  413 ASV 415
PHA03247 PHA03247
large tegument protein UL36; Provisional
2271-2475 8.54e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRPSRIPQPVRHHPPvlvssaassqaeadkmsgtstpGPSLPPPG-------AAPEAGPSAPSRrPPGADAEGS 2343
Cdd:PHA03247  268 APETARGATGPPPPPEAAAPN----------------------GAAAPPDGvwgaalaGAPLALPAPPDP-PPPAPAGDA 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2344 EREAEPIPKMKVLES-PRKGAANASG-------------SSPDAPAKDARASLGTLPLGKPRAG--AASPLNSPLSSAVP 2407
Cdd:PHA03247  325 EEEDDEDGAMEVVSPlPRPRQHYPLGfpkrrrptwtppsSLEDLSAGRHHPKRASLPTRKRRSArhAATPFARGPGGDDQ 404
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2408 SLGKEPFPPSSPLQKGGSFWSSIPASPASRPGSFTFPGDSDSLQRQTPRHAAPGKDTDRMSTCSSASE 2475
Cdd:PHA03247  405 TRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRK 472
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
2092-2216 8.94e-05

Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; Obscurin-myosin light chain kinase/Obscurin-MLCK) is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270059  Cd Length: 125  Bit Score: 44.46  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2092 LQGFDGKIVAQGKLLLQDTFLVTDQDAGLLP--RCRERRIFLFEQIVIFSEPlDKKKGFSMPGFLFKNSIKVSCLCLEEN 2169
Cdd:cd13239     2 IENYPAPLQALGEPIRQGHFTVWEEAPEVKTssRGHHRHVFLFKNCVVICKP-KRDSRTDTVTYVFKNKMKLSDIDVKDT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767934614 2170 VENDPCKFALTSRTGDVVETFILHSSSPSVRQTWIHEINQIleNQRN 2216
Cdd:cd13239    81 VEGDDRSFGLWHEHRGSVRKYTLQARSAIIKSSWLKDLRDL--QQRL 125
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
2097-2213 1.22e-04

unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest isoform is composed of 53 immunoglobulin (Ig) domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains at its N-terminus, and 2 protein kinase domains (PK1 and PK2) at its C-terminus. unc-89 mutants display disorganization of muscle A-bands, and usually lack M-lines. The COOH-terminal region of obscurin, the human homolog of unc89, interacts via two specific Ig-like domains with the NH(2)-terminal Z-disk region of titin, a protein that connects the Z line to the M line in the sarcomere and contributes to the contraction of striated muscle. obscurin is also thought to be involved in Ca2+/calmodulin via its IQ domains, as well as G protein-coupled signal transduction in the sarcomere via its RhoGEF/DH domain. The DH-PH region of OBSCN and unc89, the C. elegans homolog, has exchange activity for RhoA and Rho-1 respectively, but not for the small GTPases homologous to Cdc42 or Rac. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270134  Cd Length: 114  Bit Score: 43.88  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2097 GKIVAQGKLLLQDTFLVTDQDAgllpRCRERRIFLFEQIVIFSepldKKKGFSMPG--FLFKNSIKVScLCLEENVENDP 2174
Cdd:cd13325     1 GNIHKLGRLLRHDWFTVTDGEG----KAKERYLFLFKSRILIT----KVRRISEDRsvFILKDIIRLP-EVNVKQHPDDE 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767934614 2175 CKFALTSRTGDVVETFI-LHSSSPSVRQTWIHEINQILEN 2213
Cdd:cd13325    72 RTFELQPKLPAFGILPIdFKAHKDEIKDYWLNEIEEYAND 111
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2271-2464 2.61e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APSTSRSRPSRIPQPVRHHPPVLVSSAASSQAEADKMSGTSTPGP-------SLPPPGAAPEAGPSAPSRRPPGADAEGS 2343
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARavaaapaRRSPAPEALAAARQASARGPGGAPAPAP 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2344 EREAEPIPKMK--VLESPRKGAANASGSSPDAPA-KDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPL 2420
Cdd:PRK12323  453 APAAAPAAAARpaAAGPRPVAAAAAAAPARAAPAaAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATA 532
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767934614 2421 QKGGSFWSSIPASPASRPGSFTFPGDSDSLQRQtPRHAAPGKDT 2464
Cdd:PRK12323  533 DPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP-PRASASGLPD 575
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2318-2438 3.84e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2318 PPPGAAPEAGPSAPSRRPPGADAEGSEREAEPIPKMKVLESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASP 2397
Cdd:PHA03307  822 RSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAP 901
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767934614 2398 LNSPLSSAVPSLGkePFPPSSPLQKGGsfWSSIPASPASRP 2438
Cdd:PHA03307  902 APRPRPAPRVKLG--PMPPGGPDPRGG--FRRVPPGDLHTP 938
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
161-279 8.02e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.15  E-value: 8.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   161 FEDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKK--KVIKAPIEDLDLEGQKLLQRIQSSEsfpkkns 238
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLIDEGHYAS------- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 767934614   239 gsgnadlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQ 279
Cdd:pfam00435   76 -----------EEIQERLEELNERWEQLLELAAERKQKLEE 105
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2314-2455 9.39e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 9.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2314 GPSLPPPGAAPEAGPsAPSRRPPGADAEGSEREAEPIPkmkvlesPRKGAANASGSSPDAP----------AKDARASLG 2383
Cdd:PRK12323  444 PGGAPAPAPAPAAAP-AAAARPAAAGPRPVAAAAAAAP-------ARAAPAAAPAPADDDPppweelppefASPAPAQPD 515
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934614 2384 TLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKGGSFWSSIPASP-ASRPGSFT-FPGDSDSLQRQTP 2455
Cdd:PRK12323  516 AAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPrASASGLPDmFDGDWPALAARLP 589
PHA03247 PHA03247
large tegument protein UL36; Provisional
2271-2461 9.79e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 9.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2271 APST-SRSRPSRIPQ--PVRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAA--PEAGPSAPSRRPPGADAEGSER 2345
Cdd:PHA03247 2762 TTAGpPAPAPPAAPAagPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAlpPAASPAGPLPPPTSAQPTAPPP 2841
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2346 EAEPIPKMKVLE---SP-----RKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPS 2417
Cdd:PHA03247 2842 PPGPPPPSLPLGgsvAPggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP 2921
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767934614 2418 SPLQkggsfwssiPASPASRPGSftfPGDSDS-LQRQTPRHAAPG 2461
Cdd:PHA03247 2922 QPPP---------PPQPQPPPPP---PPRPQPpLAPTTDPAGAGE 2954
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
617-724 1.09e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.76  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614   617 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFGQQQQTTLQVTVNViKEGEDLIQQLRDSAISSNKtphnssin 696
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRV-EALNELAEKLIDEGHYASE-------- 76
                           90       100
                   ....*....|....*....|....*...
gi 767934614   697 HIETVLQQLDEAQSQMEELFQERKIKLE 724
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAERKQKLE 104
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1603-1653 1.10e-03

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 39.35  E-value: 1.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767934614 1603 VVIHDFTACNSNELTIRRGQTVEVLERphDKPDWCLVR--TTDRSPAAEGLVP 1653
Cdd:cd11853     3 PVIQDYYALKEDEICVSQGEVVQILAA--NQQNMFLVYrpATDQSPAAEGWIP 53
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2275-2392 1.52e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2275 SRSRPSRIPQPVRHHPPvlvssaassqaeadkmSGTSTPGPSLPPPGAAPEAGP-SAPSRR-----PPGADAEGSEREAE 2348
Cdd:PHA03307  811 AASRTASKRKSRSHTPD----------------GGSESSGPARPPGAAARPPPArSSESSKskpaaAGGRARGKNGRRRP 874
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767934614 2349 PIPKMKVLE---SPRKGAANA--SGSSPDAPAKDARASLGTLPLGKPRA 2392
Cdd:PHA03307  875 RPPEPRARPgaaAPPKAAAAAppAGAPAPRPRPAPRVKLGPMPPGGPDP 923
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2309-2438 1.66e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2309 GTSTPGPSLPPPGAAPEAGPSAPSRRP----------PGADAEGSEREAEPIPKMKVLESPRKGAANASGSSPDAPA-KD 2377
Cdd:PHA03307  773 ALLEPAEPQRGAGSSPPVRAEAAFRRPgrlrrsgpaaDAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARsSE 852
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934614 2378 ARASLGTLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKggsfwssiPASPASRP 2438
Cdd:PHA03307  853 SSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPP--------AGAPAPRP 905
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
2498-2553 1.96e-03

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 38.92  E-value: 1.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767934614 2498 LVTHDYTAVKEDEINVYQGEVVQIL--ASNQQNMFLVFRAATDQCPAAEGWIPGFVLG 2553
Cdd:cd11852     4 VVIEDFEATSSQELTVSKGQTVEVLerPSSRPDWCLVRTLEQDNSPPQEGLVPSSILC 61
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
2067-2213 3.31e-03

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 40.41  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2067 SELERAVEVMCIVPRRCNDM-------MNVGRLQG-FDG----KIVAQGKLLLQDTFLVtdqdagllpRCR--ERRIFLF 2132
Cdd:cd13243     2 SVVEEALDTMTQVAWHINDMkrkhehaVRVQEIQSlLDGwegpELTTYGDLVLEGTFRM---------AGAknERLLFLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614 2133 EQIVIfsepLDKKKGfsmPGFL-FKNSIKVSCLCLEENVENDPCKFALTSRTGDVVeTFILHSSSPSVRQTWIHEINQ-I 2210
Cdd:cd13243    73 DKMLL----ITKKRE---DGILqYKTHIMCSNLMLSESIPKEPLSFQVLPFDNPKL-QYTLQAKNQEQKRLWTQEIKRlI 144

                  ...
gi 767934614 2211 LEN 2213
Cdd:cd13243   145 LEN 147
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
164-280 6.98e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.51  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934614  164 YISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKKKV--IKAPIEDLDLEGQKLLQRIQSSEsfpkknsgsg 241
Cdd:cd00176   111 FFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELeaHEPRLKSLNELAEELLEEGHPDA---------- 180
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767934614  242 nadlqnlLPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQC 280
Cdd:cd00176   181 -------DEEIEEKLEELNERWEELLELAEERQKKLEEA 212
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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