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Conserved domains on  [gi|161333835|ref|NP_001104501|]
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activin receptor type-1C isoform 2 [Homo sapiens]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
149-436 0e+00

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 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: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 635.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIP 308
Cdd:cd14143   81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 309 QNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQ 388
Cdd:cd14143  161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 389 KFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQLC 436
Cdd:cd14143  241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
TFP super family cl45932
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
1-49 4.33e-28

three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU (also known as Ly-6 antigen/uPA receptor)-like extracellular domain (ECD) occurs singly in GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2) or as three-fold repeated domain in urokinase-type plasminogen activator receptor. It is a structural domain involved in protein-protein interactions, tolerating an unusual degree of variation and binding with high specificity to a broad spectrum of targets. The snake toxin domain is present in short and long neurotoxins, cytotoxins, and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. Both the LU-like ECD and the snake toxin domain belong to three-fingered protein (TFP) fold, which is characterized by containing 70 to 100 amino acids including eight to ten cysteine residues spaced at conserved distances.


The actual alignment was detected with superfamily member cd23540:

Pssm-ID: 480272  Cd Length: 76  Bit Score: 106.15  E-value: 4.33e-28
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835   1 MLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHL 49
Cdd:cd23540   28 MLTNGKEEVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHL 76
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
116-143 5.36e-11

Transforming growth factor beta type I GS-motif; This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor.


:

Pssm-ID: 462503  Cd Length: 28  Bit Score: 56.84  E-value: 5.36e-11
                          10        20
                  ....*....|....*....|....*...
gi 161333835  116 TLKDLIYDVTASGSGSGLPLLVQRTIAR 143
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
 
Name Accession Description Interval E-value
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
149-436 0e+00

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 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: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 635.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIP 308
Cdd:cd14143   81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 309 QNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQ 388
Cdd:cd14143  161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 389 KFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQLC 436
Cdd:cd14143  241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
145-428 7.26e-37

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: 135.70  E-value: 7.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  145 IVLQEIVGKGRFGEVWHGRW------CGEDVAVKI----FSSRDERSWFREAEIyqtvM--LRHENILGFIAADNKDNgt 212
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLkgegenTKIKVAVKTlkegADEEEREDFLEEASI----MkkLDHPNIVKLLGVCTQGE-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  213 wtQLWLVSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAI 289
Cdd:pfam07714  75 --PLYIVTEYMPGGDLLDFLrkHKRKLTLKDLLSMALQIAKGMEYLEsKNFV---------HRDLAARNCLVSENLVVKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  290 ADLGLAVKHDSILNTIdipqnPKVGTK---RYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIarrCSVGGIveeyql 366
Cdd:pfam07714 144 SDFGLSRDIYDDDYYR-----KRGGGKlpiKWMAPESLKD----GKFTS--KSDVWSFGVLLWEI---FTLGEQ------ 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835  367 PYYDMVPsdpsiEEMRKVVCDqKFRPSIPNQWqsCEALRvmgRIMRECWYANGAARLTALRI 428
Cdd:pfam07714 204 PYPGMSN-----EEVLEFLED-GYRLPQPENC--PDELY---DLMKQCWAYDPEDRPTFSEL 254
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
145-432 4.17e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 133.43  E-value: 4.17e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   145 IVLQEIVGKGRFGEVWHGRW------CGEDVAVKIF----SSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwt 214
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLkgkggkKKVEVAVKTLkedaSEQQIEEFLREARIMR--KLDHPNVVKLLGVCTEEE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   215 QLWLVSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHmeivgtqGKPAIaHRDIKSKNILVKKCETCAIADL 292
Cdd:smart00219  75 PLYIVMEYMEGGDLLSYLrkNRPKLSLSDLLSFALQIARGMEYLE-------SKNFI-HRDLAARNCLVGENLVVKISDF 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   293 GLAVKHDSilNTIDIPQNPKVgTKRYMAPEMLDDtmnvNIFeSFKrADIYSVGLVYWEIARRCsvggiveeyQLPYYDMv 372
Cdd:smart00219 147 GLSRDLYD--DDYYRKRGGKL-PIRWMAPESLKE----GKF-TSK-SDVWSFGVLLWEIFTLG---------EQPYPGM- 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   373 psdpSIEEMRKVVcDQKFRPSIPNqwqSCEALRVmgRIMRECWYANGAARLTALRIKKTI 432
Cdd:smart00219 208 ----SNEEVLEYL-KNGYRLPQPP---NCPPELY--DLMLQCWAEDPEDRPTFSELVEIL 257
TFP_LU_ECD_ALK7 cd23540
extracellular domain (ECD) found in activin receptor-like kinase 7 (ALK-7) and similar ...
1-49 4.33e-28

extracellular domain (ECD) found in activin receptor-like kinase 7 (ALK-7) and similar proteins; ALK-7 (EC 2.7.11.30, also called activin receptor type-1C (ACVR1C), or activin receptor type IC (ACTR-IC)) is a serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. ALK-7 is the receptor for activin AB, activin B, and NODAL. It plays a role in cell differentiation, growth arrest and apoptosis. This model corresponds to the extracellular domain (ECD) of ALK-7, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467070  Cd Length: 76  Bit Score: 106.15  E-value: 4.33e-28
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835   1 MLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHL 49
Cdd:cd23540   28 MLTNGKEEVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHL 76
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
146-350 6.69e-27

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 112.41  E-value: 6.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGR--WCGEDVAVKIFSSR-----DERSWF-REAEIYQTvmLRHENILGFIAADnKDNGTwtqLW 217
Cdd:COG0515   10 RILRLLGRGGMGVVYLARdlRLGRPVALKVLRPElaadpEARERFrREARALAR--LNHPNIVRVYDVG-EEDGR---PY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:COG0515   84 LVMEYVEGESLADLLRRRgPLPPAEALRILAQLAEALAAAH-----AAG---IVHRDIKPANILLTPDGRVKLIDFGIAR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 297 KHDSILNTidiPQNPKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWE 350
Cdd:COG0515  156 ALGGATLT---QTGTVVGTPGYMAPEQARGE------PVDPRSDVYSLGVTLYE 200
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
150-346 1.53e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 77.56  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW---HgRWCGEDVAVK-IFSSRDE---RSWFREAEIYQTVmlRHENILGfiAADNKDNGTWTQLWLvsEY 222
Cdd:PLN00034  81 RIGSGAGGTVYkviH-RPTGRLYALKvIYGNHEDtvrRQICREIEILRDV--NHPNVVK--CHDMFDHNGEIQVLL--EF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYdylNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdSIL 302
Cdd:PLN00034 154 MDGGSLE---GTHIADEQFLADVARQILSGIAYLH--------RRHIVHRDIKPSNLLINSAKNVKIADFGVS----RIL 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 303 N-TIDiPQNPKVGTKRYMAPEMLDDTMNVNIFESFKrADIYSVGL 346
Cdd:PLN00034 219 AqTMD-PCNSSVGTIAYMSPERINTDLNHGAYDGYA-GDIWSLGV 261
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
116-143 5.36e-11

Transforming growth factor beta type I GS-motif; This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor.


Pssm-ID: 462503  Cd Length: 28  Bit Score: 56.84  E-value: 5.36e-11
                          10        20
                  ....*....|....*....|....*...
gi 161333835  116 TLKDLIYDVTASGSGSGLPLLVQRTIAR 143
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
GS smart00467
GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF ...
115-145 6.09e-11

GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF beta receptors. Mutation of two or more of the serines or threonines in the TTSGSGSG of TGF-beta type I receptor impairs phosphorylation and signaling activity.


Pssm-ID: 197743  Cd Length: 30  Bit Score: 56.79  E-value: 6.09e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 161333835   115 KTLKDLIYDVTaSGSGSGLPLLVQRTIARTI 145
Cdd:smart00467   1 KTLSDLLEDTT-SGSGSGLPLLVQRTVARQI 30
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
147-350 9.92e-07

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 50.95  E-value: 9.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRwC---GEDVAVKIFSS---RDE----RswF-REAeiyQTVM-LRHENIL-----GfiaadnKD 209
Cdd:NF033483  11 IGERIGRGGMAEVYLAK-DtrlDRDVAVKVLRPdlaRDPefvaR--FrREA---QSAAsLSHPNIVsvydvG------ED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 210 NGtwtQLWLVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETC 287
Cdd:NF033483  79 GG---IPYIVMEYVDGRTLKDYIREHgPLSPEEAVEIMIQILSALEHAHrNGIV---------HRDIKPQNILITKDGRV 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 288 AIADLGLAVkhdsILNTIDIPQNPKV-GTKRYMAPE-----MLDdtmnvnifesfKRADIYSVGLVYWE 350
Cdd:NF033483 147 KVTDFGIAR----ALSSTTMTQTNSVlGTVHYLSPEqarggTVD-----------ARSDIYSLGIVLYE 200
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
2-45 4.84e-04

Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor types. This is an alignment of the hydrophilic cysteine-rich ligand-binding domains, Both receptor types, (type I and II) posses a 9 amino acid cysteine box, with the the consensus CCX{4-5}CN. The type I receptors also possess 7 extracellular residues preceding the cysteine box.


Pssm-ID: 460048  Cd Length: 78  Bit Score: 38.64  E-value: 4.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 161333835    2 LTNGKEQVI-KSCvsLPELNAQVFCHSSNN---VTKTECCFTDFCNNI 45
Cdd:pfam01064  32 DTDGFIECVkKGC--LSPEDDPFECKTSNKphsLYRIECCKTDFCNKN 77
 
Name Accession Description Interval E-value
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
149-436 0e+00

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 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: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 635.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIP 308
Cdd:cd14143   81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 309 QNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQ 388
Cdd:cd14143  161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 389 KFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQLC 436
Cdd:cd14143  241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
149-435 0e+00

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I 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: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 544.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14056    1 KTIGKGRYGEVWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGSWTQLWLITEYHEHGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIP 308
Cdd:cd14056   81 YDYLQRNTLDTEEALRLAYSAASGLAHLHTEIVGTQGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYDSDTNTIDIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 309 QNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQ 388
Cdd:cd14056  161 PNPRVGTKRYMAPEVLDDSINPKSFESFKMADIYSFGLVLWEIARRCEIGGIAEEYQLPYFGMVPSDPSFEEMRKVVCVE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 161333835 389 KFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14056  241 KLRPPIPNRWKSDPVLRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
139-435 2.48e-179

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 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: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 502.36  E-value: 2.48e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 139 RTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWL 218
Cdd:cd14142    1 RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMTSRNSCTQLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKH 298
Cdd:cd14142   81 ITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 DSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSI 378
Cdd:cd14142  161 SQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEVARRCVSGGIVEEYKPPFYDVVPSDPSF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 379 EEMRKVVCDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14142  241 EDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKI 297
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
151-435 2.63e-175

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 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: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 491.61  E-value: 2.63e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYD 230
Cdd:cd14144    3 VGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 231 YLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIPQN 310
Cdd:cd14144   83 FLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGTQGKPAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNEVDLPPN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 311 PKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQKF 390
Cdd:cd14144  163 TRVGTKRYMAPEVLDESLNRNHFDAYKMADMYSFGLVLWEIARRCISGGIVEEYQLPYYDAVPSDPSYEDMRRVVCVERR 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 391 RPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14144  243 RPSIPNRWSSDEVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
149-435 2.12e-174

Catalytic domain of Transforming Growth Factor beta Receptor-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 receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-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: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 489.64  E-value: 2.12e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd13998    1 EVIGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTALRTELWLVTAFHPNGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVG-TQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDI 307
Cdd:cd13998   81 *DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGcTQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPSTGEEDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 308 PQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSV-GGIVEEYQLPYYDMVPSDPSIEEMRKVVC 386
Cdd:cd13998  161 ANNGQVGTKRYMAPEVLEGAINLRDFESFKRVDIYAMGLVLWEMASRCTDlFGIVEEYKPPFYSEVPNHPSFEDMQEVVV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 387 DQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd13998  241 RDKQRPNIPNRWLSHPGLQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
151-435 4.38e-148

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a 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: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 422.91  E-value: 4.38e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYD 230
Cdd:cd14220    3 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 231 YLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIPQN 310
Cdd:cd14220   83 FLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVPLN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 311 PKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQKF 390
Cdd:cd14220  163 TRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPSDPSYEDMREVVCVKRL 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 391 RPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14220  243 RPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
139-442 2.30e-147

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b 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: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 421.77  E-value: 2.30e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 139 RTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWL 218
Cdd:cd14219    1 RTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKH 298
Cdd:cd14219   81 ITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 DSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSI 378
Cdd:cd14219  161 ISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 379 EEMRKVVCDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQLCVKEDCK 442
Cdd:cd14219  241 EDMREIVCIKRLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIK 304
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
149-435 5.95e-112

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 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: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 330.83  E-value: 5.95e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14053    1 EIKARGRFGAVWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGESLEAEYWLITEFHERGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQG--KPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTID 306
Cdd:cd14053   81 CDYLKGNVISWNELCKIAESMARGLAYLHEDIPATNGghKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 307 ipQNPKVGTKRYMAPEMLDDTMNVNIfESFKRADIYSVGLVYWEIARRCSVGGI-VEEYQLPYYDMVPSDPSIEEMRKVV 385
Cdd:cd14053  161 --THGQVGTRRYMAPEVLEGAINFTR-DAFLRIDMYAMGLVLWELLSRCSVHDGpVDEYQLPFEEEVGQHPTLEDMQECV 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 161333835 386 CDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14053  238 VHKKLRPQIRDEWRKHPGLAQLCETIEECWDHDAEARLSAGCVEERLSQL 287
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
149-425 1.22e-104

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 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: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 312.39  E-value: 1.22e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCG------EDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEY 222
Cdd:cd14055    1 KLVGKGRFAEVWKAKLKQnasgqyETVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEERGVGLDRQYWLITAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGtQGKP--AIAHRDIKSKNILVKKCETCAIADLGLAVKHDS 300
Cdd:cd14055   81 HENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRTP-CGRPkiPIAHRDLKSSNILVKNDGTCVLADFGLALRLDP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 301 ILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEE 380
Cdd:cd14055  160 SLSVDELANSGQVGTARYMAPEALESRVNLEDLESFKQIDVYSMALVLWEMASRCEASGEVKPYELPFGSKVRERPCVES 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 381 MRKVVCDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTA 425
Cdd:cd14055  240 MKDLVLRDRGRPEIPDSWLTHQGMCVLCDTITECWDHDPEARLTA 284
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
149-439 1.83e-92

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 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: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 281.56  E-value: 1.83e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGT-WTQLWLVSEYHEQGS 227
Cdd:cd14054    1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADgRMEYLLVLEYAPKGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYLNRNIVTVAGMIKLALSIASGLAHLHMEI-VGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVK--HDSILNT 304
Cdd:cd14054   81 LCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLrRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVlrGSSLVRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 305 IDIPQNPK----VGTKRYMAPEMLDDTMNVNIFESF-KRADIYSVGLVYWEIARRCS---VGGIVEEYQLPYYDMVPSDP 376
Cdd:cd14054  161 RPGAAENAsiseVGTLRYMAPEVLEGAVNLRDCESAlKQVDVYALGLVLWEIAMRCSdlyPGESVPPYQMPYEAELGNHP 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 377 SIEEMRKVVCDQKFRPSIPNQW-QSCEALRVMGRIMRECWYANGAARLTAlrikktisqLCVKE 439
Cdd:cd14054  241 TFEDMQLLVSREKARPKFPDAWkENSLAVRSLKETIEDCWDQDAEARLTA---------LCVEE 295
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
149-435 2.44e-83

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b 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: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 258.04  E-value: 2.44e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14140    1 EIKARGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEMELWLITAFHDKGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQG---KPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDsilnti 305
Cdd:cd14140   81 TDYLKGNIVSWNELCHIAETMARGLSYLHEDVPRCKGeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFE------ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 306 diPQNP------KVGTKRYMAPEMLDDTMNVNiFESFKRADIYSVGLVYWEIARRC-SVGGIVEEYQLPYYDMVPSDPSI 378
Cdd:cd14140  155 --PGKPpgdthgQVGTRRYMAPEVLEGAINFQ-RDSFLRIDMYAMGLVLWELVSRCkAADGPVDEYMLPFEEEIGQHPSL 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 379 EEMRKVVCDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14140  232 EDLQEVVVHKKMRPVFKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERISQI 288
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
149-435 5.86e-82

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a 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: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 254.19  E-value: 5.86e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14141    1 EIKARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTNLDVDLWLITAFHEKGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQG--KPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTID 306
Cdd:cd14141   81 TDYLKANVVSWNELCHIAQTMARGLAYLHEDIPGLKDghKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 307 ipQNPKVGTKRYMAPEMLDDTMNVNiFESFKRADIYSVGLVYWEIARRCSVG-GIVEEYQLPYYDMVPSDPSIEEMRKVV 385
Cdd:cd14141  161 --THGQVGTRRYMAPEVLEGAINFQ-RDAFLRIDMYAMGLVLWELASRCTASdGPVDEYMLPFEEEVGQHPSLEDMQEVV 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 161333835 386 CDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14141  238 VHKKKRPVLRECWQKHAGMAMLCETIEECWDHDAEARLSAGCVEERIIQM 287
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
151-415 9.32e-56

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: 185.05  E-value: 9.32e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSEYHEQGS 227
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDDNDELLKEfrrEVSILSKLRHPNIVQFIGACLSPP----PLCIVTEYMPGGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYLNRN--IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdSILNTI 305
Cdd:cd13999   77 LYDLLHKKkiPLSWSLRLKIALDIARGMNYLH--------SPPIIHRDLKSLNILLDENFTVKIADFGLS----RIKNST 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 306 DIPQNPKVGTKRYMAPEMLDDTMNvnifeSFKrADIYSVGLVYWEIARRcsvggiveeyQLPYYDMVPSDPSIEemrkvV 385
Cdd:cd13999  145 TEKMTGVVGTPRWMAPEVLRGEPY-----TEK-ADVYSFGIVLWELLTG----------EVPFKELSPIQIAAA-----V 203
                        250       260       270
                 ....*....|....*....|....*....|
gi 161333835 386 CDQKFRPSIPNQWQScealrVMGRIMRECW 415
Cdd:cd13999  204 VQKGLRPPIPPDCPP-----ELSKLIKRCW 228
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
152-351 1.39e-38

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: 138.94  E-value: 1.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGRWC--GEDVAVKIFSSRDE----RSWFREAEIYQtvMLRHENILGFIAADNKDNgtwtQLWLVSEYHEQ 225
Cdd:cd00180    2 GKGSFGKVYKARDKetGKKVAVKVIPKEKLkkllEELLREIEILK--KLNHPNIVKLYDVFETEN----FLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 GSLYDYLNRN--IVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilN 303
Cdd:cd00180   76 GSLKDLLKENkgPLSEEEALSILRQLLSALEYLHSN--------GIIHRDLKPENILLDSDGTVKLADFGLAKDLDS--D 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 304 TIDIPQNPKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWEI 351
Cdd:cd00180  146 DSLLKTTGGTTPPYYAPPELLGGR------YYGPKVDIWSLGVILYEL 187
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
145-428 7.26e-37

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: 135.70  E-value: 7.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  145 IVLQEIVGKGRFGEVWHGRW------CGEDVAVKI----FSSRDERSWFREAEIyqtvM--LRHENILGFIAADNKDNgt 212
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLkgegenTKIKVAVKTlkegADEEEREDFLEEASI----MkkLDHPNIVKLLGVCTQGE-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  213 wtQLWLVSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAI 289
Cdd:pfam07714  75 --PLYIVTEYMPGGDLLDFLrkHKRKLTLKDLLSMALQIAKGMEYLEsKNFV---------HRDLAARNCLVSENLVVKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  290 ADLGLAVKHDSILNTIdipqnPKVGTK---RYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIarrCSVGGIveeyql 366
Cdd:pfam07714 144 SDFGLSRDIYDDDYYR-----KRGGGKlpiKWMAPESLKD----GKFTS--KSDVWSFGVLLWEI---FTLGEQ------ 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835  367 PYYDMVPsdpsiEEMRKVVCDqKFRPSIPNQWqsCEALRvmgRIMRECWYANGAARLTALRI 428
Cdd:pfam07714 204 PYPGMSN-----EEVLEFLED-GYRLPQPENC--PDELY---DLMKQCWAYDPEDRPTFSEL 254
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
145-432 4.17e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 133.43  E-value: 4.17e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   145 IVLQEIVGKGRFGEVWHGRW------CGEDVAVKIF----SSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwt 214
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLkgkggkKKVEVAVKTLkedaSEQQIEEFLREARIMR--KLDHPNVVKLLGVCTEEE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   215 QLWLVSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHmeivgtqGKPAIaHRDIKSKNILVKKCETCAIADL 292
Cdd:smart00219  75 PLYIVMEYMEGGDLLSYLrkNRPKLSLSDLLSFALQIARGMEYLE-------SKNFI-HRDLAARNCLVGENLVVKISDF 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   293 GLAVKHDSilNTIDIPQNPKVgTKRYMAPEMLDDtmnvNIFeSFKrADIYSVGLVYWEIARRCsvggiveeyQLPYYDMv 372
Cdd:smart00219 147 GLSRDLYD--DDYYRKRGGKL-PIRWMAPESLKE----GKF-TSK-SDVWSFGVLLWEIFTLG---------EQPYPGM- 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   373 psdpSIEEMRKVVcDQKFRPSIPNqwqSCEALRVmgRIMRECWYANGAARLTALRIKKTI 432
Cdd:smart00219 208 ----SNEEVLEYL-KNGYRLPQPP---NCPPELY--DLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
145-432 1.63e-35

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: 131.90  E-value: 1.63e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   145 IVLQEIVGKGRFGEVWHGRW------CGEDVAVKIF----SSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwt 214
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLkgkgdgKEVEVAVKTLkedaSEQQIEEFLREARIMR--KLDHPNIVKLLGVCTEEE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   215 QLWLVSEYHEQGSLYDYL---NRNIVTVAGMIKLALSIASGLAHLHmeivgtqGKPAIaHRDIKSKNILVKKCETCAIAD 291
Cdd:smart00221  75 PLMIVMEYMPGGDLLDYLrknRPKELSLSDLLSFALQIARGMEYLE-------SKNFI-HRDLAARNCLVGENLVVKISD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   292 LGLAVKHDSilNTIDIPQNPKVgTKRYMAPEMLDDtmnvNIFeSFKrADIYSVGLVYWEIARRCsvggiveeyQLPYYDM 371
Cdd:smart00221 147 FGLSRDLYD--DDYYKVKGGKL-PIRWMAPESLKE----GKF-TSK-SDVWSFGVLLWEIFTLG---------EEPYPGM 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835   372 VPsdpsiEEMRKVVcDQKFRPSIPnqwQSCEALRVmgRIMRECWYANGAARLTALRIKKTI 432
Cdd:smart00221 209 SN-----AEVLEYL-KKGYRLPKP---PNCPPELY--KLMLQCWAEDPEDRPTFSELVEIL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
147-430 4.01e-34

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 128.03  E-value: 4.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   147 LQEIVGKGRFGEVWHGRWC--GEDVAVKI----FSSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:smart00220   3 ILEKLGEGSFGKVYLARDKktGKLVAIKVikkkKIKKDRERILREIKILK--KLKHPNIVRLYDVFEDED----KLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   221 EYHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLA--VK 297
Cdd:smart00220  77 EYCEGGDLFDLLkKRGRLSEDEARFYLRQILSALEYLH-----SKG---IVHRDLKPENILLDEDGHVKLADFGLArqLD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835   298 HDSILNTIdipqnpkVGTKRYMAPEMLDDTMnVNifesfKRADIYSVGLVYWEIARRcsvggiveeyQLPYYDmvpsDPS 377
Cdd:smart00220 149 PGEKLTTF-------VGTPEYMAPEVLLGKG-YG-----KAVDIWSLGVILYELLTG----------KPPFPG----DDQ 201
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161333835   378 IEEMRKVVCDQKFRPSIPNQWQSCEALrvmgRIMRECWYANGAARLTALRIKK 430
Cdd:smart00220 202 LLELFKKIGKPKPPFPPPEWDISPEAK----DLIRKLLVKDPEKRLTAEEALQ 250
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
149-415 8.53e-34

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: 127.27  E-value: 8.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGE-----DVAVKI---FSSRDERSWF-REAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLV 219
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGdgktvDVAVKTlkeDASESERKDFlKEARVMKK--LGHPNVVRLLGVCTEEE----PLYLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYL----------NRNIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCA 288
Cdd:cd00192   75 MEYMEGGDLLDFLrksrpvfpspEPSTLSLKDLLSFAIQIAKGMEYLAsKKFV---------HRDLAARNCLVGEDLVVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 289 IADLGLAVKHDSILNTIDipqnpKVGTK---RYMAPEMLDDtmnvNIFeSFKrADIYSVGLVYWEIarrCSVGGIveeyq 365
Cdd:cd00192  146 ISDFGLSRDIYDDDYYRK-----KTGGKlpiRWMAPESLKD----GIF-TSK-SDVWSFGVLLWEI---FTLGAT----- 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 366 lPYYDMVPsdpsiEEMRKVVCDQkFRPSIPnqwQSC-EALRvmgRIMRECW 415
Cdd:cd00192  207 -PYPGLSN-----EEVLEYLRKG-YRLPKP---ENCpDELY---ELMLSCW 244
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
151-435 5.52e-30

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: 116.77  E-value: 5.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFrEAEIYQTVMLRHENILGFIAADNKDNGTwtqlWLVSEYHEQGSLYD 230
Cdd:cd14058    1 VGRGSFGVVCKARWRNQIVAVKIIESESEKKAF-EVEVRQLSRVDHPNIIKLYGACSNQKPV----CLVMEYAEGGSLYN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 231 YL----NRNIVTVAGMIKLALSIASGLAHLHmeivGTQGKPAIaHRDIKSKNILVKKCET-CAIADLGLAV-KHDSILNT 304
Cdd:cd14058   76 VLhgkePKPIYTAAHAMSWALQCAKGVAYLH----SMKPKALI-HRDLKPPNLLLTNGGTvLKICDFGTACdISTHMTNN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 305 idipqnpkVGTKRYMAPEmlddtmnvnIFESFK---RADIYSVGLVYWEIARRcsvggiveeyQLPYYDMVPSDPSIEEM 381
Cdd:cd14058  151 --------KGSAAWMAPE---------VFEGSKyseKCDVFSWGIILWEVITR----------RKPFDHIGGPAFRIMWA 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 382 rkvVCDQKFRPSIPNQWQSCEALrvmgriMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14058  204 ---VHNGERPPLIKNCPKPIESL------MTRCWSKDPEKRPSMKEIVKIMSHL 248
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
147-350 1.35e-29

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: 115.76  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW--HGRWCGEDVAVKI----FSSRDE-RSWF-REAEIyqTVMLRHENILGFIAADnKDNGtwtQLWL 218
Cdd:cd14014    4 LVRLLGRGGMGEVYraRDTLLGRPVAIKVlrpeLAEDEEfRERFlREARA--LARLSHPNIVRVYDVG-EDDG---RPYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHMeivgtQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd14014   78 VMEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHR-----AG---IVHRDIKPANILLTEDGRVKLTDFGIARA 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 298 HDSILNTidiPQNPKVGTKRYMAPEMLDDTmNVNifesfKRADIYSVGLVYWE 350
Cdd:cd14014  150 LGDSGLT---QTGSVLGTPAYMAPEQARGG-PVD-----PRSDIYSLGVVLYE 193
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
143-425 1.69e-28

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: 113.25  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIF----SSRDERSWFReAEIYQTvMLRHENILGFIAA----DNKDNGTwt 214
Cdd:cd13979    3 EPLRLQEPLGSGGFGSVYKATYKGETVAVKIVrrrrKNRASRQSFW-AELNAA-RLRHENIVRVLAAetgtDFASLGL-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 qlwLVSEYHEQGSLYDYLNR--NIVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd13979   79 ---IIMEYCGNGTLQQLIYEgsEPLPLAHRILISLDIARALRFCH-----SHG---IVHLDVKPANILISEQGVCKLCDF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAVKHDSiLNTIDIPQNPKVGTKRYMAPEML---DDTmnvnifesfKRADIYSVGLVYWEIARRcsvggiveeyQLPYy 369
Cdd:cd13979  148 GCSVKLGE-GNEVGTPRSHIGGTYTYRAPELLkgeRVT---------PKADIYSFGITLWQMLTR----------ELPY- 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 370 dmvpsdpsiEEMRKV----VCDQKFRPSIPNQWQSCEALRvMGRIMRECWYANGAARLTA 425
Cdd:cd13979  207 ---------AGLRQHvlyaVVAKDLRPDLSGLEDSEFGQR-LRSLISRCWSAQPAERPNA 256
TFP_LU_ECD_ALK7 cd23540
extracellular domain (ECD) found in activin receptor-like kinase 7 (ALK-7) and similar ...
1-49 4.33e-28

extracellular domain (ECD) found in activin receptor-like kinase 7 (ALK-7) and similar proteins; ALK-7 (EC 2.7.11.30, also called activin receptor type-1C (ACVR1C), or activin receptor type IC (ACTR-IC)) is a serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. ALK-7 is the receptor for activin AB, activin B, and NODAL. It plays a role in cell differentiation, growth arrest and apoptosis. This model corresponds to the extracellular domain (ECD) of ALK-7, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467070  Cd Length: 76  Bit Score: 106.15  E-value: 4.33e-28
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835   1 MLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHL 49
Cdd:cd23540   28 MLTNGKEEVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHL 76
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
151-426 4.19e-27

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: 109.08  E-value: 4.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEV---WHGRWCGeDVAVKIF-----SSRDERSWFREAEIYQtvMLRHENILGFIAADNKDngtwTQLWLVSEY 222
Cdd:cd13978    1 LGSGGFGTVskaRHVSWFG-MVAIKCLhsspnCIEERKALLKEAEKME--RARHSYVLPLLGVCVER----RSLGLVMEY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIVTVAGMIK--LALSIASGLAHLHmeivgtQGKPAIAHRDIKSKNILVKKCETCAIADLGLA-VKHD 299
Cdd:cd13978   74 MENGSLKSLLEREIQDVPWSLRfrIIHEIALGMNFLH------NMDPPLLHHDLKPENILLDNHFHVKISDFGLSkLGMK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 300 SILNTIDIPQNPKVGTKRYMAPEMLDDTMnvniFESFKRADIYSVGLVYWEIARRcsvggiveeyQLPYYDmvpSDPSIE 379
Cdd:cd13978  148 SISANRRRGTENLGGTPIYMAPEAFDDFN----KKPTSKSDVYSFAIVIWAVLTR----------KEPFEN---AINPLL 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 380 EMRKVVCDQkfRPSIP--NQWQSCEALRVMGRIMRECWYANGAARLTAL 426
Cdd:cd13978  211 IMQIVSKGD--RPSLDdiGRLKQIENVQELISLMIRCWDGNPDARPTFL 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
146-350 6.69e-27

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 112.41  E-value: 6.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGR--WCGEDVAVKIFSSR-----DERSWF-REAEIYQTvmLRHENILGFIAADnKDNGTwtqLW 217
Cdd:COG0515   10 RILRLLGRGGMGVVYLARdlRLGRPVALKVLRPElaadpEARERFrREARALAR--LNHPNIVRVYDVG-EEDGR---PY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:COG0515   84 LVMEYVEGESLADLLRRRgPLPPAEALRILAQLAEALAAAH-----AAG---IVHRDIKPANILLTPDGRVKLIDFGIAR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 297 KHDSILNTidiPQNPKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWE 350
Cdd:COG0515  156 ALGGATLT---QTGTVVGTPGYMAPEQARGE------PVDPRSDVYSLGVTLYE 200
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
143-435 2.51e-26

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: 106.67  E-value: 2.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIF--SSRDERSWFREAeiyqTVM--LRHENILGFIAADNKDNGtwtqLWL 218
Cdd:cd05039    6 KDLKLGELIGKGEFGDVMLGDYRGQKVAVKCLkdDSTAAQAFLAEA----SVMttLRHPNLVQLLGVVLEGNG----LYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYL---NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd05039   78 VTEYMAKGSLVDYLrsrGRAVITRKDQLGFALDVCEGMEYLE--------SKKFVHRDLAARNVLVSEDNVAKVSDFGLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTIDIPqnpkvgtKRYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIArrcSVGgiveeyQLPYydmvPSD 375
Cdd:cd05039  150 KEASSNQDGGKLP-------IKWTAPEALRE----KKFST--KSDVWSFGILLWEIY---SFG------RVPY----PRI 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 376 PSIEEMRKVvcDQKFRPSIPnqwQSCEalRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05039  204 PLKDVVPHV--EKGYRMEAP---EGCP--PEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
151-365 2.70e-26

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: 106.97  E-value: 2.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW-CGEDVAVKIFSSRDERSWFRE--AEIYQTVMLRHENILGFIA-ADNKDNGTwtqlwLVSEYHEQG 226
Cdd:cd14066    1 IGSGGFGTVYKGVLeNGTVVAVKRLNEMNCAASKKEflTELEMLGRLRHPNLVRLLGyCLESDEKL-----LVYEYMPNG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 227 SLYDYLNRNIVTVAG----MIKLALSIASGLAHLHmeivgTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSIL 302
Cdd:cd14066   76 SLEDRLHCHKGSPPLpwpqRLKIAKGIARGLEYLH-----EECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSE 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 303 NTIDipQNPKVGTKRYMAPEmLDDTMNVNifesfKRADIYSVGLVYWEIA--RR--------CSVGGIVEEYQ 365
Cdd:cd14066  151 SVSK--TSAVKGTIGYLAPE-YIRTGRVS-----TKSDVYSFGVVLLELLtgKPavdenrenASRKDLVEWVE 215
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
143-435 5.27e-25

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: 103.14  E-value: 5.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGEDVAVK-IFSSRDERSWFREAEIyqTVMLRHENILGFIAADNKDNGTwtqLWLVSE 221
Cdd:cd05082    6 KELKLLQTIGKGEFGDVMLGDYRGNKVAVKcIKNDATAQAFLAEASV--MTQLRHSNLVQLLGVIVEEKGG---LYIVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIVTVAG---MIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKH 298
Cdd:cd05082   81 YMAKGSLVDYLRSRGRSVLGgdcLLKFSLDVCEAMEYLEGN--------NFVHRDLAARNVLVSEDNVAKVSDFGLTKEA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 DSILNTIDIPQnpkvgtkRYMAPEMLDDTMnvniFESfkRADIYSVGLVYWEIARRcsvgGIVEEYQLPYYDMVpsdPSI 378
Cdd:cd05082  153 SSTQDTGKLPV-------KWTAPEALREKK----FST--KSDVWSFGILLWEIYSF----GRVPYPRIPLKDVV---PRV 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 379 EEMRKVVCDQKFRPSIPNqwqscealrvmgrIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05082  213 EKGYKMDAPDGCPPAVYD-------------VMKNCWHLDAAMRPSFLQLREQLEHI 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
147-373 4.59e-24

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: 100.38  E-value: 4.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDerswfREAEIYQTVM--------LRHENILGFIAADNkdngTWTQL 216
Cdd:cd06627    4 LGDLIGRGAFGSVYKGlnLNTGEFVAIKQISLEK-----IPKSDLKSVMgeidllkkLNHPNIVKYIGSVK----TKDSL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSL------YDYLNRNIVtvAGMIKlalSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIA 290
Cdd:cd06627   75 YIILEYVENGSLasiikkFGKFPESLV--AVYIY---QVLEGLAYLH-----EQG---VIHRDIKGANILTTKDGLVKLA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 291 DLGLAVKhdsiLNTIDIPQNPKVGTKRYMAPEMlddtmnVNIFESFKRADIYSVGlvyweiarrCSVggiVE--EYQLPY 368
Cdd:cd06627  142 DFGVATK----LNEVEKDENSVVGTPYWMAPEV------IEMSGVTTASDIWSVG---------CTV---IEllTGNPPY 199

                 ....*
gi 161333835 369 YDMVP 373
Cdd:cd06627  200 YDLQP 204
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
149-352 8.03e-24

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: 99.90  E-value: 8.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWC--GEDVAVK---IFSSRDERSWFREAEIYqtVM--LRHENILGFIAADNKDNgtwtQLWLVSE 221
Cdd:cd06606    6 ELLGKGSFGSVYLALNLdtGELMAVKeveLSGDSEEELEALEREIR--ILssLKHPNIVRYLGTERTEN----TLNIFLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNR----NIVTVagmIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd06606   80 YVPGGSLASLLKKfgklPEPVV---RKYTRQILEGLEYLH-----SNG---IVHRDIKGANILVDSDGVVKLADFGCAKR 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 298 HDSILNTidIPQNPKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWEIA 352
Cdd:cd06606  149 LAEIATG--EGTKSLRGTPYWMAPEVIRGE------GYGRAADIWSLGCTVIEMA 195
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
146-430 9.20e-24

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: 99.51  E-value: 9.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGRWC--GEDVAVKIFS-SRDERSWF----REAEIYQtvMLRHENI---LGFIAADNKdngtwtq 215
Cdd:cd14003    3 ELGKTLGEGSFGKVKLARHKltGEKVAIKIIDkSKLKEEIEekikREIEIMK--LLNHPNIiklYEVIETENK------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNIvtvagmiKLALS--------IASGLAHLHMeivgtQGkpaIAHRDIKSKNILVKKCETC 287
Cdd:cd14003   74 IYLVMEYASGGELFDYIVNNG-------RLSEDearrffqqLISAVDYCHS-----NG---IVHRDLKLENILLDKNGNL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 288 AIADLGLA--VKHDSILNTIdipqnpkVGTKRYMAPEMLDDTMnvniFESFKrADIYSVGLV-YweiarrCSVGGiveey 364
Cdd:cd14003  139 KIIDFGLSneFRGGSLLKTF-------CGTPAYAAPEVLLGRK----YDGPK-ADVWSLGVIlY------AMLTG----- 195
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 365 QLPYydmvpSDPSIEEM-RKVVCDQKFRPSipnqWQSCEALRVMGRIMRecwyANGAARLTALRIKK 430
Cdd:cd14003  196 YLPF-----DDDNDSKLfRKILKGKYPIPS----HLSPDARDLIRRMLV----VDPSKRITIEEILN 249
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
152-422 2.06e-23

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: 98.49  E-value: 2.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGRWC--GEDVAVKIFSSRDerswfREAEIYQtvMLRHENILGFIAA--DNKDNGtwtqlwLVSEYHEQGS 227
Cdd:cd14060    2 GGGSFGSVYRAIWVsqDKEVAVKKLLKIE-----KEAEILS--VLSHRNIIQFYGAilEAPNYG------IVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYLNRNIVTVAGMIKL---ALSIASGLAHLHMEivgtqGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKH-DSILN 303
Cdd:cd14060   69 LFDYLNSNESEEMDMDQImtwATDIAKGMHYLHME-----APVKVIHRDLKSRNVVIAADGVLKICDFGASRFHsHTTHM 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 304 TIdipqnpkVGTKRYMAPEMLDDtmnvniFESFKRADIYSVGLVYWE-IARRCSVGGIvEEYQLPYydmvpsdpsieemr 382
Cdd:cd14060  144 SL-------VGTFPWMAPEVIQS------LPVSETCDTYSYGVVLWEmLTREVPFKGL-EGLQVAW-------------- 195
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 161333835 383 kVVCDQKFRPSIPnqwQSCEalRVMGRIMRECWYANGAAR 422
Cdd:cd14060  196 -LVVEKNERPTIP---SSCP--RSFAELMRRCWEADVKER 229
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
143-424 2.42e-23

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: 98.63  E-value: 2.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLV 219
Cdd:cd05068    8 KSLKLLRKLGSGQFGEVWEGLWNNTtPVAVKTLKpgTMDPEDFLREAQIMKK--LRHPKLIQLYAVCTLEE----PIYII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRN--IVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA-- 295
Cdd:cd05068   82 TELMKHGSLLEYLQGKgrSLQLPQLIDMAAQVASGMAYLESQ--------NYIHRDLAARNVLVGENNICKVADFGLArv 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTidipqnpKVGTK---RYMAPEmlddTMNVNIFeSFKrADIYSVGLVYWEiarrcsvggIVEEYQLPYydmv 372
Cdd:cd05068  154 IKVEDEYEA-------REGAKfpiKWTAPE----AANYNRF-SIK-SDVWSFGILLTE---------IVTYGRIPY---- 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 373 PSDPSIEEMRKVvcDQKFR-PSIPNqwqsCEAlrVMGRIMRECWYANGAARLT 424
Cdd:cd05068  208 PGMTNAEVLQQV--ERGYRmPCPPN----CPP--QLYDIMLECWKADPMERPT 252
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
150-351 2.54e-23

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: 98.62  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGEDVAVKIF-------SSRDERSWFREAEIYQtvMLRHENILGFIAADNKDngtwTQLWLVSEY 222
Cdd:cd14061    1 VIGVGGFGKVYRGIWRGEEVAVKAArqdpdedISVTLENVRQEARLFW--MLRHPNIIALRGVCLQP----PNLCLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqGKPAIAHRDIKSKNILVKKC--------ETCAIADLGL 294
Cdd:cd14061   75 ARGGALNRVLAGRKIPPHVLVDWAIQIARGMNYLHNE-----APVPIIHRDLKSSNILILEAienedlenKTLKITDFGL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 295 AVKHDsilNTIDIPQnpkVGTKRYMAPEMLddtmNVNIFEsfKRADIYSVGLVYWEI 351
Cdd:cd14061  150 AREWH---KTTRMSA---AGTYAWMAPEVI----KSSTFS--KASDVWSYGVLLWEL 194
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
147-373 4.22e-23

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: 97.66  E-value: 4.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVKIF---SSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSE 221
Cdd:cd05122    4 ILEKIGKGGFGVVYKARhkKTGQIVAIKKInleSKEKKESILNEIAILKK--CKHPNIVKYYGSYLKKD----ELWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIVT-----VAGMIKLALSiasGLAHLHmeivgtqgKPAIAHRDIKSKNILVK-KCETcAIADLGLA 295
Cdd:cd05122   78 FCSGGSLKDLLKNTNKTlteqqIAYVCKEVLK---GLEYLH--------SHGIIHRDIKAANILLTsDGEV-KLIDFGLS 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 296 VKhdsilNTIDIPQNPKVGTKRYMAPEMLDDTMNvnifeSFKrADIYSVGLVYWEIARRcsvggiveeyQLPYYDMVP 373
Cdd:cd05122  146 AQ-----LSDGKTRNTFVGTPYWMAPEVIQGKPY-----GFK-ADIWSLGITAIEMAEG----------KPPYSELPP 202
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
149-373 2.94e-22

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: 95.36  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVK--IFSSRDERSWFREAEIYQTvmLRHENILGFIAAdNKDNGTwtqLWLVSEYHE 224
Cdd:cd06614    6 EKIGEGASGEVYKAtdRATGKEVAIKkmRLRKQNKELIINEILIMKE--CKHPNIVDYYDS-YLVGDE---LWVVMEYMD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLNRNIVTVA-GMIK-LALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiL 302
Cdd:cd06614   80 GGSLTDIITQNPVRMNeSQIAyVCREVLQGLEYLH-----SQN---VIHRDIKSDNILLSKDGSVKLADFGFAAQ----L 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 303 NTIDIPQNPKVGTKRYMAPEML---DDTMNVnifesfkraDIYSVGLVYWEIArrcsvggiveEYQLPYYDMVP 373
Cdd:cd06614  148 TKEKSKRNSVVGTPYWMAPEVIkrkDYGPKV---------DIWSLGIMCIEMA----------EGEPPYLEEPP 202
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
152-424 1.42e-21

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: 93.12  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGRWCGE-DVAVKIF--SSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSEYHEQGSL 228
Cdd:cd05034    4 GAGQFGEVWMGVWNGTtKVAVKTLkpGTMSPEAFLQEAQIMKK--LRHDKLVQLYAVCSDEE----PIYIVTELMSKGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYL----NRNIvTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA-VKHDSILn 303
Cdd:cd05034   78 LDYLrtgeGRAL-RLPQLIDMAAQIASGMAYLESR--------NYIHRDLAARNILVGENNVCKVADFGLArLIEDDEY- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 304 tidipqNPKVGTK---RYMAPEmlddTMNVNIFeSFKrADIYSVGLVYWEiarrcsvggIVEEYQLPYydmvPSDPSIEE 380
Cdd:cd05034  148 ------TAREGAKfpiKWTAPE----AALYGRF-TIK-SDVWSFGILLYE---------IVTYGRVPY----PGMTNREV 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 161333835 381 MRKVvcDQKFRPSIPnqwQSCEALrvMGRIMRECWYANGAARLT 424
Cdd:cd05034  203 LEQV--ERGYRMPKP---PGCPDE--LYDIMLQCWKKEPEERPT 239
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
148-350 2.03e-21

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: 93.51  E-value: 2.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVWHGRWCGEDV--AVKI----FSSRDERSWFREAeiyqtVMLR---HENILGFIAAdnkdngtW---TQ 215
Cdd:cd13996   11 IELLGSGGFGSVYKVRNKVDGVtyAIKKirltEKSSASEKVLREV-----KALAklnHPNIVRYYTA-------WveePP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALS----IASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILV-KKCETCAI 289
Cdd:cd13996   79 LYIQMELCEGGTLRDWIDRRNSSSKNDRKLALElfkqILKGVSYIHsKGIV---------HRDLKPSNIFLdNDDLQVKI 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 290 ADLGLAV---KHDSILNTIDIPQNP-------KVGTKRYMAPEMLdDTMNVNifesfKRADIYSVGLVYWE 350
Cdd:cd13996  150 GDFGLATsigNQKRELNNLNNNNNGntsnnsvGIGTPLYASPEQL-DGENYN-----EKADIYSLGIILFE 214
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
146-345 2.97e-21

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: 92.54  E-value: 2.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGRW--CGEDVAVKIFS-----SRDERSWFREAEIYQtvMLRHENILGFIAA-DNKDNgtwtqLW 217
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHkkTGEEYAVKIIDkkklkSEDEEMLRREIEILK--RLDHPNIVKLYEVfEDDKN-----LY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYL-NRNIVT---VAGMIKlalSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCA---IA 290
Cdd:cd05117   76 LVMELCTGGELFDRIvKKGSFSereAAKIMK---QILSAVAYLH-----SQG---IVHRDLKPENILLASKDPDSpikII 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 291 DLGLAVKHDSilntiDIPQNPKVGTKRYMAPEMLDDTM-NvnifesfKRADIYSVG 345
Cdd:cd05117  145 DFGLAKIFEE-----GEKLKTVCGTPYYVAPEVLKGKGyG-------KKCDIWSLG 188
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
152-348 2.20e-20

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: 89.84  E-value: 2.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGR--WCGEDVAVK------IFSSRDERSWFREAEIYQTvmLRHENILGFIAA--DNKDngtwtqLWLVSE 221
Cdd:cd14007    9 GKGKFGNVYLARekKSGFIVALKvisksqLQKSGLEHQLRREIEIQSH--LRHPNILRLYGYfeDKKR------IYLILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIV----TVAGMIKlalSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd14007   81 YAPNGELYKELKKQKRfdekEAAKYIY---QLALALDYLH--------SKNIIHRDIKPENILLGSNGELKLADFGWSVH 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 298 hdsilntidIPQNPK---VGTKRYMAPEMLDDtmnvnifESF-KRADIYSVG-LVY 348
Cdd:cd14007  150 ---------APSNRRktfCGTLDYLPPEMVEG-------KEYdYKVDIWSLGvLCY 189
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
151-352 2.50e-20

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: 89.75  E-value: 2.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWH--GRWCGEDVAVK-----IFSSRDERSWFREAEIyQTVMLRHENILGFIAADNKDNgtwtQLWLVSEYH 223
Cdd:cd13997    8 IGSGSFSEVFKvrSKVDGCLYAVKkskkpFRGPKERARALREVEA-HAALGQHPNIVRYYSSWEEGG----HLYIQMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRN----IVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhd 299
Cdd:cd13997   83 ENGSLQDALEELspisKLSEAEVWDLLLQVALGLAFIHSK--------GIVHLDIKPDNIFISNKGTCKIGDFGLATR-- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 300 silntidIPQNPKV--GTKRYMAPEMLDDtmnvnIFESFKRADIYSVGLVYWEIA 352
Cdd:cd13997  153 -------LETSGDVeeGDSRYLAPELLNE-----NYTHLPKADIFSLGVTVYEAA 195
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
145-354 1.31e-19

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR 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: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 88.18  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGeDVAVKIF-----SSRDERSWFREAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLV 219
Cdd:cd14063    2 LEIKEVIGKGRFGRVHRGRWHG-DVAIKLLnidylNEEQLEAFKEEVAAYKNT--RHDNLVLFMGACMDPP----HLAIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETcAIADLGLAVK 297
Cdd:cd14063   75 TSLCKGRTLYSLIHerKEKFDFNKTVQIAQQICQGMGYLH--------AKGIIHKDLKSKNIFLENGRV-VITDFGLFSL 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 298 HDSI-----LNTIDIPQNPKVgtkrYMAPEM---LDDTMNVNIFESF-KRADIYSVGLVYWE-IARR 354
Cdd:cd14063  146 SGLLqpgrrEDTLVIPNGWLC----YLAPEIiraLSPDLDFEESLPFtKASDVYAFGTVWYElLAGR 208
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
147-429 1.66e-19

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: 87.88  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWCGE-DVAVKIFSSRDE---RSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSEY 222
Cdd:cd05148   10 LERKLGSGYFGEVWEGLWKNRvRVAIKILKSDDLlkqQDFQKEVQALKR--LRHKHLISLFAVCSVGE----PVYIITEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNR---NIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA--VK 297
Cdd:cd05148   84 MEKGSLLAFLRSpegQVLPVASLIDMACQVAEGMAYLEEQ--------NSIHRDLAARNILVGEDLVCKVADFGLArlIK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 HDsilntIDIPQNPKVGTKrYMAPEMLddtmNVNIFESfkRADIYSVGLVYWEIARRcsvGGIveeyqlPYYDMVPSdps 377
Cdd:cd05148  156 ED-----VYLSSDKKIPYK-WTAPEAA----SHGTFST--KSDVWSFGILLYEMFTY---GQV------PYPGMNNH--- 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 378 iEEMRKVvcDQKFRPSIPnqwQSCEAlrVMGRIMRECWYANGAARLT--ALRIK 429
Cdd:cd05148  212 -EVYDQI--TAGYRMPCP---AKCPQ--EIYKIMLECWAAEPEDRPSfkALREE 257
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
170-350 2.89e-19

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: 87.84  E-value: 2.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 170 AVKIFSSR---DERSWF-----REAEIYQTvmLRHENILGFIAADNKDNGTwtqLWLVSEYHEQgSLYDYLNRNIVT--- 238
Cdd:cd14001   32 AVKKINSKcdkGQRSLYqerlkEEAKILKS--LNHPNIVGFRAFTKSEDGS---LCLAMEYGGK-SLNDLIEERYEAglg 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 239 ---VAGMIKLALSIASGLAHLHMEivgtqgkPAIAHRDIKSKNILVK-KCETCAIADLGLAVKHDSILNTIDIPQNPKVG 314
Cdd:cd14001  106 pfpAATILKVALSIARALEYLHNE-------KKILHGDIKSGNVLIKgDFESVKLCDFGVSLPLTENLEVDSDPKAQYVG 178
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 161333835 315 TKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWE 350
Cdd:cd14001  179 TEPWKAKEALEEGGVIT-----DKADIFAYGLVLWE 209
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
151-354 3.75e-19

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: 86.39  E-value: 3.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW---HgRWCGEDVAVKIFSSRDER-SWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSEYHEQG 226
Cdd:cd14065    1 LGKGFFGEVYkvtH-RETGKVMVMKELKRFDEQrSFLKEVKLMRR--LSHPNILRFIGVCVKDN----KLNFITEYVNGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 227 SLYDYLNRNIVTV--AGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCE---TCAIADLGLAVKhdsi 301
Cdd:cd14065   74 TLEELLKSMDEQLpwSQRVSLAKDIASGMAYLHSK--------NIIHRDLNSKNCLVREANrgrNAVVADFGLARE---- 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 302 lnTIDIPQNPK--------VGTKRYMAPEMLDDtmnvnifESFKR-ADIYSVGLVYWEIARR 354
Cdd:cd14065  142 --MPDEKTKKPdrkkrltvVGSPYWMAPEMLRG-------ESYDEkVDVFSFGIVLCEIIGR 194
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
145-422 5.32e-19

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk 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: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 86.08  E-value: 5.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREaEIYQTVMLRHEN---ILGFIAadnkDNGtwtqLWLVSE 221
Cdd:cd05083    8 LTLGEIIGEGEFGAVLQGEYMGQKVAVKNIKCDVTAQAFLE-ETAVMTKLQHKNlvrLLGVIL----HNG----LYIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYL---NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKH 298
Cdd:cd05083   79 LMSKGNLVNFLrsrGRALVPVIQLLQFSLDVAEGMEYLESK--------KLVHRDLAARNILVSEDGVAKISDFGLAKVG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 DSILNTIDIPQnpkvgtkRYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIArrcSVGgiveeyQLPYYDMvpsdpSI 378
Cdd:cd05083  151 SMGVDNSRLPV-------KWTAPEALKN----KKFSS--KSDVWSYGVLLWEVF---SYG------RAPYPKM-----SV 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 161333835 379 EEMRKVVcDQKFRPSIPnqwQSCEALrvMGRIMRECWYANGAAR 422
Cdd:cd05083  204 KEVKEAV-EKGYRMEPP---EGCPPD--VYSIMTSCWEAEPGKR 241
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
142-435 5.44e-19

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs 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. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR 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: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 86.27  E-value: 5.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 142 ARTIVLQEIVGKGRFGEVWHGRWC-----GEDVAVKI----FSSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNgt 212
Cdd:cd05033    3 ASYVTIEKVIGGGEFGEVCSGSLKlpgkkEIDVAIKTlksgYSDKQRLDFLTEASIMG--QFDHPNVIRLEGVVTKSR-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 wtQLWLVSEYHEQGSLYDYLNRN--IVTVAGMIKLALSIASGLAHL-HMEIVgtqgkpaiaHRDIKSKNILVKKCETCAI 289
Cdd:cd05033   79 --PVMIVTEYMENGSLDKFLRENdgKFTVTQLVGMLRGIASGMKYLsEMNYV---------HRDLAARNILVNSDLVCKV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 290 ADLGLA-VKHDSilntidipqNPKVGTK------RYMAPEMLDdtmnvniFESFKRA-DIYSVGLVYWEIarrCSVGgiv 361
Cdd:cd05033  148 SDFGLSrRLEDS---------EATYTTKggkipiRWTAPEAIA-------YRKFTSAsDVWSFGIVMWEV---MSYG--- 205
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 362 eeyQLPYYDMvpsdPSIEEMRKVvcDQKFRPSIPnqwQSCEAlrVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05033  206 ---ERPYWDM----SNQDVIKAV--EDGYRLPPP---MDCPS--ALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
151-422 5.56e-19

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting 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. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K 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: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 86.04  E-value: 5.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVK-----IFSSRDERSWF-REAEIYqtVMLRHENILGFIAADNKDNgtwTQLWLVSEYHE 224
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKIVAIKryranTYCSKSDVDMFcREVSIL--CRLNHPCVIQFVGACLDDP---SQFAIVTQYVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHmeivgTQGKPAIaHRDIKSKNILVKKCETCAIADLG----LAVKH 298
Cdd:cd14064   76 GGSLFSLLHeqKRVIDLQSKLIIAVDVAKGMEYLH-----NLTQPII-HRDLNSHNILLYEDGHAVVADFGesrfLQSLD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 DSilntiDIPQNPkvGTKRYMAPEMLDDTMNVNIfesfkRADIYSVGLVYWEIARRcsvggiveeyQLPYYDMVPSDPSI 378
Cdd:cd14064  150 ED-----NMTKQP--GNLRWMAPEVFTQCTRYSI-----KADVFSYALCLWELLTG----------EIPFAHLKPAAAAA 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 379 EEMRKvvcdqKFRPSIPNQW-QSCEALRVMGrimrecWYANGAAR 422
Cdd:cd14064  208 DMAYH-----HIRPPIGYSIpKPISSLLMRG------WNAEPESR 241
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
147-401 1.08e-18

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: 85.40  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRW--CGEDVAVKIFSSR-DERSWFREAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLVSEYH 223
Cdd:cd06612    7 ILEKLGEGSYGSVYKAIHkeTGQVVAIKVVPVEeDLQEIIKEISILKQC--DSPYIVKYYGSYFKNT----DLWIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLN-RNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdSI 301
Cdd:cd06612   81 GAGSVSDIMKiTNKTLTEEEIAAILyQTLKGLEYLH--------SNKKIHRDIKAGNILLNEEGQAKLADFGVS----GQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 302 LNTIDIPQNPKVGTKRYMAPEMLDDTmNVNifesfKRADIYSVGLVYWEIArrcsvggiveEYQLPYYDMVPsdpsieeM 381
Cdd:cd06612  149 LTDTMAKRNTVIGTPFWMAPEVIQEI-GYN-----NKADIWSLGITAIEMA----------EGKPPYSDIHP-------M 205
                        250       260
                 ....*....|....*....|....
gi 161333835 382 RkVVCDQKFRP----SIPNQWQSC 401
Cdd:cd06612  206 R-AIFMIPNKPpptlSDPEKWSPE 228
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
141-351 2.22e-18

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: 85.08  E-value: 2.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 141 IARTIVLQEIVGKGRFGEVWHGRWCGeDVAVKIFSSRD----ERSWFREaEIYQTVMLRHENILGFIAADNKDNgtwtqL 216
Cdd:cd14149   10 EASEVMLSTRIGSGSFGTVYKGKWHG-DVAVKILKVVDptpeQFQAFRN-EVAVLRKTRHVNILLFMGYMTKDN-----L 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd14149   83 AIVTQWCEGSSLYKHLHvqETKFQMFQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVKIGDFGL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 295 AVKHDSILNTIDIPQnpKVGTKRYMAPEMLddTMNVNIFESFKrADIYSVGLVYWEI 351
Cdd:cd14149  155 ATVKSRWSGSQQVEQ--PTGSILWMAPEVI--RMQDNNPFSFQ-SDVYSYGIVLYEL 206
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
145-424 2.69e-18

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR 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: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 84.78  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGED--------VAVKIF----SSRDERSWFREAEIYQTVMlRHENILGFIAADNKDNgt 212
Cdd:cd05053   14 LTLGKPLGEGAFGQVVKAEAVGLDnkpnevvtVAVKMLkddaTEKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQDG-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 wtQLWLVSEYHEQGSLYDYLNRN-----------------IVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIK 275
Cdd:cd05053   91 --PLYVVVEYASKGNLREFLRARrppgeeaspddprvpeeQLTQKDLVSFAYQVARGMEYL-------ASKKCI-HRDLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 276 SKNILVKKCETCAIADLGLAvkHDsiLNTIDIPQnpKVGTKR----YMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEI 351
Cdd:cd05053  161 ARNVLVTEDNVMKIADFGLA--RD--IHHIDYYR--KTTNGRlpvkWMAPEALFD----RVYTH--QSDVWSFGVLLWEI 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 352 ArrcSVGGIveeyqlPYydmvPSDPsIEEMRKVVcDQKFRPSIPnqwQSCEalRVMGRIMRECWYANGAARLT 424
Cdd:cd05053  229 F---TLGGS------PY----PGIP-VEELFKLL-KEGHRMEKP---QNCT--QELYMLMRDCWHEVPSQRPT 281
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
145-351 2.80e-18

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: 84.32  E-value: 2.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGEDVAVKIFS-------SRDERSWFREAEIYqtVMLRHENILGFIAADNKDngtwTQLW 217
Cdd:cd14145    8 LVLEEIIGIGGFGKVYRAIWIGDEVAVKAARhdpdediSQTIENVRQEAKLF--AMLKHPNIIALRGVCLKE----PNLC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVgtqgKPAIaHRDIKSKNILV-KKCE-------TCAI 289
Cdd:cd14145   82 LVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAI----VPVI-HRDLKSSNILIlEKVEngdlsnkILKI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 290 ADLGLAVK-HDSIlntidipQNPKVGTKRYMAPEMLDDTMnvniFEsfKRADIYSVGLVYWEI 351
Cdd:cd14145  157 TDFGLAREwHRTT-------KMSAAGTYAWMAPEVIRSSM----FS--KGSDVWSYGVLLWEL 206
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
187-433 3.68e-18

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: 83.98  E-value: 3.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 187 EIYQTVMLRHENILGFIAADNKDngtwTQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLAL--SIASGLAHLHMEIVGtq 264
Cdd:cd13992   46 ELNQLKELVHDNLNKFIGICINP----PNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSSFikDIVKGMNYLHSSSIG-- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 265 gkpaiAHRDIKSKNILVKKCETCAIADLGLA-VKHDSILNTIDIPQNPKvgTKRYMAPEMLDDTMNVNifESFKRADIYS 343
Cdd:cd13992  120 -----YHGRLKSSNCLVDSRWVVKLTDFGLRnLLEEQTNHQLDEDAQHK--KLLWTAPELLRGSLLEV--RGTQKGDVYS 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 344 VGLVYWEIArrcsvggiveEYQLPYYDMVPSDPSIEEMRkvvCDQK-FRPSIPNQWQSCEALRVMgrIMRECWYANGAAR 422
Cdd:cd13992  191 FAIILYEIL----------FRSDPFALEREVAIVEKVIS---GGNKpFRPELAVLLDEFPPRLVL--LVKQCWAENPEKR 255
                        250
                 ....*....|.
gi 161333835 423 LTALRIKKTIS 433
Cdd:cd13992  256 PSFKQIKKTLT 266
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
150-351 3.75e-18

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: 83.88  E-value: 3.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGEDVAVKIFSSRDER-------SWFREAEIYqtVMLRHENILGFIAADNKDngtwTQLWLVSEY 222
Cdd:cd14148    1 IIGVGGFGKVYKGLWRGEEVAVKAARQDPDEdiavtaeNVRQEARLF--WMLQHPNIIALRGVCLNP----PHLCLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVgtqgkPAIAHRDIKSKNILV-KKCE-------TCAIADLGL 294
Cdd:cd14148   75 ARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAI-----VPIIHRDLKSSNILIlEPIEnddlsgkTLKITDFGL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 295 AVK-HDSIlntidipQNPKVGTKRYMAPEMLddtmNVNIFEsfKRADIYSVGLVYWEI 351
Cdd:cd14148  150 AREwHKTT-------KMSAAGTYAWMAPEVI----RLSLFS--KSSDVWSFGVLLWEL 194
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
151-354 3.82e-18

Catalytic domain of the Dual-specificity protein kinase, Testicular 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. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK 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: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 83.68  E-value: 3.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW---HgRWCGEDVAVKIFSSRDER-SWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSEYHEQG 226
Cdd:cd14155    1 IGSGFFSEVYkvrH-RTSGQVMALKMNTLSSNRaNMLREVQLMNR--LSHPNILRFMGVCVHQG----QLHALTEYINGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 227 SLYDYLNRNIVTVAGM-IKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCE---TCAIADLGLAVKhdsil 302
Cdd:cd14155   74 NLEQLLDSNEPLSWTVrVKLALDIARGLSYLHSK--------GIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEK----- 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 303 ntidIPQN-------PKVGTKRYMAPEMLDDtmnvnifESF-KRADIYSVGLVYWEIARR 354
Cdd:cd14155  141 ----IPDYsdgkeklAVVGSPYWMAPEVLRG-------EPYnEKADVFSYGIILCEIIAR 189
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
151-424 3.98e-18

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: 83.43  E-value: 3.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIYQtvMLRHENILGFIAADNKDngtwtQLWLVSEYHEQGS 227
Cdd:cd14203    3 LGQGCFGEVWMGTWNGTtKVAIKTLKpgTMSPEAFLEEAQIMK--KLRHDKLVQLYAVVSEE-----PIYIVTEFMSKGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYLNR---NIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGLAVKHDsiln 303
Cdd:cd14203   76 LLDFLKDgegKYLKLPQLVDMAAQIASGMAYIErMNYI---------HRDLRAANILVGDNLVCKIADFGLARLIE---- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 304 tiDIPQNPKVGTK---RYMAPEmlddtmnVNIFESFK-RADIYSVGLVYWEiarrcsvggIVEEYQLPYYDMVpsdpSIE 379
Cdd:cd14203  143 --DNEYTARQGAKfpiKWTAPE-------AALYGRFTiKSDVWSFGILLTE---------LVTKGRVPYPGMN----NRE 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 380 EMRKVvcDQKFRPSIPnqwQSCEAlrVMGRIMRECWYANGAARLT 424
Cdd:cd14203  201 VLEQV--ERGYRMPCP---PGCPE--SLHELMCQCWRKDPEERPT 238
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
149-352 4.20e-18

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: 83.51  E-value: 4.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRwCGED---VAVKIFSSR-----DERSWFREAEIYQTVMlRHENILGFIAAdnkdngtWTQ---LW 217
Cdd:cd14050    7 SKLGEGSFGEVFKVR-SREDgklYAVKRSRSRfrgekDRKRKLEEVERHEKLG-EHPNCVRFIKA-------WEEkgiLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHeQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:cd14050   78 IQTELC-DTSLQQYCEEThSLPESEVWNILLDLLKGLKHLH-----DHG---LIHLDIKPANIFLSKDGVCKLGDFGLVV 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 297 KhdsiLNTIDIpQNPKVGTKRYMAPEMLDDTMNvnifesfKRADIYSVGLVYWEIA 352
Cdd:cd14050  149 E----LDKEDI-HDAQEGDPRYMAPELLQGSFT-------KAADIFSLGITILELA 192
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
151-351 9.01e-18

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 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: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 83.07  E-value: 9.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGE---VWHgRWCGEDVAVKIFSSRDE---RSWFREAEIYQTvmLRHENILGFIAADNKDngtwTQLWLVSEYHE 224
Cdd:cd14222    1 LGKGFFGQaikVTH-KATGKVMVMKELIRCDEetqKTFLTEVKVMRS--LDHPNVLKFIGVLYKD----KRLNLLTEFIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGLA--VKHDS 300
Cdd:cd14222   74 GGTLKDFLrADDPFPWQQKVSFAKGIASGMAYLHsMSII---------HRDLNSHNCLIKLDKTVVVADFGLSrlIVEEK 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 301 ILNTIDIPQNPK--------------VGTKRYMAPEMLddtmnvNIFESFKRADIYSVGLVYWEI 351
Cdd:cd14222  145 KKPPPDKPTTKKrtlrkndrkkrytvVGNPYWMAPEML------NGKSYDEKVDIFSFGIVLCEI 203
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
143-351 1.03e-17

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: 82.77  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGEDVAVKifSSR---DE------RSWFREAEIYQtvMLRHENILGFIAADNKDngtw 213
Cdd:cd14147    3 QELRLEEVIGIGGFGKVYRGSWRGELVAVK--AARqdpDEdisvtaESVRQEARLFA--MLAHPNIIALKAVCLEE---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 TQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVgtqgKPAIaHRDIKSKNIL-----VKKC---E 285
Cdd:cd14147   75 PNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEAL----VPVI-HRDLKSNNILllqpiENDDmehK 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 286 TCAIADLGLAVK-HDSIlntidipQNPKVGTKRYMAPEMLDDTMnvniFESFkrADIYSVGLVYWEI 351
Cdd:cd14147  150 TLKITDFGLAREwHKTT-------QMSAAGTYAWMAPEVIKAST----FSKG--SDVWSFGVLLWEL 203
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
150-351 1.55e-17

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: 82.39  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGEDVAVKIFSSRDER-------SWFREAEIYQtvMLRHENILGFIAADNKDngtwTQLWLVSEY 222
Cdd:cd14146    1 IIGVGGFGKVYRATWKGQEVAVKAARQDPDEdikataeSVRQEAKLFS--MLRHPNIIKLEGVCLEE----PNLCLVMEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSlydyLNRNIVTVAG--------------MIKLALSIASGLAHLHMEIVgtqgkPAIAHRDIKSKNI-LVKKCE-- 285
Cdd:cd14146   75 ARGGT----LNRALAAANAapgprrarripphiLVNWAVQIARGMLYLHEEAV-----VPILHRDLKSSNIlLLEKIEhd 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 286 -----TCAIADLGLAVK-HDSIlntidipQNPKVGTKRYMAPEMLDDTMnvniFEsfKRADIYSVGLVYWEI 351
Cdd:cd14146  146 dicnkTLKITDFGLAREwHRTT-------KMSAAGTYAWMAPEVIKSSL----FS--KGSDIWSYGVLLWEL 204
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
132-352 1.57e-17

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: 82.36  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 132 GLPLLVQRTIARTIVLQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSRDERswfrEAEIYQTV-MLR----HENILGFIA 204
Cdd:cd06636    5 DIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVktGQLAAIKVMDVTEDE----EEEIKLEInMLKkyshHRNIATYYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 205 ADNKDN--GTWTQLWLVSEYHEQGSLYDYLNR---NIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNI 279
Cdd:cd06636   81 AFIKKSppGHDDQLWLVMEFCGAGSVTDLVKNtkgNALKEDWIAYICREILRGLAHLHAH--------KVIHRDIKGQNV 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 280 LVKKCETCAIADLGLAVKHDSILNTidipQNPKVGTKRYMAPEMLDDTMNVNIFESFkRADIYSVGLVYWEIA 352
Cdd:cd06636  153 LLTENAEVKLVDFGVSAQLDRTVGR----RNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA 220
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
145-435 2.00e-17

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: 82.03  E-value: 2.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGeDVAVKIFS----SRDERSWFREaEIYQTVMLRHENILGFIAADNKdngtwTQLWLVS 220
Cdd:cd14151   10 ITVGQRIGSGSFGTVYKGKWHG-DVAVKMLNvtapTPQQLQAFKN-EVGVLRKTRHVNILLFMGYSTK-----PQLAIVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRnIVTVAGMIKL---ALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd14151   83 QWCEGSSLYHHLHI-IETKFEMIKLidiARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIGDFGLATV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 HDSILNTIDIPQnpKVGTKRYMAPEM--LDDTmNVNIFESfkraDIYSVGLVYWEIARRcsvggiveeyQLPYYDMVPSD 375
Cdd:cd14151  154 KSRWSGSHQFEQ--LSGSILWMAPEVirMQDK-NPYSFQS----DVYAFGIVLYELMTG----------QLPYSNINNRD 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 376 PSIEemrkVVCDQKFRPSIPNQWQSCEalRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14151  217 QIIF----MVGRGYLSPDLSKVRSNCP--KAMKRLMAECLKKKRDERPLFPQILASIELL 270
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
147-352 2.01e-17

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: 82.46  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFS-SRDErswfrEAEIYQTV-MLR----HENILGFIAADNKDN--GTWTQL 216
Cdd:cd06637   10 LVELVGNGTYGQVYKGRHVktGQLAAIKVMDvTGDE-----EEEIKQEInMLKkyshHRNIATYYGAFIKKNppGMDDQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNR---NIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd06637   85 WLVMEFCGAGSVTDLIKNtkgNTLKEEWIAYICREILRGLSHLHQH--------KVIHRDIKGQNVLLTENAEVKLVDFG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 294 LAVKHDSILNTidipQNPKVGTKRYMAPEMLDDTMNVNIFESFKrADIYSVGLVYWEIA 352
Cdd:cd06637  157 VSAQLDRTVGR----RNTFIGTPYWMAPEVIACDENPDATYDFK-SDLWSLGITAIEMA 210
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
147-373 2.02e-17

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: 81.58  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVKIFS---SRDERSWFREAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLVSE 221
Cdd:cd06613    4 LIQRIGSGTYGDVYKARniATGELAAVKVIKlepGDDFEIIQQEISMLKEC--RHPNIVAYFGSYLRRD----KLWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDylnrnIVTVAGMIKlALSIA-------SGLAHLHmeivgTQGKpaiAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd06613   78 YCGGGSLQD-----IYQVTGPLS-ELQIAyvcretlKGLAYLH-----STGK---IHRDIKGANILLTEDGDVKLADFGV 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 295 AVKhdsILNTIDiPQNPKVGTKRYMAPEMLDDTMNVNIFEsfkRADIYSVGLVYWEIArrcsvggiveEYQLPYYDMVP 373
Cdd:cd06613  144 SAQ---LTATIA-KRKSFIGTPYWMAPEVAAVERKGGYDG---KCDIWALGITAIELA----------ELQPPMFDLHP 205
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
151-354 2.37e-17

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK 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: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 81.79  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGE---VWHgRWCGEDVAVKIFSSRDE---RSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSEYHE 224
Cdd:cd14154    1 LGKGFFGQaikVTH-RETGEVMVMKELIRFDEeaqRNFLKEVKVMRS--LDHPNVLKFIGVLYKDK----KLNLITEYIP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGLAVKHD-- 299
Cdd:cd14154   74 GGTLKDVLKdmARPLPWAQRVRFAKDIASGMAYLHsMNII---------HRDLNSHNCLVREDKTVVVADFGLARLIVee 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 300 ----------SILNTIDIPQNPK----VGTKRYMAPEMLddtmnvNIFESFKRADIYSVGLVYWEIARR 354
Cdd:cd14154  145 rlpsgnmspsETLRHLKSPDRKKrytvVGNPYWMAPEML------NGRSYDEKVDIFSFGIVLCEIIGR 207
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
147-347 2.49e-17

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: 81.63  E-value: 2.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW--HGRWCGEDVAVK-IFSS---RDERSWFREAEIYQTVML-----RHENILGFIaaDNKDNGTWTq 215
Cdd:cd13993    4 LISPIGEGAYGVVYlaVDLRTGRKYAIKcLYKSgpnSKDGNDFQKLPQLREIDLhrrvsRHPNIITLH--DVFETEVAI- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 lWLVSEYHEQGSLYDYL--NRNIVTVAGMIK-LALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCE-TCAIAD 291
Cdd:cd13993   81 -YIVLEYCPNGDLFEAIteNRIYVGKTELIKnVFLQLIDAVKHCH-----SLG---IYHRDIKPENILLSQDEgTVKLCD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 292 LGLAVkhdsilnTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLV 347
Cdd:cd13993  152 FGLAT-------TEKISMDFGVGSEFYMAPECFDEVGRSLKGYPCAAGDIWSLGII 200
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
151-415 2.60e-17

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: 81.00  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKifSSRDERswfrEAEIYQTVMLRHENILGFiaadnkdNGTWTQ---LWLVSEYHEQGS 227
Cdd:cd14059    1 LGSGAQGAVFLGKFRGEEVAVK--KVRDEK----ETDIKHLRKLNHPNIIKF-------KGVCTQapcYCILMEYCPYGQ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYL-NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTID 306
Cdd:cd14059   68 LYEVLrAGREITPSLLVDWSKQIASGMNYLHLH--------KIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMS 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 307 IpqnpkVGTKRYMAPEMLDdtmnvNIFESFKrADIYSVGLVYWEIarrcsVGGiveeyQLPYYDmVPSDPSIEEmrkvVC 386
Cdd:cd14059  140 F-----AGTVAWMAPEVIR-----NEPCSEK-VDIWSFGVVLWEL-----LTG-----EIPYKD-VDSSAIIWG----VG 193
                        250       260       270
                 ....*....|....*....|....*....|
gi 161333835 387 DQKFRPSIPNqwqSC-EALRVMgriMRECW 415
Cdd:cd14059  194 SNSLQLPVPS---TCpDGFKLL---MKQCW 217
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
144-424 5.00e-17

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: 80.86  E-value: 5.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd05072    8 SIKLVKKLGAGQFGEVWMGYYNNStKVAVKTLKpgTMSVQAFLEEANLMKT--LQHDKLVRLYAVVTKEE----PIYIIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNI---VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA-V 296
Cdd:cd05072   82 EYMAKGSLLDFLKSDEggkVLLPKLIDFSAQIAEGMAYIE--------RKNYIHRDLRAANVLVSESLMCKIADFGLArV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 KHDsilNTIDIPQNPKVGTKrYMAPEMLDdtmnvniFESFK-RADIYSVGLVYWEiarrcsvggIVEEYQLPYYDMVPSD 375
Cdd:cd05072  154 IED---NEYTAREGAKFPIK-WTAPEAIN-------FGSFTiKSDVWSFGILLYE---------IVTYGKIPYPGMSNSD 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 161333835 376 PsieemrKVVCDQKFR-PSIPNqwqsCEAlrVMGRIMRECWYANGAARLT 424
Cdd:cd05072  214 V------MSALQRGYRmPRMEN----CPD--ELYDIMKTCWKEKAEERPT 251
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
152-355 5.40e-17

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: 80.89  E-value: 5.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGRW------CGEDVAVKIF-------SSRDersWFREAEIYQTvmLRHENILGFIAADNKDNGTwtQLWL 218
Cdd:cd05038   13 GEGHFGSVELCRYdplgdnTGEQVAVKSLqpsgeeqHMSD---FKREIEILRT--LDHEYIVKYKGVCESPGRR--SLRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGlahlhMEIVGTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAv 296
Cdd:cd05038   86 IMEYLPSGSLRDYLqrHRDQIDLKRLLLFASQICKG-----MEYLGSQR---YIHRDLAARNILVESEDLVKISDFGLA- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 297 khdSILNTID---IPQNPKVGTKRYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIARRC 355
Cdd:cd05038  157 ---KVLPEDKeyyYVKEPGESPIFWYAPECLRE----SRFSS--ASDVWSFGVTLYELFTYG 209
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
151-351 5.61e-17

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: 81.01  E-value: 5.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKIF------SSRDERSWFrEAEIYQTVMLRHENI---LGFiaadNKDNgtwTQLWLVSE 221
Cdd:cd14158   23 LGEGGFGVVFKGYINDKNVAVKKLaamvdiSTEDLTKQF-EQEIQVMAKCQHENLvelLGY----SCDG---PQLCLVYT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYL----NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd14158   95 YMPNGSLLDRLaclnDTPPLSWHMRCKIAQGTANGINYLHEN--------NHIHRDIKSANILLDETFVPKISDFGLARA 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 298 HDSILNTIDIPQnpKVGTKRYMAPEMLDDTMNVnifesfkRADIYSVGLVYWEI 351
Cdd:cd14158  167 SEKFSQTIMTER--IVGTTAYMAPEALRGEITP-------KSDIFSFGVVLLEI 211
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
151-354 6.18e-17

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: 79.97  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWC--GEDVAVKIFSS--RDERSWFREAEIYQ--TVMLRHENILGFIaaDNKDNGTWTQLWLVSEYHE 224
Cdd:cd05118    7 IGEGAFGTVWLARDKvtGEKVAIKKIKNdfRHPKAALREIKLLKhlNDVEGHPNIVKLL--DVFEHRGGNHLCLVFELMG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QgSLYDYLNRNI--VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKC-ETCAIADLGLAVKHDSI 301
Cdd:cd05118   85 M-NLYELIKDYPrgLPLDLIKSYLYQLLQALDFLH--------SNGIIHRDLKPENILINLElGQLKLADFGLARSFTSP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 302 LNTidipqnPKVGTKRYMAPEMLddtmnVNIFESFKRADIYSVGLVYWEIARR 354
Cdd:cd05118  156 PYT------PYVATRWYRAPEVL-----LGAKPYGSSIDIWSLGCILAELLTG 197
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
145-422 9.43e-17

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: 79.91  E-value: 9.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRW--CGED---VAVKI----FSSRDERSWFREAEIYQtvMLRHENILGFIAADNKDngtwTQ 215
Cdd:cd05065    6 VKIEEVIGAGEFGEVCRGRLklPGKReifVAIKTlksgYTEKQRRDFLSEASIMG--QFDHPNIIHLEGVVTKS----RP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRN-----IVTVAGMIKlalSIASGLAHL-HMEIVgtqgkpaiaHRDIKSKNILVKKCETCAI 289
Cdd:cd05065   80 VMIITEFMENGALDSFLRQNdgqftVIQLVGMLR---GIAAGMKYLsEMNYV---------HRDLAARNILVNSNLVCKV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 290 ADLGLAVKHDSilNTIDIPQNPKVGTK---RYMAPEMLDdtmnvniFESFKRA-DIYSVGLVYWEIArrcSVGgiveeyQ 365
Cdd:cd05065  148 SDFGLSRFLED--DTSDPTYTSSLGGKipiRWTAPEAIA-------YRKFTSAsDVWSYGIVMWEVM---SYG------E 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 366 LPYYDMVPSD--PSIEemrkvvcdQKFRPSIPnqwQSCEAlrVMGRIMRECWYANGAAR 422
Cdd:cd05065  210 RPYWDMSNQDviNAIE--------QDYRLPPP---MDCPT--ALHQLMLDCWQKDRNLR 255
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
149-350 1.15e-16

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: 79.72  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREaeIYQTVM----LRHENILGFIAAdnkdngtWTQ---LWLV 219
Cdd:cd14046   12 QVLGKGAFGQVVKVRnkLDGRYYAIKKIKLRSESKNNSR--ILREVMllsrLNHQHVVRYYQA-------WIEranLYIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRNIV-TVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKH 298
Cdd:cd14046   83 MEYCEKSTLRDLIDSGLFqDTDRLWRLFRQILEGLAYIH-----SQG---IIHRDLKPVNIFLDSNGNVKIGDFGLATSN 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 299 --------------DSILNTIDIPQNPKVGTKRYMAPEMLDDTmNVNIFEsfkRADIYSVGLVYWE 350
Cdd:cd14046  155 klnvelatqdinksTSAALGSSGDLTGNVGTALYVAPEVQSGT-KSTYNE---KVDMYSLGIIFFE 216
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
151-347 1.74e-16

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: 78.91  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW--HGRWCGEDVAVKIFSSRDERSWFREA---EIYQTVMLRHENILGFIAADNkdNGTWtqLWLVSEYHEQ 225
Cdd:cd14069    9 LGEGAFGEVFlaVNRNTEEAVAVKFVDMKRAPGDCPENikkEVCIQKMLSHKNVVRFYGHRR--EGEF--QYLFLEYASG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 GSLYDYLNRNIvtvaGM-IKLA----LSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLA----V 296
Cdd:cd14069   85 GELFDKIEPDV----GMpEDVAqfyfQQLMAGLKYLH-----SCG---ITHRDIKPENLLLDENDNLKISDFGLAtvfrY 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 297 KHDSILntidipQNPKVGTKRYMAPEMLDDtmnvnifESFK--RADIYSVGLV 347
Cdd:cd14069  153 KGKERL------LNKMCGTLPYVAPELLAK-------KKYRaePVDVWSCGIV 192
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
151-375 1.84e-16

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: 78.59  E-value: 1.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGeDVAVKIFSSRDERSWFREAEIYQTVML---RHENILGFIAADNKDngtwtQLWLVSEYHEQGS 227
Cdd:cd14062    1 IGSGSFGTVYKGRWHG-DVAVKKLNVTDPTPSQLQAFKNEVAVLrktRHVNILLFMGYMTKP-----QLAIVTQWCEGSS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYLN--RNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA-VKhdSILNT 304
Cdd:cd14062   75 LYKHLHvlETKFEMLQLIDIARQTAQGMDYLHAK--------NIIHRDLKSNNIFLHEDLTVKIGDFGLAtVK--TRWSG 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 305 IDIPQNPkVGTKRYMAPE---MLDDtmnvNIFeSFkRADIYSVGLVYWEIARRcsvggiveeyQLPYYDMVPSD 375
Cdd:cd14062  145 SQQFEQP-TGSILWMAPEvirMQDE----NPY-SF-QSDVYAFGIVLYELLTG----------QLPYSHINNRD 201
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
149-352 3.06e-16

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: 78.21  E-value: 3.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSWFREA------EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd06632    6 QLLGSGSFGSVYEGfnGDTGDFFAVKEVSLVDDDKKSRESvkqleqEIALLSKLRHPNIVQYYGTEREED----NLYIFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGLAvKH 298
Cdd:cd06632   82 EYVPGGSIHKLLQRYGAFEEPVIRLyTRQILSGLAYLHsRNTV---------HRDIKGANILVDTNGVVKLADFGMA-KH 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 dsiLNTIDIPQNPKvGTKRYMAPEMLDDTMNVNIFEsfkrADIYSVGLVYWEIA 352
Cdd:cd06632  152 ---VEAFSFAKSFK-GSPYWMAPEVIMQKNSGYGLA----VDIWSLGCTVLEMA 197
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
145-428 3.74e-16

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: 78.15  E-value: 3.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGrwCGED---------VAVKIF----SSRDERSWFREAEIYQTVMLRH-ENILGFIAADNKdn 210
Cdd:cd05032    8 ITLIRELGQGSFGMVYEG--LAKGvvkgepetrVAIKTVnenaSMRERIEFLNEASVMKEFNCHHvVRLLGVVSTGQP-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 211 gtwtqLWLVSEYHEQGSLYDYL-----------NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNI 279
Cdd:cd05032   84 -----TLVVMELMAKGDLKSYLrsrrpeaennpGLGPPTLQKFIQMAAEIADGMAYLA--------AKKFVHRDLAARNC 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 280 LVKKCETCAIADLGLavkhdsilnTIDIPQNP--KVGTK-----RYMAPEMLDDTMnvniFESfkRADIYSVGLVYWEIA 352
Cdd:cd05032  151 MVAEDLTVKIGDFGM---------TRDIYETDyyRKGGKgllpvRWMAPESLKDGV----FTT--KSDVWSFGVVLWEMA 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 353 rrcSVGgiveeyQLPYYDMvpsdpSIEEMRKVVCDQKF--RP-SIPNQWQscealrvmgRIMRECWYANGAARLTALRI 428
Cdd:cd05032  216 ---TLA------EQPYQGL-----SNEEVLKFVIDGGHldLPeNCPDKLL---------ELMRMCWQYNPKMRPTFLEI 271
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
143-424 3.82e-16

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: 78.40  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRW------CGEDVAVKIFSS----RDERSWFREAEIYQTvmLRHENILGFIAADNKDNGT 212
Cdd:cd05080    4 RYLKKIRDLGEGHFGKVSLYCYdptndgTGEMVAVKALKAdcgpQHRSGWKQEIDILKT--LYHENIVKYKGCCSEQGGK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WTQLwlVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd05080   82 SLQL--IMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQ--------HYIHRDLAARNVLLDNDRLVKIGDF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAvKHdsilntidIPQNPKVGTKR--------YMAPEMLDDtmnvniFESFKRADIYSVGLVYWEIARRCsvggivEEY 364
Cdd:cd05080  152 GLA-KA--------VPEGHEYYRVRedgdspvfWYAPECLKE------YKFYYASDVWSFGVTLYELLTHC------DSS 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 365 QLP---YYDMV-PSDPSIEEMRKV-VCDQKFRPSIPNQWqSCEalrvMGRIMRECWYANGAARLT 424
Cdd:cd05080  211 QSPptkFLEMIgIAQGQMTVVRLIeLLERGERLPCPDKC-PQE----VYHLMKNCWETEASFRPT 270
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
151-424 4.03e-16

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: 78.19  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIYQTvmLRHENILGFIAADNKDngtwtQLWLVSEYHEQGS 227
Cdd:cd05069   20 LGQGCFGEVWMGTWNGTtKVAIKTLKpgTMMPEAFLQEAQIMKK--LRHDKLVPLYAVVSEE-----PIYIVTEFMGKGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYLNR---NIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilNT 304
Cdd:cd05069   93 LLDFLKEgdgKYLKLPQLVDMAAQIADGMAYIE--------RMNYIHRDLRAANILVGDNLVCKIADFGLARLIED--NE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 305 IDIPQNPKVGTKrYMAPEmlddtmnVNIFESFK-RADIYSVGLVYWEiarrcsvggIVEEYQLPYYDMVpsdpSIEEMRK 383
Cdd:cd05069  163 YTARQGAKFPIK-WTAPE-------AALYGRFTiKSDVWSFGILLTE---------LVTKGRVPYPGMV----NREVLEQ 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 161333835 384 VvcDQKFRPSIPnqwQSC-EALRVMgriMRECWYANGAARLT 424
Cdd:cd05069  222 V--ERGYRMPCP---QGCpESLHEL---MKLCWKKDPDERPT 255
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
144-424 5.77e-16

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: 77.62  E-value: 5.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGRWCG-EDVAVKIFS--SRDERSWFREAEIYQTvmLRHENILGFIAADNKDngtwtQLWLVS 220
Cdd:cd05067    8 TLKLVERLGAGQFGEVWMGYYNGhTKVAIKSLKqgSMSPDAFLAEANLMKQ--LQHQRLVRLYAVVTQE-----PIYIIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNI---VTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIADLGLAvk 297
Cdd:cd05067   81 EYMENGSLVDFLKTPSgikLTINKLLDMAAQIAEGMAFI-------EERNYI-HRDLRAANILVSDTLSCKIADFGLA-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 hdSILNtiDIPQNPKVGTK---RYMAPEMLDdtmnvniFESFK-RADIYSVGLVYWEiarrcsvggIVEEYQLPYYDMvp 373
Cdd:cd05067  151 --RLIE--DNEYTAREGAKfpiKWTAPEAIN-------YGTFTiKSDVWSFGILLTE---------IVTHGRIPYPGM-- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 374 SDPsiEEMRKVvcDQKFRPSIPNqwqSCEAlrVMGRIMRECWYANGAARLT 424
Cdd:cd05067  209 TNP--EVIQNL--ERGYRMPRPD---NCPE--ELYQLMRLCWKERPEDRPT 250
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
144-424 9.42e-16

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: 77.03  E-value: 9.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIYQTvmLRHENILGFIAADNKDngtwtQLWLVS 220
Cdd:cd05071   10 SLRLEVKLGQGCFGEVWMGTWNGTtRVAIKTLKpgTMSPEAFLQEAQVMKK--LRHEKLVQLYAVVSEE-----PIYIVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLN---RNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd05071   83 EYMSKGSLLDFLKgemGKYLRLPQLVDMAAQIASGMAYVE--------RMNYVHRDLRAANILVGENLVCKVADFGLARL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 HDSilNTIDIPQNPKVGTKrYMAPEmlddtmnVNIFESFK-RADIYSVGLVYWEIARRCSVggiveeyqlPYYDMVpsdp 376
Cdd:cd05071  155 IED--NEYTARQGAKFPIK-WTAPE-------AALYGRFTiKSDVWSFGILLTELTTKGRV---------PYPGMV---- 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 377 SIEEMRKVvcDQKFRPSIPNQwqsCEAlrVMGRIMRECWYANGAARLT 424
Cdd:cd05071  212 NREVLDQV--ERGYRMPCPPE---CPE--SLHDLMCQCWRKEPEERPT 252
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
149-432 9.73e-16

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: 76.71  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRW--CGEDVAVKI----FSSRDERSWFREAEIYQTvmLRHENILGFIaadnkdnGTWTQ---LWLV 219
Cdd:cd05041    1 EKIGRGNFGDVYRGVLkpDNTEVAVKTcretLPPDLKRKFLQEARILKQ--YDHPNIVKLI-------GVCVQkqpIMIV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd05041   72 MELVPGGSLLTFLrkKGARLTVKQLLQMCLDAAAGMEYL-------ESKNCI-HRDLAARNCLVGENNVLKISDFGMSRE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 HDSILNTIdipqnpKVGTK----RYMAPEMLddtmNVNIFESfkRADIYSVGLVYWEIArrcSVGGIveeyqlPYYDMvp 373
Cdd:cd05041  144 EEDGEYTV------SDGLKqipiKWTAPEAL----NYGRYTS--ESDVWSFGILLWEIF---SLGAT------PYPGM-- 200
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 374 sdpSIEEMRKVVcDQKFRPSIPnqwQSC-EALRvmgRIMRECWYANGAARLTALRIKKTI 432
Cdd:cd05041  201 ---SNQQTREQI-ESGYRMPAP---ELCpEAVY---RLMLQCWAYDPENRPSFSEIYNEL 250
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
150-428 9.99e-16

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: 76.88  E-value: 9.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGEDVAVKIFS--------------------SRDERSWFREAEIYQTVM--LRHENILGFIAADN 207
Cdd:cd14000    1 LLGDGGFGSVYRASYKGEPVAVKIFNkhtssnfanvpadtmlrhlrATDAMKNFRLLRQELTVLshLHHPSIVYLLGIGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 208 KdngtwtQLWLVSEYHEQGSLYDYLNRNIVTVAGMI-----KLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV- 281
Cdd:cd14000   81 H------PLMLVLELAPLGSLDHLLQQDSRSFASLGrtlqqRIALQVADGLRYLH--------SAMIIYRDLKSHNVLVw 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 282 ----KKCETCAIADLGLAVK--HDSILNTidipqnpkVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEI--AR 353
Cdd:cd14000  147 tlypNSAIIIKIADYGISRQccRMGAKGS--------EGTPGFRAPEIARGNVIYN-----EKVDVFSFGMLLYEIlsGG 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 354 RCSVGGivEEYQLPYYDMVPSDPSIEEMRKVvcdqkfrpsipnQWQSCEALrvmgriMRECWYANGAARLTALRI 428
Cdd:cd14000  214 APMVGH--LKFPNEFDIHGGLRPPLKQYECA------------PWPEVEVL------MKKCWKENPQQRPTAVTV 268
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
142-422 1.02e-15

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs 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, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA 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: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 76.83  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 142 ARTIVLQEIVGKGRFGEVWHGRW---CGEDVAVKI------FSSRDERSWFREAEIYQtvMLRHENILGFiaadnkdNGT 212
Cdd:cd05066    3 ASCIKIEKVIGAGEFGEVCSGRLklpGKREIPVAIktlkagYTEKQRRDFLSEASIMG--QFDHPNIIHL-------EGV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WTQ---LWLVSEYHEQGSLYDYLNRN-----IVTVAGMIKlalSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKK 283
Cdd:cd05066   74 VTRskpVMIVTEYMENGSLDAFLRKHdgqftVIQLVGMLR---GIASGMKYLSdMGYV---------HRDLAARNILVNS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 284 CETCAIADLGLAvkhdSILNtiDIPQNPKVGTK-----RYMAPEMLddtmnvnIFESFKRA-DIYSVGLVYWEIArrcSV 357
Cdd:cd05066  142 NLVCKVSDFGLS----RVLE--DDPEAAYTTRGgkipiRWTAPEAI-------AYRKFTSAsDVWSYGIVMWEVM---SY 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 358 GgiveeyQLPYYDMVPSD--PSIEEmrkvvcdqKFRPSIPnqwQSCEAlrVMGRIMRECWYANGAAR 422
Cdd:cd05066  206 G------ERPYWEMSNQDviKAIEE--------GYRLPAP---MDCPA--ALHQLMLDCWQKDRNER 253
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
145-351 1.12e-15

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: 76.59  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGeDVAVKIFSSRDERSwfREAEIYQTVM-----LRHENILGFIAAdnkdnGTWTQLWLV 219
Cdd:cd14150    2 VSMLKRIGTGSFGTVFRGKWHG-DVAVKILKVTEPTP--EQLQAFKNEMqvlrkTRHVNILLFMGF-----MTRPNFAII 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd14150   74 TQWCEGSSLYRHLHvtETRFDTMQLIDVARQTAQGMDYLHAK--------NIIHRDLKSNNIFLHEGLTVKIGDFGLATV 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 298 HDSILNTIDIPQnPKvGTKRYMAPEMLddTMNVNIFESFKrADIYSVGLVYWEI 351
Cdd:cd14150  146 KTRWSGSQQVEQ-PS-GSILWMAPEVI--RMQDTNPYSFQ-SDVYAYGVVLYEL 194
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
147-431 1.31e-15

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: 76.29  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVKIFS-SRDERSWFREA---EIYQTVMLRHENILGFIAAdnkdNGTWTQLWLVS 220
Cdd:cd14663    4 LGRTLGEGTFAKVKFARntKTGESVAIKIIDkEQVAREGMVEQikrEIAIMKLLRHPNIVELHEV----MATKTKIFFVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIvtvagmiKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDS 300
Cdd:cd14663   80 ELVTGGELFSKIAKNG-------RLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 301 ILNtiDIPQNPKVGTKRYMAPEMLDDtmnvNIFESFKrADIYSVGLVYWEIARRCsvggiveeyqLPYydmvpSDPSIEE 380
Cdd:cd14663  153 FRQ--DGLLHTTCGTPNYVAPEVLAR----RGYDGAK-ADIWSCGVILFVLLAGY----------LPF-----DDENLMA 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 381 MRKVVCDQKFRpsIPNqWQSCEALRVMGRIMRecwyANGAARLTALRIKKT 431
Cdd:cd14663  211 LYRKIMKGEFE--YPR-WFSPGAKSLIKRILD----PNPSTRITVEQIMAS 254
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
141-424 1.44e-15

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: 76.65  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 141 IAR-TIVLQEIVGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIYQTvmLRHENILGFIAADNKDngtwtQL 216
Cdd:cd05070    6 IPReSLQLIKRLGNGQFGEVWMGTWNGNtKVAIKTLKpgTMSPESFLEEAQIMKK--LKHDKLVQLYAVVSEE-----PI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNRN---IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd05070   79 YIVTEYMSKGSLLDFLKDGegrALKLPNLVDMAAQVAAGMAYIE--------RMNYIHRDLRSANILVGNGLICKIADFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 294 LAVKHDSilNTIDIPQNPKVGTKrYMAPEmlddtmnVNIFESFK-RADIYSVGLVYWEiarrcsvggIVEEYQLPYydmv 372
Cdd:cd05070  151 LARLIED--NEYTARQGAKFPIK-WTAPE-------AALYGRFTiKSDVWSFGILLTE---------LVTKGRVPY---- 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161333835 373 PSDPSIEEMRKVvcDQKFRPSIPnqwQSCEAlrVMGRIMRECWYANGAARLT 424
Cdd:cd05070  208 PGMNNREVLEQV--ERGYRMPCP---QDCPI--SLHELMIHCWKKDPEERPT 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
150-346 1.53e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 77.56  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW---HgRWCGEDVAVK-IFSSRDE---RSWFREAEIYQTVmlRHENILGfiAADNKDNGTWTQLWLvsEY 222
Cdd:PLN00034  81 RIGSGAGGTVYkviH-RPTGRLYALKvIYGNHEDtvrRQICREIEILRDV--NHPNVVK--CHDMFDHNGEIQVLL--EF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYdylNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdSIL 302
Cdd:PLN00034 154 MDGGSLE---GTHIADEQFLADVARQILSGIAYLH--------RRHIVHRDIKPSNLLINSAKNVKIADFGVS----RIL 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 303 N-TIDiPQNPKVGTKRYMAPEMLDDTMNVNIFESFKrADIYSVGL 346
Cdd:PLN00034 219 AqTMD-PCNSSVGTIAYMSPERINTDLNHGAYDGYA-GDIWSLGV 261
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
154-324 1.64e-15

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: 76.60  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 154 GRFGEVWHG-------RWCGEDVAVKIFSSRD-----ERSWFREAEIYQTVMlRHENILGFIAADNKDNGtwtqLWLVSE 221
Cdd:cd07832    6 GRIGEGAHGivfkakdRETGETVALKKVALRKleggiPNQALREIKALQACQ-GHPYVVKLRDVFPHGTG----FVLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YhEQGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVkhd 299
Cdd:cd07832   81 Y-MLSSLSEVLRdeERPLTEAQVKRYMRMLLKGVAYMH--------ANRIMHRDLKPANLLISSTGVLKIADFGLAR--- 148
                        170       180
                 ....*....|....*....|....*
gi 161333835 300 SILNTIDIPQNPKVGTKRYMAPEML 324
Cdd:cd07832  149 LFSEEDPRLYSHQVATRWYRAPELL 173
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
143-348 1.73e-15

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: 76.22  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIvGKGRFGEVW--HGRWCGEDVAVKIFSSRDE---RSWFREAEIYQTVMlRHENILGFIAADNKDNGTWTQLW 217
Cdd:cd13985    1 RYQVTKQL-GEGGFSYVYlaHDVNTGRRYALKRMYFNDEeqlRVAIKEIEIMKRLC-GHPNIVQYYDSAILSSEGRKEVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEqGSLYDYLNR---NIVTVAGMIKLALSIASGLAHLHmeivgtQGKPAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd13985   79 LLMEYCP-GSLVDILEKsppSPLSEEEVLRIFYQICQAVGHLH------SQSPPIIHRDIKIENILFSNTGRFKLCDFGS 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 295 AVKHDSILNT-----IDIPQNPKVGTKRYMAPEMLDDTMNVNIFEsfkRADIYSVG-LVY 348
Cdd:cd13985  152 ATTEHYPLERaeevnIIEEEIQKNTTPMYRAPEMIDLYSKKPIGE---KADIWALGcLLY 208
Pkinase pfam00069
Protein kinase domain;
149-395 2.53e-15

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 74.59  E-value: 2.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSW-----FREAEIYQtvMLRHENILGFI-AADNKDNgtwtqLWLVS 220
Cdd:pfam00069   5 RKLGSGSFGTVYKAkhRDTGKIVAIKKIKKEKIKKKkdkniLREIKILK--KLNHPNIVRLYdAFEDKDN-----LYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  221 EYHEQGSLYDYLNRNIVtvagmiklalsiasglahlhmeivgtqgkpaIAHRDIKS--KNILvkkcetcaiadlgLAVKH 298
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGA-------------------------------FSEREAKFimKQIL-------------EGLES 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  299 DSILNTIdipqnpkVGTKRYMAPEMLDDTMNvnifeSFKrADIYSVGLVYWEIARRC--------SVGGIVEEYQLPYYD 370
Cdd:pfam00069 114 GSSLTTF-------VGTPWYMAPEVLGGNPY-----GPK-VDVWSLGCILYELLTGKppfpgingNEIYELIIDQPYAFP 180
                         250       260       270
                  ....*....|....*....|....*....|
gi 161333835  371 MVPSDPSiEEMRKVVC-----DQKFRPSIP 395
Cdd:pfam00069 181 ELPSNLS-EEAKDLLKkllkkDPSKRLTAT 209
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
151-350 3.02e-15

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: 75.34  E-value: 3.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW--CGEDVAVKIFSSRD-----ERSWFREAEIYQTvmLRHENILGFIaaDNKDngTWTQLWLVSEYH 223
Cdd:cd14009    1 IGRGSFATVWKGRHkqTGEVVAIKEISRKKlnkklQENLESEIAILKS--IKHPNIVRLY--DVQK--TEDFIYLVLEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCA---IADLGLA--VK 297
Cdd:cd14009   75 AGGDLSQYIRKRgRLPEAVARHFMQQLASGLKFLRSK--------NIIHRDLKPQNLLLSTSGDDPvlkIADFGFArsLQ 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 298 HDSILNTIdipqnpkVGTKRYMAPEMLddtmnvnifeSFKR----ADIYSVGLVYWE 350
Cdd:cd14009  147 PASMAETL-------CGSPLYMAPEIL----------QFQKydakADLWSVGAILFE 186
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
149-369 3.68e-15

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: 74.98  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRW--CGEDVAVKIF-----SSRDERSWFREAEIYQTvmLRHENILGFIAADNkdngTWTQLWLVSE 221
Cdd:cd14002    7 ELIGEGSFGKVYKGRRkyTGQVVALKFIpkrgkSEKELRNLRQEIEILRK--LNHPNIIEMLDSFE----TKKEFVVVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YhEQGSLYDYL--NRNI-VTVAGMIklALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA--V 296
Cdd:cd14002   81 Y-AQGELFQILedDGTLpEEEVRSI--AKQLVSALHYLH--------SNRIIHRDMKPQNILIGKGGVVKLCDFGFAraM 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 297 KHDSI-LNTIDipqnpkvGTKRYMAPEML-----DDTmnvnifesfkrADIYSVGLVYWEIArrcsVGgiveeyQLPYY 369
Cdd:cd14002  150 SCNTLvLTSIK-------GTPLYMAPELVqeqpyDHT-----------ADLWSLGCILYELF----VG------QPPFY 200
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
157-395 3.92e-15

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 74.83  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 157 GEVWHGRWCGEDVAVKIFSSRDERSwfREAEIYQTVMLR-----HENILGFIAADNKDngtwTQLWLVSEYHEQGSLYDY 231
Cdd:cd14057    9 GELWKGRWQGNDIVAKILKVRDVTT--RISRDFNEEYPRlrifsHPNVLPVLGACNSP----PNLVVISQYMPYGSLYNV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 232 LNRN---IVTVAGMIKLALSIASGLAHLH-MEivgtqgkPAIAHRDIKSKNILVKKCETCAI--ADLGLAVkhdsilnti 305
Cdd:cd14057   83 LHEGtgvVVDQSQAVKFALDIARGMAFLHtLE-------PLIPRHHLNSKHVMIDEDMTARInmADVKFSF--------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 306 dipQNP-KVGTKRYMAPEMLD---DTMNVnifesfKRADIYSVGLVYWEIARRcsvggiveeyQLPYYDMvpsdPSIEEM 381
Cdd:cd14057  147 ---QEPgKMYNPAWMAPEALQkkpEDINR------RSADMWSFAILLWELVTR----------EVPFADL----SNMEIG 203
                        250
                 ....*....|....
gi 161333835 382 RKVVCdQKFRPSIP 395
Cdd:cd14057  204 MKIAL-EGLRVTIP 216
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
143-352 3.93e-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: 74.95  E-value: 3.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHG--RWCGEDVA---VKIFS-SRDERSWFR-EAEIYQTvmLRHENILGFIaaDNKDNGTWTQ 215
Cdd:cd13983    1 RYLKFNEVLGRGSFKTVYRAfdTEEGIEVAwneIKLRKlPKAERQRFKqEIEILKS--LKHPNIIKFY--DSWESKSKKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNIVTVAGMIK-LALSIASGLAHLHmeivgTQgKPAIAHRDIKSKNIL-------VKkcetc 287
Cdd:cd13983   77 VIFITELMTSGTLKQYLKRFKRLKLKVIKsWCRQILEGLNYLH-----TR-DPPIIHRDLKCDNIFingntgeVK----- 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 288 aIADLGLA-VKHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNvnifesfKRADIYSVGLVYWEIA 352
Cdd:cd13983  146 -IGDLGLAtLLRQSFAKSV-------IGTPEFMAPEMYEEHYD-------EKVDIYAFGMCLLEMA 196
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
147-350 4.13e-15

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: 74.76  E-value: 4.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSRDERSWFREAEIYQTVML---RHENILGFIAADNKDNgtwtQLWLVSE 221
Cdd:cd08529    4 ILNKLGKGSFGVVYKVVRKvdGRVYALKQIDISRMSRKMREEAIDEARVLsklNSPYVIKYYDSFVDKG----KLNIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNI---VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkh 298
Cdd:cd08529   80 YAENGDLHSLIKSQRgrpLPEDQIWKFFIQTLLGLSHLH--------SKKILHRDIKSMNIFLDKGDNVKIGDLGVA--- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 299 dSILNTIDIPQNPKVGTKRYMAPEMLDDT-MNvnifesfKRADIYSVGLVYWE 350
Cdd:cd08529  149 -KILSDTTNFAQTIVGTPYYLSPELCEDKpYN-------EKSDVWALGCVLYE 193
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
147-373 5.09e-15

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: 75.03  E-value: 5.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRW--CGEDVAVKIFSSRDERswfrEAEIYQTV-MLR----HENILGFIAADNK--DNGTWTQLW 217
Cdd:cd06608   10 LVEVIGEGTYGKVYKARHkkTGQLAAIKIMDIIEDE----EEEIKLEInILRkfsnHPNIATFYGAFIKkdPPGGDDQLW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDyLNRNIVTVAGMIKLAL------SIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVKKCETCAIAD 291
Cdd:cd06608   86 LVMEYCGGGSVTD-LVKGLRKKGKRLKEEWiayilrETLRGLAYLHENKV--------IHRDIKGQNILLTEEAEVKLVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 292 LGLAVKHDSILNTidipQNPKVGTKRYMAPE--MLDDTMNVNIFEsfkRADIYSVGLVYWEIArrcsvggiveEYQLPYY 369
Cdd:cd06608  157 FGVSAQLDSTLGR----RNTFIGTPYWMAPEviACDQQPDASYDA---RCDVWSLGITAIELA----------DGKPPLC 219

                 ....
gi 161333835 370 DMVP 373
Cdd:cd06608  220 DMHP 223
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
152-348 6.04e-15

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: 74.23  E-value: 6.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVwhgRWC-----GEDVAVKIFSSRDE--RSWFREAEIYQTvmLRHENILGFIAA-DNKdngtwTQLWLVSEYH 223
Cdd:cd14006    2 GRGRFGVV---KRCiekatGREFAAKFIPKRDKkkEAVLREISILNQ--LQHPRIIQLHEAyESP-----TELVLILELC 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV--KKCETCAIADLGLAVKhds 300
Cdd:cd14006   72 SGGELLDRLAERGSLSEEEVRTYMrQLLEGLQYLH--------NHHILHLDLKPENILLadRPSPQIKIIDFGLARK--- 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 301 iLNTIDIPQNPKvGTKRYMAPEMLDDTmnvNIFESfkrADIYSVG-LVY 348
Cdd:cd14006  141 -LNPGEELKEIF-GTPEFVAPEIVNGE---PVSLA---TDMWSIGvLTY 181
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
145-422 6.83e-15

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs 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, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily 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).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 74.63  E-value: 6.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHG--RWCG-EDVAVKI------FSSRDERSWFREAEIYQtvMLRHENILGFIAADNKdngtWTQ 215
Cdd:cd05063    7 ITKQKVIGAGEFGEVFRGilKMPGrKEVAVAIktlkpgYTEKQRQDFLSEASIMG--QFSHHNIIRLEGVVTK----FKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRN-----IVTVAGMIKlalSIASGLAHL-HMEIVgtqgkpaiaHRDIKSKNILVKKCETCAI 289
Cdd:cd05063   81 AMIITEYMENGALDKYLRDHdgefsSYQLVGMLR---GIAAGMKYLsDMNYV---------HRDLAARNILVNSNLECKV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 290 ADLGLAvkhdSILNtiDIPQNPKVGTK-----RYMAPEMLDdtmnvniFESFKRA-DIYSVGLVYWEIArrcSVGgivee 363
Cdd:cd05063  149 SDFGLS----RVLE--DDPEGTYTTSGgkipiRWTAPEAIA-------YRKFTSAsDVWSFGIVMWEVM---SFG----- 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 364 yQLPYYDMvpsdpSIEEMRKVVcDQKFRPSIPnqwQSCEAlrVMGRIMRECWYANGAAR 422
Cdd:cd05063  208 -ERPYWDM-----SNHEVMKAI-NDGFRLPAP---MDCPS--AVYQLMLQCWQQDRARR 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
146-353 1.10e-14

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: 73.82  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGRW--CGEDVAVKIF---SSRDERSwFREAEIYQTVMLRHENILGFIAADNKDngtwTQLWLVS 220
Cdd:cd06609    4 TLLERIGKGSFGEVYKGIDkrTNQVVAIKVIdleEAEDEIE-DIQQEIQFLSQCDSPYITKYYGSFLKG----SKLWIIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIV---TVAGMIKlalSIASGLAHLHmeivgTQGKpaiAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd06609   79 EYCGGGSVLDLLKPGPLdetYIAFILR---EVLLGLEYLH-----SEGK---IHRDIKAANILLSEEGDVKLADFGVSGQ 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 298 hdsiLNTIDIPQNPKVGTKRYMAPEMLddtmnVNIFESFKrADIYSVGLVYWEIAR 353
Cdd:cd06609  148 ----LTSTMSKRNTFVGTPFWMAPEVI-----KQSGYDEK-ADIWSLGITAIELAK 193
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
148-352 1.23e-14

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: 73.89  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDE-----RSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd07833    6 LGVVGEGAYGVVLKCRnkATGEIVAIKKFKESEDdedvkKTALREVKVLRQ--LRHENIVNLKEAFRRKG----RLYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQgSLYDYLNRNivtVAGM----IKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd07833   80 EYVER-TLLELLEAS---PGGLppdaVRSYIwQLLQAIAYCH--------SHNIIHRDIKPENILVSESGVLKLCDFGFA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 296 VKhdsilntidIPQNPK------VGTKRYMAPEMLddtmnVNIFESFKRADIYSVGLVYWEIA 352
Cdd:cd07833  148 RA---------LTARPAspltdyVATRWYRAPELL-----VGDTNYGKPVDVWAIGCIMAELL 196
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
145-424 1.65e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 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: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 73.85  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGED---------VAVKIF----SSRDERSWFREAEIYQtVMLRHENILGFIAADNKDNg 211
Cdd:cd05099   14 LVLGKPLGEGCFGQVVRAEAYGIDksrpdqtvtVAVKMLkdnaTDKDLADLISEMELMK-LIGKHKNIINLLGVCTQEG- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 212 twtQLWLVSEYHEQGSLYDYL-----------------NRNIVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDI 274
Cdd:cd05099   92 ---PLYVIVEYAAKGNLREFLrarrppgpdytfditkvPEEQLSFKDLVSCAYQVARGMEYL-------ESRRCI-HRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 275 KSKNILVKKCETCAIADLGLAVK-HDsilntIDIPQNPKVGTK--RYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEI 351
Cdd:cd05099  161 AARNVLVTEDNVMKIADFGLARGvHD-----IDYYKKTSNGRLpvKWMAPEALFDRVYTH------QSDVWSFGILMWEI 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 352 ArrcSVGGIveeyqlPYydmvPSDPsIEEMRKVVcDQKFRPSIPNqwqSCEALRVMgrIMRECWYANGAARLT 424
Cdd:cd05099  230 F---TLGGS------PY----PGIP-VEELFKLL-REGHRMDKPS---NCTHELYM--LMRECWHAVPTQRPT 282
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
151-353 1.75e-14

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: 73.11  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEV--WHGRWCGEDV--AVKIFSSRDERSWFREAEIYQT------VMLRHENILGFIAADNKDNGTWtqlWLVS 220
Cdd:cd13994    1 IGKGATSVVriVTKKNPRSGVlyAVKEYRRRDDESKRKDYVKRLTseyiisSKLHHPNIVKVLDLCQDLHGKW---CLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNR----NIVTVAGMIKlalSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:cd13994   78 EYCPGGDLFTLIEKadslSLEEKDCFFK---QILRGVAYLH-----SHG---IAHRDLKPENILLDEDGVLKLTDFGTAE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 297 KhdsilntIDIPQNPK-------VGTKRYMAPEMLddtmnvnIFESF--KRADIYSVGLVY---------WEIAR 353
Cdd:cd13994  147 V-------FGMPAEKEspmsaglCGSEPYMAPEVF-------TSGSYdgRAVDVWSCGIVLfalftgrfpWRSAK 207
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
151-385 1.95e-14

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: 73.15  E-value: 1.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW---HgRWCGEDVAVK-IFSSRDE---RSWFREAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLVSEYH 223
Cdd:cd06605    9 LGEGNGGVVSkvrH-RPSGQIMAVKvIRLEIDEalqKQILRELDVLHKC--NSPYIVGFYGAFYSEG----DISICMEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRnivtvAGMI------KLALSIASGLAHLHmeivgtqGKPAIAHRDIKSKNILVKKCETCAIADLGLA-V 296
Cdd:cd06605   82 DGGSLDKILKE-----VGRIperilgKIAVAVVKGLIYLH-------EKHKIIHRDVKPSNILVNSRGQVKLCDFGVSgQ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEIArrcsvggiVEEYQLPYYDMVPSDP 376
Cdd:cd06605  150 LVDSLAKTF-------VGTRSYMAPERISGGKYTV------KSDIWSLGLSLVELA--------TGRFPYPPPNAKPSMM 208

                 ....*....
gi 161333835 377 SIEEMRKVV 385
Cdd:cd06605  209 IFELLSYIV 217
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
149-388 2.12e-14

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: 73.01  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIV---GKGRFGEVW---HgRWCGEDVAVK---IFSSRDERSWF-REAEIYQTVmlRHENILGFIAADNKdNGtwtQLWL 218
Cdd:cd06623    4 ERVkvlGQGSSGVVYkvrH-KPTGKIYALKkihVDGDEEFRKQLlRELKTLRSC--ESPYVVKCYGAFYK-EG---EISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNIVTVAGMIK-LALSIASGLAHLHmeivgtqGKPAIAHRDIKSKNILVKKCETCAIADLGLAvk 297
Cdd:cd06623   77 VLEYMDGGSLADLLKKVGKIPEPVLAyIARQILKGLDYLH-------TKRHIIHRDIKPSNLLINSKGEVKIADFGIS-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 hdSILNTIDIPQNPKVGTKRYMAPEMLDDTMNvnifeSFKrADIYSVGLVYWEiarrCSVGgiveeyQLPYYDmvPSDPS 377
Cdd:cd06623  148 --KVLENTLDQCNTFVGTVTYMSPERIQGESY-----SYA-ADIWSLGLTLLE----CALG------KFPFLP--PGQPS 207
                        250
                 ....*....|.
gi 161333835 378 IEEMRKVVCDQ 388
Cdd:cd06623  208 FFELMQAICDG 218
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
147-347 2.61e-14

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: 72.67  E-value: 2.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFS----SRDERSWFREAEIYQTVMLRHENILGFIAA-DNKdngtwTQLWLV 219
Cdd:cd14081    5 LGKTLGKGQTGLVKLAKHCvtGQKVAIKIVNkeklSKESVLMKVEREIAIMKLIEHPNVLKLYDVyENK-----KYLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA--V 296
Cdd:cd14081   80 LEYVSGGELFDYLVKKgRLTEKEARKFFRQIISALDYCH--------SHSICHRDLKPENLLLDEKNNIKIADFGMAslQ 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 297 KHDSILNTidipqnpKVGTKRYMAPEMLDDtmnvnifESF--KRADIYSVGLV 347
Cdd:cd14081  152 PEGSLLET-------SCGSPHYACPEVIKG-------EKYdgRKADIWSCGVI 190
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
145-354 2.63e-14

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 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: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 73.08  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGEdVAVKIF----SSRDERSWFREaEIYQTVMLRHENILGFIAADNKDngtwTQLWLVS 220
Cdd:cd14152    2 IELGELIGQGRWGKVHRGRWHGE-VAIRLLeidgNNQDHLKLFKK-EVMNYRQTRHENVVLFMGACMHP----PHLAIIT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETcAIADLGL---- 294
Cdd:cd14152   76 SFCKGRTLYSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFYDNGKV-VITDFGLfgis 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 295 -AVKHDSILNTIDIPQN------PKVgtKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIARR 354
Cdd:cd14152  147 gVVQEGRRENELKLPHDwlcylaPEI--VREMTPGKDEDCLPFS-----KAADVYAFGTIWYELQAR 206
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
144-351 2.72e-14

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: 72.75  E-value: 2.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIYQTvmLRHENILGFIAADNKDngtwtQLWLVS 220
Cdd:cd05073   12 SLKLEKKLGAGQFGEVWMATYNKHtKVAVKTMKpgSMSVEAFLAEANVMKT--LQHDKLVKLHAVVTKE-----PIYIIT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNR---NIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvk 297
Cdd:cd05073   85 EFMAKGSLLDFLKSdegSKQPLPKLIDFSAQIAEGMAFIE--------QRNYIHRDLRAANILVSASLVCKIADFGLA-- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 298 hdSILNtiDIPQNPKVGTK---RYMAPEMLDdtmnvniFESFK-RADIYSVGLVYWEI 351
Cdd:cd05073  155 --RVIE--DNEYTAREGAKfpiKWTAPEAIN-------FGSFTiKSDVWSFGILLMEI 201
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
154-424 2.74e-14

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: 72.53  E-value: 2.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 154 GRFGEVW--HGRWCGEDVAVKIFS----SRDERSWFREAEIYQtvMLRHENI---LGFIAadnkDNGTWTqlwLVSEYHE 224
Cdd:cd14027    4 GGFGKVSlcFHRTQGLVVLKTVYTgpncIEHNEALLEEGKMMN--RLRHSRVvklLGVIL----EEGKYS---LVMEYME 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAV-KHDSILN 303
Cdd:cd14027   75 KGNLMHVLKKVSVPLSVKGRIILEIIEGMAYLH--------GKGVIHKDLKPENILVDNDFHIKIADLGLASfKMWSKLT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 304 TIDIPQNPKV--------GTKRYMAPEMLDDtmnVNIfESFKRADIYSVGLVYWEIARRcsvggiveeyQLPYYDMVPSD 375
Cdd:cd14027  147 KEEHNEQREVdgtakknaGTLYYMAPEHLND---VNA-KPTEKSDVYSFAIVLWAIFAN----------KEPYENAINED 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 376 psieEMRKVVCdQKFRPSIPNQWQSCEalRVMGRIMRECWYANGAARLT 424
Cdd:cd14027  213 ----QIIMCIK-SGNRPDVDDITEYCP--REIIDLMKLCWEANPEARPT 254
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
151-424 3.27e-14

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: 72.65  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW------CGEDVAVKIF--SSRDERSWFREAEIYQTVMLRHENILGF--IAADNKDNGtwtqLWLVS 220
Cdd:cd05079   12 LGEGHFGKVELCRYdpegdnTGEQVAVKSLkpESGGNHIADLKKEIEILRNLYHENIVKYkgICTEDGGNG----IKLIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDIKSKNILVKKCETCAIADLGL--AV 296
Cdd:cd05079   88 EFLPSGSLKEYLprNKNKINLKQQLKYAVQICKGMDYL--------GSRQYVHRDLAARNVLVESEHQVKIGDFGLtkAI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 KHDSILNTIDIPQNPKVgtkRYMAPEMLddtmnvnIFESFKRA-DIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSD 375
Cdd:cd05079  160 ETDKEYYTVKDDLDSPV---FWYAPECL-------IQSKFYIAsDVWSFGVTLYELLTYCDSESSPMTLFLKMIGPTHGQ 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 376 PSIEEMRKVVCDQKFRPSIPNqwqsCEalRVMGRIMRECWYANGAARLT 424
Cdd:cd05079  230 MTVTRLVRVLEEGKRLPRPPN----CP--EEVYQLMRKCWEFQPSKRTT 272
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
145-424 4.07e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 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: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 72.74  E-value: 4.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGED---------VAVKIFSS----RDERSWFREAEIYQTVMlRHENILGFIAADNKDNg 211
Cdd:cd05098   15 LVLGKPLGEGCFGQVVLAEAIGLDkdkpnrvtkVAVKMLKSdateKDLSDLISEMEMMKMIG-KHKNIINLLGACTQDG- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 212 twtQLWLVSEYHEQGSLYDYLN-----------------RNIVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDI 274
Cdd:cd05098   93 ---PLYVIVEYASKGNLREYLQarrppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYL-------ASKKCI-HRDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 275 KSKNILVKKCETCAIADLGLAVKhdsiLNTIDIPQNPKVG--TKRYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEIA 352
Cdd:cd05098  162 AARNVLVTEDNVMKIADFGLARD----IHHIDYYKKTTNGrlPVKWMAPEALFDRIYTH------QSDVWSFGVLLWEIF 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 353 rrcSVGGIveeyqlPYydmvPSDPsIEEMRKVVcDQKFRPSIPNqwqSCEALRVMgrIMRECWYANGAARLT 424
Cdd:cd05098  232 ---TLGGS------PY----PGVP-VEELFKLL-KEGHRMDKPS---NCTNELYM--MMRDCWHAVPSQRPT 283
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
149-352 4.61e-14

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: 71.72  E-value: 4.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW--HGRWCGEDVAVKI-----FSSRDERSWFREAEIYQtvMLRHENILGFIAAdNKDNGTwtqLWLVSE 221
Cdd:cd08215    6 RVIGKGSFGSAYlvRRKSDGKLYVLKEidlsnMSEKEREEALNEVKLLS--KLKHPNIVKYYES-FEENGK---LCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIVTVAGM-----IKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd08215   80 YADGGDLAQKIKKQKKKGQPFpeeqiLDWFVQICLALKYLHsRKIL---------HRDLKTQNIFLTKDGVVKLGDFGIS 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 296 vkhdSILNTIDIPQNPKVGTKRYMAPEMLDdtmnvNIFESFKrADIYSVGLVYWEIA 352
Cdd:cd08215  151 ----KVLESTTDLAKTVVGTPYYLSPELCE-----NKPYNYK-SDIWALGCVLYELC 197
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
151-351 5.47e-14

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. 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 STK_BAK1-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: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 71.76  E-value: 5.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWC-GEDVAVKIFSSR---DERSWFrEAEIYQTVMLRHENI---LGFIAadNKDngtwTQLwLVSEYH 223
Cdd:cd14664    1 IGRGGAGTVYKGVMPnGTLVAVKRLKGEgtqGGDHGF-QAEIQTLGMIRHRNIvrlRGYCS--NPT----TNL-LVYEYM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYL-----NRNIVTVAGMIKLALSIASGLAHLHMEIVgtqgkPAIAHRDIKSKNILVKKCETCAIADLGLAvkh 298
Cdd:cd14664   73 PNGSLGELLhsrpeSQPPLDWETRQRIALGSARGLAYLHHDCS-----PLIIHRDVKSNNILLDEEFEAHVADFGLA--- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 dSILNTIDIPQNPKV-GTKRYMAPEMLdDTMNVNifesfKRADIYSVGLVYWEI 351
Cdd:cd14664  145 -KLMDDKDSHVMSSVaGSYGYIAPEYA-YTGKVS-----EKSDVYSYGVVLLEL 191
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
142-351 5.65e-14

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk 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: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 72.11  E-value: 5.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 142 ARTIVLQEIVGKGRFGEVWHGRwC-----GED---VAVKIF---SSRDERSWF-REAEIYqtVMLRHENILGFIaadnkd 209
Cdd:cd05049    4 RDTIVLKRELGEGAFGKVFLGE-CynlepEQDkmlVAVKTLkdaSSPDARKDFeREAELL--TNLQHENIVKFY------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 210 nGTWTQ---LWLVSEYHEQGSLYDYLNRN---------------IVTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAH 271
Cdd:cd05049   75 -GVCTEgdpLLMVFEYMEHGDLNKFLRSHgpdaaflasedsapgELTLSQLLHIAVQIASG-----MVYLASQ---HFVH 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 272 RDIKSKNILVKKCETCAIADLGLAVkhdsilntiDIPQNP--KVGTK-----RYMAPEMLddtmnvnIFESFK-RADIYS 343
Cdd:cd05049  146 RDLATRNCLVGTNLVVKIGDFGMSR---------DIYSTDyyRVGGHtmlpiRWMPPESI-------LYRKFTtESDVWS 209

                 ....*...
gi 161333835 344 VGLVYWEI 351
Cdd:cd05049  210 FGVVLWEI 217
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
147-352 6.09e-14

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: 71.53  E-value: 6.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVK---IFSSRDERSwfREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWL 218
Cdd:cd08224    4 IEKKIGKGQFSVVYRARclLDGRLVALKkvqIFEMMDAKA--RQDclkEIDLLQQLNHPNIIKYLASFIENN----ELNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLydylnrnivtvAGMIKLA----------------LSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVK 282
Cdd:cd08224   78 VLELADAGDL-----------SRLIKHFkkqkrlipertiwkyfVQLCSALEHMHSK--------RIMHRDIKPANVFIT 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 283 KCETCAIADLGLAvkhdSILNTIDIPQNPKVGTKRYMAPEMLDDTMnvnifESFKrADIYSVGLVYWEIA 352
Cdd:cd08224  139 ANGVVKLGDLGLG----RFFSSKTTAAHSLVGTPYYMSPERIREQG-----YDFK-SDIWSLGCLLYEMA 198
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
149-353 6.49e-14

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: 71.64  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHEN--ILGFIAADNKDngtwTQLWLVSEYHE 224
Cdd:cd06641   10 EKIGKGSFGEVFKGidNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSpyVTKYYGSYLKD----TKLWIIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNT 304
Cdd:cd06641   86 GGSALDLLEPGPLDETQIATILREILKGLDYLHSE--------KKIHRDIKAANVLLSEHGEVKLADFGVAGQ----LTD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 305 IDIPQNPKVGTKRYMAPEMLDDTMnvniFESfkRADIYSVGLVYWEIAR 353
Cdd:cd06641  154 TQIKRN*FVGTPFWMAPEVIKQSA----YDS--KADIWSLGITAIELAR 196
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
145-435 6.67e-14

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR 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: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 72.13  E-value: 6.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCG---ED----VAVKIFSSRDERSWfREAEIYQTVML----RHENILGFIAADNKDNgtw 213
Cdd:cd05055   37 LSFGKTLGAGAFGKVVEATAYGlskSDavmkVAVKMLKPTAHSSE-REALMSELKIMshlgNHENIVNLLGACTIGG--- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tQLWLVSEYHEQGSLYDYLNRN---IVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIA 290
Cdd:cd05055  113 -PILVITEYCCYGDLLNFLRRKresFLTLEDLLSFSYQVAKGMAFL-------ASKNCI-HRDLAARNVLLTHGKIVKIC 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 291 DLGLA--VKHDSilNTIdIPQNPKVGTKrYMAPEMLDDtmNVNIFESfkraDIYSVGLVYWEIArrcSVGGIveeyqlPY 368
Cdd:cd05055  184 DFGLArdIMNDS--NYV-VKGNARLPVK-WMAPESIFN--CVYTFES----DVWSYGILLWEIF---SLGSN------PY 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 369 YDMvPSDPSIEEMRKvvcdQKFRPSIPNQwqsceALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05055  245 PGM-PVDSKFYKLIK----EGYRMAQPEH-----APAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQ 301
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
194-435 8.26e-14

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. 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 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-A/B 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: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 71.47  E-value: 8.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 194 LRHENILGFIAA--DNkdngtwTQLWLVSEYHEQGSLYDYL-NRNIvTVAGMIKLAL--SIASGLAHLHMEIVGTqgkpa 268
Cdd:cd14042   59 LQHDNLTRFIGAcvDP------PNICILTEYCPKGSLQDILeNEDI-KLDWMFRYSLihDIVKGMHYLHDSEIKS----- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 269 iaHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIPQNPKvgTKRYMAPEMLddTMNVNIFESFKRADIYSVGLVY 348
Cdd:cd14042  127 --HGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPPDDSHAYYA--KLLWTAPELL--RDPNPPPPGTQKGDVYSFGIIL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 349 WEIARRcsvggiveeyQLPYYDMVPSDPS---IEEMRKVVCDQKFRPSI-PNQWQSCealrvMGRIMRECWYANGAARLT 424
Cdd:cd14042  201 QEIATR----------QGPFYEEGPDLSPkeiIKKKVRNGEKPPFRPSLdELECPDE-----VLSLMQRCWAEDPEERPD 265
                        250
                 ....*....|.
gi 161333835 425 ALRIKKTISQL 435
Cdd:cd14042  266 FSTLRNKLKKL 276
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
142-435 8.92e-14

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: 71.59  E-value: 8.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 142 ARTIVLQEIVGKGRFGEVWHGRW------CGEDVAVKIFSSRDE---RSWFREAEIYQTvmLRHENIL---GFIAADNKD 209
Cdd:cd14205    3 ERHLKFLQQLGKGNFGSVEMCRYdplqdnTGEVVAVKKLQHSTEehlRDFEREIEILKS--LQHDNIVkykGVCYSAGRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 210 NgtwtqLWLVSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDIKSKNILVKKCETC 287
Cdd:cd14205   81 N-----LRLIMEYLPYGSLRDYLqkHKERIDHIKLLQYTSQICKGMEYL--------GTKRYIHRDLATRNILVENENRV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 288 AIADLGLavkhdsilnTIDIPQNPKVGTKR--------YMAPEMLDDTmnvnifeSFKRA-DIYSVGLVYWEIarrcsvg 358
Cdd:cd14205  148 KIGDFGL---------TKVLPQDKEYYKVKepgespifWYAPESLTES-------KFSVAsDVWSFGVVLYEL------- 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 359 giveeyqLPYYDMVPSDPSiEEMRKVVCDQKFRPSIpnqWQSCEALRVMGR-------------IMRECWYANGAARLTA 425
Cdd:cd14205  205 -------FTYIEKSKSPPA-EFMRMIGNDKQGQMIV---FHLIELLKNNGRlprpdgcpdeiymIMTECWNNNVNQRPSF 273
                        330
                 ....*....|
gi 161333835 426 LRIKKTISQL 435
Cdd:cd14205  274 RDLALRVDQI 283
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
140-351 1.12e-13

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: 70.91  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 140 TIART-IVLQEIVGKGRFGEVWHGRWC---GEDVAV-----KIFSSRDERSWF-REAEIYQTvmLRHENILGFIAADNKD 209
Cdd:cd05056    2 EIQREdITLGRCIGEGQFGDVYQGVYMspeNEKIAVavktcKNCTSPSVREKFlQEAYIMRQ--FDHPHIVKLIGVITEN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 210 ngtwtQLWLVSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCET 286
Cdd:cd05056   80 -----PVWIVMELAPLGELRSYLqvNKYSLDLASLILYAYQLSTALAYLEsKRFV---------HRDIAARNVLVSSPDC 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 287 CAIADLGLA-VKHDSILNTIDIPQNPkvgtKRYMAPEmlddtmNVNiFESFKRA-DIYSVGLVYWEI 351
Cdd:cd05056  146 VKLGDFGLSrYMEDESYYKASKGKLP----IKWMAPE------SIN-FRRFTSAsDVWMFGVCMWEI 201
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
149-354 1.18e-13

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 70.81  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEdVAVKIFS-SRDE----RSWFREAEIYQTVmlRHENILGFIAADNKDngtwTQLWLVSEYH 223
Cdd:cd14153    6 ELIGKGRFGQVYHGRWHGE-VAIRLIDiERDNeeqlKAFKREVMAYRQT--RHENVVLFMGACMSP----PHLAIITSLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETcAIADLGL-----AV 296
Cdd:cd14153   79 KGRTLYSVVRdaKVVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFYDNGKV-VITDFGLftisgVL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 297 KHDSILNTIDIPQnpkvGTKRYMAPEM---LDDTMNVNIFESFKRADIYSVGLVYWEIARR 354
Cdd:cd14153  150 QAGRREDKLRIQS----GWLCHLAPEIirqLSPETEEDKLPFSKHSDVFAFGTIWYELHAR 206
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
147-353 1.31e-13

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: 70.46  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVwHGRWC---GEDVAVKIFSSRDERSWFREA--EIYQTVMLRHENILG----FIAADnkdngtwtQLW 217
Cdd:cd06610    5 LIEVIGSGATAVV-YAAYClpkKEKVAIKRIDLEKCQTSMDELrkEIQAMSQCNHPNVVSyytsFVVGD--------ELW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNI-------VTVAGMIKLALSiasGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIA 290
Cdd:cd06610   76 LVMPLLSGGSLLDIMKSSYprggldeAIIATVLKEVLK---GLEYLH--------SNGQIHRDVKAGNILLGEDGSVKIA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 291 DLGLAVkhdSILNTIDIPQNPK---VGTKRYMAPEMLDDTMNVNifesFKrADIYSVGLVYWEIAR 353
Cdd:cd06610  145 DFGVSA---SLATGGDRTRKVRktfVGTPCWMAPEVMEQVRGYD----FK-ADIWSFGITAIELAT 202
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
150-345 1.38e-13

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: 70.46  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW--HGRWCGEDVAVKIF--------SSRDERSWFREAEIYQTvmLRHENILGFIAADnKDNGTwtqLWLV 219
Cdd:cd06625    7 LLGQGAFGQVYlcYDADTGRELAVKQVeidpinteASKEVKALECEIQLLKN--LQHERIVQYYGCL-QDEKS---LSIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNR-----NIVTVagmiKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd06625   81 MEYMPGGSVKDEIKAygaltENVTR----KYTRQILEGLAYLHsNMIV---------HRDIKGANILRDSNGNVKLGDFG 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 294 LAVKHDSILNTIDIpqNPKVGTKRYMAPEMLDDtmnvnifESFKR-ADIYSVG 345
Cdd:cd06625  148 ASKRLQTICSSTGM--KSVTGTPYWMSPEVING-------EGYGRkADIWSVG 191
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
145-424 1.70e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 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: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 70.81  E-value: 1.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGED---------VAVKIF----SSRDERSWFREAEIYQTVMlRHENILGFIAADNKDNg 211
Cdd:cd05101   26 LTLGKPLGEGCFGQVVMAEAVGIDkdkpkeavtVAVKMLkddaTEKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQDG- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 212 twtQLWLVSEYHEQGSLYDYL--------------NR---NIVTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDI 274
Cdd:cd05101  104 ---PLYVIVEYASKGNLREYLrarrppgmeysydiNRvpeEQMTFKDLVSCTYQLARG-----MEYLASQ---KCIHRDL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 275 KSKNILVKKCETCAIADLGLAVKhdsiLNTIDIPQNPKVG--TKRYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEIA 352
Cdd:cd05101  173 AARNVLVTENNVMKIADFGLARD----INNIDYYKKTTNGrlPVKWMAPEALFDRVYTH------QSDVWSFGVLMWEIF 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 353 rrcSVGGIveeyqlPYydmvPSDPsIEEMRKVVcDQKFRPSIPnqwQSCEALRVMgrIMRECWYANGAARLT 424
Cdd:cd05101  243 ---TLGGS------PY----PGIP-VEELFKLL-KEGHRMDKP---ANCTNELYM--MMRDCWHAVPSQRPT 294
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
149-353 1.80e-13

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: 70.47  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHEN--ILGFIAADNKDngtwTQLWLVSEYHE 224
Cdd:cd06642   10 ERIGKGSFGEVYKGidNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSpyITRYYGSYLKG----TKLWIIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNT 304
Cdd:cd06642   86 GGSALDLLKPGPLEETYIATILREILKGLDYLHSE--------RKIHRDIKAANVLLSEQGDVKLADFGVAGQ----LTD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 305 IDIPQNPKVGTKRYMAPEMLDDTMnvnifESFKrADIYSVGLVYWEIAR 353
Cdd:cd06642  154 TQIKRNTFVGTPFWMAPEVIKQSA-----YDFK-ADIWSLGITAIELAK 196
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
151-434 2.08e-13

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: 69.69  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGED-----VAVKIFSS----RDERSWFREAEIYQTvmLRHENILGFIAADNKDngtwtQLWLVSE 221
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSgkeveVAVKTLKQehekAGKKEFLREASVMAQ--LDHPCIVRLIGVCKGE-----PLMLVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGL--AVKH 298
Cdd:cd05060   76 LAPLGPLLKYLkKRREIPVSDLKELAHQVAMGMAYLESK--------HFVHRDLAARNVLLVNRHQAKISDFGMsrALGA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 DSilNTIDIPQNPKVGTKRYmAPEmlddTMNVNIFESfkRADIYSVGLVYWEIArrcSVGgiveeyQLPYYDMvpSDPSI 378
Cdd:cd05060  148 GS--DYYRATTAGRWPLKWY-APE----CINYGKFSS--KSDVWSYGVTLWEAF---SYG------AKPYGEM--KGPEV 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 379 EEMrkvvCDQKFRPSIPNqwqscEALRVMGRIMRECWYANGAARLTALRIKKTISQ 434
Cdd:cd05060  208 IAM----LESGERLPRPE-----ECPQEIYSIMLSCWKYRPEDRPTFSELESTFRR 254
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
147-398 2.22e-13

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: 69.59  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW--HGRWCGEDVAVKIFS-----SRDE-RSWFREAEIYQTvmLRHENILGFIAA--DNKDngtwtqL 216
Cdd:cd05578    4 ILRVIGKGSFGKVCivQKKDTKKMFAMKYMNkqkciEKDSvRNVLNELEILQE--LEHPFLVNLWYSfqDEED------M 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd05578   76 YMVVDLLLGGDLRYHLQQKVKFSEETVKFYICeIVLALDYLH-----SKN---IIHRDIKPDNILLDEQGHVHITDFNIA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VK-HDSILNTidipqnPKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWEIARRcsvggiveeyQLPYYdmVPS 374
Cdd:cd05578  148 TKlTDGTLAT------STSGTKPYMAPEVFMRA------GYSFAVDWWSLGVTAYEMLRG----------KRPYE--IHS 203
                        250       260
                 ....*....|....*....|....*..
gi 161333835 375 DPSIEEMRkvvcdQKF---RPSIPNQW 398
Cdd:cd05578  204 RTSIEEIR-----AKFetaSVLYPAGW 225
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
147-327 2.26e-13

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: 69.72  E-value: 2.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHG--RWCGEDVAVK------IFSSRDERSWFREAEIYQTvmLRHENILGFIAA-DNKDngtwtQLW 217
Cdd:cd14073    5 LLETLGKGTYGKVKLAieRATGREVAIKsikkdkIEDEQDMVRIRREIEIMSS--LNHPHIIRIYEVfENKD-----KIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLN-RNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA- 295
Cdd:cd14073   78 IVMEYASGGELYDYISeRRRLPEREARRIFRQIVSAVHYCH--------KNGVVHRDLKLENILLDQNGNAKIADFGLSn 149
                        170       180       190
                 ....*....|....*....|....*....|...
gi 161333835 296 -VKHDSILNTIdipqnpkVGTKRYMAPEMLDDT 327
Cdd:cd14073  150 lYSKDKLLQTF-------CGSPLYASPEIVNGT 175
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
145-351 2.45e-13

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: 70.10  E-value: 2.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGR-----WCGEDVAVKIFSSRDERS------WFREAEIYQTvmLRHENILGFIAADNKDNgtw 213
Cdd:cd05048    7 VRFLEELGEGAFGKVYKGEllgpsSEESAISVAIKTLKENASpktqqdFRREAELMSD--LQHPNIVCLLGVCTKEQ--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tQLWLVSEYHEQGSLYDYLNRN-----------------IVTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDIKS 276
Cdd:cd05048   82 -PQCMLFEYMAHGDLHEFLVRHsphsdvgvssdddgtasSLDQSDFLHIAIQIAAG-----MEYLSSH---HYVHRDLAA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 277 KNILVKKCETCAIADLGLA----------VKHDSILNTidipqnpkvgtkRYMAPEMLddtmnvnIFESFK-RADIYSVG 345
Cdd:cd05048  153 RNCLVGDGLTVKISDFGLSrdiyssdyyrVQSKSLLPV------------RWMPPEAI-------LYGKFTtESDVWSFG 213

                 ....*.
gi 161333835 346 LVYWEI 351
Cdd:cd05048  214 VVLWEI 219
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
150-345 2.82e-13

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: 69.49  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHG--RWCGEDVAVK--IFSSRDERSWFREA--------EIYQTVMLRHENILGFIaaDNKDNGTWTQLW 217
Cdd:cd06628    7 LIGSGSFGSVYLGmnASSGELMAVKqvELPSVSAENKDRKKsmldalqrEIALLRELQHENIVQYL--GSSSDANHLNIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LvsEYHEQGSLYDYLN----------RNIVTvagmiklalSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETC 287
Cdd:cd06628   85 L--EYVPGGSVATLLNnygafeeslvRNFVR---------QILKGLNYLHNR--------GIIHRDIKGANILVDNKGGI 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 288 AIADLGLAVK-HDSILNTIDIPQNPKV-GTKRYMAPEMLDDTMNVnifesfKRADIYSVG 345
Cdd:cd06628  146 KISDFGISKKlEANSLSTKNNGARPSLqGSVFWMAPEVVKQTSYT------RKADIWSLG 199
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
149-347 2.82e-13

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: 70.14  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFSSRD--ERS-WFREAEIYQTVMlRHENILGFIAADNKDNgtwtQLWLVSEYH 223
Cdd:cd14090    8 ELLGEGAYASVQTCInlYTGKEYAVKIIEKHPghSRSrVFREVETLHQCQ-GHPNILQLIEYFEDDE----RFYLVFEKM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILvkkCET------CAIADLGLAV 296
Cdd:cd14090   83 RGGPLLSHIEKRVhFTEQEASLVVRDIASALDFLH--------DKGIAHRDLKPENIL---CESmdkvspVKICDFDLGS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 297 KHDSILNTIDIPQNPK----VGTKRYMAPEMLDdtmnVNIFESF---KRADIYSVGLV 347
Cdd:cd14090  152 GIKLSSTSMTPVTTPElltpVGSAEYMAPEVVD----AFVGEALsydKRCDLWSLGVI 205
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
147-354 3.22e-13

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: 70.07  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTV----MLRHENILGFIAADNKDNGTWtqlwLVS 220
Cdd:cd06633   26 LHEI-GHGSFGAVYFATnsHTNEVVAIKKMSYSGKQTNEKWQDIIKEVkflqQLKHPNTIEYKGCYLKDHTAW----LVM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHeQGSLYDYLNRNI-----VTVAGMIKLALSiasGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd06633  101 EYC-LGSASDLLEVHKkplqeVEIAAITHGALQ---GLAYLHSH--------NMIHRDIKAGNILLTEPGQVKLADFGSA 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 296 vkhdsilnTIDIPQNPKVGTKRYMAPEMLdDTMNVNIFESfkRADIYSVGLVYWEIARR 354
Cdd:cd06633  169 --------SIASPANSFVGTPYWMAPEVI-LAMDEGQYDG--KVDIWSLGITCIELAER 216
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
133-424 3.38e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 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: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 70.43  E-value: 3.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 133 LPLLVQRTIART-IVLQEIVGKGRFGEVWHGRWCGED---------VAVKIF----SSRDERSWFREAEIYQTVMlRHEN 198
Cdd:cd05100    1 LPADPKWELSRTrLTLGKPLGEGCFGQVVMAEAIGIDkdkpnkpvtVAVKMLkddaTDKDLSDLVSEMEMMKMIG-KHKN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 199 ILGFIAADNKDNgtwtQLWLVSEYHEQGSLYDYLN-----------------RNIVTVAGMIKLALSIASGlahlhMEIV 261
Cdd:cd05100   80 IINLLGACTQDG----PLYVLVEYASKGNLREYLRarrppgmdysfdtcklpEEQLTFKDLVSCAYQVARG-----MEYL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 262 GTQgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNTIDIPQNPKVG--TKRYMAPEMLDDTMNVNifesfkRA 339
Cdd:cd05100  151 ASQ---KCIHRDLAARNVLVTEDNVMKIADFGLARD----VHNIDYYKKTTNGrlPVKWMAPEALFDRVYTH------QS 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 340 DIYSVGLVYWEIArrcSVGGIveeyqlPYydmvPSDPsIEEMRKVVcDQKFRPSIPnqwQSCEALRVMgrIMRECWYANG 419
Cdd:cd05100  218 DVWSFGVLLWEIF---TLGGS------PY----PGIP-VEELFKLL-KEGHRMDKP---ANCTHELYM--IMRECWHAVP 277

                 ....*
gi 161333835 420 AARLT 424
Cdd:cd05100  278 SQRPT 282
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
150-367 3.70e-13

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: 69.21  E-value: 3.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREaEIYQTVMLRHENILGFIAAdnkdnGTWTQLwLVSEYHEQGSLY 229
Cdd:cd14068    1 LLGDGGFGSVYRAVYRGEDVAVKIFNKHTSFRLLRQ-ELVVLSHLHHPSLVALLAA-----GTAPRM-LVMELAPKGSLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 230 DYLNRNIVTVAGMI--KLALSIASGLAHLHMEIvgtqgkpaIAHRDIKSKNILV----KKCETCA-IADLGLAvKHDSIL 302
Cdd:cd14068   74 ALLQQDNASLTRTLqhRIALHVADGLRYLHSAM--------IIYRDLKPHNVLLftlyPNCAIIAkIADYGIA-QYCCRM 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 303 NTidipqNPKVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIarrCSVGG-IVEEYQLP 367
Cdd:cd14068  145 GI-----KTSEGTPGFRAPEVARGNVIYN-----QQADVYSFGLLLYDI---LTCGErIVEGLKFP 197
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
149-352 3.91e-13

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: 69.43  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRW--CGEDVAVKIF---SSRDERSwfreaEIYQTVMLRHENILGFIAADNKDNGTW---TQLWLVS 220
Cdd:cd06917    7 ELVGRGSYGAVYRGYHvkTGRVVALKVLnldTDDDDVS-----DIQKEVALLSQLKLGQPKNIIKYYGSYlkgPSLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNrnivtvAGMIK---LALSIAS---GLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd06917   82 DYCEGGSIRTLMR------AGPIAeryIAVIMREvlvALKFIH--------KDGIIHRDIKAANILVTNTGNVKLCDFGV 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 295 AvkhdSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIfesfkRADIYSVGLVYWEIA 352
Cdd:cd06917  148 A----ASLNQNSSKRSTFVGTPYWMAPEVITEGKYYDT-----KADIWSLGITTYEMA 196
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
148-355 4.68e-13

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: 69.05  E-value: 4.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVWHGR--WCGEDVAVKI--FSSRDE---RSWFREAEIYQTvmLRHENILGF---IAADNKdngtwtqLW 217
Cdd:cd07829    4 LEKLGEGTYGVVYKAKdkKTGEIVALKKirLDNEEEgipSTALREISLLKE--LKHPNIVKLldvIHTENK-------LY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQgSLYDYLNRNIVTV-AGMIK-LALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd07829   75 LVFEYCDQ-DLKKYLDKRPGPLpPNLIKsIMYQLLRGLAYCHsHRIL---------HRDLKPQNLLINRDGVLKLADFGL 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 295 AvkhdsilNTIDIPQN---PKVGTKRYMAPEML--DDTMNVNIfesfkraDIYSVGLVYWEIARRC 355
Cdd:cd07829  145 A-------RAFGIPLRtytHEVVTLWYRAPEILlgSKHYSTAV-------DIWSVGCIFAELITGK 196
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
151-356 4.73e-13

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 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: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 68.83  E-value: 4.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGE---VWHgRWCGEDVAVK---IFSSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSEYHE 224
Cdd:cd14221    1 LGKGCFGQaikVTH-RETGEVMVMKeliRFDEETQRTFLKEVKVMRC--LEHPNVLKFIGVLYKDK----RLNFITEYIK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLnRNIVTV---AGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGLA----- 295
Cdd:cd14221   74 GGTLRGII-KSMDSHypwSQRVSFAKDIASGMAYLHsMNII---------HRDLNSHNCLVRENKSVVVADFGLArlmvd 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 296 -VKHDSILNTIDIPQNPK----VGTKRYMAPEMLDDtmnvnifESF-KRADIYSVGLVYWEIARRCS 356
Cdd:cd14221  144 eKTQPEGLRSLKKPDRKKrytvVGNPYWMAPEMING-------RSYdEKVDVFSFGIVLCEIIGRVN 203
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
148-324 4.83e-13

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: 69.13  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVWHGRwC---GEDVAVKIFSSRDERSWF-----REAEIYQtvMLRHENILGF--IAADNKDNGTWTQLW 217
Cdd:cd07840    4 IAQIGEGTYGQVYKAR-NkktGELVALKKIRMENEKEGFpitaiREIKLLQ--KLDHPNVVRLkeIVTSKGSAKYKGSIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHE---QGSLYDYLNRniVTVaGMIK-LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd07840   81 MVFEYMDhdlTGLLDNPEVK--FTE-SQIKcYMKQLLEGLQYLH--------SNGILHRDIKGSNILINNDGVLKLADFG 149
                        170       180       190
                 ....*....|....*....|....*....|.
gi 161333835 294 LAVKHDSilnTIDIPQNPKVGTKRYMAPEML 324
Cdd:cd07840  150 LARPYTK---ENNADYTNRVITLWYRPPELL 177
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
147-351 6.62e-13

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: 68.24  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGRWCGE-DVAVKIF--SSRDERSWFREAEiyqtVM--LRHENILgfiaadnKDNGTWTQ---LWL 218
Cdd:cd05059    9 LKEL-GSGQFGVVHLGKWRGKiDVAIKMIkeGSMSEDDFIEEAK----VMmkLSHPKLV-------QLYGVCTKqrpIFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAv 296
Cdd:cd05059   77 VTEYMANGCLLNYLreRRGKFQTEQLLEMCKDVCEAMEYLE--------SNGFIHRDLAARNCLVGEQNVVKVSDFGLA- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 297 khdsiLNTIDIPQNPKVGTK---RYMAPEMLDDTMnvniFESfkRADIYSVGLVYWEI 351
Cdd:cd05059  148 -----RYVLDDEYTSSVGTKfpvKWSPPEVFMYSK----FSS--KSDVWSFGVLMWEV 194
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
147-348 7.36e-13

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: 68.27  E-value: 7.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSWFREAEIYQ-----TVMLRHENILGFIAADNKDNgtwtQLWLV 219
Cdd:cd14098    4 IIDRLGSGTFAEVKKAveVETGKMRAIKQIVKRKVAGNDKNLQLFQreiniLKSLEHPGIVRLIDWYEDDQ----HIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRNivtvaGMI------KLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCET--CAIAD 291
Cdd:cd14098   80 MEYVEGGDLMDFIMAW-----GAIpeqharELTKQILEAMAYTH--------SMGITHRDLKPENILITQDDPviVKISD 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 292 LGLA-VKH-DSILNTIdipqnpkVGTKRYMAPEML--DDTMNVNIFESfkRADIYSVG-LVY 348
Cdd:cd14098  147 FGLAkVIHtGTFLVTF-------CGTMAYLAPEILmsKEQNLQGGYSN--LVDMWSVGcLVY 199
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
149-352 7.69e-13

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: 68.50  E-value: 7.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW--HGRWCGEDVAVKIFSSRDERSWFREAEiYQTV--MLRHENILGFIAAD-NKDNGTWTQLWLVSEYH 223
Cdd:cd06638   24 ETIGKGTYGKVFkvLNKKNGSKAAVKILDPIHDIDEEIEAE-YNILkaLSDHPNVVKFYGMYyKKDVKNGDQLWLVLELC 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYD----YLNRNIVTVAGMIKLALSIA-SGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKh 298
Cdd:cd06638  103 NGGSVTDlvkgFLKRGERMEEPIIAYILHEAlMGLQHLHVN--------KTIHRDVKGNNILLTTEGGVKLVDFGVSAQ- 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 dsiLNTIDIPQNPKVGTKRYMAPEM------LDDTMNvnifesfKRADIYSVGLVYWEIA 352
Cdd:cd06638  174 ---LTSTRLRRNTSVGTPFWMAPEViaceqqLDSTYD-------ARCDVWSLGITAIELG 223
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
145-438 1.03e-12

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET 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: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 68.45  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWH-------GRWCGEDVAVKIF----SSRDERSWFREAEIYQTVmlRHENILGFIAADNKDNGtw 213
Cdd:cd05045    2 LVLGKTLGEGEFGKVVKatafrlkGRAGYTTVAVKMLkenaSSSELRDLLSEFNLLKQV--NHPHVIKLYGACSQDGP-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tqLWLVSEYHEQGSLYDYL---------------NRNI----------VTVAGMIKLALSIASGLAHL-HMEIVgtqgkp 267
Cdd:cd05045   78 --LLLIVEYAKYGSLRSFLresrkvgpsylgsdgNRNSsyldnpderaLTMGDLISFAWQISRGMQYLaEMKLV------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 268 aiaHRDIKSKNILVKKCETCAIADLGLA---VKHDSILNTidipQNPKVGTKrYMAPEMLDDtmnvNIFESfkRADIYSV 344
Cdd:cd05045  150 ---HRDLAARNVLVAEGRKMKISDFGLSrdvYEEDSYVKR----SKGRIPVK-WMAIESLFD----HIYTT--QSDVWSF 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 345 GLVYWEIArrcSVGGIveeyqlPYYDMVPsdpsiEEMRKVVcDQKFRPSIPnqwQSCEalRVMGRIMRECWYANGAARLT 424
Cdd:cd05045  216 GVLLWEIV---TLGGN------PYPGIAP-----ERLFNLL-KTGYRMERP---ENCS--EEMYNLMLTCWKQEPDKRPT 275
                        330
                 ....*....|....
gi 161333835 425 ALRIKKTISQLCVK 438
Cdd:cd05045  276 FADISKELEKMMVK 289
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
146-324 1.09e-12

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: 67.94  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFGEVWHGRW--CGEDVAVKI----FSSRDERSWFREAEIYQTvMLRHENILG----FIaaDNKdngtwtQ 215
Cdd:cd07830    3 VIKQL-GDGTFGSVYLARNkeTGELVAIKKmkkkFYSWEECMNLREVKSLRK-LNEHPNIVKlkevFR--END------E 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQgSLYD-YLNRNIV-----TVAGMIklaLSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAI 289
Cdd:cd07830   73 LYFVFEYMEG-NLYQlMKDRKGKpfsesVIRSII---YQILQGLAHIH--------KHGFFHRDLKPENLLVSGPEVVKI 140
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 161333835 290 ADLGLAVKHDSILntidiPQNPKVGTKRYMAPEML 324
Cdd:cd07830  141 ADFGLAREIRSRP-----PYTDYVSTRWYRAPEIL 170
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
141-352 1.69e-12

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: 67.45  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 141 IART-IVLQEIVGKGRFGEVWHGRW--CGEDVAVKIF--SSRDERSWFREAEIYQTvmLRHENILGFIaadnkdnGTWTQ 215
Cdd:cd05052    3 IERTdITMKHKLGGGQYGEVYEGVWkkYNLTVAVKTLkeDTMEVEEFLKEAAVMKE--IKHPNLVQLL-------GVCTR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 ---LWLVSEYHEQGSLYDYL---NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAI 289
Cdd:cd05052   74 eppFYIITEFMPYGNLLDYLrecNREELNAVVLLYMATQIASAMEYLE--------KKNFIHRDLAARNCLVGENHLVKV 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 290 ADLGLA--VKHDsilnTIDIPQNPKVGTKrYMAPEMLddtmNVNIFESfkRADIYSVGLVYWEIA 352
Cdd:cd05052  146 ADFGLSrlMTGD----TYTAHAGAKFPIK-WTAPESL----AYNKFSI--KSDVWAFGVLLWEIA 199
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
149-433 1.73e-12

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. 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. Fer kinase is a member of the Fes subfamily of proteins which 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. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 66.95  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG----------RWCGEDVAVKIfssrdERSWFREAEIYQtvMLRHENILGFIaadnkdnGTWTQ--- 215
Cdd:cd05085    2 ELLGKGNFGEVYKGtlkdktpvavKTCKEDLPQEL-----KIKFLSEARILK--QYDHPNIVKLI-------GVCTQrqp 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNR--NIVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd05085   68 IYIVMELVPGGDFLSFLRKkkDELKTKQLVKFSLDAAAGMAYL-------ESKNCI-HRDLAARNCLVGENNALKISDFG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 294 LAVKHDS-ILNTIDIPQNPkvgtKRYMAPEMLddtmNVNIFESfkRADIYSVGLVYWEIArrcSVGgiveeyQLPYYDMv 372
Cdd:cd05085  140 MSRQEDDgVYSSSGLKQIP----IKWTAPEAL----NYGRYSS--ESDVWSFGILLWETF---SLG------VCPYPGM- 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 373 psdpSIEEMRKVVcDQKFRPSIPnqwQSCEalRVMGRIMRECWYANGAARLTALRIKKTIS 433
Cdd:cd05085  200 ----TNQQAREQV-EKGYRMSAP---QRCP--EDIYKIMQRCWDYNPENRPKFSELQKELA 250
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
150-352 1.99e-12

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: 66.94  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHG--RWCGEDVAVKIFSSRD-ERSWFREA--EIYQTVMLRHENILGFIAAD-NKDngtwtQLWLVSEYH 223
Cdd:cd06626    7 KIGEGTFGKVYTAvnLDTGELMAMKEIRFQDnDPKTIKEIadEMKVLEGLDHPNLVRYYGVEvHRE-----EVYIFMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHMeivgtQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHDSil 302
Cdd:cd06626   82 QEGTLEELLRHGRILDEAVIRVyTLQLLEGLAYLHE-----NG---IVHRDIKPANIFLDSNGLIKLGDFGSAVKLKN-- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 303 NTIDIPQNPK---VGTKRYMAPEMLDDTMNVNIFESfkrADIYSVGLVYWEIA 352
Cdd:cd06626  152 NTTTMAPGEVnslVGTPAYMAPEVITGNKGEGHGRA---ADIWSLGCVVLEMA 201
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
147-373 2.22e-12

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: 66.98  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVKI--FSSRDERSWFREaEIYQTVMLRHENILGFIaadnkdnGTW---TQLWLV 219
Cdd:cd06646   13 LIQRVGSGTYGDVYKARnlHTGELAAVKIikLEPGDDFSLIQQ-EIFMVKECKHCNIVAYF-------GSYlsrEKLWIC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDylnrnIVTVAGMIKlALSIA-------SGLAHLHmeivgTQGKpaiAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd06646   85 MEYCGGGSLQD-----IYHVTGPLS-ELQIAyvcretlQGLAYLH-----SKGK---MHRDIKGANILLTDNGDVKLADF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAVKhdsILNTIdIPQNPKVGTKRYMAPEMLDDTMNVNIFEsfkRADIYSVGLVYWEIArrcsvggiveEYQLPYYDMV 372
Cdd:cd06646  151 GVAAK---ITATI-AKRKSFIGTPYWMAPEVAAVEKNGGYNQ---LCDIWAVGITAIELA----------ELQPPMFDLH 213

                 .
gi 161333835 373 P 373
Cdd:cd06646  214 P 214
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
149-349 2.25e-12

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: 67.36  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVwhgRWC-----GEDVAVKIFSSRDERSW---FREAE-IYQTvmLRHENILGFIAADNKDngtwTQLWLV 219
Cdd:cd14174    8 ELLGEGAYAKV---QGCvslqnGKEYAVKIIEKNAGHSRsrvFREVEtLYQC--QGNKNILELIEFFEDD----TRFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNIL---------VKKCETcai 289
Cdd:cd14174   79 FEKLRGGSILAHIqKRKHFNEREASRVVRDIASALDFLH-----TKG---IAHRDLKPENILcespdkvspVKICDF--- 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 290 aDLGLAVKHDSILNTIDIPQ-NPKVGTKRYMAPEMLDDTMNVNIFESfKRADIYSVGLVYW 349
Cdd:cd14174  148 -DLGSGVKLNSACTPITTPElTTPCGSAEYMAPEVVEVFTDEATFYD-KRCDLWSLGVILY 206
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
151-432 2.64e-12

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, 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. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 66.67  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGED--------VAVKIF---SSRDERSWF-REAeiyqTVM--LRHENILGF--IAADNKDNgtwt 214
Cdd:cd05044    3 LGSGAFGEVFEGTAKDILgdgsgetkVAVKTLrkgATDQEKAEFlKEA----HLMsnFKHPNILKLlgVCLDNDPQ---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 qlWLVSEYHEQGSLYDYLNRN--------IVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCE 285
Cdd:cd05044   75 --YIILELMEGGDLLSYLRAArptaftppLLTLKDLLSICVDVAKGCVYLEdMHFV---------HRDLAARNCLVSSKD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 286 TC----AIADLGLAVkhdsilntiDIPQNP---KVGTK----RYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIArr 354
Cdd:cd05044  144 YRervvKIGDFGLAR---------DIYKNDyyrKEGEGllpvRWMAPESLVD----GVFTT--QSDVWAFGVLMWEIL-- 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 355 cSVGgiveeyQLPYydmvPSDPSIEEMRKVVCDQKFRPsiPNQwqsC-EALRVMgriMRECWYANGAARLTALRIKKTI 432
Cdd:cd05044  207 -TLG------QQPY----PARNNLEVLHFVRAGGRLDQ--PDN---CpDDLYEL---MLRCWSTDPEERPSFARILEQL 266
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
150-357 3.06e-12

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: 66.30  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGE-------------VWhgrwcgEDVAVKIFSSRDERSWFREAEIYQtvMLRHENIlgfIAADNK--DNGTwt 214
Cdd:cd08221    7 VLGRGAFGEavlyrktednslvVW------KEVNLSRLSEKERRDALNEIDILS--LLNHDNI---ITYYNHflDGES-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 qLWLVSEYHEQGSLYDYLNRN---IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIAD 291
Cdd:cd08221   74 -LFIEMEYCNGGNLHDKIAQQknqLFPEEVVLWYLYQIVSAVSHIH--------KAGILHRDIKTLNIFLTKADLVKLGD 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 292 LGLAvkhdSILNTIDIPQNPKVGTKRYMAPEMLDDTMnvnifESFKrADIYSVGLVYWEIARRCSV 357
Cdd:cd08221  145 FGIS----KVLDSESSMAESIVGTPYYMSPELVQGVK-----YNFK-SDIWAVGCVLYELLTLKRT 200
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
149-353 3.08e-12

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: 66.61  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENilGFIAADNKDNGTWTQLWLVSEYHEQG 226
Cdd:cd06640   10 ERIGKGSFGEVFKGidNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDS--PYVTKYYGSYLKGTKLWIIMEYLGGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 227 SLYDYLNR---NIVTVAGMIKlalSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLN 303
Cdd:cd06640   88 SALDLLRAgpfDEFQIATMLK---EILKGLDYLHSE--------KKIHRDIKAANVLLSEQGDVKLADFGVAGQ----LT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 161333835 304 TIDIPQNPKVGTKRYMAPEMLDDTMnvniFESfkRADIYSVGLVYWEIAR 353
Cdd:cd06640  153 DTQIKRNTFVGTPFWMAPEVIQQSA----YDS--KADIWSLGITAIELAK 196
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
144-347 3.10e-12

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: 66.76  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVW--HGRWCGEDVAVK-IFSSRDERSwfREAEIYQtvMLRHENILGFIAA-----DNKDNgtwTQ 215
Cdd:cd14137    5 SYTIEKVIGSGSFGVVYqaKLLETGEVVAIKkVLQDKRYKN--RELQIMR--RLKHPNIVKLKYFfyssgEKKDE---VY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQgSLYDYL---NRNIVTV-AGMIKL-ALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILV-KKCETCAI 289
Cdd:cd14137   78 LNLVMEYMPE-TLYRVIrhySKNKQTIpIIYVKLySYQLFRGLAYLH-----SLG---ICHRDIKPQNLLVdPETGVLKL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 290 ADLGLA---VKHDsilntidiPQNPKVGTKRYMAPEMLDDTMN--VNIfesfkraDIYSVGLV 347
Cdd:cd14137  149 CDFGSAkrlVPGE--------PNVSYICSRYYRAPELIFGATDytTAI-------DIWSAGCV 196
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
152-345 3.16e-12

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: 66.42  E-value: 3.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVwhgRWC-----GEDVAVKIFS-SRDERSWFRE------AEIYQTVM--------LRHENIL---GFIAADNK 208
Cdd:cd14008    2 GRGSFGKV---KLAldtetGQLYAIKIFNkSRLRKRREGKndrgkiKNALDDVRreiaimkkLDHPNIVrlyEVIDDPES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 209 DNgtwtqLWLVSEYHEQGSLYDyLNRNIVTVAGMIKLALSIA----SGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKC 284
Cdd:cd14008   79 DK-----LYLVLEYCEGGPVME-LDSGDRVPPLPEETARKYFrdlvLGLEYLH-----ENG---IVHRDIKPENLLLTAD 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 285 ETCAIADLGLAvkhdSILNTIDIPQNPKVGTKRYMAPEMLDdtMNVNIFESFKrADIYSVG 345
Cdd:cd14008  145 GTVKISDFGVS----EMFEDGNDTLQKTAGTPAFLAPELCD--GDSKTYSGKA-ADIWALG 198
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
148-351 3.21e-12

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: 66.51  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIvGKGRFGEVWHGRWCGED-VAVKIF--SSRDERSWFREAEIyqTVMLRHENILGFIAADNKDngtwTQLWLVSEYHE 224
Cdd:cd05112   10 QEI-GSGQFGLVHLGYWLNKDkVAIKTIreGAMSEEDFIEEAEV--MMKLSHPKLVQLYGVCLEQ----APICLVFEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdsiL 302
Cdd:cd05112   83 HGCLSDYLrtQRGLFSAETLLGMCLDVCEGMAYLE--------EASVIHRDLAARNCLVGENQVVKVSDFGMT------R 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 303 NTIDIPQNPKVGTK---RYMAPEMLDdtmnvniFESFK-RADIYSVGLVYWEI 351
Cdd:cd05112  149 FVLDDQYTSSTGTKfpvKWSSPEVFS-------FSRYSsKSDVWSFGVLMWEV 194
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
149-430 3.53e-12

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: 66.25  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVK---IFSSRDERSWFRE--------AEIYQTVMLRHENILGFIAADNKDNgtWTQ 215
Cdd:cd06629    7 ELIGKGTYGRVYLAMnaTTGEMLAVKqveLPKTSSDRADSRQktvvdalkSEIDTLKDLDHPNIVQYLGFEETED--YFS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLvsEYHEQGSLYDYLNRNIVTVAGMIK-LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd06629   85 IFL--EYVPGGSIGSCLRKYGKFEEDLVRfFTRQILDGLAYLH--------SKGILHRDLKADNILVDLEGICKISDFGI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 295 AVKHDSILNTiDIPQNPKvGTKRYMAPEMLDdtmNVNIFESFKrADIYSVGLVYWEI--ARRcsvggiveeyqlPYydmv 372
Cdd:cd06629  155 SKKSDDIYGN-NGATSMQ-GSVFWMAPEVIH---SQGQGYSAK-VDIWSLGCVVLEMlaGRR------------PW---- 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 373 PSDPSIEEMRKVVcDQKFRPSIPNQWQ-SCEALrvmgRIMRECWYANGAARLTALRIKK 430
Cdd:cd06629  213 SDDEAIAAMFKLG-NKRSAPPVPEDVNlSPEAL----DFLNACFAIDPRDRPTAAELLS 266
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
143-351 7.52e-12

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: 7.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGE-DVAVKIF--SSRDERSWFREAeiyQTVM-LRHENILGFIAADNKDNgtwtQLWL 218
Cdd:cd05113    4 KDLTFLKELGTGQFGVVKYGKWRGQyDVAIKMIkeGSMSEDEFIEEA---KVMMnLSHEKLVQLYGVCTKQR----PIFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIADLGLAv 296
Cdd:cd05113   77 ITEYMANGCLLNYLreMRKRFQTQQLLEMCKDVCEAMEYL-------ESKQFL-HRDLAARNCLVNDQGVVKVSDFGLS- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 297 khdsiLNTIDIPQNPKVGTK---RYMAPEMLddtmnvNIFESFKRADIYSVGLVYWEI 351
Cdd:cd05113  148 -----RYVLDDEYTSSVGSKfpvRWSPPEVL------MYSKFSSKSDVWAFGVLMWEV 194
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
150-356 8.90e-12

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: 65.30  E-value: 8.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRW------CGEDVAVKIF---SSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNGTwtQLWLVS 220
Cdd:cd05081   11 QLGKGNFGSVELCRYdplgdnTGALVAVKQLqhsGPDQQRDFQREIQILKA--LHSDFIVKYRGVSYGPGRR--SLRLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDIKSKNILVKKCETCAIADLGLA--V 296
Cdd:cd05081   87 EYLPSGCLRDFLqrHRARLDASRLLLYSSQICKG-----MEYLGSR---RCVHRDLAARNILVESEAHVKIADFGLAklL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 297 KHDSILNTIDIP-QNPKVgtkrYMAPEMLDDtmnvNIFEsfKRADIYSVGLVYWEI----ARRCS 356
Cdd:cd05081  159 PLDKDYYVVREPgQSPIF----WYAPESLSD----NIFS--RQSDVWSFGVVLYELftycDKSCS 213
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
147-351 9.29e-12

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty 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: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 65.20  E-value: 9.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWH-GRWCGE-DVAVKIFSSRDERSWFREA-EIYQTVML-RHENILGFIAA---DNKDNGTWTQLWLV 219
Cdd:cd13975    4 LGRELGRGQYGVVYAcDSWGGHfPCALKSVVPPDDKHWNDLAlEFHYTRSLpKHERIVSLHGSvidYSYGGGSSIAVLLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEyHEQGSLYDYLNRNIvTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHD 299
Cdd:cd13975   84 ME-RLHRDLYTGIKAGL-SLEERLQIALDVVEGIRFLH-----SQG---LVHRDIKLKNVLLDKKNRAKITDLGFCKPEA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161333835 300 SILNTIdipqnpkVGTKRYMAPEMLDDTMNVNIfesfkraDIYSVGLVYWEI 351
Cdd:cd13975  154 MMSGSI-------VGTPIHMAPELFSGKYDNSV-------DVYAFGILFWYL 191
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
151-400 9.69e-12

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: 65.37  E-value: 9.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEV--WHGRWCGEDVAVKI----FSSRDERSWFREAEIYQTvmLRHENIlgfIAADNKDNGTW----TQLWLVS 220
Cdd:cd14038    2 LGTGGFGNVlrWINQETGEQVAIKQcrqeLSPKNRERWCLEIQIMKR--LNHPNV---VAARDVPEGLQklapNDLPLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 -EYHEQGSLYDYLNR--NIVTV--AGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCE---TCAIADL 292
Cdd:cd14038   77 mEYCQGGDLRKYLNQfeNCCGLreGAILTLLSDISSALRYLH--------ENRIIHRDLKPENIVLQQGEqrlIHKIIDL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAVKHD--SILNTIdipqnpkVGTKRYMAPEMLDDTMnvnifesfkradiYSVGLVYWeiarrcSVGGIVEEyqlpyyd 370
Cdd:cd14038  149 GYAKELDqgSLCTSF-------VGTLQYLAPELLEQQK-------------YTVTVDYW------SFGTLAFE------- 195
                        250       260       270
                 ....*....|....*....|....*....|....
gi 161333835 371 mvpsdpsieemrkvvCDQKFRPSIPN----QWQS 400
Cdd:cd14038  196 ---------------CITGFRPFLPNwqpvQWHG 214
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
149-438 1.01e-11

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 65.21  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW---HGRWcGEDVAVKIFSS-----RDERSWFREAEIYQTVMLRHenILGFIAADNKDNGtwtqlwLVS 220
Cdd:cd14025    2 EKVGSGGFGQVYkvrHKHW-KTWLAIKCPPSlhvddSERMELLEEAKKMEMAKFRH--ILPVYGICSEPVG------LVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvKHDS 300
Cdd:cd14025   73 EYMETGSLEKLLASEPLPWELRFRIIHETAVGMNFLHCM------KPPLLHLDLKPANILLDAHYHVKISDFGLA-KWNG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 301 ILNTIDIPQNPKVGTKRYMAPEMlddtmnvnIFESFK----RADIYSVGLVYWEIARRcsvggiveeyQLPYYDmvpSDP 376
Cdd:cd14025  146 LSHSHDLSRDGLRGTIAYLPPER--------FKEKNRcpdtKHDVYSFAIVIWGILTQ----------KKPFAG---ENN 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 377 SIEEMRKVVcdQKFRPS---IPNQW-QSCEAlrvMGRIMRECWYANGAARLTALRIKKTISQLCVK 438
Cdd:cd14025  205 ILHIMVKVV--KGHRPSlspIPRQRpSECQQ---MICLMKRCWDQDPRKRPTFQDITSETENLLSL 265
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
149-351 1.14e-11

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: 64.59  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW--HGRWCGEDVAVKIFSSRDERSWFREAEIYQTVML---RHENILGFIAADNKDNgtwtQLWLVSEYH 223
Cdd:cd08225    6 KKIGEGSFGKIYlaKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLakmKHPNIVTFFASFQENG----RLFIVMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRN---IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCA-IADLGLAvkhD 299
Cdd:cd08225   82 DGGDLMKRINRQrgvLFSEDQILSWFVQISLGLKHIH--------DRKILHRDIKSQNIFLSKNGMVAkLGDFGIA---R 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161333835 300 SILNTIDIPQNPkVGTKRYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEI 351
Cdd:cd08225  151 QLNDSMELAYTC-VGTPYYLSPEICQNRPYNN------KTDIWSLGCVLYEL 195
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
149-415 1.33e-11

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: 64.57  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRD------ERSWFREAEIYQtvMLRHENILGFIaadnkdnGTWTQ---LWLV 219
Cdd:cd05084    2 ERIGRGNFGEVFSGRLRADNTPVAVKSCREtlppdlKAKFLQEARILK--QYSHPNIVRLI-------GVCTQkqpIYIV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRN--IVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd05084   73 MELVQGGDFLTFLRTEgpRLKVKELIRMVENAAAGMEYL-------ESKHCI-HRDLAARNCLVTEKNVLKISDFGMSRE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 H-DSILN-TIDIPQNPkvgtKRYMAPEMLddtmNVNIFESfkRADIYSVGLVYWEIARRCSVggiveeyqlPYydmvpSD 375
Cdd:cd05084  145 EeDGVYAaTGGMKQIP----VKWTAPEAL----NYGRYSS--ESDVWSFGILLWETFSLGAV---------PY-----AN 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 161333835 376 PSIEEMRKVVcDQKFRPSIPNQwqsCEalRVMGRIMRECW 415
Cdd:cd05084  201 LSNQQTREAV-EQGVRLPCPEN---CP--DEVYRLMEQCW 234
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
149-347 1.41e-11

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: 64.68  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVwhgRWC-----GEDVAVKIFS-----------SRDERSWFREAEIYQTVMlRHENILGFIaaDNKDNGT 212
Cdd:cd14093    9 EILGRGVSSTV---RRCieketGQEFAVKIIDitgeksseneaEELREATRREIEILRQVS-GHPNIIELH--DVFESPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WtqLWLVSEYHEQGSLYDYLNRnIVTVA--GMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIA 290
Cdd:cd14093   83 F--IFLVFELCRKGELFDYLTE-VVTLSekKTRRIMRQLFEAVEFLH--------SLNIVHRDLKPENILLDDNLNVKIS 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 291 DLGLAVKhdsilntidIPQNPK----VGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLV 347
Cdd:cd14093  152 DFGFATR---------LDEGEKlrelCGTPGYLAPEVLKCSMYDNAPGYGKEVDMWACGVI 203
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
150-351 1.49e-11

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They 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, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR 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: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 64.74  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGE------DVAVKIFSSRDERSWF----REAEIYQTVMlrHENILGFIAAdnkdnGTWTQLWLV 219
Cdd:cd05057   14 VLGSGAFGTVYKGVWIPEgekvkiPVAIKVLREETGPKANeeilDEAYVMASVD--HPHLVRLLGI-----CLSSQVQLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA-- 295
Cdd:cd05057   87 TQLMPLGCLLDYVrnHRDNIGSQLLLNWCVQIAKGMSYLEEK--------RLVHRDLAARNVLVKTPNHVKITDFGLAkl 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 296 --VKHDSILNTidipqnpkvGTK---RYMAPEmlddTMNVNIFESfkRADIYSVGLVYWEI 351
Cdd:cd05057  159 ldVDEKEYHAE---------GGKvpiKWMALE----SIQYRIYTH--KSDVWSYGVTVWEL 204
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
150-352 1.55e-11

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: 64.37  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGED--VAVKIFS----SRDER-SWFREAEIYQtvMLRHENILGFIAADNKDNGtwtqLWLVSEY 222
Cdd:cd08220    7 VVGRGAYGTVYLCRRKDDNklVIIKQIPveqmTKEERqAALNEVKVLS--MLHHPNIIEYYESFLEDKA----LMIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRN---IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV-KKCETCAIADLGLAvkh 298
Cdd:cd08220   81 APGGTLFEYIQQRkgsLLSEEEILHFFVQILLALHHVH--------SKQILHRDLKTQNILLnKKRTVVKIGDFGIS--- 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 dSILNTIDiPQNPKVGTKRYMAPEMLDDTMNVnifesfKRADIYSVGLVYWEIA 352
Cdd:cd08220  150 -KILSSKS-KAYTVVGTPCYISPELCEGKPYN------QKSDIWALGCVLYELA 195
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
151-351 1.58e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; 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. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 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: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 64.85  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKIFSSRDERSW------FReAEIYQTVMLRHENILGFiAADNKDNGTWTqlwLVSEYHE 224
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSELDWsvvknsFL-TEVEKLSRFRHPNIVDL-AGYSAQQGNYC---LIYVYLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLNRNI----VTVAGMIKLALSIASGLAHLHmeivgtQGKPAIAHRDIKSKNILVKKCETCAIADLGLA----- 295
Cdd:cd14159   76 NGSLEDRLHCQVscpcLSWSQRLHVLLGTARAIQYLH------SDSPSLIHGDVKSSNILLDAALNPKLGDFGLArfsrr 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 296 VKHDSILNTIDIPQNPKvGTKRYMAPEMLDD-TMNVNIfesfkraDIYSVGLVYWEI 351
Cdd:cd14159  150 PKQPGMSSTLARTQTVR-GTLAYLPEEYVKTgTLSVEI-------DVYSFGVVLLEL 198
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
147-347 2.01e-11

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: 63.86  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSR----DERSWFREAEIYQTVMLRHENILGFIAADNkdngTWTQLWLVS 220
Cdd:cd14162    4 VGKTLGHGSYAVVKKAYSTkhKCKVAIKIVSKKkapeDYLQKFLPREIEVIKGLKHPNLICFYEAIE----TTSRVYIIM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNivtvaGMIKLALS------IASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd14162   80 ELAENGDLLDYIRKN-----GALPEPQArrwfrqLVAGVEYCH-----SKG---VVHRDLKCENLLLDKNNNLKITDFGF 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 295 AVKHDSILNTIDIPQNPKVGTKRYMAPEML-----DDTMnvnifesfkrADIYSVGLV 347
Cdd:cd14162  147 ARGVMKTKDGKPKLSETYCGSYAYASPEILrgipyDPFL----------SDIWSMGVV 194
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
244-352 2.05e-11

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 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: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 64.37  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 244 KLALSIASGLAHLHMEIvgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKH-DSILNTIDIpqnpkvGTKRYMAPE 322
Cdd:cd06617  107 KIAVSIVKALEYLHSKL-------SVIHRDVKPSNVLINRNGQVKLCDFGISGYLvDSVAKTIDA------GCKPYMAPE 173
                         90       100       110
                 ....*....|....*....|....*....|
gi 161333835 323 MLDDTMNVNIFESfkRADIYSVGLVYWEIA 352
Cdd:cd06617  174 RINPELNQKGYDV--KSDVWSLGITMIELA 201
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
149-352 2.24e-11

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: 63.98  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR---WCGEDVAVKI-------FSSRDERswFREAEIYQTVMLR-HENILGFIAAdNKDNGtwtQLW 217
Cdd:cd14052    6 ELIGSGEFSQVYKVServPTGKVYAVKKlkpnyagAKDRLRR--LEEVSILRELTLDgHDNIVQLIDS-WEYHG---HLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNiVTVAGM-----IKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIAD 291
Cdd:cd14052   80 IQTELCENGSLDVFLSEL-GLLGRLdefrvWKILVELSLGLRFIHdHHFV---------HLDLKPANVLITFEGTLKIGD 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 292 LGLAVkHDSILNTIDIPqnpkvGTKRYMAPEMLDDTMnvnifeSFKRADIYSVGLVYWEIA 352
Cdd:cd14052  150 FGMAT-VWPLIRGIERE-----GDREYIAPEILSEHM------YDKPADIFSLGLILLEAA 198
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
148-349 2.80e-11

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: 63.83  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGE-VWHGRWCGEDVAVK-------IFSSRdERSWFREAEiyqtvmlRHENILGFIAADNKDNGTWTQLWL- 218
Cdd:cd13982    6 PKVLGYGSEGTiVFRGTFDGRPVAVKrllpeffDFADR-EVQLLRESD-------EHPNVIRYFCTEKDRQFLYIALELc 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 ---VSEYHEQGSLYDYLNRNIVTvagMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILV-----KKCETCAI 289
Cdd:cd13982   78 aasLQDLVESPRESKLFLRPGLE---PVRLLRQIASGLAHLHsLNIV---------HRDLKPQNILIstpnaHGNVRAMI 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 290 ADLGLAVKHDSILNTIDIPQNPKvGTKRYMAPEMLDDTMNVNIfesfKRA-DIYSVGLVYW 349
Cdd:cd13982  146 SDFGLCKKLDVGRSSFSRRSGVA-GTSGWIAPEMLSGSTKRRQ----TRAvDIFSLGCVFY 201
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
150-351 3.07e-11

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: 63.93  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGR--WCGEDVAVKIFSSRDER-----SWFREAEIYQTvmLRHENILGF---IAADNKDNgtwtqLWLV 219
Cdd:cd07845   14 RIGEGTYGIVYRARdtTSGEIVALKKVRMDNERdgipiSSLREITLLLN--LRHPNIVELkevVVGKHLDS-----IFLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQ--GSLYDYLNRNIvTVAGMIKLALSIASGLAHLHMEIvgtqgkpaIAHRDIKSKNILVKKCETCAIADLGLAvk 297
Cdd:cd07845   87 MEYCEQdlASLLDNMPTPF-SESQVKCLMLQLLRGLQYLHENF--------IIHRDLKVSNLLLTDKGCLKIADFGLA-- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 298 hdSILNTIDIPQNPKVGTKRYMAPEML--DDTMNVNIfesfkraDIYSVGLVYWEI 351
Cdd:cd07845  156 --RTYGLPAKPMTPKVVTLWYRAPELLlgCTTYTTAI-------DMWAVGCILAEL 202
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
151-384 3.21e-11

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: 63.62  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW--HGRWCGEDVAVKIFSSRDERSwfREAEIYQTVMLR---HENIL----GFIAADnkdngtwtQLWLVSE 221
Cdd:cd06648   15 IGEGSTGIVCiaTDKSTGRQVAVKKMDLRKQQR--RELLFNEVVIMRdyqHPNIVemysSYLVGD--------ELWVVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKhdsi 301
Cdd:cd06648   85 FLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLH-----SQG---VIHRDIKSDSILLTSDGRVKLSDFGFCAQ---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 302 lNTIDIPQNPK-VGTKRYMAPEMLD----DTmnvnifesfkRADIYSVGLVYWEIarrcsVGGiveeyQLPYYDmvpsDP 376
Cdd:cd06648  153 -VSKEVPRRKSlVGTPYWMAPEVISrlpyGT----------EVDIWSLGIMVIEM-----VDG-----EPPYFN----EP 207

                 ....*...
gi 161333835 377 SIEEMRKV 384
Cdd:cd06648  208 PLQAMKRI 215
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
150-327 3.73e-11

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: 63.11  E-value: 3.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWH--GRWCGEDVAVKIFSSRD----ERSWFREAEIYQTVmlRHENILGFIaadnKDNGTWTQLWLVSEYH 223
Cdd:cd14095    7 VIGDGNFAVVKEcrDKATDKEYALKIIDKAKckgkEHMIENEVAILRRV--KHPNIVQLI----EEYDTDTELYLVMELV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNI----VTVAGMIKlalSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCE----TCAIADLGLA 295
Cdd:cd14095   81 KGGDLFDAITSSTkfteRDASRMVT---DLAQALKYLHSL--------SIVHRDIKPENLLVVEHEdgskSLKLADFGLA 149
                        170       180       190
                 ....*....|....*....|....*....|..
gi 161333835 296 VKHDSILNTIdipqnpkVGTKRYMAPEMLDDT 327
Cdd:cd14095  150 TEVKEPLFTV-------CGTPTYVAPEILAET 174
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
151-354 3.98e-11

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: 62.92  E-value: 3.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW---HGRWCgEDVAVKIFSSR-DERSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSEYHEQG 226
Cdd:cd14156    1 IGSGFFSKVYkvtHGATG-KVMVVKIYKNDvDQHKIVREISLLQK--LSHPNIVRYLGICVKDE----KLHPILEYVSGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 227 SLYDYLNRNIVTVAGMIKLALS--IASGLAHLHMEivgtqgkpAIAHRDIKSKNILVK---KCETCAIADLGLAVKhdsi 301
Cdd:cd14156   74 CLEELLAREELPLSWREKVELAcdISRGMVYLHSK--------NIYHRDLNSKNCLIRvtpRGREAVVTDFGLARE---- 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 302 lnTIDIPQNPK------VGTKRYMAPEMLDDtmnvnifESFKR-ADIYSVGLVYWEIARR 354
Cdd:cd14156  142 --VGEMPANDPerklslVGSAFWMAPEMLRG-------EPYDRkVDVFSFGIVLCEILAR 192
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
116-143 5.36e-11

Transforming growth factor beta type I GS-motif; This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor.


Pssm-ID: 462503  Cd Length: 28  Bit Score: 56.84  E-value: 5.36e-11
                          10        20
                  ....*....|....*....|....*...
gi 161333835  116 TLKDLIYDVTASGSGSGLPLLVQRTIAR 143
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
147-354 5.40e-11

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: 62.85  E-value: 5.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTV----MLRHENILGFIAADNKDngtwTQLWLVS 220
Cdd:cd06607    6 LREI-GHGSFGAVYYARnkRTSEVVAIKKMSYSGKQSTEKWQDIIKEVkflrQLRHPNTIEYKGCYLRE----HTAWLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHeQGSLYDYLNRNI-----VTVAGMIKLALSiasGLAHLHmeivgTQGKpaiAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd06607   81 EYC-LGSASDIVEVHKkplqeVEIAAICHGALQ---GLAYLH-----SHNR---IHRDVKAGNILLTEPGTVKLADFGSA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 296 VKHDsilntidiPQNPKVGTKRYMAPEMLdDTMNVNIFESfkRADIYSVGLVYWEIARR 354
Cdd:cd06607  149 SLVC--------PANSFVGTPYWMAPEVI-LAMDEGQYDG--KVDVWSLGITCIELAER 196
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
146-424 6.08e-11

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: 62.41  E-value: 6.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSRDERSWFREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd08530    3 KVLKKLGKGSYGSVYKVKRLsdNQVYALKEVNLGSLSQKEREDsvnEIRLLASVNHPNIIRYKEAFLDGN----RLCIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYL-----NRNIVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd08530   79 EYAPFGDLSKLIskrkkKRRLFPEDDIWRIFIQMLRGLKALHdQKIL---------HRDLKSANILLSAGDLVKIGDLGI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 295 A-VKHDSILNTidipqnpKVGTKRYMAPEMLDDTMnvnifESFKrADIYSVGLVYWEIARrcsvggiveeYQLPYydmvp 373
Cdd:cd08530  150 SkVLKKNLAKT-------QIGTPLYAAPEVWKGRP-----YDYK-SDIWSLGCLLYEMAT----------FRPPF----- 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 374 SDPSIEEMRKVVCDQKFrPSIPNQWQscealRVMGRIMRECWYANGAARLT 424
Cdd:cd08530  202 EARTMQELRYKVCRGKF-PPIPPVYS-----QDLQQIIRSLLQVNPKKRPS 246
GS smart00467
GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF ...
115-145 6.09e-11

GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF beta receptors. Mutation of two or more of the serines or threonines in the TTSGSGSG of TGF-beta type I receptor impairs phosphorylation and signaling activity.


Pssm-ID: 197743  Cd Length: 30  Bit Score: 56.79  E-value: 6.09e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 161333835   115 KTLKDLIYDVTaSGSGSGLPLLVQRTIARTI 145
Cdd:smart00467   1 KTLSDLLEDTT-SGSGSGLPLLVQRTVARQI 30
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
149-352 6.55e-11

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: 63.09  E-value: 6.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWH--GRWCGEDVAVKIFSSRDERSWFREAE--IYQTvMLRHENILGFIAADNK-DNGTWTQLWLVSEYH 223
Cdd:cd06639   28 ETIGKGTYGKVYKvtNKKDGSLAAVKILDPISDVDEEIEAEynILRS-LPNHPNVVKFYGMFYKaDQYVGGQLWLVLELC 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDY----LNRNIVTVAGMIKLALSIAS-GLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKh 298
Cdd:cd06639  107 NGGSVTELvkglLKCGQRLDEAMISYILYGALlGLQHLH--------NNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ- 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 dsiLNTIDIPQNPKVGTKRYMAPEMLDDTMNVNiFESFKRADIYSVGLVYWEIA 352
Cdd:cd06639  178 ---LTSARLRRNTSVGTPFWMAPEVIACEQQYD-YSYDARCDVWSLGITAIELA 227
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
149-294 7.83e-11

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: 62.36  E-value: 7.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGED-----VAVKIFssRDER--------SWFREAEIYQTvmLRHENI--LGFIAADNKdngtw 213
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTPSgkviqVAVKCL--KSDVlsqpnamdDFLKEVNAMHS--LDHPNLirLYGVVLSSP----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tqLWLVSEYHEQGSLYDYLNRN--IVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIAD 291
Cdd:cd05040   72 --LMMVTELAPLGSLLDRLRKDqgHFLISTLCDYAVQIANGMAYL-------ESKRFI-HRDLAARNILLASKDKVKIGD 141

                 ...
gi 161333835 292 LGL 294
Cdd:cd05040  142 FGL 144
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
151-352 7.99e-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: 62.33  E-value: 7.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG---------RWCgEDVAVKIfsSRDERSWFREaEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSE 221
Cdd:cd14033    9 IGRGSFKTVYRGldtettvevAWC-ELQTRKL--SKGERQRFSE-EVEMLKGLQHPNIVRFYDSWKSTVRGHKCIILVTE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHMEIvgtqgkPAIAHRDIKSKNILVK-KCETCAIADLGLA-VKH 298
Cdd:cd14033   85 LMTSGTLKTYLKRfREMKLKLLQRWSRQILKGLHFLHSRC------PPILHRDLKCDNIFITgPTGSVKIGDLGLAtLKR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 299 DSILNTIdipqnpkVGTKRYMAPEMLDdtmnvnifESFKRA-DIYSVGLVYWEIA 352
Cdd:cd14033  159 ASFAKSV-------IGTPEFMAPEMYE--------EKYDEAvDVYAFGMCILEMA 198
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
146-428 8.54e-11

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand 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 signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 62.68  E-value: 8.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFGEVWHGrwCGED---------VAVKIF----SSRDERSWFREAEIYQTVMLRHenILGFIAADNKDNGT 212
Cdd:cd05061   10 LLREL-GQGSFGMVYEG--NARDiikgeaetrVAVKTVnesaSLRERIEFLNEASVMKGFTCHH--VVRLLGVVSKGQPT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WtqlwLVSEYHEQGSLYDYL-----------NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILV 281
Cdd:cd05061   85 L----VVMELMAHGDLKSYLrslrpeaennpGRPPPTLQEMIQMAAEIADGMAYLNAK--------KFVHRDLAARNCMV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 282 KKCETCAIADLGLavkhdsilnTIDIPQNP--KVGTK-----RYMAPEMLDDtmnvNIFESFkrADIYSVGLVYWEIArr 354
Cdd:cd05061  153 AHDFTVKIGDFGM---------TRDIYETDyyRKGGKgllpvRWMAPESLKD----GVFTTS--SDMWSFGVVLWEIT-- 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 355 csvgGIVEEyqlPYYDMvpsdpSIEEMRKVVCDQKFRpsipNQWQSCEalRVMGRIMRECWYANGAARLTALRI 428
Cdd:cd05061  216 ----SLAEQ---PYQGL-----SNEQVLKFVMDGGYL----DQPDNCP--ERVTDLMRMCWQFNPKMRPTFLEI 271
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
148-349 8.83e-11

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: 62.35  E-value: 8.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVwhgRWC-----GEDVAVKIFSSRDERSW---FREAE-IYQTvmLRHENILGFIAADNKDNgtwtQLWL 218
Cdd:cd14173    7 EEVLGEGAYARV---QTCinlitNKEYAVKIIEKRPGHSRsrvFREVEmLYQC--QGHRNVLELIEFFEEED----KFYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNR----NIVTVAGMIKlalSIASGLAHLHmeivgtqgKPAIAHRDIKSKNIL---------VKKCE 285
Cdd:cd14173   78 VFEKMRGGSILSHIHRrrhfNELEASVVVQ---DIASALDFLH--------NKGIAHRDLKPENILcehpnqvspVKICD 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 286 TcaiaDLGLAVKHDSILNTIDIPQ--NPkVGTKRYMAPEMLDD-TMNVNIFEsfKRADIYSVGLVYW 349
Cdd:cd14173  147 F----DLGSGIKLNSDCSPISTPEllTP-CGSAEYMAPEVVEAfNEEASIYD--KRCDLWSLGVILY 206
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
147-355 9.57e-11

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: 62.93  E-value: 9.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVK----IFSSR-DERSWFREAEIYQtvMLRHENILG----FIAADNKDNGTwtq 215
Cdd:cd07834    4 LLKPIGSGAYGVVCSAYdkRTGRKVAIKkisnVFDDLiDAKRILREIKILR--HLKHENIIGlldiLRPPSPEEFND--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQgSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd07834   79 VYIVTELMET-DLHKVIKSPQPLTDDHIQYFLyQILRGLKYLH--------SAGVIHRDLKPSNILVNSNCDLKICDFGL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 295 AvkhdsilNTIDIPQNPK-----VGTKRYMAPE-MLDdtmnvniFESFKRA-DIYSVGLVYWEIARRC 355
Cdd:cd07834  150 A-------RGVDPDEDKGflteyVVTRWYRAPElLLS-------SKKYTKAiDIWSVGCIFAELLTRK 203
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
151-384 1.18e-10

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: 62.20  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW--CGEDVAVK-I----FSSRDE---RSWFREAEIYQTvmLRHENILGFIAA-DNKDNgtwtqLWLV 219
Cdd:cd07841    8 LGEGTYAVVYKARDkeTGRIVAIKkIklgeRKEAKDginFTALREIKLLQE--LKHPNIIGLLDVfGHKSN-----INLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEqgslYDyL-----NRNIVTVAGMIK-LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd07841   81 FEFME----TD-LekvikDKSIVLTPADIKsYMLMTLRGLEYLH--------SNWILHRDLKPNNLLIASDGVLKLADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 294 LAVKHDSilntidiPQN---PKVGTKRYMAPEMLddtmnvnifesFKrADIYSVGLVYWeiarrcSVGGIVEEYQL--PY 368
Cdd:cd07841  148 LARSFGS-------PNRkmtHQVVTRWYRAPELL-----------FG-ARHYGVGVDMW------SVGCIFAELLLrvPF 202
                        250
                 ....*....|....*.
gi 161333835 369 YdmvPSDPSIEEMRKV 384
Cdd:cd07841  203 L---PGDSDIDQLGKI 215
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
145-347 1.38e-10

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: 61.73  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIvGKGRFGEV---WH----GRWCGEDVAVKIFSSRDERSWFREAEIYQTV----MLRHENILGFIAADNKDNgtw 213
Cdd:cd14076    4 ILGRTL-GEGEFGKVklgWPlpkaNHRSGVQVAIKLIRRDTQQENCQTSKIMREInilkGLTHPNIVRLLDVLKTKK--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tQLWLVSEYHEQGSLYDY-LNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd14076   80 -YIGIVLEFVSGGELFDYiLARRRLKDSVACRLFAQLISGVAYLH--------KKGVVHRDLKLENLLLDKNRNLVITDF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAvkhdsilNTIDIPQN----PKVGTKRYMAPEMLD-DTMNVNifesfKRADIYSVGLV 347
Cdd:cd14076  151 GFA-------NTFDHFNGdlmsTSCGSPCYAAPELVVsDSMYAG-----RKADIWSCGVI 198
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
151-347 1.58e-10

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: 61.43  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWC----GEDVAVKIF----SSRDERSWF--REAEIYqtVMLRHENI---LGFIAADNKdngtwtqLW 217
Cdd:cd14080    8 IGEGSYSKVKLAEYTksglKEKVACKIIdkkkAPKDFLEKFlpRELEIL--RKLRHPNIiqvYSIFERGSK-------VF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNivtvaGMIKLALS------IASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIAD 291
Cdd:cd14080   79 IFMEYAEHGDLLEYIQKR-----GALSESQAriwfrqLALAVQYLH-----SLD---IAHRDLKCENILLDSNNNVKLSD 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 292 LGLAVKHDSilNTIDIPQNPKVGTKRYMAPEMLDDTMnvnifESFKRADIYSVGLV 347
Cdd:cd14080  146 FGFARLCPD--DDGDVLSKTFCGSAAYAAPEILQGIP-----YDPKKYDIWSLGVI 194
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
149-351 1.60e-10

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: 61.81  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGED--VAVK-IFSSRDERSwfREA---EIYQTVMLRHENILG-FIAADNKDNGTWTQ------ 215
Cdd:cd14048   12 QCLGRGGFGVVFEAKNKVDDcnYAVKrIRLPNNELA--REKvlrEVRALAKLDHPGIVRyFNAWLERPPEGWQEkmdevy 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNiVTVAG-----MIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIA 290
Cdd:cd14048   90 LYIQMQLCRKENLKDWMNRR-CTMESrelfvCLNIFKQIASAVEYLH--------SKGLIHRDLKPSNVFFSLDDVVKVG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 291 DLGLAVKHDSILNTIDIPQNP--------KVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWEI 351
Cdd:cd14048  161 DFGLVTAMDQGEPEQTVLTPMpayakhtgQVGTRLYMSPEQIHGN------QYSEKVDIFALGLILFEL 223
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
150-324 1.85e-10

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: 61.62  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWF-----REAEIYQtvMLRHENILGFI----AADNKDNGTWTQLWL 218
Cdd:cd07865   19 KIGQGTFGEVFKARhrKTGQIVALKKVLMENEKEGFpitalREIKILQ--LLKHENVVNLIeicrTKATPYNRYKGSIYL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEY--HEQGSLYDYLNR--NIVTVAGMIKLALSiasGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd07865   97 VFEFceHDLAGLLSNKNVkfTLSEIKKVMKMLLN---GLYYIHRN--------KILHRDMKAANILITKDGVLKLADFGL 165
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 161333835 295 AvkhdsilNTIDIPQNPK-------VGTKRYMAPEML 324
Cdd:cd07865  166 A-------RAFSLAKNSQpnrytnrVVTLWYRPPELL 195
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
151-352 2.25e-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: 60.91  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW---HGRWCGEDVAVKI----FSSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNGtwtQLWLVSEYH 223
Cdd:cd08223    8 IGKGSYGEVWlvrHKRDRKQYVIKKLnlknASKRERKAAEQEAKLLSK--LKHPNIVSYKESFEGEDG---FLYIVMGFC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYL-NRNIVTV--AGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAvkhdS 300
Cdd:cd08223   83 EGGDLYTRLkEQKGVLLeeRQVVEWFVQIAMALQYMHER--------NILHRDLKTQNIFLTKSNIIKVGDLGIA----R 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 301 ILNTIDIPQNPKVGTKRYMAPEMLDDT-MNvnifesfKRADIYSVGLVYWEIA 352
Cdd:cd08223  151 VLESSSDMATTLIGTPYYMSPELFSNKpYN-------HKSDVWALGCCVYEMA 196
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
149-400 2.31e-10

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: 61.30  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGK---GRFGEVW--HGRWCGEDVAVKI--FSSRDERSWFR-EAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd06611    8 EIIGElgdGAFGKVYkaQHKETGLFAAAKIiqIESEEELEDFMvEIDILSEC--KHPNIVGLYEAYFYEN----KLWILI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDylnrnivtvagmikLALSIASGLAHLHMEIVGTQGKPA--------IAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd06611   82 EFCDGGALDS--------------IMLELERGLTEPQIRYVCRQMLEAlnflhshkVIHRDLKAGNILLTLDGDVKLADF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAVKHDSILNTIDipqnPKVGTKRYMAPE-MLDDTMNVNIFESfkRADIYSVGLVYWEIARRcsvggiveeyQLPYYDM 371
Cdd:cd06611  148 GVSAKNKSTLQKRD----TFIGTPYWMAPEvVACETFKDNPYDY--KADIWSLGITLIELAQM----------EPPHHEL 211
                        250       260       270
                 ....*....|....*....|....*....|..
gi 161333835 372 VPsdpsieeMRKVVCDQKFRP---SIPNQWQS 400
Cdd:cd06611  212 NP-------MRVLLKILKSEPptlDQPSKWSS 236
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
148-351 2.88e-10

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: 60.70  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEV---WHGRWCgEDVAVKIFS-------SRDERSWFREAEIYQTVMLR----HENILGFiaadnKDN-GT 212
Cdd:cd14182    8 KEILGRGVSSVVrrcIHKPTR-QEYAVKIIDitgggsfSPEEVQELREATLKEIDILRkvsgHPNIIQL-----KDTyET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WTQLWLVSEYHEQGSLYDYLNRNIVtvagmikLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd14182   82 NTFFFLVFDLMKKGELFDYLTEKVT-------LSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDF 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 293 GLAVKhdsilntidIPQNPKV----GTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd14182  155 GFSCQ---------LDPGEKLrevcGTPGYLAPEIIECSMDDNHPGYGKEVDMWSTGVIMYTL 208
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
166-384 3.45e-10

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: 60.82  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 166 GEDVAVKIFSSRDERSwfREAEIYQTVMLR---HENIL----GFIAADnkdngtwtQLWLVSEYHEQGSLYDYLNRNIVT 238
Cdd:cd06658   47 GKQVAVKKMDLRKQQR--RELLFNEVVIMRdyhHENVVdmynSYLVGD--------ELWVVMEFLEGGALTDIVTHTRMN 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 239 VAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilntiDIPQNPK-VGTKR 317
Cdd:cd06658  117 EEQIATVCLSVLRALSYLH-----NQG---VIHRDIKSDSILLTSDGRIKLSDFGFCAQVSK-----EVPKRKSlVGTPY 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 318 YMAPEMlddtmnVNIFESFKRADIYSVGLVYWEIArrcsvggiveEYQLPYYDmvpsDPSIEEMRKV 384
Cdd:cd06658  184 WMAPEV------ISRLPYGTEVDIWSLGIMVIEMI----------DGEPPYFN----EPPLQAMRRI 230
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
162-435 3.50e-10

Pseudokinase domain of the unknown subfamily 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: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 60.64  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 162 GRWCGEDVAVKIFSSRD-ERSWFREAEIYQTVMLRHENILGFIAADNKdngtWTQLWLVSEYHEQGSLYD-YLNRNIVTV 239
Cdd:cd14045   26 GIYDGRTVAIKKIAKKSfTLSKRIRKEVKQVRELDHPNLCKFIGGCIE----VPNVAIITEYCPKGSLNDvLLNEDIPLN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 240 AGM-IKLALSIASGLAHLHmeivgtQGKpaIAHRDIKSKNILVKKCETCAIADLGLAV--KHDSILNTIDIPQNPKvgtK 316
Cdd:cd14045  102 WGFrFSFATDIARGMAYLH------QHK--IYHGRLKSSNCVIDDRWVCKIADYGLTTyrKEDGSENASGYQQRLM---Q 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 317 RYMAPEMlddtMNVNIFESFKRADIYSVGLVYWEIARRCsvggiveeyqlpyyDMVPSD-PSIEEmrkvvcdqKFRPSIP 395
Cdd:cd14045  171 VYLPPEN----HSNTDTEPTQATDVYSYAIILLEIATRN--------------DPVPEDdYSLDE--------AWCPPLP 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 396 -----NQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14045  225 elisgKTENSCPCPADYVELIRRCRKNNPAQRPTFEQIKKTLHKI 269
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
147-351 3.84e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily 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).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 60.35  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGR----WCGEDVAVKIF----SSRDERSWFREAEIYQTvmLRHENILGFIaadnkdnGTWTQ--- 215
Cdd:cd14206    2 LQEI-GNGWFGKVILGEifsdYTPAQVVVKELrvsaGPLEQRKFISEAQPYRS--LQHPNILQCL-------GLCTEtip 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLN--------------RNIVTVAGMiklALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV 281
Cdd:cd14206   72 FLLIMEFCQLGDLKRYLRaqrkadgmtpdlptRDLRTLQRM---AYEITLGLLHLH--------KNNYIHSDLALRNCLL 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 282 KKCETCAIADLGLA---VKHDSIL--NTIDIPQnpkvgtkRYMAPEMLDDTM-NVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd14206  141 TSDLTVRIGDYGLShnnYKEDYYLtpDRLWIPL-------RWVAPELLDELHgNLIVVDQSKESNVWSLGVTIWEL 209
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
141-430 4.17e-10

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: 60.10  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 141 IARTIvlqeivGKGRFGEVWHGRWC--GEDVAVKIF--SSRDE---RSWFREAEIYQtvMLRHENILGFIAADNkdngTW 213
Cdd:cd14071    4 IERTI------GKGNFAVVKLARHRitKTEVAIKIIdkSQLDEenlKKIYREVQIMK--MLNHPHIIKLYQVME----TK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 TQLWLVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd14071   72 DMLYLVTEYASNGEIFDYLAQHgRMSEKEARKKFWQILSAVEYCH--------KRHIVHRDLKAENLLLDANMNIKIADF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLA--VKHDSILNTIdipqnpkVGTKRYMAPEmlddtmnvnIFESFK----RADIYSVGLVYWEIArrCSVggiveeyqL 366
Cdd:cd14071  144 GFSnfFKPGELLKTW-------CGSPPYAAPE---------VFEGKEyegpQLDIWSLGVVLYVLV--CGA--------L 197
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 367 PYydmvpSDPSIEEMRKVVCDQKFRpsIPnQWQS--CEALrvmgriMRECWYANGAARLTALRIKK 430
Cdd:cd14071  198 PF-----DGSTLQTLRDRVLSGRFR--IP-FFMStdCEHL------IRRMLVLDPSKRLTIEQIKK 249
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
170-347 4.22e-10

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: 60.39  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 170 AVKIFSSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNGTWTQ-LWLVSEYHEQGSLYDYLNRNIVTVAGM-----I 243
Cdd:cd13986   32 KILCHSKEDVKEAMREIENYR--LFNHPNILRLLDSQIVKEAGGKKeVYLLLPYYKRGSLQDEIERRLVKGTFFpedriL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 244 KLALSIASGLAHLHmeivgTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIPQNPKV-----GTKRY 318
Cdd:cd13986  110 HIFLGICRGLKAMH-----EPELVPYAHRDIKPGNVLLSEDDEPILMDLGSMNPARIEIEGRREALALQDwaaehCTMPY 184
                        170       180
                 ....*....|....*....|....*....
gi 161333835 319 MAPEMLDDTMNVNIFEsfkRADIYSVGLV 347
Cdd:cd13986  185 RAPELFDVKSHCTIDE---KTDIWSLGCT 210
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
216-348 4.49e-10

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: 59.84  E-value: 4.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd05123   68 LYLVLDYVPGGELFSHLSKEGRFPEERARFyAAEIVLALEYLH-----SLG---IIYRDLKPENILLDSDGHIKLTDFGL 139
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 295 AVKHDSILNTIDIPqnpkVGTKRYMAPEML---DDTMNVnifesfkraDIYSVG-LVY 348
Cdd:cd05123  140 AKELSSDGDRTYTF----CGTPEYLAPEVLlgkGYGKAV---------DWWSLGvLLY 184
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
149-415 4.76e-10

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: 60.05  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGE----DVAVKIF----SSRDERSWFREAEIYqTVMLRHENILGFIAA-DNKDngtwtQLWLV 219
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDglrmDAAIKRMkeyaSKDDHRDFAGELEVL-CKLGHHPNIINLLGAcEHRG-----YLYLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRNIV-----------------TVAGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDIKSKNILVK 282
Cdd:cd05047   75 IEYAPHGNLLDFLRKSRVletdpafaianstastlSSQQLLHFAADVARGMDYL--------SQKQFIHRDLAARNILVG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 283 KCETCAIADLGLAvKHDSILNTIDIPQNPkvgtKRYMAPEmlddTMNVNIFESfkRADIYSVGLVYWEIArrcSVGGIve 362
Cdd:cd05047  147 ENYVAKIADFGLS-RGQEVYVKKTMGRLP----VRWMAIE----SLNYSVYTT--NSDVWSYGVLLWEIV---SLGGT-- 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 363 eyqlPYYDMVPSdpsiEEMRKVvcDQKFRPSIPnqwQSCEalRVMGRIMRECW 415
Cdd:cd05047  211 ----PYCGMTCA----ELYEKL--PQGYRLEKP---LNCD--DEVYDLMRQCW 248
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
149-354 5.04e-10

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: 59.76  E-value: 5.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWC-GEDVAVK--IFSSRD----ERSWFR---EAEIYQTvmLRHENILGFIAADNKDNgtwtqlwL 218
Cdd:cd06631    7 NVLGKGAYGTVYCGLTStGQLIAVKqvELDTSDkekaEKEYEKlqeEVDLLKT--LKHVNIVGYLGTCLEDN-------V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VS---EYHEQGSLYDYLNRNIVTVAGM-IKLALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNIL------VKKCE-TC 287
Cdd:cd06631   78 VSifmEFVPGGSIASILARFGALEEPVfCRYTKQILEGVAYLHNNNV--------IHRDIKGNNIMlmpngvIKLIDfGC 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 288 A--IADLGLAVKHDSILNTIDipqnpkvGTKRYMAPEMLDDTMNvnifesFKRADIYSVGLVYWEIARR 354
Cdd:cd06631  150 AkrLCINLSSGSQSQLLKSMR-------GTPYWMAPEVINETGH------GRKSDIWSIGCTVFEMATG 205
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
152-345 5.29e-10

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: 59.87  E-value: 5.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGR--WCGEDVAVKIFSSR---DERSW---FREAEIYQTvmLRHENILGFIAA-DNKDNgtwtqLWLVSEY 222
Cdd:cd14099   10 GKGGFAKCYEVTdmSTGKVYAGKVVPKSsltKPKQReklKSEIKIHRS--LKHPNIVKFHDCfEDEEN-----VYILLEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsi 301
Cdd:cd14099   83 CSNGSLMELLkRRKALTEPEVRYFMRQILSGVKYLH--------SNRIIHRDLKLGNLFLDENMNVKIGDFGLAAR---- 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 161333835 302 lntIDIPQNPKV---GTKRYMAPEMLDDTMNvnifESFKrADIYSVG 345
Cdd:cd14099  151 ---LEYDGERKKtlcGTPNYIAPEVLEKKKG----HSFE-VDIWSLG 189
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
146-352 5.32e-10

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: 60.00  E-value: 5.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGRWCG--EDVAVKifSSrdERSwfREAEIYQTVM----LRHENILGFIAadnkdngtW--TQ-- 215
Cdd:cd14010    3 VLYDEIGRGKHSVVYKGRRKGtiEFVAIK--CV--DKS--KRPEVLNEVRltheLKHPNVLKFYE--------WyeTSnh 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd14010   69 LWLVVEYCTGGDLETLLRQDGnLPESSVRKFGRDLVRGLHYIH--------SKGIIYCDLKPSNILLDGNGTLKLSDFGL 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 295 AVKHDSILNTIDIP------------QNPKVGTKRYMAPEMLddTMNVNIFESfkraDIYSVGLVYWEIA 352
Cdd:cd14010  141 ARREGEILKELFGQfsdegnvnkvskKQAKRGTPYYMAPELF--QGGVHSFAS----DLWALGCVLYEMF 204
pknD PRK13184
serine/threonine-protein kinase PknD;
150-351 5.35e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 61.71  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW--HGRWCGEDVAVK------IFSSRDERSWFREAEIyqTVMLRHENILG-FIAADNKD----------- 209
Cdd:PRK13184   9 LIGKGGMGEVYlaYDPVCSRRVALKkiredlSENPLLKKRFLREAKI--AADLIHPGIVPvYSICSDGDpvyytmpyieg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 210 -------NGTWTQLWLVSEYHEQGSlydylnrnivtVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVK 282
Cdd:PRK13184  87 ytlksllKSVWQKESLSKELAEKTS-----------VGAFLSIFHKICATIEYVH-----SKG---VLHRDLKPDNILLG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 283 KCETCAIADLGLAV---KHDSILNTIDIPQNPK-----------VGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVY 348
Cdd:PRK13184 148 LFGEVVILDWGAAIfkkLEEEDLLDIDVDERNIcyssmtipgkiVGTPDYMAPERLLGV------PASESTDIYALGVIL 221

                 ...
gi 161333835 349 WEI 351
Cdd:PRK13184 222 YQM 224
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
147-351 6.10e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 59.62  E-value: 6.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGR----WCGEDVAVKIFSS----RDERSWFREAEIYQTvmLRHENILGFIAadnkDNGTWTQLWL 218
Cdd:cd05087    2 LKEI-GHGWFGKVFLGEvnsgLSSTQVVVKELKAsasvQDQMQFLEEAQPYRA--LQHTNLLQCLA----QCAEVTPYLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLnRNIVTVAGMI-------KLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIAD 291
Cdd:cd05087   75 VMEFCPLGDLKGYL-RSCRAAESMApdpltlqRMACEVACGLLHLH--------RNNFVHSDLALRNCLLTADLTVKIGD 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 292 LGLA-VKH-DSILNTIDIPQNPkvgtKRYMAPEMLDDTM-NVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd05087  146 YGLShCKYkEDYFVTADQLWVP----LRWIAPELVDEVHgNLLVVDQTKQSNVWSLGVTIWEL 204
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
152-384 7.30e-10

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: 59.77  E-value: 7.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEV--WHGRWCGEDVAVKI------FSSRDERSWFREAEIYQTvmLRHENILGFI-AADNKDNGTWTQLWLVS-E 221
Cdd:cd13989    2 GSGGFGYVtlWKHQDTGEYVAIKKcrqelsPSDKNRERWCLEVQIMKK--LNHPNVVSARdVPPELEKLSPNDLPLLAmE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRnIVTVAGMIKLAL-----SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCE---TCAIADLG 293
Cdd:cd13989   80 YCSGGDLRKVLNQ-PENCCGLKESEVrtllsDISSAISYLH--------ENRIIHRDLKPENIVLQQGGgrvIYKLIDLG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 294 LAVKHD-SILNTidipqnPKVGTKRYMAPEmlddtmnvnIFESFKradiYSVGLVYWeiarrcSVGGIVEEYQLPYYDMV 372
Cdd:cd13989  151 YAKELDqGSLCT------SFVGTLQYLAPE---------LFESKK----YTCTVDYW------SFGTLAFECITGYRPFL 205
                        250
                 ....*....|..
gi 161333835 373 PSDPSIEEMRKV 384
Cdd:cd13989  206 PNWQPVQWHGKV 217
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
144-351 8.05e-10

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: 59.65  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGRWCG-------EDVAVKIFSSRDERSwFREAEIYQTVM---LRHENILGFIAADNKDNgtw 213
Cdd:cd05091    7 AVRFMEELGEDRFGKVYKGHLFGtapgeqtQAVAIKTLKDKAEGP-LREEFRHEAMLrsrLQHPNIVCLLGVVTKEQ--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tQLWLVSEYHEQGSLYDYL--------------NRNIVTV---AGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDIKS 276
Cdd:cd05091   83 -PMSMIFSYCSHGDLHEFLvmrsphsdvgstddDKTVKSTlepADFLHIVTQIAAGMEYLSSHHV--------VHKDLAT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 277 KNILVKKCETCAIADLGL-----AVKHDSILNTIDIPqnpkvgtKRYMAPEMLddtmnvnIFESFK-RADIYSVGLVYWE 350
Cdd:cd05091  154 RNVLVFDKLNVKISDLGLfrevyAADYYKLMGNSLLP-------IRWMSPEAI-------MYGKFSiDSDIWSYGVVLWE 219

                 .
gi 161333835 351 I 351
Cdd:cd05091  220 V 220
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
147-422 1.10e-09

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 59.01  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEI--VGKGRFGEVWHGRWCGED-------VAVKIFSSRDER---SWF-REAEIYQTvmLRHENI---LGFIAADNKDn 210
Cdd:cd05046    7 LQEIttLGRGEFGEVFLAKAKGIEeeggetlVLVKALQKTKDEnlqSEFrRELDMFRK--LSHKNVvrlLGLCREAEPH- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 211 gtwtqlWLVSEYHEQGSLYDYLNRNI----------VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNIL 280
Cdd:cd05046   84 ------YMILEYTDLGDLKQFLRATKskdeklkpppLSTKQKVALCTQIALGMDHLS--------NARFVHRDLAARNCL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 281 VKKCETCAIADLGLA--------VKHDSILntidIPQnpkvgtkRYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEia 352
Cdd:cd05046  150 VSSQREVKVSLLSLSkdvynseyYKLRNAL----IPL-------RWLAPEAVQE----DDFST--KSDVWSFGVLMWE-- 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 353 rrcsvggIVEEYQLPYYDMvpsdpSIEEMRKVVCDQKFRPSIPnqwQSC-EALRvmgRIMRECWYANGAAR 422
Cdd:cd05046  211 -------VFTQGELPFYGL-----SDEEVLNRLQAGKLELPVP---EGCpSRLY---KLMTRCWAVNPKDR 263
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
147-319 1.47e-09

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 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: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 58.62  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSRDERS-WFREAEIYQTVMlrheNILGF-----IAADNKDNgtwtqlWL 218
Cdd:cd14016    4 LVKKIGSGSFGEVYLGIDLktGEEVAIKIEKKDSKHPqLEYEAKVYKLLQ----GGPGIprlywFGQEGDYN------VM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHeqG-SLYDYLNR-----NIVTVagmIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILV---KKCETCA 288
Cdd:cd14016   74 VMDLL--GpSLEDLFNKcgrkfSLKTV---LMLADQMISRLEYLHsKGYI---------HRDIKPENFLMglgKNSNKVY 139
                        170       180       190
                 ....*....|....*....|....*....|....
gi 161333835 289 IADLGLAVKHDSILNTIDIPQNPK---VGTKRYM 319
Cdd:cd14016  140 LIDFGLAKKYRDPRTGKHIPYREGkslTGTARYA 173
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
151-350 1.50e-09

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: 58.84  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW----CGEDVAVKIF-SSRDERSWFREAEIYQTVMLR---HENILG----FIAADNKdngtwtQLWL 218
Cdd:cd07842    8 IGRGTYGRVYKAKRkngkDGKEYAIKKFkGDKEQYTGISQSACREIALLRelkHENVVSlvevFLEHADK------SVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEqgslYDYL--------NRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV----KKCE 285
Cdd:cd07842   82 LFDYAE----HDLWqiikfhrqAKRVSIPPSMVKSLLwQILNGIHYLH--------SNWVLHRDLKPANILVmgegPERG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 286 TCAIADLGLAVKHDSILNTIdIPQNPKVGTKRYMAPEML----DDTmnvnifesfKRADIYSVGLVYWE 350
Cdd:cd07842  150 VVKIGDLGLARLFNAPLKPL-ADLDPVVVTIWYRAPELLlgarHYT---------KAIDIWAIGCIFAE 208
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
148-397 1.76e-09

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: 58.48  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVWHGRWCGE---DVAVKIFSSRD--ERSWFREAEIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSEY 222
Cdd:cd14202    7 KDLIGHGAFAVVFKGRHKEKhdlEVAVKCINKKNlaKSQTLLGKEIKILKELKHENIVALYDFQEIAN----SVYLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIVTVAGMIKLALSIASGLahlhMEIVGTQGkpaIAHRDIKSKNILVkKCET----------CAIADL 292
Cdd:cd14202   83 CNGGDLADYLHTMRTLSEDTIRLFLQQIAGA----MKMLHSKG---IIHRDLKPQNILL-SYSGgrksnpnnirIKIADF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLA--VKHDSILNTIdipqnpkVGTKRYMAPEMLddtMNVNiFESfkRADIYSVGLVYWEiarrCSVGgiveeyQLPYYD 370
Cdd:cd14202  155 GFAryLQNNMMAATL-------CGSPMYMAPEVI---MSQH-YDA--KADLWSIGTIIYQ----CLTG------KAPFQA 211
                        250       260
                 ....*....|....*....|....*..
gi 161333835 371 MVPSDPSIEEMRkvvcDQKFRPSIPNQ 397
Cdd:cd14202  212 SSPQDLRLFYEK----NKSLSPNIPRE 234
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
143-351 1.81e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 58.44  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVW----HGRWCGED---VAVKIFSSRDERS---WFREAEIYqtVMLRHENILGFIaadnkdnGT 212
Cdd:cd05092    5 RDIVLKWELGEGAFGKVFlaecHNLLPEQDkmlVAVKALKEATESArqdFQREAELL--TVLQHQHIVRFY-------GV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WTQ---LWLVSEYHEQGSLYDYLNRN----------------IVTVAGMIKLALSIASG---LAHLHMeivgtqgkpaiA 270
Cdd:cd05092   76 CTEgepLIMVFEYMRHGDLNRFLRSHgpdakildggegqapgQLTLGQMLQIASQIASGmvyLASLHF-----------V 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 271 HRDIKSKNILVKKCETCAIADLGLAvkhDSILNTidipQNPKVGTK-----RYMAPEMLddtmnvnIFESFK-RADIYSV 344
Cdd:cd05092  145 HRDLATRNCLVGQGLVVKIGDFGMS---RDIYST----DYYRVGGRtmlpiRWMPPESI-------LYRKFTtESDIWSF 210

                 ....*..
gi 161333835 345 GLVYWEI 351
Cdd:cd05092  211 GVVLWEI 217
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
150-347 1.84e-09

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: 58.33  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHG-------RWcgedvAVKIFSSRDERSWF-----REAEIYQTVmlRHENILGFiaadNKDNGTWTQLW 217
Cdd:cd14097    8 KLGQGSFGVVIEAthketqtKW-----AIKKINREKAGSSAvklleREVDILKHV--NHAHIIHL----EEVFETPKRMY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNIVTVAGMIK-LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCE-------TCAI 289
Cdd:cd14097   77 LVMELCEDGELKELLLRKGFFSENETRhIIQSLASAVAYLH--------KNDIVHRDLKLENILVKSSIidnndklNIKV 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 290 ADLGLAVKHDSIlnTIDIPQNpKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLV 347
Cdd:cd14097  149 TDFGLSVQKYGL--GEDMLQE-TCGTPIYMAPEVISAH------GYSQQCDIWSIGVI 197
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
151-352 1.92e-09

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: 58.52  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG---------RWCG-EDVAVkifsSRDERSWFREaEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVS 220
Cdd:cd14030   33 IGRGSFKTVYKGldtettvevAWCElQDRKL----SKSERQRFKE-EAGMLKGLQHPNIVRFYDSWESTVKGKKCIVLVT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHMEivgtqgKPAIAHRDIKSKNILVK-KCETCAIADLGLA-VK 297
Cdd:cd14030  108 ELMTSGTLKTYLKRfKVMKIKVLRSWCRQILKGLQFLHTR------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLAtLK 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 298 HDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNIfesfkraDIYSVGLVYWEIA 352
Cdd:cd14030  182 RASFAKSV-------IGTPEFMAPEMYEEKYDESV-------DVYAFGMCMLEMA 222
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
141-349 2.10e-09

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: 58.47  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 141 IARTIVLQEIVGKGRFGEVW--HGRWCGEDVAVK-IFSSRDERSWFREAEIYQTVMLRHENILGFiaADNKDNGTwtQLW 217
Cdd:cd14166    1 IRETFIFMEVLGSGAFSEVYlvKQRSTGKLYALKcIKKSPLSRDSSLENEIAVLKRIKHENIVTL--EDIYESTT--HYY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYD-YLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCA---IADLG 293
Cdd:cd14166   77 LVMQLVSGGELFDrILERGVYTEKDASRVINQVLSAVKYLH--------ENGIVHRDLKPENLLYLTPDENSkimITDFG 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 294 LA-VKHDSILNTidipqnpKVGTKRYMAPEMLDDtmnvnifESFKRA-DIYSVGLVYW 349
Cdd:cd14166  149 LSkMEQNGIMST-------ACGTPGYVAPEVLAQ-------KPYSKAvDCWSIGVITY 192
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
147-354 2.15e-09

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: 58.52  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTVM----LRHENILGFIAADNKDNGTWtqlwLVS 220
Cdd:cd06635   30 LREI-GHGSFGAVYFARdvRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKflqrIKHPNSIEYKGCYLREHTAW----LVM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHeQGSLYDYLNRNI-----VTVAGMIKLALSiasGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd06635  105 EYC-LGSASDLLEVHKkplqeIEIAAITHGALQ---GLAYLHSH--------NMIHRDIKAGNILLTEPGQVKLADFGSA 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 296 vkhdsilnTIDIPQNPKVGTKRYMAPEMLdDTMNVNIFESfkRADIYSVGLVYWEIARR 354
Cdd:cd06635  173 --------SIASPANSFVGTPYWMAPEVI-LAMDEGQYDG--KVDVWSLGITCIELAER 220
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
149-348 2.23e-09

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: 58.00  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFSSR------DERSWFREAEIYQtvMLRHENI--LGFIAADNkdngtwTQLWL 218
Cdd:cd05581    7 KPLGEGSYSTVVLAKekETGKEYAIKVLDKRhiikekKVKYVTIEKEVLS--RLAHPGIvkLYYTFQDE------SKLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHmeivgTQGkpaIAHRDIKSKNILV-KKCETCaIADLGLAV 296
Cdd:cd05581   79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAeIVLALEYLH-----SKG---IIHRDLKPENILLdEDMHIK-ITDFGTAK 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 297 ----KHDSILNTIDIPQNPK---------VGTKRYMAPEMLDDtmnvNIFEsfKRADIYSVG-LVY 348
Cdd:cd05581  150 vlgpDSSPESTKGDADSQIAynqaraasfVGTAEYVSPELLNE----KPAG--KSSDLWALGcIIY 209
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
148-397 2.50e-09

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: 58.10  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVWHGR------WcgeDVAVKIFSSRD--ERSWFREAEIYQTVMLRHENILGFIAADNKDNgtwtQLWLV 219
Cdd:cd14201   11 KDLVGHGAFAVVFKGRhrkktdW---EVAIKSINKKNlsKSQILLGKEIKILKELQHENIVALYDVQEMPN----SVFLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHMEivgtqgkpAIAHRDIKSKNILV-----KKCETCA----I 289
Cdd:cd14201   84 MEYCNGGDLADYLQAKGTLSEDTIRVFLqQIAAAMRILHSK--------GIIHRDLKPQNILLsyasrKKSSVSGirikI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 290 ADLGLAVKHDSILNTIDIpqnpkVGTKRYMAPEMLddtMNVNiFESfkRADIYSVGLVYWEiarrCSVGgiveeyQLPYY 369
Cdd:cd14201  156 ADFGFARYLQSNMMAATL-----CGSPMYMAPEVI---MSQH-YDA--KADLWSIGTVIYQ----CLVG------KPPFQ 214
                        250       260
                 ....*....|....*....|....*...
gi 161333835 370 DMVPSDPSIEEMRkvvcDQKFRPSIPNQ 397
Cdd:cd14201  215 ANSPQDLRMFYEK----NKNLQPSIPRE 238
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
154-354 2.51e-09

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: 58.00  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 154 GRFGEVWHGR--WCGEDVAVKIFSSRDERSWF-----REAEIYqtVMLRHENILG---FIAADNKDngtwtQLWLVSEY- 222
Cdd:cd07843   16 GTYGVVYRARdkKTGEIVALKKLKMEKEKEGFpitslREINIL--LKLQHPNIVTvkeVVVGSNLD-----KIYMVMEYv 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 -HEQGSLYDYLNRNIVTvaGMIK-LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDS 300
Cdd:cd07843   89 eHDLKSLMETMKQPFLQ--SEVKcLMLQLLSGVAHLH--------DNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 301 ILNtidiPQNPKVGTKRYMAPEMLDDTmnvnifESFKRA-DIYSVGLVYWEIARR 354
Cdd:cd07843  159 PLK----PYTQLVVTLWYRAPELLLGA------KEYSTAiDMWSVGCIFAELLTK 203
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
199-352 2.79e-09

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: 58.22  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 199 ILGFIAADNKDNgtwtQLWLVSEYHEQGSLYDYLNRnivtvAGMI------KLALSIASGLAHLHMEIvgtqgkpAIAHR 272
Cdd:cd06615   61 IVGFYGAFYSDG----EISICMEHMDGGSLDQVLKK-----AGRIpenilgKISIAVLRGLTYLREKH-------KIMHR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 273 DIKSKNILVKKCETCAIADLGLAVK-HDSILNTIdipqnpkVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWEI 351
Cdd:cd06615  125 DVKPSNILVNSRGEIKLCDFGVSGQlIDSMANSF-------VGTRSYMSPERLQGT------HYTVQSDIWSLGLSLVEM 191

                 .
gi 161333835 352 A 352
Cdd:cd06615  192 A 192
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
146-354 2.81e-09

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: 58.06  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTVMLR------HENILGFI-AADNKDNGTWTQL 216
Cdd:cd07838    3 EVAEI-GEGAYGTVYKARdlQDGRFVALKKVRVPLSEEGIPLSTIREIALLKqlesfeHPNVVRLLdVCHGPRTDRELKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQgSLYDYLNRniVTVAGM----IK-LALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIAD 291
Cdd:cd07838   82 TLVFEHVDQ-DLATYLDK--CPKPGLppetIKdLMRQLLRGLDFLHSH--------RIVHRDLKPQNILVTSDGQVKLAD 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 292 LGLAVKHdsilnTIDIPQNPKVGTKRYMAPE-MLDDTMNVNIfesfkraDIYSVGLVYWEIARR 354
Cdd:cd07838  151 FGLARIY-----SFEMALTSVVVTLWYRAPEvLLQSSYATPV-------DMWSVGCIFAELFNR 202
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
147-354 3.15e-09

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: 58.11  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTVM----LRHENILGFIAADNKDNGTWtqlwLVS 220
Cdd:cd06634   20 LREI-GHGSFGAVYFARdvRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKflqkLRHPNTIEYRGCYLREHTAW----LVM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHeQGSLYDYLNRNI-----VTVAGMIKLALSiasGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd06634   95 EYC-LGSASDLLEVHKkplqeVEIAAITHGALQ---GLAYLHSH--------NMIHRDVKAGNILLTEPGLVKLGDFGSA 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 296 vkhdsilnTIDIPQNPKVGTKRYMAPEMLdDTMNVNIFESfkRADIYSVGLVYWEIARR 354
Cdd:cd06634  163 --------SIMAPANSFVGTPYWMAPEVI-LAMDEGQYDG--KVDVWSLGITCIELAER 210
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
147-350 3.18e-09

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: 58.09  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVwH---GRWCGEDVAVKIFS-----SRDERSWFREAeiyQTVMLRHEN----ILGFiAADNKDNgtwt 214
Cdd:cd05601    5 VKNVIGRGHFGEV-QvvkEKATGDIYAMKVLKksetlAQEEVSFFEEE---RDIMAKANSpwitKLQY-AFQDSEN---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 qLWLVSEYHEQGSLYDYLNR--NIVTvAGMIKLALS-IASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIA 290
Cdd:cd05601   76 -LYLVMEYHPGGDLLSLLSRydDIFE-ESMARFYLAeLVLAIHSLHsMGYV---------HRDIKPENILIDRTGHIKLA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 291 DLGLAVKHDSilnTIDIPQNPKVGTKRYMAPEMLdDTMNVNIFESFK-RADIYSVGLVYWE 350
Cdd:cd05601  145 DFGSAAKLSS---DKTVTSKMPVGTPDYIAPEVL-TSMNGGSKGTYGvECDWWSLGIVAYE 201
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
149-354 3.36e-09

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: 57.92  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKI--FSSRDE---RSWFREAEIYQtvMLRHEN-ILGFIAADNKDNGTWTQLWLVS 220
Cdd:cd07837    7 EKIGEGTYGKVYKARdkNTGKLVALKKtrLEMEEEgvpSTALREVSLLQ--MLSQSIyIVRLLDVEHVEENGKPLLYLVF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQgSLYDYLNR------NIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCE-TCAIADLG 293
Cdd:cd07837   85 EYLDT-DLKKFIDSygrgphNPLPAKTIQSFMYQLCKGVAHCH--------SHGVMHRDLKPQNLLVDKQKgLLKIADLG 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 294 LAvkhdsilNTIDIPQNP---KVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIARR 354
Cdd:cd07837  156 LG-------RAFTIPIKSythEIVTLWYRAPEVLLGSTHYS-----TPVDMWSVGCIFAEMSRK 207
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
147-394 3.43e-09

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: 57.73  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWCGEDVAV-----KIFSSRDERS---WFREAEIYQtvMLRHENILGFIAADNKDNgtwtQLWL 218
Cdd:cd08229   28 IEKKIGRGQFSEVYRATCLLDGVPValkkvQIFDLMDAKAradCIKEIDLLK--QLNHPNVIKYYASFIEDN----ELNI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYL-----NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd08229  102 VLELADAGDLSRMIkhfkkQKRLIPEKTVWKYFVQLCSALEHMHSR--------RVMHRDIKPANVFITATGVVKLGDLG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 294 LAvkhdSILNTIDIPQNPKVGTKRYMAPEMLDDtmNVNIFESfkraDIYSVGLVYWEIAR--------RCSVGGIVEEYQ 365
Cdd:cd08229  174 LG----RFFSSKTTAAHSLVGTPYYMSPERIHE--NGYNFKS----DIWSLGCLLYEMAAlqspfygdKMNLYSLCKKIE 243
                        250       260       270
                 ....*....|....*....|....*....|....
gi 161333835 366 LPYYDMVPSDPSIEEMRKVV--C---DQKFRPSI 394
Cdd:cd08229  244 QCDYPPLPSDHYSEELRQLVnmCinpDPEKRPDI 277
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
145-415 3.51e-09

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. 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. Tie1 is a receptor tyr kinase (RTK) 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. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 57.70  E-value: 3.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGE----DVAVKIF----SSRDERSWFREAEIYqTVMLRHENILGFIAA-DNKDngtwtQ 215
Cdd:cd05089    4 IKFEDVIGEGNFGQVIKAMIKKDglkmNAAIKMLkefaSENDHRDFAGELEVL-CKLGHHPNIINLLGAcENRG-----Y 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNIV-----------------TVAGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDIKSKN 278
Cdd:cd05089   78 LYIAIEYAPYGNLLDFLRKSRVletdpafakehgtastlTSQQLLQFASDVAKGMQYL--------SEKQFIHRDLAARN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 279 ILVKKCETCAIADLGLAvKHDSILNTIDIPQNPkvgtKRYMAPEmlddTMNVNIFESfkRADIYSVGLVYWEIArrcSVG 358
Cdd:cd05089  150 VLVGENLVSKIADFGLS-RGEEVYVKKTMGRLP----VRWMAIE----SLNYSVYTT--KSDVWSFGVLLWEIV---SLG 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 359 GIveeyqlPY--------YDMVPSDPSIEEMRKvvCDQKfrpsipnqwqscealrvMGRIMRECW 415
Cdd:cd05089  216 GT------PYcgmtcaelYEKLPQGYRMEKPRN--CDDE-----------------VYELMRQCW 255
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
151-440 3.75e-09

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: 57.39  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG---------RWCgeDVAVKIFSSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNGTWTQLWLVSE 221
Cdd:cd14032    9 LGRGSFKTVYKGldtetwvevAWC--ELQDRKLTKVERQRFKEEAEMLKG--LQHPNIVRFYDFWESCAKGKRCIVLVTE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIVTVAGMIK-LALSIASGLAHLHMEivgtqgKPAIAHRDIKSKNILVK-KCETCAIADLGLA-VKH 298
Cdd:cd14032   85 LMTSGTLKTYLKRFKVMKPKVLRsWCRQILKGLLFLHTR------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLAtLKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 DSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNIfesfkraDIYSVGLVYWEIArrcsvggiVEEYqlPYYDmvpSDPSI 378
Cdd:cd14032  159 ASFAKSV-------IGTPEFMAPEMYEEHYDESV-------DVYAFGMCMLEMA--------TSEY--PYSE---CQNAA 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 379 EEMRKVVCDqkFRPSIPNQWQSCEALRVMGrimrECWYANGAARltaLRIKKTISQLCVKED 440
Cdd:cd14032  212 QIYRKVTCG--IKPASFEKVTDPEIKEIIG----ECICKNKEER---YEIKDLLSHAFFAED 264
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
149-352 3.94e-09

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: 57.43  E-value: 3.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRW--CGEDVAVKIFSSRDERSWFREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSEYH 223
Cdd:cd07846    7 GLVGEGSYGMVMKCRHkeTGQIVAIKKFLESEDDKMVKKIamrEIKMLKQLRHENLVNLIEVFRRKK----RWYLVFEFV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDY------LNRNIVTvagmiKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAvk 297
Cdd:cd07846   83 DHTVLDDLekypngLDESRVR-----KYLFQILRGIDFCHSH--------NIIHRDIKPENILVSQSGVVKLCDFGFA-- 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 hdsilNTIDIPQ---NPKVGTKRYMAPEML-DDTmnvnifeSFKRA-DIYSVGLVYWEIA 352
Cdd:cd07846  148 -----RTLAAPGevyTDYVATRWYRAPELLvGDT-------KYGKAvDVWAVGCLVTEML 195
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
151-348 4.11e-09

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: 56.99  E-value: 4.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW---CGEDVAVKIFSSRD--ERSWFREAEIYQTVMLRHENILGFIaaDNKDNGTwtQLWLVSEYHEQ 225
Cdd:cd14120    1 IGHGAFAVVFKGRHrkkPDLPVAIKCITKKNlsKSQNLLGKEIKILKELSHENVVALL--DCQETSS--SVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 GSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCA---------IADLGLA 295
Cdd:cd14120   77 GDLADYLQAKGTLSEDTIRVFLqQIAAAMKALH--------SKGIVHRDLKPQNILLSHNSGRKpspndirlkIADFGFA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 296 --VKHDSILNTIdipqnpkVGTKRYMAPEMLddtMNVNiFESfkRADIYSVG-LVY 348
Cdd:cd14120  149 rfLQDGMMAATL-------CGSPMYMAPEVI---MSLQ-YDA--KADLWSIGtIVY 191
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
150-352 4.31e-09

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: 57.03  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWCGEDV--AVKIFSSRDER-SWFREAEIYQTVMLRHENILGFIAADNKDNgtwtqlwLVSEYHEQ- 225
Cdd:cd06624   15 VLGKGTFGVVYAARDLSTQVriAIKEIPERDSReVQPLHEEIALHSRLSHKNIVQYLGSVSEDG-------FFKIFMEQv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 --GSLYDY-------LNRNIVTVAGMIKlalSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCE-TCAIADLGLA 295
Cdd:cd06624   88 pgGSLSALlrskwgpLKDNENTIGYYTK---QILEGLKYLHDN--------KIVHRDIKGDNVLVNTYSgVVKISDFGTS 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 296 VKHDSIlntidipqNPKV----GTKRYMAPEMLDDTMnvnifesfkR-----ADIYSVGLVYWEIA 352
Cdd:cd06624  157 KRLAGI--------NPCTetftGTLQYMAPEVIDKGQ---------RgygppADIWSLGCTIIEMA 205
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
151-352 4.56e-09

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: 57.04  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG---------RWCgeDVAVKIFSSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNGTWTQLWLVSE 221
Cdd:cd14031   18 LGRGAFKTVYKGldtetwvevAWC--ELQDRKLTKAEQQRFKEEAEMLKG--LQHPNIVRFYDSWESVLKGKKCIVLVTE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIVTVAGMIK-LALSIASGLAHLHMEivgtqgKPAIAHRDIKSKNILVK-KCETCAIADLGLA-VKH 298
Cdd:cd14031   94 LMTSGTLKTYLKRFKVMKPKVLRsWCRQILKGLQFLHTR------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLAtLMR 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 DSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNIfesfkraDIYSVGLVYWEIA 352
Cdd:cd14031  168 TSFAKSV-------IGTPEFMAPEMYEEHYDESV-------DVYAFGMCMLEMA 207
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
149-327 4.78e-09

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: 56.96  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWH--GRWCGEDVAVKIFSSRD--ERSWFREAEIYQTVMLRHENILGFIaadnKDNGTWTQLWLVSEYHE 224
Cdd:cd14184    7 KVIGDGNFAVVKEcvERSTGKEFALKIIDKAKccGKEHLIENEVSILRRVKHPNIIMLI----EEMDTPAELYLVMELVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVkkCE------TCAIADLGLAVK 297
Cdd:cd14184   83 GGDLFDAITSSTkYTERDASAMVYNLASALKYLH--------GLCIVHRDIKPENLLV--CEypdgtkSLKLGDFGLATV 152
                        170       180       190
                 ....*....|....*....|....*....|
gi 161333835 298 HDSILNTIdipqnpkVGTKRYMAPEMLDDT 327
Cdd:cd14184  153 VEGPLYTV-------CGTPTYVAPEIIAET 175
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
152-324 4.90e-09

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: 57.32  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGRW--CGEDVAVKIFSSRDERSWF-----REAEIYQtvMLRHENILGFI--AADNKDNGTWTQ--LWLVS 220
Cdd:cd07866   17 GEGTFGEVYKARQikTGRVVALKKILMHNEKDGFpitalREIKILK--KLKHPNVVPLIdmAVERPDKSKRKRgsVYMVT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EY--HEQGSLYDylNRNI-VTVAGmIKL-ALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA- 295
Cdd:cd07866   95 PYmdHDLSGLLE--NPSVkLTESQ-IKCyMLQLLEGINYLH--------ENHILHRDIKAANILIDNQGILKIADFGLAr 163
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 161333835 296 VKHDSILNtidiPQNPKVGTKR----------YMAPEML 324
Cdd:cd07866  164 PYDGPPPN----PKGGGGGGTRkytnlvvtrwYRPPELL 198
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
149-358 5.13e-09

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: 57.12  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSwfrEAEIYQTVMLRHENILGFIAA-DNKDNGTWTQ---------- 215
Cdd:cd14047   12 ELIGSGGFGQVFKAkhRIDGKTYAIKRVKLNNEKA---EREVKALAKLDHPNIVRYNGCwDGFDYDPETSssnssrsktk 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 -LWLVSEYHEQGSLYDYL-NRNIVTVAGMIKLAL--SIASGLAHLHmeivgtqGKPAIaHRDIKSKNILVKKCETCAIAD 291
Cdd:cd14047   89 cLFIQMEFCEKGTLESWIeKRNGEKLDKVLALEIfeQITKGVEYIH-------SKKLI-HRDLKPSNIFLVDTGKVKIGD 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 292 LGLAVKHdsilnTIDIPQNPKVGTKRYMAPEMLddtmNVNIFEsfKRADIYSVGLVYWEIARRCSVG 358
Cdd:cd14047  161 FGLVTSL-----KNDGKRTKSKGTLSYMSPEQI----SSQDYG--KEVDIYALGLILFELLHVCDSA 216
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
151-347 5.80e-09

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: 56.47  E-value: 5.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHgrwC-----GEDVAVKIF---SSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwtQLWLVSEY 222
Cdd:cd14103    1 LGRGKFGTVYR---CvekatGKELAAKFIkcrKAKDREDVRNEIEIMN--QLRHPRLLQLYDAFETPR----EMVLVMEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDylnRNI-----VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV--KKCETCAIADLGLA 295
Cdd:cd14103   72 VAGGELFE---RVVdddfeLTERDCILFMRQICEGVQYMH--------KQGILHLDLKPENILCvsRTGNQIKIIDFGLA 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 296 VKHDsilntidiPQNP-KV--GTKRYMAPEMlddtmnVNiFE--SFKrADIYSVGLV 347
Cdd:cd14103  141 RKYD--------PDKKlKVlfGTPEFVAPEV------VN-YEpiSYA-TDMWSVGVI 181
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
146-325 6.12e-09

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: 56.69  E-value: 6.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEV--WHGRWCGEDVAVKIFS-------------------SRDERSwFREAEIYQtvMLRHENILGFia 204
Cdd:cd14077    4 EFVKTIGAGSMGKVklAKHIRTGEKCAIKIIPrasnaglkkerekrlekeiSRDIRT-IREAALSS--LLNHPHICRL-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 205 adnKDN-GTWTQLWLVSEYHEQGSLYDY-LNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVK 282
Cdd:cd14077   79 ---RDFlRTPNHYYMLFEYVDGGQLLDYiISHGKLKEKQARKFARQIASALDYLH--------RNSIVHRDLKIENILIS 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 283 KCETCAIADLGLA--VKHDSILNTIdipqnpkVGTKRYMAPEMLD 325
Cdd:cd14077  148 KSGNIKIIDFGLSnlYDPRRLLRTF-------CGSLYFAAPELLQ 185
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
151-350 6.40e-09

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: 56.50  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGED--VAVKI-FSSRDERSWF-----REAEIYQtvMLRHENILGFIAADNKDngtwTQLWLVSEY 222
Cdd:cd14116   13 LGKGKFGNVYLAREKQSKfiLALKVlFKAQLEKAGVehqlrREVEIQS--HLRHPNILRLYGYFHDA----TRVYLILEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRniVTVAGMIKLALSI---ASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKHD 299
Cdd:cd14116   87 APLGTVYRELQK--LSKFDEQRTATYItelANALSYCHSK--------RVIHRDIKPENLLLGSAGELKIADFGWSVHAP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 300 SILNTIdipqnpKVGTKRYMAPEMLDDTMNVnifesfKRADIYSVGLVYWE 350
Cdd:cd14116  157 SSRRTT------LCGTLDYLPPEMIEGRMHD------EKVDLWSLGVLCYE 195
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
148-351 6.85e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 56.44  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIvGKGRFGEVWHGR-WCGEDVAVKIF-------SSRDERSWFREAEIYQTvmLRHENILGFIAADNKDngtwTQLWLV 219
Cdd:cd05042    1 QEI-GNGWFGKVLLGEiYSGTSVAQVVVkelkasaNPKEQDTFLKEGQPYRI--LQHPNILQCLGQCVEA----IPYLLV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRNIVTVAG------MIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd05042   74 MEFCDLGDLKAYLRSEREHERGdsdtrtLQRMACEVAAGLAHLH--------KLNFVHSDLALRNCLLTSDLTVKIGDYG 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 294 LA---VKHDSILNTidipqNPKVGTKRYMAPEMLDDTM-NVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd05042  146 LAhsrYKEDYIETD-----DKLWFPLRWTAPELVTEFHdRLLVVDQTKYSNIWSLGVTLWEL 202
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
149-325 7.09e-09

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: 56.50  E-value: 7.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR-WCGEDVAVKIFSS---RDERSWF---REAEIYQTvmLRHENILGFIAA-DNKDngtwtQLWLVS 220
Cdd:cd14161    9 ETLGKGTYGRVKKARdSSGRLVAIKSIRKdriKDEQDLLhirREIEIMSS--LNHPHIISVYEVfENSS-----KIVIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA--VK 297
Cdd:cd14161   82 EYASRGDLYDYIsERQRLSELEARHFFRQIVSAVHYCH--------ANGIVHRDLKLENILLDANGNIKIADFGLSnlYN 153
                        170       180
                 ....*....|....*....|....*...
gi 161333835 298 HDSILNTIdipqnpkVGTKRYMAPEMLD 325
Cdd:cd14161  154 QDKFLQTY-------CGSPLYASPEIVN 174
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
151-432 7.12e-09

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: 56.49  E-value: 7.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGE----DVAVKIFSSRDERS----WFREAEIYQtvMLRHENILGFIAADNKDNgtwtqLWLVSEY 222
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRkkqiDVAIKVLKQGNEKAvrdeMMREAQIMH--QLDNPYIVRMIGVCEAEA-----LMLVMEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIADLGLAvkhdS 300
Cdd:cd05115   85 ASGGPLNKFLsgKKDEITVSNVVELMHQVSMGMKYL-------EEKNFV-HRDLAARNVLLVNQHYAKISDFGLS----K 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 301 ILNTIDIPQNPKVGTK---RYMAPEmlddTMNVNIFESfkRADIYSVGLVYWEIArrcSVGgiveeyQLPYYDMVPSD-- 375
Cdd:cd05115  153 ALGADDSYYKARSAGKwplKWYAPE----CINFRKFSS--RSDVWSYGVTMWEAF---SYG------QKPYKKMKGPEvm 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 376 PSIEEMRKVVCDqkfrPSIPNQwqscealrvMGRIMRECWYANGAARLTALRIKKTI 432
Cdd:cd05115  218 SFIEQGKRMDCP----AECPPE---------MYALMSDCWIYKWEDRPNFLTVEQRM 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
194-352 7.85e-09

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: 56.40  E-value: 7.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 194 LRHENILGFIAAD-NKDNgtwTQLWLVSEYHEQGSLYDYLNRNI-----VTVAGMIKLALSIASGLAHLHMeivGTQGKP 267
Cdd:cd08217   56 LKHPNIVRYYDRIvDRAN---TTLYIVMEYCEGGDLAQLIKKCKkenqyIPEEFIWKIFTQLLLALYECHN---RSVGGG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 268 AIAHRDIKSKNILVKKCETCAIADLGLAvkhdSILNTIDIPQNPKVGTKRYMAPEMLDDtMNVNifesfKRADIYSVGLV 347
Cdd:cd08217  130 KILHRDLKPANIFLDSDNNVKLGDFGLA----RVLSHDSSFAKTYVGTPYYMSPELLNE-QSYD-----EKSDIWSLGCL 199

                 ....*
gi 161333835 348 YWEIA 352
Cdd:cd08217  200 IYELC 204
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
147-352 7.91e-09

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: 56.60  E-value: 7.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEV---WHgRWCGEDVAVK-IFSSRDERSWFREAEIYQTVMLRH--ENILGFIAADNKDNGTWTQLWLVS 220
Cdd:cd06616   11 LGEI-GRGAFGTVnkmLH-KPSGTIMAVKrIRSTVDEKEQKRLLMDLDVVMRSSdcPYIVKFYGALFREGDCWICMELMD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMI-KLALSIASGLAHLHMEIvgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVK-H 298
Cdd:cd06616   89 ISLDKFYKYVYEVLDSVIPEEILgKIAVATVKALNYLKEEL-------KIIHRDVKPSNILLDRNGNIKLCDFGISGQlV 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 DSILNTIDipqnpkVGTKRYMAPEMLDDTMNVNIFESfkRADIYSVGLVYWEIA 352
Cdd:cd06616  162 DSIAKTRD------AGCRPYMAPERIDPSASRDGYDV--RSDVWSLGITLYEVA 207
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
140-373 8.40e-09

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 56.31  E-value: 8.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 140 TIAR-TIVLQEIVGKGRFGEVWHGRW---CGEDVAVKIFSSRDERSWFREAEIYQTVM----LRHENILGFIAADNKDNG 211
Cdd:cd05043    2 AVSReRVTLSDLLQEGTFGRIFHGILrdeKGKEEEVLVKTVKDHASEIQVTMLLQESSllygLSHQNLLPILHVCIEDGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 212 T---------WTQLWLvseYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNilvk 282
Cdd:cd05043   82 KpmvlypymnWGNLKL---FLQQCRLSEANNPQALSTQQLVHMALQIACGMSYLH--------RRGVIHKDIAARN---- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 283 kcetCAIADLgLAVK-HDSILNTIDIP---------QNPKVgtkRYMAPEMLddtmnVNIFESFKrADIYSVGLVYWEIa 352
Cdd:cd05043  147 ----CVIDDE-LQVKiTDNALSRDLFPmdyhclgdnENRPI---KWMSLESL-----VNKEYSSA-SDVWSFGVLLWEL- 211
                        250       260
                 ....*....|....*....|.
gi 161333835 353 rrCSVGgiveeyQLPYYDMVP 373
Cdd:cd05043  212 --MTLG------QTPYVEIDP 224
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
145-371 1.04e-08

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: 55.86  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIvGKGRFGEVWHGRWCGE--DVAVK-IFSSRD-ERSWFR---------EAEIYQTV-MLRHENILGFIAA-DNKD 209
Cdd:cd14004    3 TILKEM-GEGAYGQVNLAIYKSKgkEVVIKfIFKERIlVDTWVRdrklgtvplEIHILDTLnKRSHPNIVKLLDFfEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 210 NgtwtqLWLVSEYHEQG-SLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETC 287
Cdd:cd14004   82 F-----YYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFrQVADAVKHLH-----DQG---IVHRDIKDENVILDGNGTI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 288 AIADLGLAV-----KHDSILNTIDipqnpkvgtkrYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIarrcsvggIVE 362
Cdd:cd14004  149 KLIDFGSAAyiksgPFDTFVGTID-----------YAAPEVLRGNPYGG-----KEQDIWALGVLLYTL--------VFK 204

                 ....*....
gi 161333835 363 EYqlPYYDM 371
Cdd:cd14004  205 EN--PFYNI 211
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
151-354 1.11e-08

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 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: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 56.08  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW---HGRWcGEDVAVK------IFSSRDERSWFREAEIYQTVMLRHenILGFIAADNKDNGtwtqLWLVSE 221
Cdd:cd14026    5 LSRGAFGTVSrarHADW-RVTVAIKclkldsPVGDSERNCLLKEAEILHKARFSY--ILPILGICNEPEF----LGIVTE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIV--TVAGMIKLAL--SIASGLAHLHmeivgtQGKPAIAHRDIKSKNILVKKCETCAIADLGLAV- 296
Cdd:cd14026   78 YMTNGSLNELLHEKDIypDVAWPLRLRIlyEIALGVNYLH------NMSPPLLHHDLKTQNILLDGEFHVKIADFGLSKw 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 297 KHDSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNifESFKRaDIYSVGLVYWEIARR 354
Cdd:cd14026  152 RQLSISQSRSSKSAPEGGTIIYMPPEEYEPSQKRR--ASVKH-DIYSYAIIMWEVLSR 206
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
149-398 1.18e-08

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: 56.19  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGK---GRFGEVWHG--RWCGEDVAVKIFSSRDE---RSWFREAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd06644   15 EIIGElgdGAFGKVYKAknKETGALAAAKVIETKSEeelEDYMVEIEILATC--NHPYIVKLLGAFYWDG----KLWIMI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDY---LNRNIvTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:cd06644   89 EFCPGGAVDAImleLDRGL-TEPQIQVICRQMLEALQYLHsMKII---------HRDLKAGNVLLTLDGDIKLADFGVSA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 KHDSILNTIDipqnPKVGTKRYMAPE-MLDDTMNVNIFESfkRADIYSVGLVYWEIArrcsvggiveEYQLPYYDMVPsd 375
Cdd:cd06644  159 KNVKTLQRRD----SFIGTPYWMAPEvVMCETMKDTPYDY--KADIWSLGITLIEMA----------QIEPPHHELNP-- 220
                        250       260
                 ....*....|....*....|....*.
gi 161333835 376 psieeMRKVVCDQKFRP---SIPNQW 398
Cdd:cd06644  221 -----MRVLLKIAKSEPptlSQPSKW 241
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
151-415 1.23e-08

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: 55.74  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW----CGEDVAVKIF-------SSRDErsWFREAEIYQTV----MLRhenILGFIAADNkdngtwtq 215
Cdd:cd05116    3 LGSGNFGTVKKGYYqmkkVVKTVAVKILkneandpALKDE--LLREANVMQQLdnpyIVR---MIGICEAES-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd05116   70 WMLVMEMAELGPLNKFLQKNRhVTEKNITELVHQVSMGMKYLE--------ESNFVHRDLAARNVLLVTQHYAKISDFGL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 295 AVKHDSILNTIDIPQNPKVGTKRYmAPEmlddTMNVNIFESfkRADIYSVGLVYWEIArrcSVGgiveeyQLPYYDMVPS 374
Cdd:cd05116  142 SKALRADENYYKAQTHGKWPVKWY-APE----CMNYYKFSS--KSDVWSFGVLMWEAF---SYG------QKPYKGMKGN 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 161333835 375 DPS--IEEMRKVVCDQKFRPSIPNqwqscealrvmgrIMRECW 415
Cdd:cd05116  206 EVTqmIEKGERMECPAGCPPEMYD-------------LMKLCW 235
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
124-384 1.31e-08

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: 56.15  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 124 VTASGSGSGLPLLVQRTIARTIVLQEI-VGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSwfREAEIYQTVMLR---HE 197
Cdd:cd06659    1 VTHEQFKAALRMVVDQGDPRQLLENYVkIGEGSTGVVCIARekHSGRQVAVKMMDLRKQQR--RELLFNEVVIMRdyqHP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 198 NILGFIaadnKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSK 277
Cdd:cd06659   79 NVVEMY----KSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLH-----SQG---VIHRDIKSD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 278 NILVKKCETCAIADLGLAVKHDSilntiDIPQNPK-VGTKRYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEIarrcs 356
Cdd:cd06659  147 SILLTLDGRVKLSDFGFCAQISK-----DVPKRKSlVGTPYWMAPEVISRCPYGT------EVDIWSLGIMVIEM----- 210
                        250       260
                 ....*....|....*....|....*...
gi 161333835 357 VGGiveeyQLPYYdmvpSDPSIEEMRKV 384
Cdd:cd06659  211 VDG-----EPPYF----SDSPVQAMKRL 229
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
151-401 1.37e-08

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: 55.74  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTVMLR------HENILGFI---AADNKDNGTwtQLWLV 219
Cdd:cd07863    8 IGVGAYGTVYKARdpHSGHFVALKSVRVQTNEDGLPLSTVREVALLKrleafdHPNIVRLMdvcATSRTDRET--KVTLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQgSLYDYLNRniVTVAGM----IK-LALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd07863   86 FEHVDQ-DLRTYLDK--VPPPGLpaetIKdLMRQFLRGLDFLHAN--------CIVHRDLKPENILVTSGGQVKLADFGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 295 AVkhdsiLNTIDIPQNPKVGTKRYMAPE-MLDDTMNVNIfesfkraDIYSVGLVYWEIARR----C------SVGGIVEE 363
Cdd:cd07863  155 AR-----IYSCQMALTPVVVTLWYRAPEvLLQSTYATPV-------DMWSVGCIFAEMFRRkplfCgnseadQLGKIFDL 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 161333835 364 YQLPYYDMVPSDPSIEEmrkvvcdQKFRPSIPNQWQSC 401
Cdd:cd07863  223 IGLPPEDDWPRDVTLPR-------GAFSPRGPRPVQSV 253
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
184-352 1.72e-08

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: 55.52  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 184 REAEIYQTVmlRHENILGFIAADNKDNGTwtqLWLVSEYHEQGSLydylnRNIVTVAGMI------KLALSIASGLAHLH 257
Cdd:cd06620   52 RELQILHEC--HSPYIVSFYGAFLNENNN---IIICMEYMDCGSL-----DKILKKKGPFpeevlgKIAVAVLEGLTYLY 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 258 meivgTQGKpaIAHRDIKSKNILVKKCETCAIADLGLAVKH-DSILNTIdipqnpkVGTKRYMAPEMLD-DTMNVnifes 335
Cdd:cd06620  122 -----NVHR--IIHRDIKPSNILVNSKGQIKLCDFGVSGELiNSIADTF-------VGTSTYMSPERIQgGKYSV----- 182
                        170
                 ....*....|....*..
gi 161333835 336 fkRADIYSVGLVYWEIA 352
Cdd:cd06620  183 --KSDVWSLGLSIIELA 197
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
141-327 1.72e-08

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: 55.34  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 141 IARTIvlqeivGKGRFGEVWHGRWCGED--VAVKIF--SSRDERSWFREAEIYQTVMLRHENILGFIaadnKDNGTWTQL 216
Cdd:cd14185    4 IGRTI------GDGNFAVVKECRHWNENqeYAMKIIdkSKLKGKEDMIESEILIIKSLSHPNIVKLF----EVYETEKEI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVK----KCETCAIAD 291
Cdd:cd14185   74 YLILEYVRGGDLFDAIIESVkFTEHDAALMIIDLCEALVYIHSK--------HIVHRDLKPENLLVQhnpdKSTTLKLAD 145
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 161333835 292 LGLAVKHDSILNTIdipqnpkVGTKRYMAPEMLDDT 327
Cdd:cd14185  146 FGLAKYVTGPIFTV-------CGTPTYVAPEILSEK 174
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
139-415 1.78e-08

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK 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: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 55.47  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 139 RTIAR-TIVLQEIVGKGRFGEVWHGRWCGED-------VAVK----IFSSRDERSWFREAEIYQTvmLRHENILGFIAAD 206
Cdd:cd05036    1 KEVPRkNLTLIRALGQGAFGEVYEGTVSGMPgdpsplqVAVKtlpeLCSEQDEMDFLMEALIMSK--FNHPNIVRCIGVC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 207 NKDngtwTQLWLVSEYHEQGSLYDYL--NRN------IVTVAGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKN 278
Cdd:cd05036   79 FQR----LPRFILLELMAGGDLKSFLreNRPrpeqpsSLTMLDLLQLAQDVAKGCRYL-------EENHFI-HRDIAARN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 279 ILVKKCET---CAIADLGLAVkhdsilntiDIPQNP--KVGTK-----RYMAPEMLDDtmnvNIFESfkRADIYSVGLVY 348
Cdd:cd05036  147 CLLTCKGPgrvAKIGDFGMAR---------DIYRADyyRKGGKamlpvKWMPPEAFLD----GIFTS--KTDVWSFGVLL 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 349 WEIArrcSVGgiveeyQLPYydmvPSDPSIEEMRKVVCDQKFRPsiPNQWQSCealrvMGRIMRECW 415
Cdd:cd05036  212 WEIF---SLG------YMPY----PGKSNQEVMEFVTSGGRMDP--PKNCPGP-----VYRIMTQCW 258
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
147-352 1.93e-08

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: 55.03  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRwCGED---VAVK---IFSSRDERSwfRE---AEIYQTVMLRHENILGFIAADNKDNgtwtQLW 217
Cdd:cd08228    6 IEKKIGRGQFSEVYRAT-CLLDrkpVALKkvqIFEMMDAKA--RQdcvKEIDLLKQLNHPNVIKYLDSFIEDN----ELN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYL-----NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd08228   79 IVLELADAGDLSQMIkyfkkQKRLIPERTVWKYFVQLCSAVEHMHSR--------RVMHRDIKPANVFITATGVVKLGDL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAvkhdSILNTIDIPQNPKVGTKRYMAPEMLDDtmNVNIFESfkraDIYSVGLVYWEIA 352
Cdd:cd08228  151 GLG----RFFSSKTTAAHSLVGTPYYMSPERIHE--NGYNFKS----DIWSLGCLLYEMA 200
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
151-383 1.94e-08

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: 55.04  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWC--GEDVAVKIFS-----SRDERSWFREaeIYQTVMLRHENILGFIAADNkdngTWTQLWLVSEYH 223
Cdd:cd14075   10 LGSGNFSQVKLGIHQltKEKVAIKILDktkldQKTQRLLSRE--ISSMEKLHHPNIIRLYEVVE----TLSKLHLVMEYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA--VKHDS 300
Cdd:cd14075   84 SGGELYTKISTEGKLSESEAKPLFAqIVSAVKHMH--------ENNIIHRDLKAENVFYASNNCVKVGDFGFSthAKRGE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 301 ILNTIdipqnpkVGTKRYMAPEMLDDTMNVNIFesfkrADIYSVG-LVYWEIA-----RRCSVGG----IVE-EYQLPYY 369
Cdd:cd14075  156 TLNTF-------CGSPPYAAPELFKDEHYIGIY-----VDIWALGvLLYFMVTgvmpfRAETVAKlkkcILEgTYTIPSY 223
                        250       260
                 ....*....|....*....|....*...
gi 161333835 370 -------------DMVPSD-PSIEEMRK 383
Cdd:cd14075  224 vsepcqelirgilQPVPSDrYSIDEIKN 251
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
152-403 2.28e-08

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: 54.83  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVwhgRWCGEDVAVKIFSSRD-------ERSWFREAEIYQTvmLRHENILGFIAAdnkdNGTWTQLWLVSEY-H 223
Cdd:cd14111   12 ARGRFGVI---RRCRENATGKNFPAKIvpyqaeeKQGVLQEYEILKS--LHHERIMALHEA----YITPRYLVLIAEFcS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKHdsilN 303
Cdd:cd14111   83 GKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGR--------RVLHLDIKPDNIMVTNLNAIKIVDFGSAQSF----N 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 304 TIDIPQ-NPKVGTKRYMAPEMLD-DTMNvnifesfKRADIYSVGLVYWeiarrcsvggIVEEYQLPYYDMvpsDPSIEEM 381
Cdd:cd14111  151 PLSLRQlGRRTGTLEYMAPEMVKgEPVG-------PPADIWSIGVLTY----------IMLSGRSPFEDQ---DPQETEA 210
                        250       260
                 ....*....|....*....|....
gi 161333835 382 RKVVcdQKFRPS--IPNQWQSCEA 403
Cdd:cd14111  211 KILV--AKFDAFklYPNVSQSASL 232
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
146-322 2.45e-08

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: 54.58  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEV---WHGRwCGEDVAVKIFSSRDERSW------FREAEIYQtvMLRHENILGF---IAadnkdngTW 213
Cdd:cd14079    5 ILGKTLGVGSFGKVklaEHEL-TGHKVAVKILNRQKIKSLdmeekiRREIQILK--LFRHPHIIRLyevIE-------TP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 TQLWLVSEYHEQGSLYDYlnrnIVTVAGM-----IKLALSIASGLA--HLHMeivgtqgkpaIAHRDIKSKNILVKKCET 286
Cdd:cd14079   75 TDIFMVMEYVSGGELFDY----IVQKGRLsedeaRRFFQQIISGVEycHRHM----------VVHRDLKPENLLLDSNMN 140
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 161333835 287 CAIADLGLA-VKHD-SILNTidipqnpKVGTKRYMAPE 322
Cdd:cd14079  141 VKIADFGLSnIMRDgEFLKT-------SCGSPNYAAPE 171
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
147-348 2.60e-08

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: 54.70  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSR----DERSWFREAEIYQTvmLRHENILGF---IAADNKdngtwtqLW 217
Cdd:cd14078    7 LHETIGSGGFAKVKLATHIltGEKVAIKIMDKKalgdDLPRVKTEIEALKN--LSHQHICRLyhvIETDNK-------IF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYlnrnIVTvagmiKLALS----------IASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETC 287
Cdd:cd14078   78 MVLEYCPGGELFDY----IVA-----KDRLSedearvffrqIVSAVAYVH-----SQG---YAHRDLKPENLLLDEDQNL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 288 AIADLGLAVK----HDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNifesfKRADIYSVG-LVY 348
Cdd:cd14078  141 KLIDFGLCAKpkggMDHHLETC-------CGSPAYAAPELIQGKPYIG-----SEADVWSMGvLLY 194
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
187-382 2.72e-08

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: 55.06  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 187 EIYQTVMLRHE----NILGFIAADNKDNgtwtQLWLVSEYHEQGSLYDYLNRnivtvAGMI------KLALSIASGLAHL 256
Cdd:cd06650   49 QIIRELQVLHEcnspYIVGFYGAFYSDG----EISICMEHMDGGSLDQVLKK-----AGRIpeqilgKVSIAVIKGLTYL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 257 hmeivgtQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsilnTIDIPQNPKVGTKRYMAPEMLDDTmnvnifESF 336
Cdd:cd06650  120 -------REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQ------LIDSMANSFVGTRSYMSPERLQGT------HYS 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161333835 337 KRADIYSVGLVYWEIArrcsVGGI------VEEYQLPYYDMVPSDPSIEEMR 382
Cdd:cd06650  181 VQSDIWSMGLSLVEMA----VGRYpipppdAKELELMFGCQVEGDAAETPPR 228
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
240-353 3.26e-08

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: 54.46  E-value: 3.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 240 AGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVkhdsilntiDIPQNPK----VGT 315
Cdd:cd05577   95 ARAIFYAAEIICGLEHLHNR--------FIVYRDLKPENILLDDHGHVRISDLGLAV---------EFKGGKKikgrVGT 157
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 161333835 316 KRYMAPEMLddtMNVNIFESfkRADIYSVGLVYWEIAR 353
Cdd:cd05577  158 HGYMAPEVL---QKEVAYDF--SVDWFALGCMLYEMIA 190
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
137-324 3.28e-08

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: 54.87  E-value: 3.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 137 VQRTIARTIVLQEIVGKGRFGEVWHG--RWCGEDVAVK-IF----SSRDERSWFREAeIYQTVMLRHENI---LGFIAAD 206
Cdd:cd07852    1 IDKHILRRYEILKKLGKGAYGIVWKAidKKTGEVVALKkIFdafrNATDAQRTFREI-MFLQELNDHPNIiklLNVIRAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 207 N-KDngtwtqLWLVSEYHEQgSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILV-KKC 284
Cdd:cd07852   80 NdKD------IYLVFEYMET-DLHAVIRANILEDIHKQYIMYQLLKALKYLH-----SGG---VIHRDLKPSNILLnSDC 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 161333835 285 eTCAIADLGLAvkhDSILNTIDIPQNPK----VGTKRYMAPEML 324
Cdd:cd07852  145 -RVKLADFGLA---RSLSQLEEDDENPVltdyVATRWYRAPEIL 184
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
149-354 3.85e-08

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 54.40  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGED-----VAVK----IFSSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNGTwtqLWLV 219
Cdd:cd05058    1 EVIGKGHFGCVYHGTLIDSDgqkihCAVKslnrITDIEEVEQFLKEGIIMKD--FSHPNVLSLLGICLPSEGS---PLVV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYL---NRNiVTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDIKSKNILVKKCETCAIADLGLAv 296
Cdd:cd05058   76 LPYMKHGDLRNFIrseTHN-PTVKDLIGFGLQVAKG-----MEYLASK---KFVHRDLAARNCMLDESFTVKVADFGLA- 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 297 kHDSILNTIDIPQNpKVGTK---RYMAPEMLddtmNVNIFESfkRADIYSVGLVYWEIARR 354
Cdd:cd05058  146 -RDIYDKEYYSVHN-HTGAKlpvKWMALESL----QTQKFTT--KSDVWSFGVLLWELMTR 198
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
151-395 3.98e-08

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: 54.10  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGED--VAVKI-FSSRDERSWF-----REAEIyqTVMLRHENILGFIAADNKDngtwTQLWLVSEY 222
Cdd:cd14117   14 LGKGKFGNVYLAREKQSKfiVALKVlFKSQIEKEGVehqlrREIEI--QSHLRHPNILRLYNYFHDR----KRIYLILEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIV-----TVAGMIKLAlsiaSGLAHLHmeivgtqGKPAIaHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd14117   88 APRGELYKELQKHGRfdeqrTATFMEELA----DALHYCH-------EKKVI-HRDIKPENLLMGYKGELKIADFGWSVH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 HDSilntidIPQNPKVGTKRYMAPEMLDDTMNVnifesfKRADIYSVGLVYWEiarrCSVGgiveeyqLPYYDmvpSDPS 377
Cdd:cd14117  156 APS------LRRRTMCGTLDYLPPEMIEGRTHD------EKVDLWCIGVLCYE----LLVG-------MPPFE---SASH 209
                        250
                 ....*....|....*....
gi 161333835 378 IEEMRKVV-CDQKFRPSIP 395
Cdd:cd14117  210 TETYRRIVkVDLKFPPFLS 228
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
145-354 4.30e-08

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 54.08  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGED-----VAVK-----IFSSRDERSWFREAEIYQTvmLRHENILGFI--AADNKDNGT 212
Cdd:cd05035    1 LKLGKILGEGEFGSVMEAQLKQDDgsqlkVAVKtmkvdIHTYSEIEEFLSEAACMKD--FDHPNVMRLIgvCFTASDLNK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WTQLWLVSEYHEQGSLYDYL-------NRNIVTVAGMIKLALSIASGlahlhMEIVGTQGkpaIAHRDIKSKNILVKKCE 285
Cdd:cd05035   79 PPSPMVILPFMKHGDLHSYLlysrlggLPEKLPLQTLLKFMVDIAKG-----MEYLSNRN---FIHRDLAARNCMLDENM 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 286 TCAIADLGLAVK--HDSILNTIDIPQNPkvgtKRYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIARR 354
Cdd:cd05035  151 TVCVADFGLSRKiySGDYYRQGRISKMP----VKWIALESLAD----NVYTS--KSDVWSFGVTMWEIATR 211
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
149-352 4.32e-08

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: 53.97  E-value: 4.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFS-SRDERSwfREAEIYQTVM--------LRHENILGFIAADNKDngtwTQLW 217
Cdd:cd06630    6 PLLGTGAFSSCYQARdvKTGTLMAVKQVSfCRNSSS--EQEEVVEAIReeirmmarLNHPNIVRMLGATQHK----SHFN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKC-ETCAIADLGLA 295
Cdd:cd06630   80 IFVEWMAGGSVASLLSKyGAFSENVIINYTLQILRGLAYLH--------DNQIIHRDLKGANLLVDSTgQRLRIADFGAA 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 296 VKHDSILNTIDIPQNPKVGTKRYMAPEMLDDtmnvnifESFKRA-DIYSVGLVYWEIA 352
Cdd:cd06630  152 ARLASKGTGAGEFQGQLLGTIAFMAPEVLRG-------EQYGRScDVWSVGCVIIEMA 202
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
246-327 4.46e-08

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: 54.28  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 246 ALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsilntidIPQNP----KVGTKRYMAP 321
Cdd:cd05605  108 AAEITCGLEHLHSE--------RIVYRDLKPENILLDDHGHVRISDLGLAVE---------IPEGEtirgRVGTVGYMAP 170

                 ....*.
gi 161333835 322 EMLDDT 327
Cdd:cd05605  171 EVVKNE 176
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
148-351 4.50e-08

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: 54.21  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVwhgRWC-----GEDVAVKIFSSRDER------SWFREAEIYQTVMLR----HENILGFIaaDNKDNGT 212
Cdd:cd14181   15 KEVIGRGVSSVV---RRCvhrhtGQEFAVKIIEVTAERlspeqlEEVRSSTLKEIHILRqvsgHPSIITLI--DSYESST 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WtqLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIAD 291
Cdd:cd14181   90 F--IFLVFDLMRRGELFDYLTEKVTLSEKETRSIMrSLLEAVSYLHAN--------NIVHRDLKPENILLDDQLHIKLSD 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 292 LGLAV--KHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd14181  160 FGFSChlEPGEKLREL-------CGTPGYLAPEILKCSMDETHPGYGKEVDLWACGVILFTL 214
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
142-435 4.97e-08

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 53.77  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 142 ARTIVLQEIVGKGRFGEVWHGrwCGE-------DVAVKIF----SSRDERSWFREAEIYQtvMLRHENIL---GFIAADN 207
Cdd:cd05064    4 NKSIKIERILGTGRFGELCRG--CLKlpskrelPVAIHTLragcSDKQRRGFLAEALTLG--QFDHSNIVrleGVITRGN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 208 KdngtwtqLWLVSEYHEQGSLYDYLNRN--IVTVAGMIKLALSIASGLAHL-HMEIVgtqgkpaiaHRDIKSKNILVKKC 284
Cdd:cd05064   80 T-------MMIVTEYMSNGALDSFLRKHegQLVAGQLMGMLPGLASGMKYLsEMGYV---------HKGLAAHKVLVNSD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 285 ETCAIADLGLAV--KHDSILNTIDiPQNPKVgtkrYMAPEMLDdtmnvniFESFKRA-DIYSVGLVYWEIArrcSVGgiv 361
Cdd:cd05064  144 LVCKISGFRRLQedKSEAIYTTMS-GKSPVL----WAAPEAIQ-------YHHFSSAsDVWSFGIVMWEVM---SYG--- 205
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 362 eeyQLPYYDMvpsdpSIEEMRKVVCDqKFRPSIPnqwQSCEALrvMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05064  206 ---ERPYWDM-----SGQDVIKAVED-GFRLPAP---RNCPNL--LHQLMLDCWQKERGERPRFSQIHSILSKM 265
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
183-355 4.99e-08

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: 53.97  E-value: 4.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 183 FREAEIYQTVmlRHENILGFIAA--DNKDngtwTQLWLVSEYHEQGSLyDYLNRNIVTVAGMI------KLALSIASGLA 254
Cdd:cd06621   47 LRELEINKSC--ASPYIVKYYGAflDEQD----SSIGIAMEYCEGGSL-DSIYKKVKKKGGRIgekvlgKIAESVLKGLS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 255 HLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGL---AVkhDSILNTIdipqnpkVGTKRYMAPEMLDDtMNVN 331
Cdd:cd06621  120 YLHSR--------KIIHRDIKPSNILLTRKGQVKLCDFGVsgeLV--NSLAGTF-------TGTSYYMAPERIQG-GPYS 181
                        170       180
                 ....*....|....*....|....
gi 161333835 332 IfesfkRADIYSVGLVYWEIARRC 355
Cdd:cd06621  182 I-----TSDVWSLGLTLLEVAQNR 200
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
151-347 6.50e-08

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: 53.55  E-value: 6.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEV---WHGRWCgEDVAVKI----FSSRDERSWF-------REAEIYQTvmLRHENILG---FIAADNkdngtw 213
Cdd:cd14084   14 LGSGACGEVklaYDKSTC-KKVAIKIinkrKFTIGSRREInkprnieTEIEILKK--LSHPCIIKiedFFDAED------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVK-KCETC--AI 289
Cdd:cd14084   85 -DYYIVLELMEGGELFDRVVSNKRLKEAICKLyFYQMLLAVKYLH-----SNG---IIHRDLKPENVLLSsQEEECliKI 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 290 ADLGLA--VKHDSILNTIdipqnpkVGTKRYMAPEMLddtmNVNIFESFKRA-DIYSVGLV 347
Cdd:cd14084  156 TDFGLSkiLGETSLMKTL-------CGTPTYLAPEVL----RSFGTEGYTRAvDCWSLGVI 205
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
150-326 6.98e-08

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: 53.75  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVwhgrwCGEDV-------AVKIFSSR------DERSWFREAEIYQTVMLRHENILGFiAADNKdngtwTQL 216
Cdd:cd05607    9 VLGKGGFGEV-----CAVQVkntgqmyACKKLDKKrlkkksGEKMALLEKEILEKVNSPFIVSLAY-AFETK-----THL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSL----YDYLNRNIvTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAIAD 291
Cdd:cd05607   78 CLVMSLMNGGDLkyhiYNVGERGI-EMERVIFYSAQITCGILHLHsLKIV---------YRDMKPENVLLDDNGNCRLSD 147
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 161333835 292 LGLAVKHDSilntiDIPQNPKVGTKRYMAPEMLDD 326
Cdd:cd05607  148 LGLAVEVKE-----GKPITQRAGTNGYMAPEILKE 177
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
147-324 8.12e-08

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: 53.58  E-value: 8.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVwhgRWC-----GEDVAVKI-----FSSRDERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwtQL 216
Cdd:cd14086    5 LKEELGKGAFSVV---RRCvqkstGQEFAAKIintkkLSARDHQKLEREARICR--LLKHPNIVRLHDSISEEG----FH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLY-DYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV-KKCETCA--IADL 292
Cdd:cd14086   76 YLVFDLVTGGELFeDIVAREFYSEADASHCIQQILESVNHCH--------QNGIVHRDLKPENLLLaSKSKGAAvkLADF 147
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 161333835 293 GLAvkhdsilntIDIPQNPK-----VGTKRYMAPEML 324
Cdd:cd14086  148 GLA---------IEVQGDQQawfgfAGTPGYLSPEVL 175
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
147-395 8.18e-08

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: 53.29  E-value: 8.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVKI-----FSSRDERSWFREAEIYQtvMLRHENILGFIAADNKDngtwTQLWLV 219
Cdd:cd14072    4 LLKTIGKGNFAKVKLARhvLTGREVAIKIidktqLNPSSLQKLFREVRIMK--ILNHPNIVKLFEVIETE----KTLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLnrniVTVAGM------IKLAlSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd14072   78 MEYASGGEVFDYL----VAHGRMkekearAKFR-QIVSAVQYCHQK--------RIVHRDLKAENLLLDADMNIKIADFG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 294 LAVKHdSILNTIDIpqnpKVGTKRYMAPEMlddtmnvniFESFK----RADIYSVGLVYWEIarrcsVGGiveeyQLPYy 369
Cdd:cd14072  145 FSNEF-TPGNKLDT----FCGSPPYAAPEL---------FQGKKydgpEVDVWSLGVILYTL-----VSG-----SLPF- 199
                        250       260
                 ....*....|....*....|....*.
gi 161333835 370 dmvpSDPSIEEMRKVVCDQKFRpsIP 395
Cdd:cd14072  200 ----DGQNLKELRERVLRGKYR--IP 219
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
151-352 8.18e-08

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: 53.28  E-value: 8.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGE--VWHGRWCGEDVAVKIFS----SRDERSWFREaEIYQTVMLRHENILGFiAADNKDNGTwtqLWLVSEYHE 224
Cdd:cd08218    8 IGEGSFGKalLVKSKEDGKQYVIKEINiskmSPKEREESRK-EVAVLSKMKHPNIVQY-QESFEENGN---LYIVMDYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLN--RNIVTVAGMI-KLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdSI 301
Cdd:cd08218   83 GGDLYKRINaqRGVLFPEDQIlDWFVQLCLALKHVH--------DRKILHRDIKSQNIFLTKDGIIKLGDFGIA----RV 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 302 LNTIDIPQNPKVGTKRYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEIA 352
Cdd:cd08218  151 LNSTVELARTCIGTPYYLSPEICENKPYNN------KSDIWALGCVLYEMC 195
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
143-434 8.35e-08

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 53.46  E-value: 8.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVwH-------GRWCGED------------VAVKIFSS---RDERSWFREaEIYQTVMLRHENIL 200
Cdd:cd05095    5 KLLTFKEKLGEGQFGEV-HlceaegmEKFMDKDfalevsenqpvlVAVKMLRAdanKNARNDFLK-EIKIMSRLKDPNII 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 201 GFIAADNKDNgtwtQLWLVSEYHEQGSLYDYLNRN-------------IVTVAGMIKLALSIASGLAHLhmeivgtqGKP 267
Cdd:cd05095   83 RLLAVCITDD----PLCMITEYMENGDLNQFLSRQqpegqlalpsnalTVSYSDLRFMAAQIASGMKYL--------SSL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 268 AIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNTIDI--PQNPKVGTKRYMAPEMLddtmnvnIFESFKRA-DIYSV 344
Cdd:cd05095  151 NFVHRDLATRNCLVGKNYTIKIADFGMSRN----LYSGDYyrIQGRAVLPIRWMSWESI-------LLGKFTTAsDVWAF 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 345 GLVYWEIARRCSvggiveeyQLPYYDMvpSDPS-IEEMRKVVCDQKFRPSIPNQWQSCEALRvmgRIMRECWYANGAARL 423
Cdd:cd05095  220 GVTLWETLTFCR--------EQPYSQL--SDEQvIENTGEFFRDQGRQTYLPQPALCPDSVY---KLMLSCWRRDTKDRP 286
                        330
                 ....*....|.
gi 161333835 424 TALRIKKTISQ 434
Cdd:cd05095  287 SFQEIHTLLQE 297
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
149-370 8.90e-08

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: 53.47  E-value: 8.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFS-----SRDERSW-FREAEIYQTVmlRHEnilgFIAADNKDNGTWTQLWLVS 220
Cdd:cd05595    1 KLLGKGTFGKVILVRekATGRYYAMKILRkeviiAKDEVAHtVTESRVLQNT--RHP----FLTALKYAFQTHDRLCFVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVKKCETCAIADLGL---AV 296
Cdd:cd05595   75 EYANGGELFFHLSRERVFTEDRARFyGAEIVSALEYLHSRDV--------VYRDIKLENLMLDKDGHIKITDFGLckeGI 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEMLDDTmnvnifeSFKRA-DIYSVGLVYWEIArrCSvggiveeyQLPYYD 370
Cdd:cd05595  147 TDGATMKTF-------CGTPEYLAPEVLEDN-------DYGRAvDWWGLGVVMYEMM--CG--------RLPFYN 197
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
194-415 9.40e-08

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. 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 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-2D 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: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 53.18  E-value: 9.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 194 LRHENI---LGFIAADNKdngtwtqLWLVSEYHEQGSLYDYLNRNIVTVAGMIK--LALSIASGLAHLHmeivgtqgKPA 268
Cdd:cd14043   53 LRHENVnlfLGLFVDCGI-------LAIVSEHCSRGSLEDLLRNDDMKLDWMFKssLLLDLIKGMRYLH--------HRG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 269 IAHRDIKSKNILVKKCETCAIADLGLAvkhdSILNTIDIPQNPKVGTKRY-MAPEMLDDTMNVNifESFKRADIYSVGLV 347
Cdd:cd14043  118 IVHGRLKSRNCVVDGRFVLKITDYGYN----EILEAQNLPLPEPAPEELLwTAPELLRDPRLER--RGTFPGDVFSFAII 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 348 YWEIARRCsvggiveeyqLPYYDM-VPSDPSIEEMRK--VVCdqkfRPSIPNQWQSCEALRVmgriMRECW 415
Cdd:cd14043  192 MQEVIVRG----------APYCMLgLSPEEIIEKVRSppPLC----RPSVSMDQAPLECIQL----MKQCW 244
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
149-351 9.59e-08

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: 53.04  E-value: 9.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGED------VAVKIFSSRDERSWFREAEIYQTVM--LRHENILGFIAAdnkdnGTWTQLWLVS 220
Cdd:cd05111   13 KVLGSGVFGTVHKGIWIPEGdsikipVAIKVIQDRSGRQSFQAVTDHMLAIgsLDHAYIVRLLGI-----CPGASLQLVT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA--V 296
Cdd:cd05111   88 QLLPLGSLLDHVrqHRGSLGPQLLLNWCVQIAKGMYYLE--------EHRMVHRNLAARNVLLKSPSQVQVADFGVAdlL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 297 KHDS---ILNTIDIPqnpkvgtKRYMAPEMLddtmnvnIFESFK-RADIYSVGLVYWEI 351
Cdd:cd05111  160 YPDDkkyFYSEAKTP-------IKWMALESI-------HFGKYThQSDVWSYGVTVWEM 204
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
196-348 1.01e-07

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: 53.06  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 196 HENILGFI--AADNKDNGTWTQLWLVsEYHEQGSLYDYLNRNI---VTVAGMIKLALSIASGLAHLHmeivgtQGKPAIA 270
Cdd:cd14037   60 HKNIVGYIdsSANRSGNGVYEVLLLM-EYCKGGGVIDLMNQRLqtgLTESEILKIFCDVCEAVAAMH------YLKPPLI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 271 HRDIKSKNILVKKCETCAIADLGlavkhdSILNTIDIPQNP-----------KVGTKRYMAPEMLDDTMNVNIFEsfkRA 339
Cdd:cd14037  133 HRDLKVENVLISDSGNYKLCDFG------SATTKILPPQTKqgvtyveedikKYTTLQYRAPEMIDLYRGKPITE---KS 203
                        170
                 ....*....|
gi 161333835 340 DIYSVG-LVY 348
Cdd:cd14037  204 DIWALGcLLY 213
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
149-428 1.05e-07

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: 53.11  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGK---GRFGEVW--HGRWCGEDVAVKIFSSRDE---RSWFREAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd06643    8 EIVGElgdGAFGKVYkaQNKETGILAAAKVIDTKSEeelEDYMVEIDILASC--DHPNIVKLLDAFYYEN----NLWILI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYdylnrnivtvagmiKLALSIASGLAHLHMEIVGTQGKPA--------IAHRDIKSKNILVKKCETCAIADL 292
Cdd:cd06643   82 EFCAGGAVD--------------AVMLELERPLTEPQIRVVCKQTLEAlvylhenkIIHRDLKAGNILFTLDGDIKLADF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 293 GLAVKHDSILNTIDipqnPKVGTKRYMAPEMLDDTMNVNIFESFKrADIYSVGLVYWEIArrcsvggiveEYQLPYYDMV 372
Cdd:cd06643  148 GVSAKNTRTLQRRD----SFIGTPYWMAPEVVMCETSKDRPYDYK-ADVWSLGVTLIEMA----------QIEPPHHELN 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 373 PsdpsieeMRKVVCDQKFRP---SIPNQWQScealrVMGRIMRECWYANGAARLTALRI 428
Cdd:cd06643  213 P-------MRVLLKIAKSEPptlAQPSRWSP-----EFKDFLRKCLEKNVDARWTTSQL 259
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
147-351 1.36e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR 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: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 52.88  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWCGED-------VAVKIF----SSRDERSWFREAEIYqTVMLRHENILGFIAADNKDNGTwtq 215
Cdd:cd05054   11 LGKPLGRGAFGKVIQASAFGIDksatcrtVAVKMLkegaTASEHKALMTELKIL-IHIGHHLNVVNLLGACTKPGGP--- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYL---------NRNI------------------VTVAGMIKLALSIASGlahlhMEIVGTqgKPA 268
Cdd:cd05054   87 LMVIVEFCKFGNLSNYLrskreefvpYRDKgardveeeedddelykepLTLEDLICYSFQVARG-----MEFLAS--RKC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 269 IaHRDIKSKNILVKKCETCAIADLGLAVkhdsilntiDIPQNPKVGTK-------RYMAPEMLDDTMNVNifesfkRADI 341
Cdd:cd05054  160 I-HRDLAARNILLSENNVVKICDFGLAR---------DIYKDPDYVRKgdarlplKWMAPESIFDKVYTT------QSDV 223
                        250
                 ....*....|
gi 161333835 342 YSVGLVYWEI 351
Cdd:cd05054  224 WSFGVLLWEI 233
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
151-391 1.66e-07

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: 52.96  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW--CGEDVAVKIFSsrdERSWFREAEIYQTVMLRheNIL--------GFIAADNKDNGTWTQLWLVS 220
Cdd:cd05586    1 IGKGTFGQVYQVRKkdTRRIYAMKVLS---KKVIVAKKEVAHTIGER--NILvrtaldesPFIVGLKFSFQTPTDLYLVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA---V 296
Cdd:cd05586   76 DYMSGGELFWHLQKEGRFSEDRAKFYIAeLVLALEHLH--------KNDIVYRDLKPENILLDANGHIALCDFGLSkadL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIARRCSvggiveeyqlPYYdmvpsDP 376
Cdd:cd05586  148 TDNKTTNTF-------CGTTEYLAPEVLLDEKGYT-----KMVDFWSLGVLVFEMCCGWS----------PFY-----AE 200
                        250
                 ....*....|....*
gi 161333835 377 SIEEMRKVVCDQKFR 391
Cdd:cd05586  201 DTQQMYRNIAFGKVR 215
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
145-354 1.74e-07

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 52.32  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGED----VAVKIFS----SRDE-RSWFREAEIYQTvmLRHENILGFIAA--DNKDNGTW 213
Cdd:cd05075    2 LALGKTLGEGEFGSVMEGQLNQDDsvlkVAVKTMKiaicTRSEmEDFLSEAVCMKE--FDHPNVMRLIGVclQNTESEGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 TQLWLVSEYHEQGSLYDYLNRN-------IVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCET 286
Cdd:cd05075   80 PSPVVILPFMKHGDLHSFLLYSrlgdcpvYLPTQMLVKFMTDIASGMEYLSSK--------NFIHRDLAARNCMLNENMN 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 287 CAIADLGLAVKhdsILNTiDIPQNPKVGTK--RYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEIARR 354
Cdd:cd05075  152 VCVADFGLSKK---IYNG-DYYRQGRISKMpvKWIAIESLADRVYTT------KSDVWSFGVTMWEIATR 211
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
149-352 2.01e-07

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: 52.10  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSWFREA--EIYQTVMLRHENILGF---IAADNKdngtwtqLWLVSE 221
Cdd:cd07836    6 EKLGEGTYATVYKGrnRTTGEIVALKEIHLDAEEGTPSTAirEISLMKELKHENIVRLhdvIHTENK-------LMLVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQgSLYDYLNRNivTVAGMIKLAL------SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd07836   79 YMDK-DLKKYMDTH--GVRGALDPNTvksftyQLLKGIAFCH--------ENRVLHRDLKPQNLLINKRGELKLADFGLA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 296 vkhdsilNTIDIPQNP---KVGTKRYMAPEML--DDTMNVNIfesfkraDIYSVGLVYWEIA 352
Cdd:cd07836  148 -------RAFGIPVNTfsnEVVTLWYRAPDVLlgSRTYSTSI-------DIWSVGCIMAEMI 195
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
146-351 2.08e-07

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: 52.32  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWHGRWCGE--DVAVKIfsSRDERSW------------FREAEIYQtvMLRHENILGFIAADNKDNG 211
Cdd:cd13990    3 LLLNLLGKGGFSEVYKAFDLVEqrYVACKI--HQLNKDWseekkqnyikhaLREYEIHK--SLDHPRIVKLYDVFEIDTD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 212 TWTQlwlVSEYHEQGSLYDYLNRNivtvaGMI--KLALSI----ASGLAHLHmeivgtQGKPAIAHRDIKSKNILV---K 282
Cdd:cd13990   79 SFCT---VLEYCDGNDLDFYLKQH-----KSIpeREARSIimqvVSALKYLN------EIKPPIIHYDLKPGNILLhsgN 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 283 KCETCAIADLGLA--VKHDSILN-TIDIpQNPKVGTKRYMAPEMLDDTMNVNIFESfkRADIYSVGLVYWEI 351
Cdd:cd13990  145 VSGEIKITDFGLSkiMDDESYNSdGMEL-TSQGAGTYWYLPPECFVVGKTPPKISS--KVDVWSVGVIFYQM 213
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
152-351 2.25e-07

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: 51.89  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHGRwC---GEDVAVK----IFSSRDERSWFREAEiyqtVMLR---HENILGFIAA--DNKDNgtwtQLWLV 219
Cdd:cd07831    8 GEGTFSEVLKAQ-SrktGKYYAIKcmkkHFKSLEQVNNLREIQ----ALRRlspHPNILRLIEVlfDRKTG----RLALV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQgSLYDYL-NRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKcETCAIADLG---- 293
Cdd:cd07831   79 FELMDM-NLYELIkGRKRPLPEKRVKNYMyQLLKSLDHMH--------RNGIFHRDIKPENILIKD-DILKLADFGscrg 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 294 LAVKHdsilntidiPQNPKVGTKRYMAPE-MLDDTmnvniFESFKrADIYSVGLVYWEI 351
Cdd:cd07831  149 IYSKP---------PYTEYISTRWYRAPEcLLTDG-----YYGPK-MDIWAVGCVFFEI 192
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
136-373 2.36e-07

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: 51.97  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 136 LVQRTIARTIVLQEIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSW-FREAEIYQTVMLRHENILGFIAADNKDNgt 212
Cdd:cd06645    4 LSRRNPQEDFELIQRIGSGTYGDVYKARnvNTGELAAIKVIKLEPGEDFaVVQQEIIMMKDCKHSNIVAYFGSYLRRD-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 wtQLWLVSEYHEQGSLYD-YLNRNIVTVAGMIKLALSIASGLAHLHmeivgTQGKpaiAHRDIKSKNILVKKCETCAIAD 291
Cdd:cd06645   82 --KLWICMEFCGGGSLQDiYHVTGPLSESQIAYVSRETLQGLYYLH-----SKGK---MHRDIKGANILLTDNGHVKLAD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 292 LGLAVKHDSILNTidipQNPKVGTKRYMAPEM--LDDTMNVNifesfKRADIYSVGLVYWEIArrcsvggiveEYQLPYY 369
Cdd:cd06645  152 FGVSAQITATIAK----RKSFIGTPYWMAPEVaaVERKGGYN-----QLCDIWAVGITAIELA----------ELQPPMF 212

                 ....
gi 161333835 370 DMVP 373
Cdd:cd06645  213 DLHP 216
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
145-359 2.36e-07

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) 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. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. 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. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 52.31  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGE----DVAVKIF----SSRDERSWFREAEIYqTVMLRHENILGFIAADNKDNgtwtQL 216
Cdd:cd05088    9 IKFQDVIGEGNFGQVLKARIKKDglrmDAAIKRMkeyaSKDDHRDFAGELEVL-CKLGHHPNIINLLGACEHRG----YL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAH---LHMEIVGTQGKPAIA-----HRDIKSKNILVKKCETC 287
Cdd:cd05088   84 YLAIEYAPHGNLLDFLRKSrVLETDPAFAIANSTASTLSSqqlLHFAADVARGMDYLSqkqfiHRDLAARNILVGENYVA 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 288 AIADLGLAVKHDsilntIDIPQNPKVGTKRYMAPEmlddTMNVNIFESfkRADIYSVGLVYWEIArrcSVGG 359
Cdd:cd05088  164 KIADFGLSRGQE-----VYVKKTMGRLPVRWMAIE----SLNYSVYTT--NSDVWSYGVLLWEIV---SLGG 221
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
219-422 2.73e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 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: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 52.31  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDIKSKNILVKKCETCAIADLGLAVkh 298
Cdd:cd14207  159 LSDVEEEEEDSGDFYKRPLTMEDLISYSFQVARG-----MEFLSSR---KCIHRDLAARNILLSENNVVKICDFGLAR-- 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 dsilntiDIPQNPKVGTK-------RYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIArrcSVGGIveeyqlPYydm 371
Cdd:cd14207  229 -------DIYKNPDYVRKgdarlplKWMAPESIFD----KIYST--KSDVWSYGVLLWEIF---SLGAS------PY--- 283
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 372 vpsdPSIeEMRKVVCD---QKFRPSIPNQwqsceALRVMGRIMRECWYANGAAR 422
Cdd:cd14207  284 ----PGV-QIDEDFCSklkEGIRMRAPEF-----ATSEIYQIMLDCWQGDPNER 327
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
151-349 2.80e-07

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: 51.84  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEV--WHGRWCGEDVAVKI----FSSRDERSWFREAEIYQTvmLRHENILGFIAADNKDNGTWTQLWLVS-EYH 223
Cdd:cd14039    1 LGTGGFGNVclYQNQETGEKIAIKScrleLSVKNKDRWCHEIQIMKK--LNHPNVVKACDVPEEMNFLVNDVPLLAmEYC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNR--NIVTV--AGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCE---TCAIADLGLA- 295
Cdd:cd14039   79 SGGDLRKLLNKpeNCCGLkeSQVLSLLSDIGSGIQYLH--------ENKIIHRDLKPENIVLQEINgkiVHKIIDLGYAk 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 296 -VKHDSILNTIdipqnpkVGTKRYMAPEMLDDTMnvnifesfkradiYSVGLVYW 349
Cdd:cd14039  151 dLDQGSLCTSF-------VGTLQYLAPELFENKS-------------YTVTVDYW 185
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
166-347 2.85e-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: 51.74  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 166 GEDVAVKIFSSRDERSwfREAEIYQTVMLR----HENILGFIAADN---KDNGT-WTQLWLVSEYHEqGSLYDYLNRN-- 235
Cdd:cd14036   25 GKEYALKRLLSNEEEK--NKAIIQEINFMKklsgHPNIVQFCSAASigkEESDQgQAEYLLLTELCK-GQLVDFVKKVea 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 236 --IVTVAGMIKLALSIASGLAHLHMEivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVK-----------HDSIL 302
Cdd:cd14036  102 pgPFSPDTVLKIFYQTCRAVQHMHKQ------SPPIIHRDLKIENLLIGNQGQIKLCDFGSATTeahypdyswsaQKRSL 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 303 NTIDIPQNPkvgTKRYMAPEMLDDTMNVNIFEsfkRADIYSVGLV 347
Cdd:cd14036  176 VEDEITRNT---TPMYRTPEMIDLYSNYPIGE---KQDIWALGCI 214
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
149-347 3.37e-07

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: 51.26  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKI-----FSSRDERSWFREAEIYQTV----MLRHENILG-----FIAADnKDNGT 212
Cdd:cd14082    9 EVLGSGQFGIVYGGkhRKTGRDVAIKVidklrFPTKQESQLRNEVAILQQLshpgVVNLECMFEtpervFVVME-KLHGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WTQLWLVSEyheQGSLYDYLNRNIVTvagmiklalSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCE---TCAI 289
Cdd:cd14082   88 MLEMILSSE---KGRLPERITKFLVT---------QILVALRYLHSK--------NIVHCDLKPENVLLASAEpfpQVKL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 290 ADLGLA--VKHDSILNTIdipqnpkVGTKRYMAPEMLDDtmnvnifESFKRA-DIYSVGLV 347
Cdd:cd14082  148 CDFGFAriIGEKSFRRSV-------VGTPAYLAPEVLRN-------KGYNRSlDMWSVGVI 194
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
271-434 3.44e-07

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 52.21  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 271 HRDIKSKNILVKKCETCAIADLGLA--VKHDSilNTIdIPQNPKVGTKrYMAPEMLDDTmnVNIFESfkraDIYSVGLVY 348
Cdd:cd05104  237 HRDLAARNILLTHGRITKICDFGLArdIRNDS--NYV-VKGNARLPVK-WMAPESIFEC--VYTFES----DVWSYGILL 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 349 WEIArrcSVGgiveeyQLPYYDMvPSDPSIEEMRKvvcdQKFRPSIPnqwqSCEALRvMGRIMRECWYANGAARLTALRI 428
Cdd:cd05104  307 WEIF---SLG------SSPYPGM-PVDSKFYKMIK----EGYRMDSP----EFAPSE-MYDIMRSCWDADPLKRPTFKQI 367

                 ....*.
gi 161333835 429 KKTISQ 434
Cdd:cd05104  368 VQLIEQ 373
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
150-351 3.59e-07

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: 51.35  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGR-------WCGEDVAVKIFSSRDERSWFREAEIYQTvmLRHENILGFIAAdnkdngtW--------- 213
Cdd:cd14049   13 RLGKGGYGKVYKVRnkldgqyYAIKKILIKKVTKRDCMKVLREVKVLAG--LQHPNIVGYHTA-------Wmehvqlmly 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 --TQL-------WLVS------EYHEQGSLYDYLNRNIVTvagmiKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSK 277
Cdd:cd14049   84 iqMQLcelslwdWIVErnkrpcEEEFKSAPYTPVDVDVTT-----KILQQLLEGVTYIHsMGIV---------HRDLKPR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 278 NILVKKCE-TCAIADLGLAVKHDSILNTIDIPQNPK--------VGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVY 348
Cdd:cd14049  150 NIFLHGSDiHVRIGDFGLACPDILQDGNDSTTMSRLnglthtsgVGTCLYAAPEQLEGS------HYDFKSDMYSIGVIL 223

                 ...
gi 161333835 349 WEI 351
Cdd:cd14049  224 LEL 226
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
144-347 3.66e-07

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: 51.45  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVwHG---RWCGEDVAVKIFSSRDERSwfREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLW 217
Cdd:cd14193    5 NVNKEEILGGGRFGQV-HKceeKSSGLKLAAKIIKARSQKE--KEEvknEIEVMNQLNHANLIQLYDAFESRN----DIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYL---NRNIvTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCET--CAIADL 292
Cdd:cd14193   78 LVMEYVDGGELFDRIideNYNL-TELDTILFIKQICEGIQYMH--------QMYILHLDLKPENILCVSREAnqVKIIDF 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 293 GLAVKHDSilntidiPQNPKV--GTKRYMAPEMLDDTmnvniFESFKrADIYSVGLV 347
Cdd:cd14193  149 GLARRYKP-------REKLRVnfGTPEFLAPEVVNYE-----FVSFP-TDMWSLGVI 192
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
149-324 3.89e-07

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: 51.43  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW---HGRWcGEDVAVKIFSSRD------ERSWFREAEIYQtvMLRHENILGFIAA--DNKdngtwtQLW 217
Cdd:cd05580    7 KTLGTGSFGRVRlvkHKDS-GKYYALKILKKAKiiklkqVEHVLNEKRILS--EVRHPFIVNLLGSfqDDR------NLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:cd05580   78 MVMEYVPGGELFSLLRRSGRFPNDVAKFyAAEVVLALEYLHSL--------DIVYRDLKPENLLLDSDGHIKITDFGFAK 149
                        170       180
                 ....*....|....*....|....*...
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEML 324
Cdd:cd05580  150 RVKDRTYTL-------CGTPEYLAPEII 170
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
185-393 4.07e-07

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: 51.21  E-value: 4.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 185 EAEIYQTVMLRHENILGFIA---ADNKDNGTWTqLWLVSEYHEQGSLYDYLNR----NIVTVAGMiklALSIASGLAHLH 257
Cdd:cd14012   46 EKELESLKKLRHPNLVSYLAfsiERRGRSDGWK-VYLLTEYAPGGSLSELLDSvgsvPLDTARRW---TLQLLEALEYLH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 258 meivgTQGkpaIAHRDIKSKNILVKKCETCAIADLglavKHDSILNTI---------DIPQNPKvgtkrYMAPEMLDDTm 328
Cdd:cd14012  122 -----RNG---VVHKSLHAGNVLLDRDAGTGIVKL----TDYSLGKTLldmcsrgslDEFKQTY-----WLPPELAQGS- 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 329 nvniFESFKRADIYSVGLVYWEIarrcSVGG-IVEEYQLPYYDMVPS--DPSIEEM-RKVVC-DQKFRPS 393
Cdd:cd14012  184 ----KSPTRKTDVWDLGLLFLQM----LFGLdVLEKYTSPNPVLVSLdlSASLQDFlSKCLSlDPKKRPT 245
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
150-324 4.18e-07

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: 51.52  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGR--WCGEDVAVKIFSSRDerswfreaeiyqtvMLRHENILGFIAadNKD-----NGTW-TQL----- 216
Cdd:cd05573    8 VIGRGAFGEVWLVRdkDTGQVYAMKILRKSD--------------MLKREQIAHVRA--ERDiladaDSPWiVRLhyafq 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 -----WLVSEYHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCAI 289
Cdd:cd05573   72 dedhlYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAeLVLALDSLHkLGFI---------HRDIKPDNILLDADGHIKL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 290 ADLGLAVK----HDSILNTIDIPQNPK---------------------VGTKRYMAPEML 324
Cdd:cd05573  143 ADFGLCTKmnksGDRESYLNDSVNTLFqdnvlarrrphkqrrvraysaVGTPDYIAPEVL 202
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
216-354 4.33e-07

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L 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: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 51.40  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCE---TCAIADL 292
Cdd:cd13977  110 LWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLH--------RNQIVHRDLKPDNILISHKRgepILKVADF 181
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 293 GLAVKHDSILNTIDIPQN-------PKVGTKRYMAPEMLDDTMNVnifesfkRADIYSVGLVYWEIARR 354
Cdd:cd13977  182 GLSKVCSGSGLNPEEPANvnkhflsSACGSDFYMAPEVWEGHYTA-------KADIFALGIIIWAMVER 243
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
145-355 4.36e-07

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 51.52  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVwhgRWCGED-------------------VAVKIFSS---RDERSWFREaEIYQTVMLRHENILGF 202
Cdd:cd05097    7 LRLKEKLGEGQFGEV---HLCEAEglaeflgegapefdgqpvlVAVKMLRAdvtKTARNDFLK-EIKIMSRLKNPNIIRL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 203 IAADNKDNgtwtQLWLVSEYHEQGSLYDYLNR-----------NI--VTVAGMIKLALSIASGLAHLhmeivgtqGKPAI 269
Cdd:cd05097   83 LGVCVSDD----PLCMITEYMENGDLNQFLSQreiestfthanNIpsVSIANLLYMAVQIASGMKYL--------ASLNF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 270 AHRDIKSKNILVKKCETCAIADLGLAVK-HDSILNTIdipQNPKVGTKRYMAPEMLddtmnvnIFESFKRA-DIYSVGLV 347
Cdd:cd05097  151 VHRDLATRNCLVGNHYTIKIADFGMSRNlYSGDYYRI---QGRAVLPIRWMAWESI-------LLGKFTTAsDVWAFGVT 220

                 ....*...
gi 161333835 348 YWEIARRC 355
Cdd:cd05097  221 LWEMFTLC 228
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
151-345 4.47e-07

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: 51.53  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG--RWCGEDVAVK-----IFSSRDERSWFREAEIYQtvMLRHENILG----FIAADNKDNgtWTQLWLV 219
Cdd:cd07851   23 VGSGAYGQVCSAfdTKTGRKVAIKklsrpFQSAIHAKRTYRELRLLK--HMKHENVIGlldvFTPASSLED--FQDVYLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQgSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKK-CETcAIADLGLAVKH 298
Cdd:cd07851   99 THLMGA-DLNNIVKCQKLSDDHIQFLVYQILRGLKYIH--------SAGIIHRDLKPSNLAVNEdCEL-KILDFGLARHT 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 161333835 299 DSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNifesfKRADIYSVG 345
Cdd:cd07851  169 DDEMTGY-------VATRWYRAPEIMLNWMHYN-----QTVDIWSVG 203
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
194-390 4.70e-07

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: 51.15  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 194 LRHENILGFIaadnKDNGTWTQLWLVSEYHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHR 272
Cdd:cd14183   61 VKHPNIVLLI----EEMDMPTELYLVMELVKGGDLFDAItSTNKYTERDASGMLYNLASAIKYLH--------SLNIVHR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 273 DIKSKNILVKK----CETCAIADLGLAVKHDSILNTIdipqnpkVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVY 348
Cdd:cd14183  129 DIKPENLLVYEhqdgSKSLKLGDFGLATVVDGPLYTV-------CGTPTYVAPEIIAET------GYGLKVDIWAAGVIT 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 349 W----------------EIARRCSVGGIVeEYQLPYYDMVpSDPS---IEEMRKVVCDQKF 390
Cdd:cd14183  196 YillcgfppfrgsgddqEVLFDQILMGQV-DFPSPYWDNV-SDSAkelITMMLQVDVDQRY 254
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
192-435 4.84e-07

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 51.56  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 192 VMLRHENILGFIAADNKDNGTWTQLWLVSE---YHE-QGSLYD----YLNRNI--------------VTVAGMIKLALSI 249
Cdd:cd05105  167 VILSFENKGDYMDMKQADTTQYVPMLEIKEaskYSDiQRSNYDrpasYKGSNDsevknllsddgsegLTTLDLLSFTYQV 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 250 ASGlahlhMEIVGTQGkpaIAHRDIKSKNILVKKCETCAIADLGLA--VKHDSILntidIPQNPKVGTKRYMAPEMLDDt 327
Cdd:cd05105  247 ARG-----MEFLASKN---CVHRDLAARNVLLAQGKIVKICDFGLArdIMHDSNY----VSKGSTFLPVKWMAPESIFD- 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 328 mnvNIFESFkrADIYSVGLVYWEIArrcSVGGIveeyqlPYYDMVPSDPSIEEMRkvvcdQKFRPSIPNQwqsceALRVM 407
Cdd:cd05105  314 ---NLYTTL--SDVWSYGILLWEIF---SLGGT------PYPGMIVDSTFYNKIK-----SGYRMAKPDH-----ATQEV 369
                        250       260
                 ....*....|....*....|....*...
gi 161333835 408 GRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05105  370 YDIMVKCWNSEPEKRPSFLHLSDIVESL 397
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
163-351 4.98e-07

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: 51.18  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 163 RWCGEDVAVKIFSSRDERSwfREAEIYQTVMLR---HENIL----GFIAADnkdngtwtQLWLVSEYHEQGSLYDYLNRN 235
Cdd:cd06657   42 KSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRdyqHENVVemynSYLVGD--------ELWVVMEFLEGGALTDIVTHT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 236 IVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilntiDIPQNPK-VG 314
Cdd:cd06657  112 RMNEEQIAAVCLAVLKALSVLH-----AQG---VIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK-----EVPRRKSlVG 178
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 161333835 315 TKRYMAPEMlddtmnVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd06657  179 TPYWMAPEL------ISRLPYGPEVDIWSLGIMVIEM 209
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
147-393 5.22e-07

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: 50.79  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW--HGRWCGEDVAVKIF--------SSRDERSWfrEAEIYQTVMLRHENILGFIAADNkdNGTWTQL 216
Cdd:cd06653    6 LGKLLGRGAFGEVYlcYDADTGRELAVKQVpfdpdsqeTSKEVNAL--ECEIQLLKNLRHDRIVQYYGCLR--DPEEKKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHMEIvgtqgkpaIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd06653   82 SIFVEYMPGGSVKDQLKAyGALTENVTRRYTRQILQGVSYLHSNM--------IVHRDIKGANILRDSAGNVKLGDFGAS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTiDIPQNPKVGTKRYMAPEMLDDtmnvnifESF-KRADIYSVGLVYWEI-------ARRCSVGGIVEEYQLP 367
Cdd:cd06653  154 KRIQTICMS-GTGIKSVTGTPYWMSPEVISG-------EGYgRKADVWSVACTVVEMltekppwAEYEAMAAIFKIATQP 225
                        250       260
                 ....*....|....*....|....*....
gi 161333835 368 YYDMVP---SDPSIEEMRKVVCDQKFRPS 393
Cdd:cd06653  226 TKPQLPdgvSDACRDFLRQIFVEEKRRPT 254
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
151-383 5.59e-07

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: 51.28  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWH---GRwCGEDVAVK--------IFSSRdeRSwFREAEiyqtvML---RHENILGFI-AADNKDNGTWTQ 215
Cdd:cd07853    8 IGYGAFGVVWSvtdPR-DGKRVALKkmpnvfqnLVSCK--RV-FRELK-----MLcffKHDNVLSALdILQPPHIDPFEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHeQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd07853   79 IYVVTELM-QSDLHKIIVSPQPLSSDHVKVFLyQILRGLKYLH--------SAGILHRDIKPGNLLVNSNCVLKICDFGL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 295 AVKHDsilntIDIPQN--PKVGTKRYMAPEMLddtMNVNIFESfkRADIYSVGLVYWE-IARRcsvggIVEEYQLPY--Y 369
Cdd:cd07853  150 ARVEE-----PDESKHmtQEVVTQYYRAPEIL---MGSRHYTS--AVDIWSVGCIFAElLGRR-----ILFQAQSPIqqL 214
                        250
                 ....*....|....*..
gi 161333835 370 DMVPS---DPSIEEMRK 383
Cdd:cd07853  215 DLITDllgTPSLEAMRS 231
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
150-324 5.74e-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: 50.96  E-value: 5.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWF-----REAEIYQtvMLRHENILGF--IAADN-------KDNGTW 213
Cdd:cd07864   14 IIGEGTYGQVYKAKdkDTGELVALKKVRLDNEKEGFpitaiREIKILR--QLNHRSVVNLkeIVTDKqdaldfkKDKGAF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 tqlWLVSEYHEQgSLYDYLNRNIVT-----VAGMIKLALSiasGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCA 288
Cdd:cd07864   92 ---YLVFEYMDH-DLMGLLESGLVHfsedhIKSFMKQLLE---GLNYCH--------KKNFLHRDIKCSNILLNNKGQIK 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 161333835 289 IADLGLAvkhdSILNTIDI-PQNPKVGTKRYMAPEML 324
Cdd:cd07864  157 LADFGLA----RLYNSEESrPYTNKVITLWYRPPELL 189
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
149-422 6.92e-07

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) 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. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR 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: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 50.79  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIFSSRDErswFREA-----------EIYqtVMLRHEN-----ILGFIAAdnkdngt 212
Cdd:cd05108   13 KVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE---LREAtspkankeildEAY--VMASVDNphvcrLLGICLT------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 wTQLWLVSEYHEQGSLYDYLNRNIVTVAG--MIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIA 290
Cdd:cd05108   81 -STVQLITQLMPFGCLLDYVREHKDNIGSqyLLNWCVQIAKGMNYLE--------DRRLVHRDLAARNVLVKTPQHVKIT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 291 DLGLAVkhdsiLNTIDIPQNPKVGTK---RYMAPE-MLDDTMNvnifesfKRADIYSVGLVYWEIArrcsvggiveEYQL 366
Cdd:cd05108  152 DFGLAK-----LLGAEEKEYHAEGGKvpiKWMALEsILHRIYT-------HQSDVWSYGVTVWELM----------TFGS 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 367 PYYDMVPSdpsiEEMRKVVCDQKFRPSIPnqwqSCEALRVMgrIMRECWYANGAAR 422
Cdd:cd05108  210 KPYDGIPA----SEISSILEKGERLPQPP----ICTIDVYM--IMVKCWMIDADSR 255
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
187-352 8.74e-07

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: 50.43  E-value: 8.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 187 EIYQTVMLRHE----NILGFIAADNKDNgtwtQLWLVSEYHEQGSLyDYLNRNIVTVAGMI--KLALSIASGLAHLhmei 260
Cdd:cd06649   49 QIIRELQVLHEcnspYIVGFYGAFYSDG----EISICMEHMDGGSL-DQVLKEAKRIPEEIlgKVSIAVLRGLAYL---- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 261 vgtQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsilnTIDIPQNPKVGTKRYMAPEMLDDTmnvnifESFKRAD 340
Cdd:cd06649  120 ---REKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQ------LIDSMANSFVGTRSYMSPERLQGT------HYSVQSD 184
                        170
                 ....*....|..
gi 161333835 341 IYSVGLVYWEIA 352
Cdd:cd06649  185 IWSMGLSLVELA 196
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
151-395 9.20e-07

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: 50.43  E-value: 9.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVwhgrwCG-------EDVAVKIFSsRDERSWFREAEIYQTVML----RHENILG----FIAADNKDNgtWTQ 215
Cdd:cd07878   23 VGSGAYGSV-----CSaydtrlrQKVAVKKLS-RPFQSLIHARRTYRELRLlkhmKHENVIGlldvFTPATSIEN--FNE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSeyheqgSLYDYLNRNIVTVAGMIK-----LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKK-CETcAI 289
Cdd:cd07878   95 VYLVT------NLMGADLNNIVKCQKLSDehvqfLIYQLLRGLKYIH--------SAGIIHRDLKPSNVAVNEdCEL-RI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 290 ADLGLAVKHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIARrcsvGGIV---EEY-- 364
Cdd:cd07878  160 LDFGLARQADDEMTGY-------VATRWYRAPEIMLNWMHYN-----QTVDIWSVGCIMAELLK----GKALfpgNDYid 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 161333835 365 QLPYYDMVPSDPSIEEMRKVVCD--QKFRPSIP 395
Cdd:cd07878  224 QLKRIMEVVGTPSPEVLKKISSEhaRKYIQSLP 256
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
149-324 9.62e-07

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: 50.40  E-value: 9.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDV--AVKIFSSRDERSWFREAEIYQTVMLRHENILG-FIAADNKDNGTWTQLWLVSEYHEQ 225
Cdd:cd05602   13 KVIGKGSFGKVLLARHKSDEKfyAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHpFLVGLHFSFQTTDKLYFVLDYING 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 GSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA---VKHDSI 301
Cdd:cd05602   93 GELFYHLQRERCFLEPRARFyAAEIASALGYLH--------SLNIVYRDLKPENILLDSQGHIVLTDFGLCkenIEPNGT 164
                        170       180
                 ....*....|....*....|...
gi 161333835 302 LNTIdipqnpkVGTKRYMAPEML 324
Cdd:cd05602  165 TSTF-------CGTPEYLAPEVL 180
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
149-370 9.72e-07

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: 50.41  E-value: 9.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW--HGRWCGEDVAVKIFS-----SRDERSW-FREAEIYQTVmlRHEnilgFIAADNKDNGTWTQLWLVS 220
Cdd:cd05594   31 KLLGKGTFGKVIlvKEKATGRYYAMKILKkevivAKDEVAHtLTENRVLQNS--RHP----FLTALKYSFQTHDRLCFVM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHMEivgtqgkPAIAHRDIKSKNILVKKCETCAIADLGL---AV 296
Cdd:cd05594  105 EYANGGELFFHLSRERVFSEDRARFyGAEIVSALDYLHSE-------KNVVYRDLKLENLMLDKDGHIKITDFGLckeGI 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEMLDDTmnvnifeSFKRA-DIYSVGLVYWEIArrCSvggiveeyQLPYYD 370
Cdd:cd05594  178 KDGATMKTF-------CGTPEYLAPEVLEDN-------DYGRAvDWWGLGVVMYEMM--CG--------RLPFYN 228
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
147-350 9.92e-07

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 50.95  E-value: 9.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRwC---GEDVAVKIFSS---RDE----RswF-REAeiyQTVM-LRHENIL-----GfiaadnKD 209
Cdd:NF033483  11 IGERIGRGGMAEVYLAK-DtrlDRDVAVKVLRPdlaRDPefvaR--FrREA---QSAAsLSHPNIVsvydvG------ED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 210 NGtwtQLWLVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETC 287
Cdd:NF033483  79 GG---IPYIVMEYVDGRTLKDYIREHgPLSPEEAVEIMIQILSALEHAHrNGIV---------HRDIKPQNILITKDGRV 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 288 AIADLGLAVkhdsILNTIDIPQNPKV-GTKRYMAPE-----MLDdtmnvnifesfKRADIYSVGLVYWE 350
Cdd:NF033483 147 KVTDFGIAR----ALSSTTMTQTNSVlGTVHYLSPEqarggTVD-----------ARSDIYSLGIVLYE 200
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
150-324 1.05e-06

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: 50.48  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW-----HGRWCGEDVAVKIFssrderswfREAEIYQ----TVMLRHE-NILG-----FIAADNKDNGTWT 214
Cdd:cd05584    3 VLGKGGYGKVFqvrktTGSDKGKIFAMKVL---------KKASIVRnqkdTAHTKAErNILEavkhpFIVDLHYAFQTGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 QLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd05584   74 KLYLILEYLSGGELFMHLEREGIFMEDTACFYLAeITLALGHLH-----SLG---IIYRDLKPENILLDAQGHVKLTDFG 145
                        170       180       190
                 ....*....|....*....|....*....|....
gi 161333835 294 L---AVKHDSILNTIdipqnpkVGTKRYMAPEML 324
Cdd:cd05584  146 LckeSIHDGTVTHTF-------CGTIEYMAPEIL 172
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
143-354 1.11e-06

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 49.92  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGED-----VAVK-----IFSSRDERSWFREAEIYQTvmLRHENILGFIAAD--NKDN 210
Cdd:cd05074    9 QQFTLGRMLGKGEFGSVREAQLKSEDgsfqkVAVKmlkadIFSSSDIEEFLREAACMKE--FDHPNVIKLIGVSlrSRAK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 211 GTWTQLWLVSEYHEQGSLYDYL-------NRNIVTVAGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDIKSKNILVKK 283
Cdd:cd05074   87 GRLPIPMVILPFMKHGDLHTFLlmsrigeEPFTLPLQTLVRFMIDIASGMEYL--------SSKNFIHRDLAARNCMLNE 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 284 CETCAIADLGLAVKhdsILNTIDIPQN--PKVGTKrYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIARR 354
Cdd:cd05074  159 NMTVCVADFGLSKK---IYSGDYYRQGcaSKLPVK-WLALESLAD----NVYTT--HSDVWAFGVTMWEIMTR 221
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
146-294 1.13e-06

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 50.03  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVwH------------GRWCGED-------VAVKIF---SSRDERSWFREaEIYQTVMLRHENILGFI 203
Cdd:cd05051    8 EFVEKLGEGQFGEV-HlceanglsdltsDDFIGNDnkdepvlVAVKMLrpdASKNAREDFLK-EVKIMSQLKDPNIVRLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 204 AADNKDNgtwtQLWLVSEYHEQGSLYDYL-------------NRNIVTVAGMIKLALSIASGLAHL-HMEIVgtqgkpai 269
Cdd:cd05051   86 GVCTRDE----PLCMIVEYMENGDLNQFLqkheaetqgasatNSKTLSYGTLLYMATQIASGMKYLeSLNFV-------- 153
                        170       180
                 ....*....|....*....|....*
gi 161333835 270 aHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd05051  154 -HRDLATRNCLVGPNYTIKIADFGM 177
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
216-351 1.17e-06

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: 50.19  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQgSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVK----KCETCAIAD 291
Cdd:cd14018  115 LFLVMKNYPC-TLRQYLWVNTPSYRLARVMILQLLEGVDHLV--------RHGIAHRDLKSDNILLEldfdGCPWLVIAD 185
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 292 LGLAVKHDSILNTIDIPQN--PKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd14018  186 FGCCLADDSIGLQLPFSSWyvDRGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEI 247
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
151-351 1.28e-06

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: 50.04  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG--RWCGEDVAVKIFSsRDERSWFREAEIYQTVML----RHENILGF--IAADNKDNGTWTQLWLVSey 222
Cdd:cd07877   25 VGSGAYGSVCAAfdTKTGLRVAVKKLS-RPFQSIIHAKRTYRELRLlkhmKHENVIGLldVFTPARSLEEFNDVYLVT-- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSlydYLNrNIVTVAGMIK-----LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKK-CETcAIADLGLAv 296
Cdd:cd07877  102 HLMGA---DLN-NIVKCQKLTDdhvqfLIYQILRGLKYIH--------SADIIHRDLKPSNLAVNEdCEL-KILDFGLA- 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 297 KHdsilntIDIPQNPKVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEI 351
Cdd:cd07877  168 RH------TDDEMTGYVATRWYRAPEIMLNWMHYN-----QTVDIWSVGCIMAEL 211
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
150-351 1.32e-06

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) 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. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 49.64  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRWC--GED----VAVKIF----SSRDERSWFREAEIYQTVMLRH-ENILGFIAAdnkdngtwTQLWL 218
Cdd:cd05109   14 VLGSGAFGTVYKGIWIpdGENvkipVAIKVLrentSPKANKEILDEAYVMAGVGSPYvCRLLGICLT--------STVQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:cd05109   86 VTQLMPYGCLLDYVreNKDRIGSQDLLNWCVQIAKGMSYLE--------EVRLVHRDLAARNVLVKSPNHVKITDFGLAR 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 297 KHDsilntIDIPQNPKVGTK---RYMAPEMLddtmnvnIFESFK-RADIYSVGLVYWEI 351
Cdd:cd05109  158 LLD-----IDETEYHADGGKvpiKWMALESI-------LHRRFThQSDVWSYGVTVWEL 204
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
149-351 1.52e-06

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: 49.54  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDERSwfREAEIYQTVMLR---HENILGFIaaDNKDNGTwtQLWLVSEYH 223
Cdd:cd06647   13 EKIGQGASGTVYTAidVATGQEVAIKQMNLQQQPK--KELIINEILVMRenkNPNIVNYL--DSYLVGD--ELWVVMEYL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVKKCETCAIADLGLAVkhdsiln 303
Cdd:cd06647   87 AGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQV--------IHRDIKSDNILLGMDGSVKLTDFGFCA------- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 304 TIDIPQNPK---VGTKRYMAPEMlddtmnVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd06647  152 QITPEQSKRstmVGTPYWMAPEV------VTRKAYGPKVDIWSLGIMAIEM 196
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
143-404 1.53e-06

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: 49.39  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEV--WHGRWCGEDVAVKIFSSRD------ERSWFREAEIYqtVMLRHENILG----FIAADNKdn 210
Cdd:cd14165    1 RGYILGINLGEGSYAKVksAYSERLKCNVAIKIIDKKKapddfvEKFLPRELEIL--ARLNHKSIIKtyeiFETSDGK-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 211 gtwtqLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAI 289
Cdd:cd14165   77 -----VYIVMELGVQGDLLEFIKLRGALPEDVARKMFhQLSSAIKYCH--------ELDIVHRDLKCENLLLDKDFNIKL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 290 ADLGLAVKHDSILNTIDIPQNPKVGTKRYMAPEMLDdtmnvNIFESFKRADIYSVGLVYWEIArrCSvggiveeyQLPYy 369
Cdd:cd14165  144 TDFGFSKRCLRDENGRIVLSKTFCGSAAYAAPEVLQ-----GIPYDPRIYDIWSLGVILYIMV--CG--------SMPY- 207
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 161333835 370 dmvpSDPSIEEMRKVVCDQKFR-PSIPNQWQSCEAL 404
Cdd:cd14165  208 ----DDSNVKKMLKIQKEHRVRfPRSKNLTSECKDL 239
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
151-357 1.76e-06

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 49.50  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGEDVAVKIFSSRDERSW-------FREAEIYQtvMLRHENILGFIAADNKDNgtwtQLWLVSEYH 223
Cdd:cd14160    1 IGEGEIFEVYRVRIGNRSYAVKLFKQEKKMQWkkhwkrfLSELEVLL--LFQHPNILELAAYFTETE----KFCLVYPYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALSIASGLA----HLHmeivgTQGKPAIAHRDIKSKNILVKKCETCAIADLGLA-VKH 298
Cdd:cd14160   75 QNGTLFDRLQCHGVTKPLSWHERINILIGIAkaihYLH-----NSQPCTVICGNISSANILLDDQMQPKLTDFALAhFRP 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 299 DSILNTIDIPQNPKVGTKRYMAPE--MLDDTMNVnifesfkRADIYSVGLVYWEIARRCSV 357
Cdd:cd14160  150 HLEDQSCTINMTTALHKHLWYMPEeyIRQGKLSV-------KTDVYSFGIVIMEVLTGCKV 203
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
150-326 1.96e-06

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: 49.22  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW--HGRWCGEDVAVK------IFSSRDERSWFREAEIYQTVMLRHENILGFiAADNKDngtwtQLWLVSE 221
Cdd:cd05631    7 VLGKGGFGEVCacQVRATGKMYACKklekkrIKKRKGEAMALNEKRILEKVNSRFVVSLAY-AYETKD-----ALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSL----YDYLNRNIVTVAGMIkLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd05631   81 IMNGGDLkfhiYNMGNPGFDEQRAIF-YAAELCCGLEDLQRE--------RIVYRDLKPENILLDDRGHIRISDLGLAVQ 151
                        170       180       190
                 ....*....|....*....|....*....|...
gi 161333835 298 hdsilntidIPQNP----KVGTKRYMAPEMLDD 326
Cdd:cd05631  152 ---------IPEGEtvrgRVGTVGYMAPEVINN 175
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
145-434 1.98e-06

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (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, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 49.26  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCG-------EDVAVKIF----SSRDERSWFREAEIYQTVMLRHE-NILGFIAADNKDngt 212
Cdd:cd05062    8 ITMSRELGQGSFGMVYEGIAKGvvkdepeTRVAIKTVneaaSMRERIEFLNEASVMKEFNCHHVvRLLGVVSQGQPT--- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 wtqlWLVSEYHEQGSLYDYLN-----------RNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILV 281
Cdd:cd05062   85 ----LVIMELMTRGDLKSYLRslrpemennpvQAPPSLKKMIQMAGEIADGMAYLNAN--------KFVHRDLAARNCMV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 282 KKCETCAIADLGLavkhdsilnTIDIPQNP--KVGTK-----RYMAPEMLDDtmnvNIFESFkrADIYSVGLVYWEIARr 354
Cdd:cd05062  153 AEDFTVKIGDFGM---------TRDIYETDyyRKGGKgllpvRWMSPESLKD----GVFTTY--SDVWSFGVVLWEIAT- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 355 csvggIVEEyqlPYYDMvpsdpSIEEMRKVVCDQkfrpSIPNQWQSCEALrvMGRIMRECWYANGAARLTALRIKKTISQ 434
Cdd:cd05062  217 -----LAEQ---PYQGM-----SNEQVLRFVMEG----GLLDKPDNCPDM--LFELMRMCWQYNPKMRPSFLEIISSIKE 277
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
147-351 2.12e-06

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 49.09  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIvGKGRFGEVWHGR-WCGEDVAVKIF-------SSRDERSWFREAEIYQtvMLRHENILGFIaadnkdnGTWTQ--- 215
Cdd:cd05086    2 IQEI-GNGWFGKVLLGEiYTGTSVARVVVkelkasaNPKEQDDFLQQGEPYY--ILQHPNILQCV-------GQCVEaip 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRNIVTVAG------MIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAI 289
Cdd:cd05086   72 YLLVFEFCDLGDLKTYLANQQEKLRGdsqimlLQRMACEIAAGLAHMH--------KHNFLHSDLALRNCYLTSDLTVKV 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 290 ADLGLA---VKHDSILNTIDipqnpKVGTKRYMAPEMLDDTMN-VNIFESFKRADIYSVGLVYWEI 351
Cdd:cd05086  144 GDYGIGfsrYKEDYIETDDK-----KYAPLRWTAPELVTSFQDgLLAAEQTKYSNIWSLGVTLWEL 204
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
145-435 2.15e-06

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 49.16  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRWCGED-----VAVKI-----FSSRDERSWFREAEIYQTvmLRHENILGFIAA-DNKDNGTW 213
Cdd:cd14204    9 LSLGKVLGEGEFGSVMEGELQQPDgtnhkVAVKTmkldnFSQREIEEFLSEAACMKD--FNHPNVIRLLGVcLEVGSQRI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 TQLWLVSEYHEQGSLYDYLNRN-------IVTVAGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDIKSKNILVKKCET 286
Cdd:cd14204   87 PKPMVILPFMKYGDLHSFLLRSrlgsgpqHVPLQTLLKFMIDIALGMEYL--------SSRNFLHRDLAARNCMLRDDMT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 287 CAIADLGLAVKhdsiLNTIDIPQNPKVGTK--RYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEIARRcsvgGIVeey 364
Cdd:cd14204  159 VCVADFGLSKK----IYSGDYYRQGRIAKMpvKWIAVESLAD----RVYTV--KSDVWAFGVTMWEIATR----GMT--- 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 365 qlPYydmvPSDPSIEEMRKVVCDQKFRpsipnqwQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14204  222 --PY----PGVQNHEIYDYLLHGHRLK-------QPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKL 279
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
147-353 2.29e-06

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: 49.28  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSRdeRSWFREAEiyqTVMLRHENILG--------FIAADNKDNGTWTQL 216
Cdd:cd14223    4 VHRIIGRGGFGEVYGCRKAdtGKMYAMKCLDKK--RIKMKQGE---TLALNERIMLSlvstgdcpFIVCMSYAFHTPDKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd14223   79 SFILDLMNGGDLHYHLSQHgVFSEAEMRFYAAEIILGLEHMHSRFV--------VYRDLKPANILLDEFGHVRISDLGLA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 296 VKHDSilntidIPQNPKVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIAR 353
Cdd:cd14223  151 CDFSK------KKPHASVGTHGYMAPEVLQKGVAYD-----SSADWFSLGCMLFKLLR 197
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
149-354 2.33e-06

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: 48.83  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVK-I-FSSRDE---RSWFREAEIYQtvMLRHENI---LGFIAADNKdngtwtqLWL 218
Cdd:cd07835    5 EKIGEGTYGVVYKARdkLTGEIVALKkIrLETEDEgvpSTAIREISLLK--ELNHPNIvrlLDVVHSENK-------LYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQgSLYDYLNRNIVTVAG--MIKLALS-IASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd07835   76 VFEFLDL-DLKKYMDSSPLTGLDppLIKSYLYqLLQGIAFCHSH--------RVLHRDLKPQNLLIDTEGALKLADFGLA 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 296 vkhdsilNTIDIPQNP---KVGTKRYMAPEMLDDTmnvnifESFKRA-DIYSVGLVYWEIARR 354
Cdd:cd07835  147 -------RAFGVPVRTythEVVTLWYRAPEILLGS------KHYSTPvDIWSVGCIFAEMVTR 196
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
169-382 2.37e-06

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 49.22  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 169 VAVKIF---SSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSEYHEQGSLYDYLNRNIVTvaGMIKL 245
Cdd:cd08216   28 VAVKKInleSDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDN----DLYVVTPLMAYGSCRDLLKTHFPE--GLPEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 246 ALS-----IASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA---VKHDSILNTIDIPqnPKVGTKR 317
Cdd:cd08216  102 AIAfilrdVLNALEYIH--------SKGYIHRSVKASHILISGDGKVVLSGLRYAysmVKHGKRQRVVHDF--PKSSEKN 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 318 --YMAPEMLDDtmnvNIFESFKRADIYSVGLVYWEIArrcsvGGIVeeyqlPYYDMVPSDPSIEEMR 382
Cdd:cd08216  172 lpWLSPEVLQQ----NLLGYNEKSDIYSVGITACELA-----NGVV-----PFSDMPATQMLLEKVR 224
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
192-351 2.37e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 49.37  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 192 VM--LRHENILGFIAADNKDNgtwtQLWLVSEYHEqGSLYDYLNRNIVTVAGMIK-LALSIASGLAHLHmeivgtqgKPA 268
Cdd:PTZ00024  73 IMneIKHENIMGLVDVYVEGD----FINLVMDIMA-SDLKKVVDRKIRLTESQVKcILLQILNGLNVLH--------KWY 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 269 IAHRDIKSKNILVKKCETCAIADLGLAVK--HDSILNTIDIPQN--------PKVGTKRYMAPEMLddtMNVNIFESfkR 338
Cdd:PTZ00024 140 FMHRDLSPANIFINSKGICKIADFGLARRygYPPYSDTLSKDETmqrreemtSKVVTLWYRAPELL---MGAEKYHF--A 214
                        170
                 ....*....|...
gi 161333835 339 ADIYSVGLVYWEI 351
Cdd:PTZ00024 215 VDMWSVGCIFAEL 227
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
150-351 2.41e-06

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: 48.82  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGE---VWH----GRWCGEDVAVKIFSSRDERSwfREAEIYQTVMlRHENILGFIAADNKDNgtwtQLWLVSEY 222
Cdd:cd08219    7 VVGEGSFGRallVQHvnsdQKYAMKEIRLPKSSSAVEDS--RKEAVLLAKM-KHPNIVAFKESFEADG----HLYIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRN---IVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhd 299
Cdd:cd08219   80 CDGGDLMQKIKLQrgkLFPEDTILQWFVQMCLGVQHIH--------EKRVLHRDIKSKNIFLTQNGKVKLGDFGSA---- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161333835 300 SILNTIDIPQNPKVGTKRYMAPEMLDDtMNVNifesfKRADIYSVGLVYWEI 351
Cdd:cd08219  148 RLLTSPGAYACTYVGTPYYVPPEIWEN-MPYN-----NKSDIWSLGCILYEL 193
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
166-353 2.45e-06

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: 49.33  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 166 GEDVAVKIFS------SRDERSwFREAEIYQTVmlRHENILGFIAA--DNKDNGTWTQLWLVSEYheqgslydyLNRNIV 237
Cdd:cd07850   25 GQNVAIKKLSrpfqnvTHAKRA-YRELVLMKLV--NHKNIIGLLNVftPQKSLEEFQDVYLVMEL---------MDANLC 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 238 TVAGMI-------KLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA-VKHDSILNTidipq 309
Cdd:cd07850   93 QVIQMDldhermsYLLYQMLCGIKHLH--------SAGIIHRDLKPSNIVVKSDCTLKILDFGLArTAGTSFMMT----- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 161333835 310 nPKVGTKRYMAPEM---LDDTMNVnifesfkraDIYSVGLVYWEIAR 353
Cdd:cd07850  160 -PYVVTRYYRAPEVilgMGYKENV---------DIWSVGCIMGEMIR 196
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
151-324 2.51e-06

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: 48.66  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWC--GEDVAVKIFSSRDER-------SWFREAEIYQtvMLRHENILGFIAADNKDNgtwtQLWLVSE 221
Cdd:cd14070   10 LGEGSFAKVREGLHAvtGEKVAIKVIDKKKAKkdsyvtkNLRREGRIQQ--MIRHPNITQLLDILETEN----SYYLVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhds 300
Cdd:cd14070   84 LCPGGNLMHRIyDKKRLEEREARRYIRQLVSAVEHLH--------RAGVVHRDLKIENLLLDENDNIKLIDFGLS----- 150
                        170       180
                 ....*....|....*....|....*....
gi 161333835 301 ilNTIDI-----PQNPKVGTKRYMAPEML 324
Cdd:cd14070  151 --NCAGIlgysdPFSTQCGSPAYAAPELL 177
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
150-326 2.59e-06

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: 48.87  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW--HGRWCGEDVAVK------IFSSRDERSWFREAEIYQTVMLRHENILGFiAADNKDngtwtQLWLVSE 221
Cdd:cd05630    7 VLGKGGFGEVCacQVRATGKMYACKklekkrIKKRKGEAMALNEKQILEKVNSRFVVSLAY-AYETKD-----ALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRniVTVAGM-----IKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAV 296
Cdd:cd05630   81 LMNGGDLKFHIYH--MGQAGFpearaVFYAAEICCGLEDLHRE--------RIVYRDLKPENILLDDHGHIRISDLGLAV 150
                        170       180       190
                 ....*....|....*....|....*....|
gi 161333835 297 kHDSILNTIdipqNPKVGTKRYMAPEMLDD 326
Cdd:cd05630  151 -HVPEGQTI----KGRVGTVGYMAPEVVKN 175
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
147-393 2.65e-06

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: 48.50  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW--HGRWCGEDVAVKIF--------SSRDERSWfrEAEIYQTVMLRHENILGFIAAdNKDNGTWTqL 216
Cdd:cd06652    6 LGKLLGQGAFGRVYlcYDADTGRELAVKQVqfdpespeTSKEVNAL--ECEIQLLKNLLHERIVQYYGC-LRDPQERT-L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHMEIvgtqgkpaIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd06652   82 SIFMEYMPGGSIKDQLKSyGALTENVTRKYTRQILEGVHYLHSNM--------IVHRDIKGANILRDSVGNVKLGDFGAS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKhdsiLNTIDIP---QNPKVGTKRYMAPEMLDDtmnvnifESFKR-ADIYSVGLVYWEI-------ARRCSVGGIVEEY 364
Cdd:cd06652  154 KR----LQTICLSgtgMKSVTGTPYWMSPEVISG-------EGYGRkADIWSVGCTVVEMltekppwAEFEAMAAIFKIA 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 161333835 365 QLPYYDMVP---SDPSIEEMRKVVCDQKFRPS 393
Cdd:cd06652  223 TQPTNPQLPahvSDHCRDFLKRIFVEAKLRPS 254
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
246-326 3.37e-06

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: 48.81  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 246 ALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsilntidIPQNP----KVGTKRYMAP 321
Cdd:cd05632  110 AAEILCGLEDLHRE--------NTVYRDLKPENILLDDYGHIRISDLGLAVK---------IPEGEsirgRVGTVGYMAP 172

                 ....*
gi 161333835 322 EMLDD 326
Cdd:cd05632  173 EVLNN 177
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
154-347 3.55e-06

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: 48.30  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 154 GRF---GEVWHGRWC------------GEDVAVKIFS-SRDERSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLW 217
Cdd:cd14112    3 GRFsfgSEIFRGRFSvivkavdsttetDAHCAVKIFEvSDEASEAVREFESLRT--LQHENVQRLIAAFKPSN----FAY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEyHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHMEivgtqgkpAIAHRDIKSKNILV--KKCETCAIADLGL 294
Cdd:cd14112   77 LVME-KLQEDVFTRFSSNDYYSEEQVATTVRqILDALHYLHFK--------GIAHLDVQPDNIMFqsVRSWQVKLVDFGR 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 295 AVKHDSILNTidipqnPKVGTKRYMAPEMLDDTMNVnifesFKRADIYSVGLV 347
Cdd:cd14112  148 AQKVSKLGKV------PVDGDTDWASPEFHNPETPI-----TVQSDIWGLGVL 189
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
215-399 3.71e-06

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: 48.23  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 QLWLVSEYHEQGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCE---TCAIA 290
Cdd:cd14171   83 RLLIVMELMEGGELFDRISQHRhFTEKQAAQYTKQIALAVQHCHSL--------NIAHRDLKPENLLLKDNSedaPIKLC 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 291 DLGLAVKHDSILNTidiPQNpkvgTKRYMAPEMLDdtmnVNIFESFKRADIYSVGLVYWeIARRC---SVGGIVeeYQL- 366
Cdd:cd14171  155 DFGFAKVDQGDLMT---PQF----TPYYVAPQVLE----AQRRHRKERSGIPTSPTPYT-YDKSCdmwSLGVII--YIMl 220
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 161333835 367 ----PYYDMVPSDPSIEEMRKVVCDQKFR-PSipNQWQ 399
Cdd:cd14171  221 cgypPFYSEHPSRTITKDMKRKIMTGSYEfPE--EEWS 256
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
149-352 4.18e-06

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: 48.20  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG--RWCGEDVAVKIFSSRDE-----RSWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLWLVSE 221
Cdd:cd07839    6 EKIGEGTYGTVFKAknRETHEIVALKRVRLDDDdegvpSSALREICLLKE--LKHKNIVRLYDVLHSDK----KLTLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQG------SLYDYLNRNIVTvagmiKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd07839   80 YCDQDlkkyfdSCNGDIDPEIVK-----SFMFQLLKGLAFCHSH--------NVLHRDLKPQNLLINKNGELKLADFGLA 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 vkhdsilNTIDIP---QNPKVGTKRYMAPEMLddtMNVNIFESfkRADIYSVGLVYWEIA 352
Cdd:cd07839  147 -------RAFGIPvrcYSAEVVTLWYRPPDVL---FGAKLYST--SIDMWSAGCIFAELA 194
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
149-349 4.62e-06

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: 48.03  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHgrwCGE-----DVAVKIFSSRDERSwfREA---EIYQTVMLRHENILG-FIAADNKDNGTwtqlwLV 219
Cdd:cd14192   10 EVLGGGRFGQVHK---CTElstglTLAAKIIKVKGAKE--REEvknEINIMNQLNHVNLIQlYDAFESKTNLT-----LI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHMEIvgtqgkpaIAHRDIKSKNILV--KKCETCAIADLGLA 295
Cdd:cd14192   80 MEYVDGGELFDRItdESYQLTELDAILFTRQICEGVHYLHQHY--------ILHLDLKPENILCvnSTGNQIKIIDFGLA 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 296 VKHDSilntidiPQNPKV--GTKRYMAPEMLDDTmnvniFESFKrADIYSVGLVYW 349
Cdd:cd14192  152 RRYKP-------REKLKVnfGTPEFLAPEVVNYD-----FVSFP-TDMWSVGVITY 194
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
151-351 5.23e-06

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: 47.75  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW--HGRWCGEDVAVKIFSSRDERSWFREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSEYHEQ 225
Cdd:cd07847    9 IGEGSYGVVFkcRNRETGQIVAIKKFVESEDDPVIKKIalrEIRMLKQLKHPNLVNLIEVFRRKR----KLHLVFEYCDH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 gSLYDYLNRNIVTV-AGMIK-LALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdSILN 303
Cdd:cd07847   85 -TVLNELEKNPRGVpEHLIKkIIWQTLQAVNFCH--------KHNCIHRDVKPENILITKQGQIKLCDFGFA----RILT 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 304 TIDIPQNPKVGTKRYMAPEML-DDTmnvnifESFKRADIYSVGLVYWEI 351
Cdd:cd07847  152 GPGDDYTDYVATRWYRAPELLvGDT------QYGPPVDVWAIGCVFAEL 194
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
151-435 5.34e-06

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: 47.55  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCGE-DVAVKIFS--SRDERSWFREAEIyqTVMLRHENILGFIaadnkdnGTWTQ---LWLVSEYHE 224
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQyKVAIKAIRegAMSEEDFIEEAKV--MMKLTHPKLVQLY-------GVCTQqkpIYIVTEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYL--NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhdsiL 302
Cdd:cd05114   83 NGCLLNYLrqRRGKLSRDMLLSMCQDVCEGMEYLE--------RNNFIHRDLAARNCLVNDTGVVKVSDFGMT------R 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 303 NTIDIPQNPKVGTK---RYMAPEMLddtmNVNIFESfkRADIYSVGLVYWEiarrcsvggIVEEYQLPYydmvPSDPSIE 379
Cdd:cd05114  149 YVLDDQYTSSSGAKfpvKWSPPEVF----NYSKFSS--KSDVWSFGVLMWE---------VFTEGKMPF----ESKSNYE 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 380 EMRKVVC-DQKFRPSIpnqwqsceALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05114  210 VVEMVSRgHRLYRPKL--------ASKSVYEVMYSCWHEKPEGRPTFADLLRTITEI 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
169-352 5.90e-06

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: 47.64  E-value: 5.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 169 VAVKIFSSRD-------ERSWFREAEIYQtvMLRHENILGFIaaDNKDNGTWTQLWLVSEYHeQGSLYDYLNRnivtvAG 241
Cdd:cd14119   21 RAVKILKKRKlrripngEANVKREIQILR--RLNHRNVIKLV--DVLYNEEKQKLYMVMEYC-VGGLQEMLDS-----AP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 242 MIKLALSIA--------SGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHDSI--LNTIDIPQnp 311
Cdd:cd14119   91 DKRLPIWQAhgyfvqliDGLEYLH-----SQG---IIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFaeDDTCTTSQ-- 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 161333835 312 kvGTKRYMAPEML--DDTmnvniFESFKrADIYSVGLVYWEIA 352
Cdd:cd14119  161 --GSPAFQPPEIAngQDS-----FSGFK-VDIWSAGVTLYNMT 195
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
149-370 6.68e-06

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: 47.77  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW--HGRWCGEDVAVKIFS-----SRDERSW-FREAEIYQTVmlRHEnilgFIAADNKDNGTWTQLWLVS 220
Cdd:cd05593   21 KLLGKGTFGKVIlvREKASGKYYAMKILKkeviiAKDEVAHtLTESRVLKNT--RHP----FLTSLKYSFQTKDRLCFVM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHmeivgtQGKpaIAHRDIKSKNILVKKCETCAIADLGL---AV 296
Cdd:cd05593   95 EYVNGGELFFHLSRERVFSEDRTRFyGAEIVSALDYLH------SGK--IVYRDLKLENLMLDKDGHIKITDFGLckeGI 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEMLDDTmnvnifeSFKRA-DIYSVGLVYWEIArrCSvggiveeyQLPYYD 370
Cdd:cd05593  167 TDAATMKTF-------CGTPEYLAPEVLEDN-------DYGRAvDWWGLGVVMYEMM--CG--------RLPFYN 217
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
144-347 6.77e-06

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: 47.35  E-value: 6.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVwhgRWC-----GEDVAVKiFSSRDERSWFREAEIyqtvmlRHENILGFIAADN-------KDNG 211
Cdd:cd14106    9 YTVESTPLGRGKFAVV---RKCihketGKEYAAK-FLRKRRRGQDCRNEI------LHEIAVLELCKDCprvvnlhEVYE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 212 TWTQLWLVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKK---CETC 287
Cdd:cd14106   79 TRSELILILELAAGGELQTLLDEEeCLTEADVRRLMRQILEGVQYLHER--------NIVHLDLKPQNILLTSefpLGDI 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 288 AIADLGLA--VKHDSILNTIdipqnpkVGTKRYMAPEMLDdtmnvniFESFKRA-DIYSVGLV 347
Cdd:cd14106  151 KLCDFGISrvIGEGEEIREI-------LGTPDYVAPEILS-------YEPISLAtDMWSIGVL 199
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
223-351 7.04e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 47.95  E-value: 7.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIVTV----AGMIKLAlsIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVkh 298
Cdd:PHA03209 138 HYSSDLYTYLTKRSRPLpidqALIIEKQ--ILEGLRYLHAQ--------RIIHRDVKTENIFINDVDQVCIGDLGAAQ-- 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 dsiLNTIDIPQNPKVGTKRYMAPEML-DDTMNvnifesfKRADIYSVGLVYWEI 351
Cdd:PHA03209 206 ---FPVVAPAFLGLAGTVETNAPEVLaRDKYN-------SKADIWSAGIVLFEM 249
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
242-435 7.05e-06

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 47.92  E-value: 7.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 242 MIKLALSIASGLAHLhmeivgtQGKPAIaHRDIKSKNILVKKCETCAIADLGLA--VKHDSilNTIdIPQNPKVGTKrYM 319
Cdd:cd05106  214 LLRFSSQVAQGMDFL-------ASKNCI-HRDVAARNVLLTDGRVAKICDFGLArdIMNDS--NYV-VKGNARLPVK-WM 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 320 APE-MLDDTMNVnifesfkRADIYSVGLVYWEIArrcSVGgiveeyQLPYydmvpsdPSIeemrkvVCDQKFRPSIPNQW 398
Cdd:cd05106  282 APEsIFDCVYTV-------QSDVWSYGILLWEIF---SLG------KSPY-------PGI------LVNSKFYKMVKRGY 332
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 161333835 399 QSCE---ALRVMGRIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd05106  333 QMSRpdfAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQ 372
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
150-352 8.52e-06

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: 47.30  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVWHGRW--CGEDVAVKIFSSRDERSWFREAEIYQTVMLR---HENILGFIAADNKDNgtwtQLWLVSEYHE 224
Cdd:cd07848    8 VVGEGAYGVVLKCRHkeTKEIVAIKKFKDSEENEEVKETTLRELKMLRtlkQENIVELKEAFRRRG----KLYLVFEYVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYdyLNRNIVTVAGMIKLALSIASGLAHLHMeivgtQGKPAIAHRDIKSKNILVKKCETCAIADLGLAvkhDSILNT 304
Cdd:cd07848   84 KNMLE--LLEEMPNGVPPEKVRSYIYQLIKAIHW-----CHKNDIVHRDIKPENLLISHNDVLKLCDFGFA---RNLSEG 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 305 IDIPQNPKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWEIA 352
Cdd:cd07848  154 SNANYTEYVATRWYRSPELLLGA------PYGKAVDMWSVGCILGELS 195
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
151-354 8.65e-06

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: 47.33  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWC---GEDVAVKIFSSRDERSWFREAEIYQTVMLR------HENILG-FIAADNKDNGTWTQLWLVS 220
Cdd:cd07862    9 IGEGAYGKVFKARDLkngGRFVALKRVRVQTGEEGMPLSTIREVAVLRhletfeHPNVVRlFDVCTVSRTDRETKLTLVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQgSLYDYLNRNI---VTVAGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd07862   89 EHVDQ-DLTTYLDKVPepgVPTETIKDMMFQLLRGLDFLHSHRV--------VHRDLKPQNILVTSSGQIKLADFGLARI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 298 HDSILNTIDIpqnpkVGTKRYMAPEMLddtmnvnIFESFKR-ADIYSVGLVYWEIARR 354
Cdd:cd07862  160 YSFQMALTSV-----VVTLWYRAPEVL-------LQSSYATpVDLWSVGCIFAEMFRR 205
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
144-391 8.72e-06

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: 47.30  E-value: 8.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDER------SWFREAEIYQTvmLRHENILGFiaadNKDNGTWTQLW 217
Cdd:cd07873    3 TYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHeegapcTAIREVSLLKD--LKHANIVTL----HDIIHTEKSLT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQgSLYDYLNR--NIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd07873   77 LVFEYLDK-DLKQYLDDcgNSINMHNVKLFLFQLLRGLAYCH--------RRKVLHRDLKPQNLLINERGELKLADFGLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTIDipqnPKVGTKRYMAPEMLddtmnVNIFESFKRADIYSVGLVYWEIA--RRCSVGGIVEEyQLPYYDMVP 373
Cdd:cd07873  148 RAKSIPTKTYS----NEVVTLWYRPPDIL-----LGSTDYSTQIDMWGVGCIFYEMStgRPLFPGSTVEE-QLHFIFRIL 217
                        250
                 ....*....|....*...
gi 161333835 374 SDPSIEEMRKVVCDQKFR 391
Cdd:cd07873  218 GTPTEETWPGILSNEEFK 235
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
146-347 8.75e-06

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: 47.20  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFGEVWH--GRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGtwtqLWLVSEYH 223
Cdd:cd14108    6 IHKEI-GRGAFSYLRRvkEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRV----VIIVTELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV--KKCETCAIADLGLAVKHdsi 301
Cdd:cd14108   81 HEELLERITKRPTVCESEVRSYMRQLLEGIEYLH--------QNDVLHLDLKPENLLMadQKTDQVRICDFGNAQEL--- 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 161333835 302 lnTIDIPQNPKVGTKRYMAPEMlddtmnVNIFESFKRADIYSVGLV 347
Cdd:cd14108  150 --TPNEPQYCKYGTPEFVAPEI------VNQSPVSKVTDIWPVGVI 187
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
147-324 9.33e-06

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: 47.02  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGR--WCGEDVAVKIF--SSRDERSwfrEAEIYQTV----MLRHENILGFIAADNkdngTWTQLWL 218
Cdd:cd14074    7 LEETLGRGHFAVVKLARhvFTGEKVAVKVIdkTKLDDVS---KAHLFQEVrcmkLVQHPNVVRLYEVID----TQTKLYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNIVTVAGmiKLALS----IASGLAHLHmeivgtqgKPAIAHRDIKSKNILV-KKCETCAIADLG 293
Cdd:cd14074   80 ILELGDGGDMYDYIMKHENGLNE--DLARKyfrqIVSAISYCH--------KLHVVHRDLKPENVVFfEKQGLVKLTDFG 149
                        170       180       190
                 ....*....|....*....|....*....|...
gi 161333835 294 LAVKHD--SILNTidipqnpKVGTKRYMAPEML 324
Cdd:cd14074  150 FSNKFQpgEKLET-------SCGSLAYSAPEIL 175
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
202-350 9.35e-06

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: 47.09  E-value: 9.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 202 FIAADNKDNgtwtqLWLVSEYHEQGSLydylnRNIVTVAGMI------KLALSIASGLAHLHmeivgtqgKPAIAHRDIK 275
Cdd:cd05611   63 YYSFQSKDY-----LYLVMEYLNGGDC-----ASLIKTLGGLpedwakQYIAEVVLGVEDLH--------QRGIIHRDIK 124
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 276 SKNILVKKCETCAIADLGLAvkhdsiLNTIDIPQNPK-VGTKRYMAPEML---DDTmnvnifesfKRADIYSVGLVYWE 350
Cdd:cd05611  125 PENLLIDQTGHLKLTDFGLS------RNGLEKRHNKKfVGTPDYLAPETIlgvGDD---------KMSDWWSLGCVIFE 188
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
146-347 9.85e-06

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: 46.90  E-value: 9.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWH--GRWCGEDVAVKIFssRDERSWFREAEIYQTVMLrHENILGFIAA-DNKDNGTwTQLWLVSEY 222
Cdd:cd14089    4 ISKQVLGLGINGKVLEcfHKKTGEKFALKVL--RDNPKARREVELHWRASG-CPHIVRIIDVyENTYQGR-KCLLVVMEC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYLNRNIVT------VAGMIKlalSIASGLAHLH-MEIvgtqgkpaiAHRDIKSKNILVKKCETCAI---ADL 292
Cdd:cd14089   80 MEGGELFSRIQERADSaftereAAEIMR---QIGSAVAHLHsMNI---------AHRDLKPENLLYSSKGPNAIlklTDF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 293 GLAvKHDSILNTIDIPQNpkvgTKRYMAPEMLDdtmnvniFESF-KRADIYSVGLV 347
Cdd:cd14089  148 GFA-KETTTKKSLQTPCY----TPYYVAPEVLG-------PEKYdKSCDMWSLGVI 191
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
184-352 1.06e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.53  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 184 REAEIYQTvmLRHENILGFIAADNkdngtWTQLWLVSEYHEQGSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHmeivg 262
Cdd:PHA03207 135 REIDILKT--ISHRAIINLIHAYR-----WKSTVCMVMPKYKCDLFTYVDRsGPLPLEQAITIQRRLLEALAYLH----- 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 263 tqGKpAIAHRDIKSKNILVKKCETCAIADLGLAVKHDsilntiDIPQNPK----VGTKRYMAPEMLD-DTMNVnifesfk 337
Cdd:PHA03207 203 --GR-GIIHRDVKTENIFLDEPENAVLGDFGAACKLD------AHPDTPQcygwSGTLETNSPELLAlDPYCA------- 266
                        170
                 ....*....|....*
gi 161333835 338 RADIYSVGLVYWEIA 352
Cdd:PHA03207 267 KTDIWSAGLVLFEMS 281
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
149-351 1.11e-05

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: 47.02  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSwfREAEIYQTVMLRHE---NILGFIaaDNKDNGTwtQLWLVSEYH 223
Cdd:cd06656   25 EKIGQGASGTVYTAIdiATGQEVAIKQMNLQQQPK--KELIINEILVMRENknpNIVNYL--DSYLVGD--ELWVVMEYL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLN 303
Cdd:cd06656   99 AGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSN--------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQ----IT 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 304 TIDIPQNPKVGTKRYMAPEMlddtmnVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd06656  167 PEQSKRSTMVGTPYWMAPEV------VTRKAYGPKVDIWSLGIMAIEM 208
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
151-356 1.15e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 47.81  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  151 VGKGRFGEVW---HGR----WCGEDVAVKIFSSRDERSWFREAEIYQTvmLRHENILGFIaaDNKDNGTWTQLWLVSEYH 223
Cdd:PTZ00266   21 IGNGRFGEVFlvkHKRtqefFCWKAISYRGLKEREKSQLVIEVNVMRE--LKHKNIVRYI--DRFLNKANQKLYILMEFC 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835  224 EQGSlydyLNRNIVTVAGM---------IKLALSIASGLAHLHMEIVGTQGKpAIAHRDIKSKNILVkkceTCAIADLGL 294
Cdd:PTZ00266   97 DAGD----LSRNIQKCYKMfgkieehaiVDITRQLLHALAYCHNLKDGPNGE-RVLHRDLKPQNIFL----STGIRHIGK 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835  295 AVKHDSILNTIDIPQ----------------NPKVGTKRYMAPE-MLDDTMNVNifesfKRADIYSVGLVYWEIarrCS 356
Cdd:PTZ00266  168 ITAQANNLNGRPIAKigdfglsknigiesmaHSCVGTPYYWSPElLLHETKSYD-----DKSDMWALGCIIYEL---CS 238
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
149-351 1.33e-05

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: 46.64  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSwfREAEIYQTVMLRHE---NILGFIaaDNKDNGTwtQLWLVSEYH 223
Cdd:cd06654   26 EKIGQGASGTVYTAMdvATGQEVAIRQMNLQQQPK--KELIINEILVMRENknpNIVNYL--DSYLVGD--ELWVVMEYL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLN 303
Cdd:cd06654  100 AGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSN--------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQ----IT 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 161333835 304 TIDIPQNPKVGTKRYMAPEMlddtmnVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd06654  168 PEQSKRSTMVGTPYWMAPEV------VTRKAYGPKVDIWSLGIMAIEM 209
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
249-385 1.63e-05

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: 46.48  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 249 IASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVK---HDSILNTidipqnpKVGTKRYMAPEMLD 325
Cdd:cd14200  133 IVLGIEYLHYQ--------KIVHRDIKPSNLLLGDDGHVKIADFGVSNQfegNDALLSS-------TAGTPAFMAPETLS 197
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 326 DTMnvnifESF--KRADIYSVGLVYWeiarrCSVGG---IVEEYQLPYYDMV-------PSDPSI-EEMRKVV 385
Cdd:cd14200  198 DSG-----QSFsgKALDVWAMGVTLY-----CFVYGkcpFIDEFILALHNKIknkpvefPEEPEIsEELKDLI 260
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
187-370 1.64e-05

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: 46.50  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 187 EIYQTVM----LRHENILGFIAAdnKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivg 262
Cdd:cd14199   71 RVYQEIAilkkLDHPNVVKLVEV--LDDPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQ--- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 263 tqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVK---HDSILNTidipqnpKVGTKRYMAPEMLDDTMnvNIFeSFKRA 339
Cdd:cd14199  146 -----KIIHRDVKPSNLLVGEDGHIKIADFGVSNEfegSDALLTN-------TVGTPAFMAPETLSETR--KIF-SGKAL 210
                        170       180       190
                 ....*....|....*....|....*....|.
gi 161333835 340 DIYSVGLVYWeiarrCSVGGiveeyQLPYYD 370
Cdd:cd14199  211 DVWAMGVTLY-----CFVFG-----QCPFMD 231
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
147-353 1.72e-05

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: 46.59  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWC--GEDVAVKIFSSRdeRSWFREAEiyqTVMLRHENILG--------FIAADNKDNGTWTQL 216
Cdd:cd05633    9 VHRIIGRGGFGEVYGCRKAdtGKMYAMKCLDKK--RIKMKQGE---TLALNERIMLSlvstgdcpFIVCMTYAFHTPDKL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd05633   84 CFILDLMNGGDLHYHLSQHgVFSEKEMRFYATEIILGLEHMHNRFV--------VYRDLKPANILLDEHGHVRISDLGLA 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 296 VKHDSilntidIPQNPKVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIAR 353
Cdd:cd05633  156 CDFSK------KKPHASVGTHGYMAPEVLQKGTAYD-----SSADWFSLGCMLFKLLR 202
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
169-395 1.72e-05

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: 46.14  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 169 VAVKIFSSRD------ERSWFREAEIYQTvmLRHENILGFIAADNKDNGtwtQLWLVSEYHEQGSLYDYlnrniVTVAGm 242
Cdd:cd14163   28 VAIKIIDKSGgpeefiQRFLPRELQIVER--LDHKNIIHVYEMLESADG---KIYLVMELAEDGDVFDC-----VLHGG- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 243 iKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKcETCAIADLGLA----VKHDSILNTIdipqnpkVGTKRY 318
Cdd:cd14163   97 -PLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQG-FTLKLTDFGFAkqlpKGGRELSQTF-------CGSTAY 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 319 MAPEMLDdtmnvNIFESFKRADIYSVGLVYWEIArrCSvggiveeyQLPYYDMvpsdpsieEMRKVVCDQKFRPSIP 395
Cdd:cd14163  168 AAPEVLQ-----GVPHDSRKGDIWSMGVVLYVML--CA--------QLPFDDT--------DIPKMLCQQQKGVSLP 221
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
151-432 1.86e-05

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 46.36  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCG----ED---VAVKIF----SSRDERSWFREAEIYQTvmLRHENILGFIA--ADNKdngtwtQLW 217
Cdd:cd05050   13 IGQGAFGRVFQARAPGllpyEPftmVAVKMLkeeaSADMQADFQREAALMAE--FDHPNIVKLLGvcAVGK------PMC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNI-----------------------VTVAGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDI 274
Cdd:cd05050   85 LLFEYMAYGDLNEFLRHRSpraqcslshstssarkcglnplpLSCTEQLCIAKQVAAGMAYL--------SERKFVHRDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 275 KSKNILVKKCETCAIADLGLAVKHDSI----LNTID-IPqnpkvgtKRYMAPEMLddtmnvnIFESFK-RADIYSVGLVY 348
Cdd:cd05050  157 ATRNCLVGENMVVKIADFGLSRNIYSAdyykASENDaIP-------IRWMPPESI-------FYNRYTtESDVWAYGVVL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 349 WEIArrcsvggiveEYQL-PYYDMvpsdpSIEEMRKVVCDQKFRPSIPNQWQSCEALrvmgriMRECWYANGAARLTALR 427
Cdd:cd05050  223 WEIF----------SYGMqPYYGM-----AHEEVIYYVRDGNVLSCPDNCPLELYNL------MRLCWSKLPSDRPSFAS 281

                 ....*
gi 161333835 428 IKKTI 432
Cdd:cd05050  282 INRIL 286
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
145-351 1.98e-05

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 46.19  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGR---WCGED----VAVKIFSSRDE---RSWFREAEIYQTvmLRHENILGFIAADNKDNgtwt 214
Cdd:cd05093    7 IVLKRELGEGAFGKVFLAEcynLCPEQdkilVAVKTLKDASDnarKDFHREAELLTN--LQHEHIVKFYGVCVEGD---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 QLWLVSEYHEQGSLYDYLNRN--------------IVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNIL 280
Cdd:cd05093   81 PLIMVFEYMKHGDLNKFLRAHgpdavlmaegnrpaELTQSQMLHIAQQIAAGMVYLASQ--------HFVHRDLATRNCL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 281 VKKCETCAIADLGLAvkhdsilNTIDIPQNPKVGTK-----RYMAPEMLddtmnvnIFESF-KRADIYSVGLVYWEI 351
Cdd:cd05093  153 VGENLLVKIGDFGMS-------RDVYSTDYYRVGGHtmlpiRWMPPESI-------MYRKFtTESDVWSLGVVLWEI 215
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
144-382 2.10e-05

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: 46.14  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDER------SWFREAEIYQTvmLRHENILGFIAADNKDNgtwtQLW 217
Cdd:cd07872    7 TYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHeegapcTAIREVSLLKD--LKHANIVTLHDIVHTDK----SLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQgSLYDYLNR--NIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd07872   81 LVFEYLDK-DLKQYMDDcgNIMSMHNVKIFLYQILRGLAYCH--------RRKVLHRDLKPQNLLINERGELKLADFGLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTIdipqNPKVGTKRYMAPEMLddtmnVNIFESFKRADIYSVGLVYWEIA--RRCSVGGIVEE-----YQL-- 366
Cdd:cd07872  152 RAKSVPTKTY----SNEVVTLWYRPPDVL-----LGSSEYSTQIDMWGVGCIFFEMAsgRPLFPGSTVEDelhliFRLlg 222
                        250
                 ....*....|....*..
gi 161333835 367 -PYYDMVPSDPSIEEMR 382
Cdd:cd07872  223 tPTEETWPGISSNDEFK 239
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
151-429 2.11e-05

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: 45.75  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFG--EVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFiaadNKDNGTWTQLWLVSEYHEQGSL 228
Cdd:cd14665    8 IGSGNFGvaRLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRF----KEVILTPTHLAIVMEYAAGGEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 229 YDYL-NRNIVTVAGMIKLALSIASGLAHLH-MEIvgtqgkpaiAHRDIKSKNILV--KKCETCAIADLGLAvkHDSILNT 304
Cdd:cd14665   84 FERIcNAGRFSEDEARFFFQQLISGVSYCHsMQI---------CHRDLKLENTLLdgSPAPRLKICDFGYS--KSSVLHS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 305 idipqNPK--VGTKRYMAPEMLDDTMnvnifESFKRADIYSVGLVYWEIarrcsvggIVEEYqlPYYDmvPSDPsiEEMR 382
Cdd:cd14665  153 -----QPKstVGTPAYIAPEVLLKKE-----YDGKIADVWSCGVTLYVM--------LVGAY--PFED--PEEP--RNFR 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161333835 383 KVVcdQKF---RPSIPNQWQ-SCEALRVMGRImrecWYANGAARLTALRIK 429
Cdd:cd14665  209 KTI--QRIlsvQYSIPDYVHiSPECRHLISRI----FVADPATRITIPEIR 253
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
149-366 2.20e-05

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: 45.96  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTVMLR---HENI---LGFIAADNKdngtwtqLWLVS 220
Cdd:cd07860    6 EKIGEGTYGVVYKARnkLTGEVVALKKIRLDTETEGVPSTAIREISLLKelnHPNIvklLDVIHTENK-------LYLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQgSLYDYLNrniVTVAGMIKLAL------SIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd07860   79 EFLHQ-DLKKFMD---ASALTGIPLPLiksylfQLLQGLAFCHSHRV--------LHRDLKPQNLLINTEGAIKLADFGL 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 295 AVKHDSILNTIdipqNPKVGTKRYMAPEMLddtMNVNIFESfkRADIYSVGLVYWE-IARRCSVGGIVEEYQL 366
Cdd:cd07860  147 ARAFGVPVRTY----THEVVTLWYRAPEIL---LGCKYYST--AVDIWSLGCIFAEmVTRRALFPGDSEIDQL 210
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
151-349 2.29e-05

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: 45.74  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVwhgRWCGED-----VAVKIFSS----RDERSwfREAEIYQTvmLRHENILGFIaaDNKDngTWTQLWLVSE 221
Cdd:cd14113   15 LGRGRFSVV---KKCDQRgtkraVATKFVNKklmkRDQVT--HELGVLQS--LQHPQLVGLL--DTFE--TPTSYILVLE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 YHEQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKC---ETCAIADLGLAVK 297
Cdd:cd14113   84 MADQGRLLDYVVRWGNLTEEKIRFYLrEILEALQYLH--------NCRIAHLDLKPENILVDQSlskPTIKLADFGDAVQ 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835 298 hdsiLNTIDIpQNPKVGTKRYMAPEM-LDDTMNVNifesfkrADIYSVGLVYW 349
Cdd:cd14113  156 ----LNTTYY-IHQLLGSPEFAAPEIiLGNPVSLT-------SDLWSIGVLTY 196
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
149-351 2.41e-05

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: 45.87  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVK-IFSSRDERSWFREAEIYQTVMLRHENILGFIaaDNKDNGTwtQLWLVSEYHEQ 225
Cdd:cd06655   25 EKIGQGASGTVFTAIdvATGQEVAIKqINLQKQPKKELIINEILVMKELKNPNIVNFL--DSFLVGD--ELFVVMEYLAG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 GSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNTI 305
Cdd:cd06655  101 GSLTDVVTETCMDEAQIAAVCRECLQALEFLHAN--------QVIHRDIKSDNVLLGMDGSVKLTDFGFCAQ----ITPE 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 161333835 306 DIPQNPKVGTKRYMAPEMlddtmnVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd06655  169 QSKRSTMVGTPYWMAPEV------VTRKAYGPKVDIWSLGIMAIEM 208
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
151-405 2.83e-05

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: 45.39  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW---HgRWCGEDVAVKIF--SSRDERSWFREAEIyqTVMLR-HENILGF--IAADNKDNGTWTQlwlvsEY 222
Cdd:cd13987    1 LGEGTYGKVLlavH-KGSGTKMALKFVpkPSTKLKDFLREYNI--SLELSvHPHIIKTydVAFETEDYYVFAQ-----EY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDylnrNIVTVAG----MIKL-ALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILV--KKCETCAIADLGLA 295
Cdd:cd13987   73 APYGDLFS----IIPPQVGlpeeRVKRcAAQLASALDFMHSK--------NLVHRDIKPENVLLfdKDCRRVKLCDFGLT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTIDipqnpkvGTKRYMAPEMLDDTMNvnifESF---KRADIYSVGLVYWeiarrCSVGGiveeyQLPYYDMV 372
Cdd:cd13987  141 RRVGSTVKRVS-------GTIPYTAPEVCEAKKN----EGFvvdPSIDVWAFGVLLF-----CCLTG-----NFPWEKAD 199
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 161333835 373 PSDPSIEEMRKVvcdQKFR-PSIPNQWQ--SCEALR 405
Cdd:cd13987  200 SDDQFYEEFVRW---QKRKnTAVPSQWRrfTPKALR 232
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
184-325 2.97e-05

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: 45.39  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 184 REAEIYQTvmLRHENILGFIAA-DNKDNgtwtqLWLVSEYHEQGSLYDYLN-RNIVTVAGMIKLALSIASGLAHLHMEiv 261
Cdd:cd14188   50 KEIELHRI--LHHKHVVQFYHYfEDKEN-----IYILLEYCSRRSMAHILKaRKVLTEPEVRYYLRQIVSGLKYLHEQ-- 120
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 262 gtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNTIDIPQNPKVGTKRYMAPEMLD 325
Cdd:cd14188  121 ------EILHRDLKLGNFFINENMELKVGDFGLAAR----LEPLEHRRRTICGTPNYLSPEVLN 174
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
219-351 3.05e-05

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 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: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 45.74  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDIKSKNILVKKCETCAIADLGLAVkh 298
Cdd:cd05103  158 LSDVEEEEAGQEDLYKDFLTLEDLICYSFQVAKG-----MEFLASR---KCIHRDLAARNILLSENNVVKICDFGLAR-- 227
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 299 dsilntiDIPQNPKVGTK-------RYMAPEMLDDTMNVNifesfkRADIYSVGLVYWEI 351
Cdd:cd05103  228 -------DIYKDPDYVRKgdarlplKWMAPETIFDRVYTI------QSDVWSFGVLLWEI 274
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
141-351 3.09e-05

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: 45.76  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 141 IARTIVLQEIVGKGRFGEVwhgrwC-------GEDVAVK--------IFSSRDERswfreaEIYQTVMLRHENILGF--- 202
Cdd:cd07849    3 VGPRYQNLSYIGEGAYGMV-----CsavhkptGQKVAIKkispfehqTYCLRTLR------EIKILLRFKHENIIGIldi 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 203 IAADNKDNgtWTQLWLVSEYHEQgSLYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVK 282
Cdd:cd07849   72 QRPPTFES--FKDVYIVQELMET-DLYKLIKTQHLSNDHIQYFLYQILRGLKYIH--------SANVLHRDLKPSNLLLN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 283 kcETC--AIADLGLAVKHDsilntidiPQNPK-------VGTKRYMAPE-MLDdtmnvniFESFKRA-DIYSVGLVYWEI 351
Cdd:cd07849  141 --TNCdlKICDFGLARIAD--------PEHDHtgflteyVATRWYRAPEiMLN-------SKGYTKAiDIWSVGCILAEM 203
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
145-415 3.12e-05

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 45.70  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVwhgRWCGED---------------------VAVKIF---SSRDERSWF-REAEIYQTvmLRHENI 199
Cdd:cd05096    7 LLFKEKLGEGQFGEV---HLCEVVnpqdlptlqfpfnvrkgrpllVAVKILrpdANKNARNDFlKEVKILSR--LKDPNI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 200 LGFIAADNKDNgtwtQLWLVSEYHEQGSLYDYLNRN--------------------IVTVAGMIKLALSIASGLAHLhme 259
Cdd:cd05096   82 IRLLGVCVDED----PLCMITEYMENGDLNQFLSSHhlddkeengndavppahclpAISYSSLLHVALQIASGMKYL--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 260 ivgtqGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNTIDI--PQNPKVGTKRYMAPEMLddtmnvnIFESFK 337
Cdd:cd05096  155 -----SSLNFVHRDLATRNCLVGENLTIKIADFGMSRN----LYAGDYyrIQGRAVLPIRWMAWECI-------LMGKFT 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 338 RA-DIYSVGLVYWEIARRCSvggiveeyQLPYYDMVPSDpSIEEMRKVVCDQK-----FRPSIPNQwqscealrVMGRIM 411
Cdd:cd05096  219 TAsDVWAFGVTLWEILMLCK--------EQPYGELTDEQ-VIENAGEFFRDQGrqvylFRPPPCPQ--------GLYELM 281

                 ....
gi 161333835 412 RECW 415
Cdd:cd05096  282 LQCW 285
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
151-351 3.54e-05

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: 45.66  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG--RWCGEDVAVK---------IFSSRDerswFREAEIYQtvMLRHENILG----FIAADNKDNgtWTQ 215
Cdd:cd07879   23 VGSGAYGSVCSAidKRTGEKVAIKklsrpfqseIFAKRA----YRELTLLK--HMQHENVIGlldvFTSAVSGDE--FQD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHE---QGSLYDYLNRNIVTVagmikLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKK-CETcAIAD 291
Cdd:cd07879   95 FYLVMPYMQtdlQKIMGHPLSEDKVQY-----LVYQMLCGLKYIH--------SAGIIHRDLKPGNLAVNEdCEL-KILD 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 292 LGLAVKHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEI 351
Cdd:cd07879  161 FGLARHADAEMTGY-------VVTRWYRAPEVILNWMHYN-----QTVDIWSVGCIMAEM 208
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
147-324 3.60e-05

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: 45.06  E-value: 3.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW--HGRWCGEDVAVKIFS----SRDERSWFREAEIYQTvmLRHENILGFIaaDNKDNGTwtQLWLVS 220
Cdd:cd14083    7 FKEVLGTGAFSEVVlaEDKATGKLVAIKCIDkkalKGKEDSLENEIAVLRK--IKHPNIVQLL--DIYESKS--HLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYD-------YLNRNIVTVAGMIKLALSiasglaHLHmeivgTQGkpaIAHRDIKSKNILVKKCE---TCAIA 290
Cdd:cd14083   81 ELVTGGELFDrivekgsYTEKDASHLIRQVLEAVD------YLH-----SLG---IVHRDLKPENLLYYSPDedsKIMIS 146
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 161333835 291 DLGLAVKHDS-ILNTidipqnpKVGTKRYMAPEML 324
Cdd:cd14083  147 DFGLSKMEDSgVMST-------ACGTPGYVAPEVL 174
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
146-351 3.62e-05

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: 45.11  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIVGKGRFGEVWhgrwcgedvAVKIFSSRDERSWFREAEIY-------QTV----------MLRHENILGFIAA-DN 207
Cdd:cd08222    3 RVVRKLGSGNFGTVY---------LVSDLKATADEELKVLKEISvgelqpdETVdanreakllsKLDHPAIVKFHDSfVE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 208 KDNgtwtqLWLVSEYHEQGSLYDYL-----NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVK 282
Cdd:cd08222   74 KES-----FCIVTEYCEGGDLDDKIseykkSGTTIDENQILDWFIQLLLAVQYMH--------ERRILHRDLKAKNIFLK 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 283 KcETCAIADLGLAvkhDSILNTIDIPQNpKVGTKRYMAPEMLDDtmnvNIFESfkRADIYSVGLVYWEI 351
Cdd:cd08222  141 N-NVIKVGDFGIS---RILMGTSDLATT-FTGTPYYMSPEVLKH----EGYNS--KSDIWSLGCILYEM 198
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
252-429 3.82e-05

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: 45.04  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 252 GLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilntIDIPQNPKVGTKRYMAPEMLDDTMNvn 331
Cdd:cd14118  127 GIEYLHYQ--------KIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEG----DDALLSSTAGTPAFMAPEALSESRK-- 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 332 iFESFKRADIYSVGLVYWeiarrCSVGGiveeyQLPYydmvpSDPSIEEMRKVVCDQKFRpsIPNQWQSCEALRVMGRIM 411
Cdd:cd14118  193 -KFSGKALDIWAMGVTLY-----CFVFG-----RCPF-----EDDHILGLHEKIKTDPVV--FPDDPVVSEQLKDLILRM 254
                        170
                 ....*....|....*...
gi 161333835 412 REcwyANGAARLTALRIK 429
Cdd:cd14118  255 LD---KNPSERITLPEIK 269
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
151-351 3.95e-05

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: 45.33  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHG--RWCGEDVAVK---------IFSSRDerswFREAEIYQtvMLRHENILG----FIAADNKDNgtWTQ 215
Cdd:cd07880   23 VGSGAYGTVCSAldRRTGAKVAIKklyrpfqseLFAKRA----YRELRLLK--HMKHENVIGlldvFTPDLSLDR--FHD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYH--EQGSL--YDYLNRNIVTVagmikLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV-KKCETcAIA 290
Cdd:cd07880   95 FYLVMPFMgtDLGKLmkHEKLSEDRIQF-----LVYQMLKGLKYIH--------AAGIIHRDLKPGNLAVnEDCEL-KIL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 291 DLGLAVKHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEI 351
Cdd:cd07880  161 DFGLARQTDSEMTGY-------VVTRWYRAPEVILNWMHYT-----QTVDIWSVGCIMAEM 209
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
151-351 4.75e-05

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: 45.26  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGR--WCGEDVAVKI----FSSRD-ERSWFREAEIYQtvMLRHENILG----FIAAdnkdngtWTQLWLV 219
Cdd:cd07856   18 VGMGAFGLVCSARdqLTGQNVAVKKimkpFSTPVlAKRTYRELKLLK--HLRHENIISlsdiFISP-------LEDIYFV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYheQGS-LYDYLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKkcETC--AIADLGLAV 296
Cdd:cd07856   89 TEL--LGTdLHRLLTSRPLEKQFIQYFLYQILRGLKYVH--------SAGVIHRDLKPSNILVN--ENCdlKICDFGLAR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEMLDDTMNVNIfesfkRADIYSVGLVYWEI 351
Cdd:cd07856  157 IQDPQMTGY-------VSTRYYRAPEIMLTWQKYDV-----EVDIWSAGCIFAEM 199
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
149-422 4.94e-05

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. 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 Ror1 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: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 45.00  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWC--GED----VAVKIFSSRDERSWFREAEIYQTVM--LRHENILGFIAADNKDNgtwtQLWLVS 220
Cdd:cd05090   11 EELGECAFGKIYKGHLYlpGMDhaqlVAIKTLKDYNNPQQWNEFQQEASLMteLHHPNIVCLLGVVTQEQ----PVCMLF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYL-NRNIVTVAGMIKLAL-SIASGLAH---LHMEIVGTQGKPAIA-----HRDIKSKNILVKKCETCAIA 290
Cdd:cd05090   87 EFMNQGDLHEFLiMRSPHSDVGCSSDEDgTVKSSLDHgdfLHIAIQIAAGMEYLSshffvHKDLAARNILVGEQLHVKIS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 291 DLGLAVKhdsiLNTIDI--PQNPKVGTKRYMAPEMLddtmnvnIFESFKR-ADIYSVGLVYWEIArrcsvggiveEYQL- 366
Cdd:cd05090  167 DLGLSRE----IYSSDYyrVQNKSLLPIRWMPPEAI-------MYGKFSSdSDIWSFGVVLWEIF----------SFGLq 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 367 PYYDMvpsdpSIEEMRKVVCDQKFRPSIpnqwQSCEAlRVMGrIMRECWYANGAAR 422
Cdd:cd05090  226 PYYGF-----SNQEVIEMVRKRQLLPCS----EDCPP-RMYS-LMTECWQEIPSRR 270
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
145-355 5.60e-05

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: 44.84  E-value: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIvGKGRFGEVWHGRwcgEDVAVKIFSSRDERSWFREAEIYQTVM---LRHENILGFIAadnKDNGTWTQ---LWL 218
Cdd:cd06622    4 EVLDEL-GKGNYGSVYKVL---HRPTGVTMAMKEIRLELDESKFNQIIMeldILHKAVSPYIV---DFYGAFFIegaVYM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 219 VSEYHEQGSLyDYLNRNIVTVAG-----MIKLALSIASGLAHLHMEIvgtqgkpAIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd06622   77 CMEYMDAGSL-DKLYAGGVATEGipedvLRRITYAVVKGLKFLKEEH-------NIIHRDVKPTNVLVNGNGQVKLCDFG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161333835 294 LAVKHDSILNTIDIpqnpkvGTKRYMAPEMLD-DTMNVNIFESFKrADIYSVGLVYWEIARRC 355
Cdd:cd06622  149 VSGNLVASLAKTNI------GCQSYMAPERIKsGGPNQNPTYTVQ-SDVWSLGLSILEMALGR 204
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
185-393 5.62e-05

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: 44.69  E-value: 5.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 185 EAEIYQTVMLRHENILGFIAAdNKDNGTWTqLWLVSEYHEQGSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHMEIvgt 263
Cdd:cd06651   57 ECEIQLLKNLQHERIVQYYGC-LRDRAEKT-LTIFMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNM--- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 264 qgkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTiDIPQNPKVGTKRYMAPEMLDDtmnvnifESF-KRADIY 342
Cdd:cd06651  132 -----IVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS-GTGIRSVTGTPYWMSPEVISG-------EGYgRKADVW 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 343 SVGLVYWEI-------ARRCSVGGIVEEYQLPYYDMVPSDPSIEE---MRKVVCDQKFRPS 393
Cdd:cd06651  199 SLGCTVVEMltekppwAEYEAMAAIFKIATQPTNPQLPSHISEHArdfLGCIFVEARHRPS 259
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
185-351 5.70e-05

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: 44.59  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 185 EAEIYQTvmLRHENILGFiaadnKDNgTWTQ--LWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHMEiv 261
Cdd:cd14121   45 EIELLKK--LKHPHIVEL-----KDF-QWDEehIYLIMEYCSGGDLSRFIRSRRTLPESTVRRFLQqLASALQFLREH-- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 262 gtqgkpAIAHRDIKSKNILVKKCET--CAIADLGLAvKHdsiLNTIDIPQNPKvGTKRYMAPEM-LDDTMNVnifesfkR 338
Cdd:cd14121  115 ------NISHMDLKPQNLLLSSRYNpvLKLADFGFA-QH---LKPNDEAHSLR-GSPLYMAPEMiLKKKYDA-------R 176
                        170
                 ....*....|...
gi 161333835 339 ADIYSVGLVYWEI 351
Cdd:cd14121  177 VDLWSVGVILYEC 189
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
148-347 5.75e-05

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: 44.53  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 148 QEIVGKGRFGEVWH--GRWCGEDVAVKIFSSRDERSwfREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSEY 222
Cdd:cd14190    9 KEVLGGGKFGKVHTctEKRTGLKLAAKVINKQNSKD--KEMvllEIQVMNQLNHRNLIQLYEAIETPN----EIVLFMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYL---NRNIVTVAGMIkLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV--KKCETCAIADLGLAVK 297
Cdd:cd14190   83 VEGGELFERIvdeDYHLTEVDAMV-FVRQICEGIQFMH--------QMRVLHLDLKPENILCvnRTGHQVKIIDFGLARR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 298 HdsilntidipqNPK------VGTKRYMAPEMlddtmnVNI-FESFKrADIYSVGLV 347
Cdd:cd14190  154 Y-----------NPReklkvnFGTPEFLSPEV------VNYdQVSFP-TDMWSMGVI 192
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
147-349 5.80e-05

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: 44.63  E-value: 5.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEV--WHGRWCGEDVAVKIFSSR--DERSWFREAEIYQTVMLRHENILGFiaADNKDNGTwtQLWLVSEY 222
Cdd:cd14167    7 FREVLGTGAFSEVvlAEEKRTQKLVAIKCIAKKalEGKETSIENEIAVLHKIKHPNIVAL--DDIYESGG--HLYLIMQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 HEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCE---TCAIADLGLAVKH 298
Cdd:cd14167   83 VSGGELFDRIvEKGFYTERDASKLIFQILDAVKYLH--------DMGIVHRDLKPENLLYYSLDedsKIMISDFGLSKIE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 299 D--SILNTidipqnpKVGTKRYMAPEMLDDtmnvnifESFKRA-DIYSVGLVYW 349
Cdd:cd14167  155 GsgSVMST-------ACGTPGYVAPEVLAQ-------KPYSKAvDCWSIGVIAY 194
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
244-352 6.30e-05

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: 44.67  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 244 KLALSIASGLAHLhmeivgtQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKH-DSILNTidipqnPKVGTKRYMAPE 322
Cdd:cd06618  118 KMTVSIVKALHYL-------KEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRLvDSKAKT------RSAGCAAYMAPE 184
                         90       100       110
                 ....*....|....*....|....*....|..
gi 161333835 323 MLD--DTMNVNIfesfkRADIYSVGLVYWEIA 352
Cdd:cd06618  185 RIDppDNPKYDI-----RADVWSLGISLVELA 211
PHA02988 PHA02988
hypothetical protein; Provisional
218-355 6.45e-05

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 44.73  E-value: 6.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNI-VTVAGMIKLALSIASGLAHLHMEIvgtqGKPaiaHRDIKSKNILVKKCETCAIADLGLAv 296
Cdd:PHA02988  99 LILEYCTRGYLREVLDKEKdLSFKTKLDMAIDCCKGLYNLYKYT----NKP---YKNLTSVSFLVTENYKLKIICHGLE- 170
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 khdsilNTIDIPQNPKVGTKRYMAPEMLDDtmnvnIFESFK-RADIYSVGLVYWEIARRC 355
Cdd:PHA02988 171 ------KILSSPPFKNVNFMVYFSYKMLND-----IFSEYTiKDDIYSLGVVLWEIFTGK 219
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
143-351 6.64e-05

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 44.62  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 143 RTIVLQEIVGKGRFGEVWHGRWCGED-------VAVKIFSSRD---ERSWFREAEIYQTvmLRHENILGFIAAdnkdNGT 212
Cdd:cd05094    5 RDIVLKRELGEGAFGKVFLAECYNLSptkdkmlVAVKTLKDPTlaaRKDFQREAELLTN--LQHDHIVKFYGV----CGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 213 WTQLWLVSEYHEQGSLYDYLNRN----IVTVAG-------------MIKLALSIASGLAHLHMEivgtqgkpAIAHRDIK 275
Cdd:cd05094   79 GDPLIMVFEYMKHGDLNKFLRAHgpdaMILVDGqprqakgelglsqMLHIATQIASGMVYLASQ--------HFVHRDLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 276 SKNILVKKCETCAIADLGLAvkhdsilNTIDIPQNPKVGTK-----RYMAPEMLddtmnvnIFESFK-RADIYSVGLVYW 349
Cdd:cd05094  151 TRNCLVGANLLVKIGDFGMS-------RDVYSTDYYRVGGHtmlpiRWMPPESI-------MYRKFTtESDVWSFGVILW 216

                 ..
gi 161333835 350 EI 351
Cdd:cd05094  217 EI 218
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
145-352 6.66e-05

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: 44.48  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWHGRW--CGEDVAVKIF----SSRDERSWFREAEI-YQTVMLRhenILGFIAADNKDNgtwtQLW 217
Cdd:cd06619    3 IQYQEILGHGNGGTVYKAYHllTRRILAVKVIpldiTVELQKQIMSELEIlYKCDSPY---IIGFYGAFFVEN----RIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLyDYLNRNIVTVAGMIklALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd06619   76 ICTEFMDGGSL-DVYRKIPEHVLGRI--AVAVVKGLTYLW--------SLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQ 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 298 hdsILNTIdipQNPKVGTKRYMAPE-MLDDTMNVNifesfkrADIYSVGLVYWEIA 352
Cdd:cd06619  145 ---LVNSI---AKTYVGTNAYMAPErISGEQYGIH-------SDVWSLGISFMELA 187
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
150-351 7.04e-05

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: 44.49  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW--HGRWCGEDVAVKIFSSR--DERSWFREAEIYQTVMLR-HENilgFIAADNKDNGTWTQLWLVSEYHE 224
Cdd:cd05608    8 VLGKGGFGEVSacQMRATGKLYACKKLNKKrlKKRKGYEGAMVEKRILAKvHSR---FIVSLAYAFQTKTDLCLVMTIMN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSL----YDYLNRNivtvAGM-----IKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd05608   85 GGDLryhiYNVDEEN----PGFqepraCFYTAQIISGLEHLHQR--------RIIYRDLKPENVLLDDDGNVRISDLGLA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 296 VKhdsiLNTIDIPQNPKVGTKRYMAPEMLDDtmnvnifESFKRA-DIYSVGLVYWEI 351
Cdd:cd05608  153 VE----LKDGQTKTKGYAGTPGFMAPELLLG-------EEYDYSvDYFTLGVTLYEM 198
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
151-280 8.87e-05

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: 44.40  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRW--CGEDVAVKIFSS----RDERSWFREAEIYQTvmLRHENILGFIAADNKDNGTwtQLWLVSEYHE 224
Cdd:cd13988    1 LGQGATANVFRGRHkkTGDLYAVKVFNNlsfmRPLDVQMREFEVLKK--LNHKNIVKLFAIEEELTTR--HKVLVMELCP 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYL----NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNIL 280
Cdd:cd13988   77 CGSLYTVLeepsNAYGLPESEFLIVLRDVVAGMNHLR--------ENGIVHRDIKPGNIM 128
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
147-356 1.04e-04

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: 44.02  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVwhgRWC-----GEDVAVKIFSSRDERSWFR-------EAEIYQTVMLRHENILGFIAA-DNKdngtw 213
Cdd:cd14105    9 IGEELGSGQFAVV---KKCrekstGLEYAAKFIKKRRSKASRRgvsrediEREVSILRQVLHPNIITLHDVfENK----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 TQLWLVSEYHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNI-LVKKCET---CA 288
Cdd:cd14105   81 TDVVLILELVAGGELFDFLaEKESLSEEEATEFLKQILDGVNYLHTK--------NIAHFDLKPENImLLDKNVPiprIK 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 289 IADLGLAVKhdsilntIDIPQNPK--VGTKRYMAPEMLDdtmnvniFESFK-RADIYSVGLVYWEIARRCS 356
Cdd:cd14105  153 LIDFGLAHK-------IEDGNEFKniFGTPEFVAPEIVN-------YEPLGlEADMWSIGVITYILLSGAS 209
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
242-353 1.11e-04

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: 44.25  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 242 MIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilntiDIPQNPKVGTKRYMAP 321
Cdd:cd07876  125 MSYLLYQMLCGIKHLH--------SAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACT-----NFMMTPYVVTRYYRAP 191
                         90       100       110
                 ....*....|....*....|....*....|..
gi 161333835 322 EMLddtMNVNIFESfkrADIYSVGLVYWEIAR 353
Cdd:cd07876  192 EVI---LGMGYKEN---VDIWSVGCIMGELVK 217
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
149-351 1.21e-04

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) 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. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 43.90  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGED------VAVKIFSS----RDERSWFREAEIYQTVMLRH-ENILGFIAADNkdngtwtqLW 217
Cdd:cd05110   13 KVLGSGAFGTVYKGIWVPEGetvkipVAIKILNEttgpKANVEFMDEALIMASMDHPHlVRLLGVCLSPT--------IQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNIVTVAGMIKL--ALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd05110   85 LVTQLMPHGCLLDYVHEHKDNIGSQLLLnwCVQIAKGMMYLE--------ERRLVHRDLAARNVLVKSPNHVKITDFGLA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 296 vkhdSILNTIDIPQNPKVGTK--RYMAPEMLDdtmnvniFESFK-RADIYSVGLVYWEI 351
Cdd:cd05110  157 ----RLLEGDEKEYNADGGKMpiKWMALECIH-------YRKFThQSDVWSYGVTIWEL 204
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
146-347 1.25e-04

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: 43.34  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFG---EVWHgRWCGEDVAVKI--FSSRDERSWFREAEIYQTvmLRHENILGFIaadnKDNGTWTQLWLVS 220
Cdd:cd14107    6 VKEEI-GRGTFGfvkRVTH-KGNGECCAAKFipLRSSTRARAFQERDILAR--LSHRRLTCLL----DQFETRKTLILIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV--KKCETCAIADLGLAVK 297
Cdd:cd14107   78 ELCSSEELLDRLFLKGVVTEAEVKLYIqQVLEGIGYLH--------GMNILHLDIKPDNILMvsPTREDIKICDFGFAQE 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 161333835 298 HDSILntidiPQNPKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLV 347
Cdd:cd14107  150 ITPSE-----HQFSKYGSPEFVAPEIVHQE------PVSAATDIWALGVI 188
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
242-353 1.36e-04

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: 43.92  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 242 MIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA-VKHDSILNTidipqnPKVGTKRYMA 320
Cdd:cd07874  121 MSYLLYQMLCGIKHLH--------SAGIIHRDLKPSNIVVKSDCTLKILDFGLArTAGTSFMMT------PYVVTRYYRA 186
                         90       100       110
                 ....*....|....*....|....*....|...
gi 161333835 321 PEMLddtMNVNIFESfkrADIYSVGLVYWEIAR 353
Cdd:cd07874  187 PEVI---LGMGYKEN---VDIWSVGCIMGEMVR 213
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
146-430 1.36e-04

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: 43.22  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFG--EVWHGRWCGEDVAVKIFssrdERSWFREAEIYQTVM----LRHENILGFIAADNkdngTWTQLWLV 219
Cdd:cd14662    4 LVKDI-GSGNFGvaRLMRNKETKELVAVKYI----ERGLKIDENVQREIInhrsLRHPNIIRFKEVVL----TPTHLAIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYL-NRNIVTVAGMIKLALSIASGLAHLH-MEIvgtqgkpaiAHRDIKSKNILVKKCET--CAIADLGLA 295
Cdd:cd14662   75 MEYAAGGELFERIcNAGRFSEDEARYFFQQLISGVSYCHsMQI---------CHRDLKLENTLLDGSPAprLKICDFGYS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 vkHDSILNTidipqNPK--VGTKRYMAPEMLDDTMnvnifESFKRADIYSVGLVYWEIarrcsvggIVEEYqlPYYDmvP 373
Cdd:cd14662  146 --KSSVLHS-----QPKstVGTPAYIAPEVLSRKE-----YDGKVADVWSCGVTLYVM--------LVGAY--PFED--P 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 374 SDPsiEEMRKVVCD-QKFRPSIPNQWQ-SCEALRVMGRImrecWYANGAARLTALRIKK 430
Cdd:cd14662  202 DDP--KNFRKTIQRiMSVQYKIPDYVRvSQDCRHLLSRI----FVANPAKRITIPEIKN 254
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
236-415 1.40e-04

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 43.85  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 236 IVTVAGMIKLALSIASGlahlhMEIVGTQGkpaIAHRDIKSKNILVKKCETCAIADLGLA--VKHDSILntidIPQNPKV 313
Cdd:cd05107  235 ALSYMDLVGFSYQVANG-----MEFLASKN---CVHRDLAARNVLICEGKLVKICDFGLArdIMRDSNY----ISKGSTF 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 314 GTKRYMAPEmlddtmnvNIFESF--KRADIYSVGLVYWEIArrcSVGGIveeyqlPYydmvPSDPSIEEMRKVVcDQKFR 391
Cdd:cd05107  303 LPLKWMAPE--------SIFNNLytTLSDVWSFGILLWEIF---TLGGT------PY----PELPMNEQFYNAI-KRGYR 360
                        170       180
                 ....*....|....*....|....
gi 161333835 392 PSIPNQwqsceALRVMGRIMRECW 415
Cdd:cd05107  361 MAKPAH-----ASDEIYEIMQKCW 379
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
244-428 1.44e-04

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: 43.41  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 244 KLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV-----KKCETCAIADLGLAVK--HDSILNTidipqnpkVGTK 316
Cdd:cd14067  118 KIAYQIAAGLAYLH--------KKNIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQsfHEGALGV--------EGTP 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 317 RYMAPEMLDDTmnvnIFEsfKRADIYSVGLVYWEI--ARRCSVGgiveEYQLpyydmvpsdpsiEEMRKVvcDQKFRPSI 394
Cdd:cd14067  182 GYQAPEIRPRI----VYD--EKVDMFSYGMVLYELlsGQRPSLG----HHQL------------QIAKKL--SKGIRPVL 237
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 161333835 395 --PNQWQsceaLRVMGRIMRECWYANGAARLTALRI 428
Cdd:cd14067  238 gqPEEVQ----FFRLQALMMECWDTKPEKRPLACSV 269
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
147-349 1.53e-04

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: 43.31  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRW--CGEDVAVKIFssrDERSWFR---------EAEIYqtVMLRHENILGFIAADNKDNgtwtQ 215
Cdd:cd14186    5 VLNLLGKGSFACVYRARSlhTGLEVAIKMI---DKKAMQKagmvqrvrnEVEIH--CQLKHPSILELYNYFEDSN----Y 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLN--RNIVTVAGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd14186   76 VYLVLEMCHNGEMSRYLKnrKKPFTEDEARHFMHQIVTGMLYLH-----SHG---ILHRDLTLSNLLLTRNMNIKIADFG 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 294 LAVKhdsiLNTIDIPQNPKVGTKRYMAPEMLddTMNVNIFESfkraDIYSVGLVYW 349
Cdd:cd14186  148 LATQ----LKMPHEKHFTMCGTPNYISPEIA--TRSAHGLES----DVWSLGCMFY 193
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
149-351 1.60e-04

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: 43.42  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHG-RWC-GEDVAVKIFSsrdERSWFREAEiyQTVMLRHENIL------GFIAADNKDNGTWTQLWLVS 220
Cdd:cd05603    1 KVIGKGSFGKVLLAkRKCdGKFYAVKVLQ---KKTILKKKE--QNHIMAERNVLlknlkhPFLVGLHYSFQTSEKLYFVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGL---AV 296
Cdd:cd05603   76 DYVNGGELFFHLQRERCFLEPRARFyAAEVASAIGYLHSL--------NIIYRDLKPENILLDCQGHVVLTDFGLckeGM 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 297 KHDSILNTIdipqnpkVGTKRYMAPEMLDDtmnvnifESFKRA-DIYSVGLVYWEI 351
Cdd:cd05603  148 EPEETTSTF-------CGTPEYLAPEVLRK-------EPYDRTvDWWCLGAVLYEM 189
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
166-385 1.63e-04

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 43.39  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 166 GEDVAVK---IFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSEYHEQGSLYDYLNRNIVTvaGM 242
Cdd:cd08227   25 GEYVTVRrinLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADN----ELWVVTSFMAYGSAKDLICTHFMD--GM 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 243 IKLALS-----IASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILV----KKCETCAIADLGLaVKHDSILNTI-DIPQNp 311
Cdd:cd08227   99 SELAIAyilqgVLKALDYIHhMGYV---------HRSVKASHILIsvdgKVYLSGLRSNLSM-INHGQRLRVVhDFPKY- 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 312 KVGTKRYMAPEMLDDtmNVNIFESfkRADIYSVGLVYWEIARRcsvggiveeyQLPYYDMVPSDPSIEEMRKVV 385
Cdd:cd08227  168 SVKVLPWLSPEVLQQ--NLQGYDA--KSDIYSVGITACELANG----------HVPFKDMPATQMLLEKLNGTV 227
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
218-358 1.63e-04

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 43.01  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVK 297
Cdd:cd05078   80 LVQEYVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLE------EKTLVHGNVCAKNILLIREEDRKTGNPPFIKL 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 298 HDSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIfesfkRADIYSVGLVYWEIarrCSVG 358
Cdd:cd05078  154 SDPGISITVLPKDILLERIPWVPPECIENPKNLSL-----ATDKWSFGTTLWEI---CSGG 206
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
151-351 1.67e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 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: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 43.51  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWCG----EDVAVK-IFSSRDERSWFREAEIYQTvmLRHENILGF--IAADNKDNGTWT-------QL 216
Cdd:cd07868   25 VGRGTYGHVYKAKRKDgkddKDYALKqIEGTGISMSACREIALLRE--LKHPNVISLqkVFLSHADRKVWLlfdyaehDL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLydylNRNIVTVA-GMIK-LALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILV----KKCETCAIA 290
Cdd:cd07868  103 WHIIKFHRASKA----NKKPVQLPrGMVKsLLYQILDGIHYLHANWV--------LHRDLKPANILVmgegPERGRVKIA 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 291 DLGLAVKHDSILNTI-DIpqNPKVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEI 351
Cdd:cd07868  171 DMGFARLFNSPLKPLaDL--DPVVVTFWYRAPELLLGARHYT-----KAIDIWAIGCIFAEL 225
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
144-382 1.72e-04

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: 43.46  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDER----SWFREAEIYQTvmLRHENILGFIAADNKDNGtwtqLW 217
Cdd:cd07871    6 TYVKLDKLGEGTYATVFKGRskLTENLVALKEIRLEHEEgapcTAIREVSLLKN--LKHANIVTLHDIIHTERC----LT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQgSLYDYLNR--NIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA 295
Cdd:cd07871   80 LVFEYLDS-DLKQYLDNcgNLMSMHNVKIFMFQLLRGLSYCH--------KRKILHRDLKPQNLLINEKGELKLADFGLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTIdipqNPKVGTKRYMAPEMLddtmnVNIFESFKRADIYSVGLVYWEIA--RRCSVGGIV-EEYQL------ 366
Cdd:cd07871  151 RAKSVPTKTY----SNEVVTLWYRPPDVL-----LGSTEYSTPIDMWGVGCILYEMAtgRPMFPGSTVkEELHLifrllg 221
                        250
                 ....*....|....*..
gi 161333835 367 -PYYDMVPSDPSIEEMR 382
Cdd:cd07871  222 tPTEETWPGVTSNEEFR 238
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
147-351 1.79e-04

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: 43.19  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW---HGRWCGEDVAVKIFS----SRDERSWFREAEIYQTV----MLRHENILGFIAADNKDNgtwtQ 215
Cdd:cd14096    5 LINKIGEGAFSNVYkavPLRNTGKPVAIKVVRkadlSSDNLKGSSRANILKEVqimkRLSHPNIVKLLDFQESDE----Y 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDY----------LNRNIVTvagmiklalSIASGLAHLHmeivgtqgKPAIAHRDIKSKNIL----- 280
Cdd:cd14096   81 YYIVLELADGGEIFHQivrltyfsedLSRHVIT---------QVASAVKYLH--------EIGVVHRDIKPENLLfepip 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 281 -----VKKCET-----------------------CAIADLGLAVKHDSilNTIDIPqnpkVGTKRYMAPEMLDDtmnvni 332
Cdd:cd14096  144 fipsiVKLRKAdddetkvdegefipgvggggigiVKLADFGLSKQVWD--SNTKTP----CGTVGYTAPEVVKD------ 211
                        250       260
                 ....*....|....*....|
gi 161333835 333 fESF-KRADIYSVGLVYWEI 351
Cdd:cd14096  212 -ERYsKKVDMWALGCVLYTL 230
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
152-293 2.07e-04

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: 41.27  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVwhgRWC-----GEDVAVKIFSSR--DERSWF-REAEIYQTVMLRHENILGFIaaDNKDNGTWtqLWLVSEYH 223
Cdd:cd13968    2 GEGASAKV---FWAegectTIGVAVKIGDDVnnEEGEDLeSEMDILRRLKGLELNIPKVL--VTEDVDGP--NILLMELV 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGtqgkpaiaHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd13968   75 KGGTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLI--------HRDLNNDNILLSEDGNVKLIDFG 136
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
226-324 2.14e-04

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: 42.81  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 GSLYDYLNR-NIVTVAGMIKLALSIASGLAHLHMEIvgtqgkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilnt 304
Cdd:cd05606   83 GDLHYHLSQhGVFSEAEMRFYAAEVILGLEHMHNRF--------IVYRDLKPANILLDEHGHVRISDLGLACDFSK---- 150
                         90       100
                 ....*....|....*....|..
gi 161333835 305 idipQNPK--VGTKRYMAPEML 324
Cdd:cd05606  151 ----KKPHasVGTHGYMAPEVL 168
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
152-352 2.31e-04

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: 42.81  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 152 GKGRFGEVWHG-----RWCGEDVAVKIFSSRDerswFREAEIYQTVMLRH------ENILGFIAADNKDNGTWTQLWLVS 220
Cdd:cd14013    4 GEGGFGTVYKGsllqkDPGGEKRRVVLKKAKE----YGEVEIWMNERVRRacpsscAEFVGAFLDTTSKKFTKPSLWLVW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLN------------------------RNIVTVAGMIKlalSIASGLAHLHmeivGTqgkpAIAHRDIKS 276
Cdd:cd14013   80 KYEGDATLADLMQgkefpynlepiifgrvlipprgpkRENVIIKSIMR---QILVALRKLH----ST----GIVHRDVKP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 277 KNILV-KKCETCAIADLGLAVKHdsilnTIDIPQNPKVGT--KRYMAPE---MLDDT------------------MNvni 332
Cdd:cd14013  149 QNIIVsEGDGQFKIIDLGAAADL-----RIGINYIPKEFLldPRYAPPEqyiMSTQTpsappapvaaalspvlwqMN--- 220
                        250       260
                 ....*....|....*....|
gi 161333835 333 feSFKRADIYSVGLVYWEIA 352
Cdd:cd14013  221 --LPDRFDMYSAGVILLQMA 238
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
237-351 2.35e-04

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 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: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 43.04  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 237 VTVAGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDIKSKNILVKKCETCAIADLGLAVkhdsilntiDIPQNP---KV 313
Cdd:cd05102  169 LTMEDLICYSFQVARG-----MEFLASR---KCIHRDLAARNILLSENNVVKICDFGLAR---------DIYKDPdyvRK 231
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 161333835 314 GTKR----YMAPEMLDDTMNVNifesfkRADIYSVGLVYWEI 351
Cdd:cd05102  232 GSARlplkWMAPESIFDKVYTT------QSDVWSFGVLLWEI 267
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
149-324 3.37e-04

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: 42.64  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW--HGRWCGEDVAVK------IFSSRDERSWFREaeiyQTVMLRHENiLGFIAADNKDNGTWTQLWLVS 220
Cdd:cd05604    2 KVIGKGSFGKVLlaKRKRDGKYYAVKvlqkkvILNRKEQKHIMAE----RNVLLKNVK-HPFLVGLHYSFQTTDKLYFVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHD 299
Cdd:cd05604   77 DFVNGGELFFHLQRERSFPEPRARFyAAEIASALGYLH--------SINIVYRDLKPENILLDSQGHIVLTDFGLCKEGI 148
                        170       180
                 ....*....|....*....|....*
gi 161333835 300 SILNTidipQNPKVGTKRYMAPEML 324
Cdd:cd05604  149 SNSDT----TTTFCGTPEYLAPEVI 169
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
225-352 3.46e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 42.96  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 225 QGSLYDYLNR--NIVTVAGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAV------ 296
Cdd:PHA03211 243 RSDLYTYLGArlRPLGLAQVTAVARQLLSAIDYIHGE--------GIIHRDIKTENVLVNGPEDICLGDFGAACfargsw 314
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 ---KHDSILNTIDIPqnpkvgtkrymAPEML-DDTMNVNIfesfkraDIYSVGLVYWEIA 352
Cdd:PHA03211 315 stpFHYGIAGTVDTN-----------APEVLaGDPYTPSV-------DIWSAGLVIFEAA 356
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
249-351 3.59e-04

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: 42.22  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 249 IASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsiLNTIDIPQNPKVGTKRYMAPEMLDDTM 328
Cdd:cd14189  110 IISGLKYLHLK--------GILHRDLKLGNFFINENMELKVGDFGLAAR----LEPPEQRKKTICGTPNYLAPEVLLRQG 177
                         90       100
                 ....*....|....*....|...
gi 161333835 329 NvnifesFKRADIYSVGLVYWEI 351
Cdd:cd14189  178 H------GPESDVWSLGCVMYTL 194
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
228-352 3.76e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 42.67  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 228 LYDYL-NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKhdsilnTID 306
Cdd:PHA03212 169 LYCYLaAKRNIAICDILAIERSVLRAIQYLH--------ENRIIHRDIKAENIFINHPGDVCLGDFGAACF------PVD 234
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 161333835 307 IPQNPK---VGTKRYMAPEMLDDtmnvnifESFKRA-DIYSVGLVYWEIA 352
Cdd:PHA03212 235 INANKYygwAGTIATNAPELLAR-------DPYGPAvDIWSAGIVLFEMA 277
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
149-347 3.78e-04

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: 41.82  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW---------HGRWCGEDVAVK--IFSSRDERSwFREAEIYQTvmLR-HENILGFIAA-DNKDngtwtQ 215
Cdd:cd14019    7 EKIGEGTFSSVYkaedklhdlYDRNKGRLVALKhiYPTSSPSRI-LNELECLER--LGgSNNVSGLITAfRNED-----Q 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 216 LWLVSEYHEQGSLYDYLNRniVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILV-KKCETCAIADLGL 294
Cdd:cd14019   79 VVAVLPYIEHDDFRDFYRK--MSLTDIRIYLRNLFKALKHVH--------SFGIIHRDVKPGNFLYnRETGKGVLVDFGL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161333835 295 AVkhdsilntiDIPQN-----PKVGTKRYMAPEMLddtmnvniFESFKRA---DIYSVGLV 347
Cdd:cd14019  149 AQ---------REEDRpeqraPRAGTRGFRAPEVL--------FKCPHQTtaiDIWSAGVI 192
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
147-347 4.10e-04

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: 41.77  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEV---WHGRWCGEdVAVKIFSSRDERSWF------REAEIYQTVmlRHENILGFIAADNKDNGtwtQLW 217
Cdd:cd14164    4 LGTTIGEGSFSKVklaTSQKYCCK-VAIKIVDRRRASPDFvqkflpRELSILRRV--NHPNIVQMFECIEVANG---RLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQgSLYDYLNRN-IVTVAGMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILVKKCETCA-IADLGL 294
Cdd:cd14164   78 IVMEAAAT-DLLQKIQEVhHIPKDLARDMFAQMVGAVNYLHdMNIV---------HRDLKCENILLSADDRKIkIADFGF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 295 A--VKHDSILNTIdipqnpKVGTKRYMAPEMLddtmnVNIFESFKRADIYSVGLV 347
Cdd:cd14164  148 ArfVEDYPELSTT------FCGSRAYTPPEVI-----LGTPYDPKKYDVWSLGVV 191
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
2-45 4.84e-04

Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor types. This is an alignment of the hydrophilic cysteine-rich ligand-binding domains, Both receptor types, (type I and II) posses a 9 amino acid cysteine box, with the the consensus CCX{4-5}CN. The type I receptors also possess 7 extracellular residues preceding the cysteine box.


Pssm-ID: 460048  Cd Length: 78  Bit Score: 38.64  E-value: 4.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 161333835    2 LTNGKEQVI-KSCvsLPELNAQVFCHSSNN---VTKTECCFTDFCNNI 45
Cdd:pfam01064  32 DTDGFIECVkKGC--LSPEDDPFECKTSNKphsLYRIECCKTDFCNKN 77
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
149-370 5.25e-04

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: 41.96  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRW--CGEDVAVKIFS-----SRDERSW-FREAEIYQTVmlRHEnilgFIAADNKDNGTWTQLWLVS 220
Cdd:cd05571    1 KVLGKGTFGKVILCREkaTGELYAIKILKkeviiAKDEVAHtLTENRVLQNT--RHP----FLTSLKYSFQTNDRLCFVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYDYLNRNIVTVAGMIKL-ALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGLAVKHD 299
Cdd:cd05571   75 EYVNGGELFFHLSRERVFSEDRTRFyGAEIVLALGYLH-----SQG---IVYRDLKLENLLLDKDGHIKITDFGLCKEEI 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 300 SILNTIdipqNPKVGTKRYMAPEMLDDTmnvnifeSFKRA-DIYSVGLVYWEIArrCSvggiveeyQLPYYD 370
Cdd:cd05571  147 SYGATT----KTFCGTPEYLAPEVLEDN-------DYGRAvDWWGLGVVMYEMM--CG--------RLPFYN 197
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
147-351 5.33e-04

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: 41.91  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVW-----HGRWCGEDVAVKIFSSRDERSWFREAEIYQT--VMLRHENILGFIAADNKDNGTWTQLWLV 219
Cdd:cd05613    4 LLKVLGTGAYGKVFlvrkvSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTerQVLEHIRQSPFLVTLHYAFQTDTKLHLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNRNIVTVAGMIKLAL-SIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKH 298
Cdd:cd05613   84 LDYINGGELFTHLSQRERFTENEVQIYIgEIVLALEHLH--------KLGIIYRDIKLENILLDSSGHVVLTDFGLSKEF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161333835 299 --DSILNTIDIpqnpkVGTKRYMAPEMLD--DTMNVnifesfKRADIYSVGLVYWEI 351
Cdd:cd05613  156 llDENERAYSF-----CGTIEYMAPEIVRggDSGHD------KAVDWWSLGVLMYEL 201
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
183-351 5.48e-04

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: 41.95  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 183 FREAEIYQTVmlRHENILGFIaadnkdnGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGM-------IKLALSIASGLAH 255
Cdd:cd07875   71 YRELVLMKCV--NHKNIIGLL-------NVFTPQKSLEEFQDVYIVMELMDANLCQVIQMeldhermSYLLYQMLCGIKH 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 256 LHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSilntiDIPQNPKVGTKRYMAPEMLddtMNVNIFES 335
Cdd:cd07875  142 LH--------SAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGT-----SFMMTPYVVTRYYRAPEVI---LGMGYKEN 205
                        170
                 ....*....|....*.
gi 161333835 336 fkrADIYSVGLVYWEI 351
Cdd:cd07875  206 ---VDIWSVGCIMGEM 218
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
269-412 6.39e-04

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: 41.58  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 269 IAHRDIKSKNILVKKCETCAIADLGLA-------VKHDSILNTidipqnpKVGTKRYMAPEMLddtmnvNIFESFKRA-D 340
Cdd:cd07855  130 VIHRDLKPSNLLVNENCELKIGDFGMArglctspEEHKYFMTE-------YVATRWYRAPELM------LSLPEYTQAiD 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 341 IYSVGLVYWE-IARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCD------QKFRPSIPNQWQ------SCEALRVM 407
Cdd:cd07855  197 MWSVGCIFAEmLGRRQLFPGKNYVHQLQLILTVLGTPSQAVINAIGADrvrryiQNLPNKQPVPWEtlypkaDQQALDLL 276

                 ....*
gi 161333835 408 GRIMR 412
Cdd:cd07855  277 SQMLR 281
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
149-289 7.51e-04

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: 41.10  E-value: 7.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW--HGRWCGEDVAVKIFssRDERSWFREA--EIYQTVMLR------HENILGFIaadnkDNGTWTQ-LW 217
Cdd:cd14133    5 EVLGKGTFGQVVkcYDLLTGEEVALKII--KNNKDYLDQSldEIRLLELLNkkdkadKYHIVRLK-----DVFYFKNhLC 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161333835 218 LVSEYHEQgSLYDYLNRNI---VTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAI 289
Cdd:cd14133   78 IVFELLSQ-NLYEFLKQNKfqyLSLPRIRKIAQQILEALVFLH--------SLGLIHCDLKPENILLASYSRCQI 143
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
214-435 8.78e-04

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 41.02  E-value: 8.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 214 TQLWLVSEYHEQGSLYDYLNRNIVTVAGM-------IKLALSIASGLAHLHMEIVGTQGKpaiahrdIKSKNILVKKCET 286
Cdd:cd14044   76 TMIFGVIEYCERGSLRDVLNDKISYPDGTfmdwefkISVMYDIAKGMSYLHSSKTEVHGR-------LKSTNCVVDSRMV 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 287 CAIADLGLavkhDSILntidiPQNPKVGTkrymAPEMLddtMNVNIFEsfkRADIYSVGLVYWEIARRcsvggiveeyQL 366
Cdd:cd14044  149 VKITDFGC----NSIL-----PPSKDLWT----APEHL---RQAGTSQ---KGDVYSYGIIAQEIILR----------KE 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 367 PYYDMVPSDPSiEEMRKVVCDQK---FRPSIPNQWQSCEALRVMGrIMRECWYANGAARLTALRIKKTISQL 435
Cdd:cd14044  200 TFYTAACSDRK-EKIYRVQNPKGmkpFRPDLNLESAGEREREVYG-LVKNCWEEDPEKRPDFKKIENTLAKI 269
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
140-350 9.17e-04

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: 41.20  E-value: 9.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 140 TIARTIVLQEIVGKGRFGEVWHGRWCGED--VAVKIF----SSRDERS------WFREAEIYQTvmLRHENILGFIAADN 207
Cdd:cd14041    3 TLNDRYLLLHLLGRGGFSEVYKAFDLTEQryVAVKIHqlnkNWRDEKKenyhkhACREYRIHKE--LDHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 208 KDNGTWTQlwlVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHmEIvgtqgKPAIAHRDIKSKNILVKKCET 286
Cdd:cd14041   81 LDTDSFCT---VLEYCEGNDLDFYLKQHkLMSEKEARSIIMQIVNALKYLN-EI-----KPPIIHYDLKPGNILLVNGTA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 287 CA---IADLGLA-VKHDSILNTIDIPQ--NPKVGTKRYMAPEMLddTMNVNIFESFKRADIYSVGLVYWE 350
Cdd:cd14041  152 CGeikITDFGLSkIMDDDSYNSVDGMEltSQGAGTYWYLPPECF--VVGKEPPKISNKVDVWSVGVIFYQ 219
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
147-348 9.34e-04

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: 41.08  E-value: 9.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVwhgRWC-----GEDVAVKIF--SSRDERSwfrEAEIyqtvMLR---HENILGFiaADNKDNGTWTql 216
Cdd:cd14091    4 IKEEIGKGSYSVC---KRCihkatGKEYAVKIIdkSKRDPSE---EIEI----LLRygqHPNIITL--RDVYDDGNSV-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLNR----------NIVTVagmiklalsIASGLAHLHmeivgTQGkpaIAHRDIKSKNILV----K 282
Cdd:cd14091   70 YLVTELLRGGELLDRILRqkffsereasAVMKT---------LTKTVEYLH-----SQG---VVHRDLKPSNILYadesG 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333835 283 KCETCAIADLGLA--VKHDS-ILNTidiPqnpkVGTKRYMAPEMLddtmnvnifesfKRA------DIYSVG-LVY 348
Cdd:cd14091  133 DPESLRICDFGFAkqLRAENgLLMT---P----CYTANFVAPEVL------------KKQgydaacDIWSLGvLLY 189
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
147-325 1.03e-03

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: 40.64  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWHGRWCGED--VAVKIFSSRDERSwfREA----EIYQTVMLRHENILGFiaadNKDNGTWTQLWLVS 220
Cdd:cd14169    7 LKEKLGEGAFSEVVLAQERGSQrlVALKCIPKKALRG--KEAmvenEIAVLRRINHENIVSL----EDIYESPTHLYLAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 221 EYHEQGSLYD-YLNRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVK---KCETCAIADLGLA- 295
Cdd:cd14169   81 ELVTGGELFDrIIERGSYTEKDASQLIGQVLQAVKYLH--------QLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSk 152
                        170       180       190
                 ....*....|....*....|....*....|
gi 161333835 296 VKHDSILNTidipqnpKVGTKRYMAPEMLD 325
Cdd:cd14169  153 IEAQGMLST-------ACGTPGYVAPELLE 175
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
271-393 1.15e-03

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 41.01  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 271 HRDIKSKNILVKKCETCAIADLGLAvKHDSILNTIDIPQNpKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYWE 350
Cdd:PTZ00283 166 HRDIKSANILLCSNGLVKLGDFGFS-KMYAATVSDDVGRT-FCGTPYYVAPEIWRRK------PYSKKADMFSLGVLLYE 237
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161333835 351 I--ARRCSVGGIVEEYQ----LPYYDMVPSDPSiEEMRKVVC-----DQKFRPS 393
Cdd:PTZ00283 238 LltLKRPFDGENMEEVMhktlAGRYDPLPPSIS-PEMQEIVTallssDPKRRPS 290
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
271-351 1.28e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 41.16  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 271 HRDIKSKNILVKKCETCAIADLGLAVKH-DSIlnTIDIPQNpKVGTKRYMAPEMLDDTmnvnifESFKRADIYSVGLVYW 349
Cdd:PTZ00267 192 HRDLKSANIFLMPTGIIKLGDFGFSKQYsDSV--SLDVASS-FCGTPYYLAPELWERK------RYSKKADMWSLGVILY 262

                 ..
gi 161333835 350 EI 351
Cdd:PTZ00267 263 EL 264
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
150-324 1.31e-03

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: 40.21  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW--HGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAA-DNKDngtwtQLWLVSEYHEQG 226
Cdd:cd14087    8 LIGRGSFSRVVrvEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEVfETKE-----RVYMVMELATGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 227 SLYD-------YLNRNIVTVAGMIklalsiASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCA---IADLGLAV 296
Cdd:cd14087   83 ELFDriiakgsFTERDATRVLQMV------LDGVKYLH--------GLGITHRDLKPENLLYYHPGPDSkimITDFGLAS 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 161333835 297 KH----DSILNTIdipqnpkVGTKRYMAPEML 324
Cdd:cd14087  149 TRkkgpNCLMKTT-------CGTPEYIAPEIL 173
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
149-404 1.32e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 40.57  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFREAEIYQTVML---RHENILGFIAADNKDNgtwtQLWLVSEY- 222
Cdd:PLN00009   8 EKIGEGTYGVVYKARdrVTNETIALKKIRLEQEDEGVPSTAIREISLLkemQHGNIVRLQDVVHSEK----RLYLVFEYl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 223 ----HEQGSLYDYLNRNIVtvagMIKLAL-SIASGLAHLHMEivgtqgkpAIAHRDIKSKNILV-KKCETCAIADLGLAv 296
Cdd:PLN00009  84 dldlKKHMDSSPDFAKNPR----LIKTYLyQILRGIAYCHSH--------RVLHRDLKPQNLLIdRRTNALKLADFGLA- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 297 khdsilNTIDIPQNP---KVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEIARrcsvggiveeyQLPYYdmvP 373
Cdd:PLN00009 151 ------RAFGIPVRTfthEVVTLWYRAPEILLGSRHYS-----TPVDIWSVGCIFAEMVN-----------QKPLF---P 205
                        250       260       270
                 ....*....|....*....|....*....|....
gi 161333835 374 SDPSIEEMRKVvcdqkFRP-SIPNQ--WQSCEAL 404
Cdd:PLN00009 206 GDSEIDELFKI-----FRIlGTPNEetWPGVTSL 234
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
253-394 1.33e-03

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: 40.56  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 253 LAHLHMEivgtqgkPAIAHRDIKSKNILVKKCETCAIADLGLAVK---HDSILNTIdipqnpkVGTKRYMAPEMLDDtmn 329
Cdd:cd08528  126 LRYLHKE-------KQIVHRDLKPNNIMLGEDDKVTITDFGLAKQkgpESSKMTSV-------VGTILYSCPEIVQN--- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 330 vniFESFKRADIYSVGLVYWEIArrcsvggiveEYQLPY----------------YDMVPSDPSIEEMRKVV--C---DQ 388
Cdd:cd08528  189 ---EPYGEKADIWALGCILYQMC----------TLQPPFystnmltlatkiveaeYEPLPEGMYSDDITFVIrsCltpDP 255

                 ....*.
gi 161333835 389 KFRPSI 394
Cdd:cd08528  256 EARPDI 261
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
146-321 1.36e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK 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: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 40.32  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFGEVWHGR--WCGEDVAVKIFSSRDERSWFR--EAEIYQTVMLRHenILGFIAADNKDNGTWTQLWLVSE 221
Cdd:cd14017    4 VVKKI-GGGGFGEIYKVRdvVDGEEVAMKVESKSQPKQVLKmeVAVLKKLQGKPH--FCRLIGCGRTERYNYIVMTLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 222 yheqgSLYDY---LNRNIVTVAGMIKLALSIASGLAHLHMeiVGtqgkpaIAHRDIKSKNILV----KKCETCAIADLGL 294
Cdd:cd14017   81 -----NLAELrrsQPRGKFSVSTTLRLGIQILKAIEDIHE--VG------FLHRDVKPSNFAIgrgpSDERTVYILDFGL 147
                        170       180       190
                 ....*....|....*....|....*....|..
gi 161333835 295 AVKHdsILNTIDIPQNPK-----VGTKRYMAP 321
Cdd:cd14017  148 ARQY--TNKDGEVERPPRnaagfRGTVRYASV 177
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
151-351 1.43e-03

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 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: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 40.44  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVWHGRWC-GED---VAVK-IFSSRDERSWFREAEIYQTvmLRHENILGF--IAADNKDNGTWT-------QL 216
Cdd:cd07867   10 VGRGTYGHVYKAKRKdGKDekeYALKqIEGTGISMSACREIALLRE--LKHPNVIALqkVFLSHSDRKVWLlfdyaehDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLydylNRNIVTVA-GMIK-LALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILV----KKCETCAIA 290
Cdd:cd07867   88 WHIIKFHRASKA----NKKPMQLPrSMVKsLLYQILDGIHYLHANWV--------LHRDLKPANILVmgegPERGRVKIA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333835 291 DLGLAVKHDSILNTI-DIpqNPKVGTKRYMAPEMLDDTMNVNifesfKRADIYSVGLVYWEI 351
Cdd:cd07867  156 DMGFARLFNSPLKPLaDL--DPVVVTFWYRAPELLLGARHYT-----KAIDIWAIGCIFAEL 210
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
140-350 1.48e-03

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: 40.43  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 140 TIARTIVLQEIVGKGRFGEVWHGRWCGED--VAVKIF----SSRDERS------WFREAEIYQTvmLRHENILGFIAADN 207
Cdd:cd14040    3 TLNERYLLLHLLGRGGFSEVYKAFDLYEQryAAVKIHqlnkSWRDEKKenyhkhACREYRIHKE--LDHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 208 KDNGTWTQlwlVSEYHEQGSLYDYLNRN-IVTVAGMIKLALSIASGLAHLHmEIvgtqgKPAIAHRDIKSKNILVKKCET 286
Cdd:cd14040   81 LDTDTFCT---VLEYCEGNDLDFYLKQHkLMSEKEARSIVMQIVNALRYLN-EI-----KPPIIHYDLKPGNILLVDGTA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 287 CA---IADLGLA--VKHDSI-LNTIDIPQNpKVGTKRYMAPEMLddTMNVNIFESFKRADIYSVGLVYWE 350
Cdd:cd14040  152 CGeikITDFGLSkiMDDDSYgVDGMDLTSQ-GAGTYWYLPPECF--VVGKEPPKISNKVDVWSVGVIFFQ 218
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
144-281 1.58e-03

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 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: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 40.42  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 144 TIVLQEIVGKGRFG---EVWHGRWCGED--VAVKIfssrdERS---WfrEAEIYQTVMLRHEN------ILGFIAADNKD 209
Cdd:cd13981    1 TYVISKELGEGGYAsvyLAKDDDEQSDGslVALKV-----EKPpsiW--EFYICDQLHSRLKNsrlresISGAHSAHLFQ 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 210 NGTWtqlwLVSEYHEQGSLYDYLNR-NIVTVAGM-----IKLALSIASGLAHLH-MEIVgtqgkpaiaHRDIKSKNILV 281
Cdd:cd13981   74 DESI----LVMDYSSQGTLLDVVNKmKNKTGGGMdeplaMFFTIELLKVVEALHeVGII---------HGDIKPDNFLL 139
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
149-282 1.68e-03

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: 40.22  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVW----HGRwcGEDVAVKIFssRDERSWFR----EAEIYQTVMLRHENILGFIAaDNKDNGTWTQ-LWLV 219
Cdd:cd14210   19 SVLGKGSFGQVVkcldHKT--GQLVAIKII--RNKKRFHQqalvEVKILKHLNDNDPDDKHNIV-RYKDSFIFRGhLCIV 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 220 SEYHEQgSLYDYLNRNivTVAGM----IKL-ALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVK 282
Cdd:cd14210   94 FELLSI-NLYELLKSN--NFQGLslslIRKfAKQILQALQFLH--------KLNIIHCDLKPENILLK 150
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
151-347 1.68e-03

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: 40.29  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVwhgRWC-----GEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQ 225
Cdd:cd14198   16 LGRGKFAVV---RQCiskstGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 226 GSLYDYL---NRNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCA---IADLGLAVKHD 299
Cdd:cd14198   93 GEIFNLCvpdLAEMVSENDIIRLIRQILEGVYYLH--------QNNIVHLDLKPQNILLSSIYPLGdikIVDFGMSRKIG 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 161333835 300 SILNTIDIpqnpkVGTKRYMAPEMLDdtmnvniFESFKRA-DIYSVGLV 347
Cdd:cd14198  165 HACELREI-----MGTPEYLAPEILN-------YDPITTAtDMWNIGVI 201
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
149-391 1.69e-03

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: 40.38  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 149 EIVGKGRFGEVWHGRWCGED--VAVKIFSS-----RDERSWFREAeiyQTVMLRHEN--ILGFIAADNKDNgtwtQLWLV 219
Cdd:cd05623   78 KVIGRGAFGEVAVVKLKNADkvFAMKILNKwemlkRAETACFREE---RDVLVNGDSqwITTLHYAFQDDN----NLYLV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 220 SEYHEQGSLYDYLNR------NIVTVAGMIKLALSIASgLAHLHMeivgtqgkpaiAHRDIKSKNILVKKCETCAIADLG 293
Cdd:cd05623  151 MDYYVGGDLLTLLSKfedrlpEDMARFYLAEMVLAIDS-VHQLHY-----------VHRDIKPDNILMDMNGHIRLADFG 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 294 LAVKhdsILNTIDIPQNPKVGTKRYMAPEMLdDTMNVNIFESFKRADIYSVGLVYWEI----------ARRCSVGGIV-- 361
Cdd:cd05623  219 SCLK---LMEDGTVQSSVAVGTPDYISPEIL-QAMEDGKGKYGPECDWWSLGVCMYEMlygetpfyaeSLVETYGKIMnh 294
                        250       260       270
                 ....*....|....*....|....*....|.
gi 161333835 362 -EEYQLPYYDMVPSDPSIEEMRKVVCDQKFR 391
Cdd:cd05623  295 kERFQFPTQVTDVSENAKDLIRRLICSREHR 325
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
150-351 1.72e-03

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: 40.08  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 150 IVGKGRFGEVW-----HGRWCGEDVAVKIF--SSRDERSWFReaeiyqTVMLRheNILG-----FIAADNKDNGTWTQLW 217
Cdd:cd05582    2 VLGQGSFGKVFlvrkiTGPDAGTLYAMKVLkkATLKVRDRVR------TKMER--DILAdvnhpFIVKLHYAFQTEGKLY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 218 LVSEYHEQGSLYDYLNRNIVTVAGMIKLALS-IASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGL-- 294
Cdd:cd05582   74 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAeLALALDHLH-----SLG---IIYRDLKPENILLDEDGHIKLTDFGLsk 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161333835 295 -AVKHDSILNTIdipqnpkVGTKRYMAPEMlddtmnVNIFESFKRADIYSVGLVYWEI 351
Cdd:cd05582  146 eSIDHEKKAYSF-------CGTVEYMAPEV------VNRRGHTQSADWWSFGVLMFEM 190
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
153-324 1.85e-03

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: 39.89  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 153 KGRFGEVWHGRWC--GEDVAVKIFSSRDER------SWFREAEIYqtVMLRHENILGFIAA-DNKDNgtwtqLWLVSEYH 223
Cdd:cd05579    3 RGAYGRVYLAKKKstGDLYAIKVIKKRDMIrknqvdSVLAERNIL--SQAQNPFVVKLYYSfQGKKN-----LYLVMEYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 224 EQGSLYDYLnRNI----VTVAGMIklALSIASGLAHLHmeivgTQGkpaIAHRDIKSKNILVKKCETCAIADLGL----- 294
Cdd:cd05579   76 PGGDLYSLL-ENVgaldEDVARIY--IAEIVLALEYLH-----SHG---IIHRDLKPDNILIDANGHLKLTDFGLskvgl 144
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 161333835 295 ---AVKHDSILNTIDIPQNPK---VGTKRYMAPEML 324
Cdd:cd05579  145 vrrQIKLSIQKKSNGAPEKEDrriVGTPDYLAPEIL 180
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
151-324 1.90e-03

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: 40.11  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 151 VGKGRFGEVW--HGRWCGEDVAVKIFSSRD------------ERSWFREaeiyqtvmLRHENILGFIAADNKDNgtwtQL 216
Cdd:cd05612    9 IGTGTFGRVHlvRDRISEHYYALKVMAIPEvirlkqeqhvhnEKRVLKE--------VSHPFIIRLFWTEHDQR----FL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSLYDYLnRNIVTVAGMIKL--ALSIASGLAHLHMEivgtqgkpAIAHRDIKSKNILVKKCETCAIADLGL 294
Cdd:cd05612   77 YMLMEYVPGGELFSYL-RNSGRFSNSTGLfyASEIVCALEYLHSK--------EIVYRDLKPENILLDKEGHIKLTDFGF 147
                        170       180       190
                 ....*....|....*....|....*....|
gi 161333835 295 AVKHDSILNTIdipqnpkVGTKRYMAPEML 324
Cdd:cd05612  148 AKKLRDRTWTL-------CGTPEYLAPEVI 170
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
146-351 1.99e-03

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: 40.08  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 146 VLQEIvGKGRFGEV----WHGRWCGEDVAVK----IFSSR--DERSwFREAEIYQtvMLR-HENILGFIAADNKDNGTWT 214
Cdd:cd07857    4 LIKEL-GQGAYGIVcsarNAETSEEETVAIKkitnVFSKKilAKRA-LRELKLLR--HFRgHKNITCLYDMDIVFPGNFN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 215 QLWLVSEYHEqgslYDyLNRNI-----VTVAGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDIKSKNILVK-KCETcA 288
Cdd:cd07857   80 ELYLYEELME----AD-LHQIIrsgqpLTDAHFQSFIYQILCGLKYIHSANV--------LHRDLKPGNLLVNaDCEL-K 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161333835 289 IADLGLAVkhdsilntiDIPQNPK---------VGTKRYMAPE-MLDdtmnvniFESFKRA-DIYSVGLVYWEI 351
Cdd:cd07857  146 ICDFGLAR---------GFSENPGenagfmteyVATRWYRAPEiMLS-------FQSYTKAiDVWSVGCILAEL 203
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
149-190 2.60e-03

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 39.23  E-value: 2.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 161333835 149 EIVGKGRFGEVWHGRWCGEDVAVKIF---SSRDerSWFREAEIYQ 190
Cdd:COG2112   46 RLLGKGYRGVVFLGKLGGKKVALKIRrtdSPRP--SLKKEAEILK 88
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
212-324 3.54e-03

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: 38.91  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 212 TWTQLWLVSEYHEQGSLYDYLN-RNIVTVAGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIA 290
Cdd:cd05583   70 TDAKLHLILDYVNGGELFTHLYqREHFTESEVRIYIGEIVLALEHLH--------KLGIIYRDIKLENILLDSEGHVVLT 141
                         90       100       110
                 ....*....|....*....|....*....|....
gi 161333835 291 DLGLAvkhDSILNTIDIPQNPKVGTKRYMAPEML 324
Cdd:cd05583  142 DFGLS---KEFLPGENDRAYSFCGTIEYMAPEVV 172
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
252-352 3.85e-03

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: 39.10  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 252 GLAHLHmeivgtqGKPAIAHRDIKSKNIL--VKKCEtCAIADLGLAV---KHdsilNTIDIpQnpkvgTKRYMAPEMLdd 326
Cdd:cd14136  131 GLDYLH-------TKCGIIHTDIKPENVLlcISKIE-VKIADLGNACwtdKH----FTEDI-Q-----TRQYRSPEVI-- 190
                         90       100
                 ....*....|....*....|....*.
gi 161333835 327 tMNVNIFESfkrADIYSVGLVYWEIA 352
Cdd:cd14136  191 -LGAGYGTP---ADIWSTACMAFELA 212
TFP_LU_ECD_Sax cd23600
extracellular domain (ECD) found in Drosophila melanogaster Saxophone and similar proteins; ...
3-44 4.24e-03

extracellular domain (ECD) found in Drosophila melanogaster Saxophone and similar proteins; Saxophone (Sax) is the Drosophila bone morphogenetic protein (BMP) type I receptor that transmits signal through Mad. It functions as a Dpp (Decapentaplegic) receptor in Drosophila embryos, but that its activity is normally inhibited by the O-linked glycosyltransferase Sxc (Super sex combs). Saxophone is the ortholog of the human activin receptor-like kinase (ALK)-1/2. It contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467129  Cd Length: 89  Bit Score: 36.13  E-value: 4.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161333835   3 TNGKEQVIKSCVSLPElNAQVFC----HSSNNVTK-------TECCFTDFCNN 44
Cdd:cd23600   34 SDGKERVSRGCITEPD-QVPFTCntksHSGSSKKKpnsgqysVECCQGDFCNN 85
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
147-324 4.47e-03

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: 39.06  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 147 LQEIVGKGRFGEVWH--GRWCGEDVAVKI-----FSSRDERSWF---REAEIYQtvMLRHENILGFIAADNKDNgtwtQL 216
Cdd:cd14094    7 LCEVIGKGPFSVVRRciHRETGQQFAVKIvdvakFTSSPGLSTEdlkREASICH--MLKHPHIVELLETYSSDG----ML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 217 WLVSEYHEQGSL-YDYLNRnivTVAGMIkLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADL-GL 294
Cdd:cd14094   81 YMVFEFMDGADLcFEIVKR---ADAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLgGF 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 161333835 295 AVKHDsiLNTIDIPQNPKVGTKRYMAPEML 324
Cdd:cd14094  157 GVAIQ--LGESGLVAGGRVGTPHFMAPEVV 184
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
145-323 5.54e-03

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: 38.65  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 145 IVLQEIVGKGRFGEVWhgrwCGED-----------VAVKIFSSRDERSWF-----REAEIYQTVmlrHENILGFIAADNK 208
Cdd:cd13991    8 ATHQLRIGRGSFGEVH----RMEDkqtgfqcavkkVRLEVFRAEELMACAgltspRVVPLYGAV---REGPWVNIFMDLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333835 209 DNGTWTQLwlvseYHEQGSLYDylnrnivtvagmiKLALS----IASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKK- 283
Cdd:cd13991   81 EGGSLGQL-----IKEQGCLPE-------------DRALHylgqALEGLEYLH--------SRKILHGDVKADNVLLSSd 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 161333835 284 CETCAIADLGLAVK-HDSILNTIDIPQNPKVGTKRYMAPEM 323
Cdd:cd13991  135 GSDAFLCDFGHAEClDPDGLGKSLFTGDYIPGTETHMAPEV 175
TFP cd00117
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
3-43 6.63e-03

three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU (also known as Ly-6 antigen/uPA receptor)-like extracellular domain (ECD) occurs singly in GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2) or as three-fold repeated domain in urokinase-type plasminogen activator receptor. It is a structural domain involved in protein-protein interactions, tolerating an unusual degree of variation and binding with high specificity to a broad spectrum of targets. The snake toxin domain is present in short and long neurotoxins, cytotoxins, and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. Both the LU-like ECD and the snake toxin domain belong to three-fingered protein (TFP) fold, which is characterized by containing 70 to 100 amino acids including eight to ten cysteine residues spaced at conserved distances.


Pssm-ID: 467060  Cd Length: 81  Bit Score: 35.54  E-value: 6.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 161333835   3 TNGKEQVIKSCVSLPELNAQVFCH--SSNNVTKTECCFTDFCN 43
Cdd:cd00117   39 GGGETLVIRGCATECECGCTECCSgtGTSGTTCTSCCDTDLCN 81
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
249-324 7.07e-03

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: 38.35  E-value: 7.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333835 249 IASGLAHLHmeivgtqgKPAIAHRDIKSKNILVKKCETCAIADLGLA---VKHDSILNTIdipqnpkVGTKRYMAPEML 324
Cdd:cd05570  105 ICLALQFLH--------ERGIIYRDLKLDNVLLDAEGHIKIADFGMCkegIWGGNTTSTF-------CGTPDYIAPEIL 168
 
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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