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Conserved domains on  [gi|1784638851|ref|NP_001364065|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 isoform b [Homo sapiens]

Protein Classification

EFh_PI-PLCbeta4 and PI-PLCc_beta domain-containing protein( domain architecture ID 11598256)

protein containing domains PH_PLC_beta, EFh_PI-PLCbeta4, PI-PLCc_beta, and C2_PLC_like

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 312-668 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PLC-beta isozymes (1-4). They are activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. The beta-gamma subunits of heterotrimeric G proteins are known to activate the PLC-beta2 and -beta3 isozymes only. Aside from four PLC-beta isozymes identified in mammals, some eukaryotic PLC-beta homologs have been classified into this subfamily, such as NorpA and PLC-21 from Drosophila and PLC-beta from turkey, Xenopus, sponge, and hydra.


:

Pssm-ID: 176533 [Multi-domain]  Cd Length: 257  Bit Score: 556.57  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08591        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08591    154 -------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDS 220

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08591    221 SNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 148-300 1.05e-102

EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4, or phospholipase C-beta-4 (PLC-beta4), is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It may play a critical role in linking anxiety behaviors and theta rhythm heterogeneity. PI-PLC-beta4 is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta4 functions as a downstream signaling molecule of type 1 metabotropic glutamate receptors (mGluR1s). The thalamic mGluR1-PI-PLC-beta4 cascade is essential for formalin-induced inflammatory pain by regulating the response of ventral posterolateral thalamic nucleus (VPL) neurons. Moreover, PI-PLC-beta4 is essential for long-term depression (LTD) in the rostral cerebellum, which may be required for the acquisition of the conditioned eyeblink response. Besides, PI-PLC-beta4 may play an important role in maintenance of the status epilepticus. The mutations of PI-PLC-beta4 has been identified as the major cause of autosomal dominant auriculocondylar syndrome (ACS). PI-PLC-beta4 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


:

Pssm-ID: 320041  Cd Length: 153  Bit Score: 320.52  E-value: 1.05e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  148 KKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16211      1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16211     81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-143 6.15e-62

Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


:

Pssm-ID: 270167  Cd Length: 127  Bit Score: 206.65  E-value: 6.15e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   17 LQEGAVFDRYEEESfVFEPNCLFKVDEFGFFLTWRSEGKEGQVLECSLINSIRSGAIPKDPKILAALE-AVGKSENDLEG 95
Cdd:cd13361      1 LLKGSKFDKWDEDS-SLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREvNVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1784638851   96 RIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSP 143
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 702-818 3.79e-42

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


:

Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 150.38  E-value: 3.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  702 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 775
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1784638851  776 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 818
Cdd:cd00275     80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 913-955 1.32e-17

Protein of unknown function (DUF1154); This family represents a small conserved region of unknown function within eukaryotic phospholipase C (EC:3.1.4.3). All members also contain pfam00387 and pfam00388.


:

Pssm-ID: 461969  Cd Length: 45  Bit Score: 77.30  E-value: 1.32e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1784638851  913 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 955
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PTZ00121 super family cl31754
MAEBL; Provisional
 839-1170 2.54e-08

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  839 KKFLSITEKRADQMRAMGIETSDIADVP-SDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASGVEAKKGIELipQV 917
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KK 1398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  918 RIEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEMKKE 997
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-----EAKKA 1472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  998 TEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQ--EIRDLHLSQQCELLKKllinAHE-QQTQQLKLSHD-RES 1073
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKK----AEEaKKADEAKKAEEkKKA 1548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1074 KEMRAHQAKISMENSKAISQdksiKNKAERE-----RRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHL--EF 1146
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEE----AKKAEEDknmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEE 1624

                          330       340
                   ....*....|....*....|....
gi 1784638851 1147 LEKQNEQAKEMQQMVKLEAEMDRR 1170
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKK 1648
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 312-668 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PLC-beta isozymes (1-4). They are activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. The beta-gamma subunits of heterotrimeric G proteins are known to activate the PLC-beta2 and -beta3 isozymes only. Aside from four PLC-beta isozymes identified in mammals, some eukaryotic PLC-beta homologs have been classified into this subfamily, such as NorpA and PLC-21 from Drosophila and PLC-beta from turkey, Xenopus, sponge, and hydra.


Pssm-ID: 176533 [Multi-domain]  Cd Length: 257  Bit Score: 556.57  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08591        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08591    154 -------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDS 220

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08591    221 SNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 148-300 1.05e-102

EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4, or phospholipase C-beta-4 (PLC-beta4), is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It may play a critical role in linking anxiety behaviors and theta rhythm heterogeneity. PI-PLC-beta4 is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta4 functions as a downstream signaling molecule of type 1 metabotropic glutamate receptors (mGluR1s). The thalamic mGluR1-PI-PLC-beta4 cascade is essential for formalin-induced inflammatory pain by regulating the response of ventral posterolateral thalamic nucleus (VPL) neurons. Moreover, PI-PLC-beta4 is essential for long-term depression (LTD) in the rostral cerebellum, which may be required for the acquisition of the conditioned eyeblink response. Besides, PI-PLC-beta4 may play an important role in maintenance of the status epilepticus. The mutations of PI-PLC-beta4 has been identified as the major cause of autosomal dominant auriculocondylar syndrome (ACS). PI-PLC-beta4 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320041  Cd Length: 153  Bit Score: 320.52  E-value: 1.05e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  148 KKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16211      1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16211     81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 315-462 1.88e-77

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 250.89  E-value: 1.88e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  315 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 394
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWD--GPDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1784638851  395 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgraLPSPNDLKRKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLDDDLTE----LPSPEDLKGKILIKG 142
PLN02228 PLN02228
Phosphoinositide phospholipase C
 218-807 2.17e-72

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 252.26  E-value: 2.17e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  218 PRTDIEDLFKKINGDktDYLTVDQLVSFLNEHQ--RDPRLNEILFPFYDAKRAmqiiEMYEPdedlkkKGLISSDGFCRY 295
Cdd:PLN02228    22 PPVSIKRLFEAYSRN--GKMSFDELLRFVSEVQgeRHAGLDYVQDIFHSVKHH----NVFHH------HGLVHLNAFYRY 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  296 LMSDENAPVFLDRlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCW-DGKGEDQEpiIT 374
Cdd:PLN02228    90 LFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWpNPSGNAAE--VR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  375 HGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShplepGRALPSPNDL 454
Cdd:PLN02228   167 HGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHLPPNLQAQVAKMLTKTFRGMLFRCTSES-----TKHFPSPEEL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  455 KRKILIKNKRLKPEVEKKQLEALRSMMEagESASPANILEDDNEEEIESADQEEEAhpefkfgnelsaddLGHKEAVAns 534
Cdd:PLN02228   242 KNKILISTKPPKEYLESKTVQTTRTPTV--KETSWKRVADAENKILEEYKDEESEA--------------VGYRDLIA-- 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  535 vkkglvtvedeqawmasykyvgattnIHPylstmINYAQPVKfQGFHVAEERNIHYNMS-SFNESVglgyLKTHAIEFVN 613
Cdd:PLN02228   304 --------------------------IHA-----ANCKDPLK-DCLSDDPEKPIRVSMDeQWLETM----VRTRGTDLVR 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  614 YNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSET 693
Cdd:PLN02228   348 FTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILLDEHTLFDPCKRL 427

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  694 PvdgvIAATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIrkEFRTRMVMNNGLnPVYNEESFVFrKVI 763
Cdd:PLN02228   428 P----IKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV--SYRTETAVDQWF-PIWGNDEFLF-QLR 499

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1784638851  764 LPDLAVLRIAV--YDDN--NKLIGQRILPLDGLQAGYRHISLRNEGNK 807
Cdd:PLN02228   500 VPELALLWFKVqdYDNDtqNDFAGQTCLPLPELKSGVRAVRLHDRAGK 547
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 566-680 4.61e-66

Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 128454 [Multi-domain]  Cd Length: 115  Bit Score: 217.88  E-value: 4.61e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   566 STMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQ 645
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1784638851   646 MVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFM 680
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-143 6.15e-62

Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 270167  Cd Length: 127  Bit Score: 206.65  E-value: 6.15e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   17 LQEGAVFDRYEEESfVFEPNCLFKVDEFGFFLTWRSEGKEGQVLECSLINSIRSGAIPKDPKILAALE-AVGKSENDLEG 95
Cdd:cd13361      1 LLKGSKFDKWDEDS-SLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREvNVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1784638851   96 RIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSP 143
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-140 3.42e-58

PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C enzymes.


Pssm-ID: 465506  Cd Length: 131  Bit Score: 196.44  E-value: 3.42e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   12 EVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVLECSLINSIRSGA---IPKDPKILAALeAVGK 88
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPNVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKfakIPKDPKLREVL-SMGG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1784638851   89 SENDLEGRIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANN 140
Cdd:pfam17787   80 SDNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 702-818 3.79e-42

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 150.38  E-value: 3.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  702 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 775
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1784638851  776 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 818
Cdd:cd00275     80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 913-955 1.32e-17

Protein of unknown function (DUF1154); This family represents a small conserved region of unknown function within eukaryotic phospholipase C (EC:3.1.4.3). All members also contain pfam00387 and pfam00388.


Pssm-ID: 461969  Cd Length: 45  Bit Score: 77.30  E-value: 1.32e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1784638851  913 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 955
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 705-801 5.50e-14

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 69.05  E-value: 5.50e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   705 VQVISGQFLSDKKIGT----YVEVDMYGLPtdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN-- 778
Cdd:smart00239    4 VKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVKNT-LNPVWNET-FEF-EVPPPELAELEIEVYDKDrf 76

                            90       100
                    ....*....|....*....|....*
gi 1784638851   779 --NKLIGQRILPLDGLQAGYRHISL 801
Cdd:smart00239   77 grDDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 209-300 5.79e-14

Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are predominantly found in phosphoinositide-specific phospholipase C. They adopt a structure consisting of a core of four alpha helices, in an EF like fold, and are required for functioning of the enzyme.


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 68.43  E-value: 5.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  209 FY-ELTQkicpRTDIEDLFKKINGDkTDYLTVDQLVSFLNEHQRDPRlneilfpfYDAKRAMQIIEMYEPDEDLKKKGLI 287
Cdd:pfam09279    1 FYkMLTQ----REEIDEIFQEYSGD-GQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAM 67

                           90
                   ....*....|...
gi 1784638851  288 SSDGFCRYLMSDE 300
Cdd:pfam09279   68 TKDGFLMYLCSPD 80
C2 pfam00168
C2 domain;
704-798 2.25e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.79  E-value: 2.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  704 SVQVISGQFLSDKKIG----TYVEVDMYGLptdtiRKEFRTRmVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 778
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNgtsdPYVKVYLLDG-----KQKKKTK-VVKNTLNPVWNET-FTF-SVPDPENAVLEIEVYDYDr 75

                           90       100
                   ....*....|....*....|...
gi 1784638851  779 ---NKLIGQRILPLDGLQAGYRH 798
Cdd:pfam00168   76 fgrDDFIGEVRIPLSELDSGEGL 98
PTZ00121 PTZ00121
MAEBL; Provisional
 839-1170 2.54e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  839 KKFLSITEKRADQMRAMGIETSDIADVP-SDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASGVEAKKGIELipQV 917
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KK 1398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  918 RIEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEMKKE 997
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-----EAKKA 1472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  998 TEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQ--EIRDLHLSQQCELLKKllinAHE-QQTQQLKLSHD-RES 1073
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKK----AEEaKKADEAKKAEEkKKA 1548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1074 KEMRAHQAKISMENSKAISQdksiKNKAERE-----RRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHL--EF 1146
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEE----AKKAEEDknmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEE 1624

                          330       340
                   ....*....|....*....|....
gi 1784638851 1147 LEKQNEQAKEMQQMVKLEAEMDRR 1170
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKK 1648
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 1035-1174 2.13e-07

PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 51.99  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1035 EQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMrahQAKISMENSKAISQ-DKSIKNKAERERRVRELNSS 1113
Cdd:pfam08703   25 EKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEM---KKKLERKRLESIQEaKKRTSDKAAQERLKKEINNS 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1784638851 1114 NTKKFLEERKRLAMKQSKEMDQLKKVQ---LEHLEFLEKQNEQakemQQMVKLEAEMDRRPATV 1174
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQaecLQQIKEEEPQLQA----ELNAEYEEKLKGLPAEV 161
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 798-1162 3.22e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  798 HISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSiteKRADQMRAmgiETSDIAdvPSDTSKNDKKGK 877
Cdd:TIGR00618  354 EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC---KELDILQR---EQATID--TRTSAFRDLQGQ 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  878 ANTAKANVTPQssseLRPTTTAALASGVEAKKGIELIP-----QVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHST 952
Cdd:TIGR00618  426 LAHAKKQQELQ----QRYAELCAAAITCTAQCEKLEKIhlqesAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  953 MQKLHCTQV----DKIVAQYDKEKST--------HEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSkvkEIVAQH 1020
Cdd:TIGR00618  502 EPCPLCGSCihpnPARQDIDNPGPLTrrmqrgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF---SILTQC 578

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1021 TKEWSEMINTHSAEEQEIRDLhLSQQCELLKKLLInahEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQ-DKSIKN 1099
Cdd:TIGR00618  579 DNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLAC---EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlHALQLT 654

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851 1100 KAERERRVRELNSSNTKKFLEERKRLAMkqsKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMVK 1162
Cdd:TIGR00618  655 LTQERVREHALSIRVLPKELLASRQLAL---QKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1022-1170 3.77e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1022 KEWSEMINTHSAEEQEIRDLHLSQQCELLKKLL-------------INAHEQQTQQLKLSHDRESKEMRAHQAKISMENS 1088
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELeeleaeleeleaeLAELEAELEELRLELEELELELEEAQAEEYELLA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1089 KAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMD 1168
Cdd:COG1196    296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                   ..
gi 1784638851 1169 RR 1170
Cdd:COG1196    376 EA 377
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 312-668 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PLC-beta isozymes (1-4). They are activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. The beta-gamma subunits of heterotrimeric G proteins are known to activate the PLC-beta2 and -beta3 isozymes only. Aside from four PLC-beta isozymes identified in mammals, some eukaryotic PLC-beta homologs have been classified into this subfamily, such as NorpA and PLC-21 from Drosophila and PLC-beta from turkey, Xenopus, sponge, and hydra.


Pssm-ID: 176533 [Multi-domain]  Cd Length: 257  Bit Score: 556.57  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08591        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08591    154 -------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDS 220

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08591    221 SNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 312-668 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 4. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta4 is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension.


Pssm-ID: 176563 [Multi-domain]  Cd Length: 257  Bit Score: 531.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08626      1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08626     81 IKDTAFVTSDYPVILSFENHCSKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08626        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08626    154 -------------LSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDS 220

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08626    221 SNYMPQIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 312-668 5.19e-134

Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; This family corresponds to the catalytic domain present in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) and similar proteins. The higher eukaryotic PI-PLCs play a critical role in most signal transduction pathways, controlling numerous cellular events such as cell growth, proliferation, excitation and secretion. They strictly require Ca2+ for the catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated membrane phospholipids PI-analogues, phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP), to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. The eukaryotic PI-PLCs have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, such as the pleckstrin homology (PH) domain, EF-hand motif, and C2 domain. The catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a linker region. The catalytic mechanism of eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. The mammalian PI-PLCs consist of 13 isozymes, which are classified into six-subfamilies, PI-PLC-delta (1,3 and 4), -beta(1-4), -gamma(1,2), -epsilon, -zeta, and -eta (1,2). Ca2+ is required for the activation of all forms of mammalian PI-PLCs, and the concentration of calcium influences substrate specificity. This family also includes metazoan phospholipase C related but catalytically inactive proteins (PRIP), which belong to a group of novel inositol trisphosphate binding proteins. Due to the replacement of critical catalytic residues, PRIP does not have PLC enzymatic activity.


Pssm-ID: 176501 [Multi-domain]  Cd Length: 226  Bit Score: 406.45  E-value: 5.19e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08558      1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGP--DGEPVVYHGHTLTSKILFKDVIEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgraLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08558     79 IKEYAFVTSPYPVILSLENHCSLEQQKKMAQILKEIFGDKLLTPPLDENPVQ----LPSPEQLKGKILIKGKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08558        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08558    148 --------------------------------------YHMSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDS 189

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08558    190 SNYNPQPFWNAGCQMVALNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 312-668 2.48e-116

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 361.30  E-value: 2.48e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLkpeve 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKKY----- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  471 kkqlealrsmmeagesaspanileddnEEeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawma 550
Cdd:cd08624    156 ---------------------------EE--------------------------------------------------- 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  551 sykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVD 630
Cdd:cd08624    158 --------------MSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMD 223

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1784638851  631 SSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08624    224 SSNYMPQMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 314-668 5.37e-114

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 3. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta3 is widely expressed at highest levels in brain, liver, and parotid gland. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176562 [Multi-domain]  Cd Length: 258  Bit Score: 355.13  E-value: 5.37e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  314 EMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIK 393
Cdd:cd08625      3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  394 ETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRlkpevekk 472
Cdd:cd08625     83 ESAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  473 qlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmasy 552
Cdd:cd08625        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  553 kyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSS 632
Cdd:cd08625    155 ------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSS 222

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1784638851  633 NYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08625    223 NYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 312-668 1.19e-109

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This CD corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. Aside from three PI-PLC-delta isozymes identified in mammals, some eukaryotic PI-PLC-delta homologs have been classified to this CD.


Pssm-ID: 176535 [Multi-domain]  Cd Length: 257  Bit Score: 343.17  E-value: 1.19e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08593      1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWD--GPDGEPIIYHGHTLTSKILFKDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShplePGRALPSPNDLKRKILIKNKRLKpevek 471
Cdd:cd08593     79 IREYAFKVSPYPVILSLENHCSVEQQKVMAQHLKSILGDKLLTQPLDG----VLTALPSPEELKGKILVKGKKLK----- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08593        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08593    150 ---------LAKELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDS 220

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08593    221 SNYDPQEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 148-300 1.05e-102

EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4, or phospholipase C-beta-4 (PLC-beta4), is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It may play a critical role in linking anxiety behaviors and theta rhythm heterogeneity. PI-PLC-beta4 is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta4 functions as a downstream signaling molecule of type 1 metabotropic glutamate receptors (mGluR1s). The thalamic mGluR1-PI-PLC-beta4 cascade is essential for formalin-induced inflammatory pain by regulating the response of ventral posterolateral thalamic nucleus (VPL) neurons. Moreover, PI-PLC-beta4 is essential for long-term depression (LTD) in the rostral cerebellum, which may be required for the acquisition of the conditioned eyeblink response. Besides, PI-PLC-beta4 may play an important role in maintenance of the status epilepticus. The mutations of PI-PLC-beta4 has been identified as the major cause of autosomal dominant auriculocondylar syndrome (ACS). PI-PLC-beta4 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320041  Cd Length: 153  Bit Score: 320.52  E-value: 1.05e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  148 KKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16211      1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16211     81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 313-668 2.59e-98

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta1 is expressed at highest levels in specific regions of the brain. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension.


Pssm-ID: 176560 [Multi-domain]  Cd Length: 258  Bit Score: 313.17  E-value: 2.59e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08623      2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  393 KETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08623     82 AECAFKTSPFPILLSFENHVdSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08623        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08623    155 -------------MSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDS 221

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08623    222 SNYMPQLFWNAGCQMVALNFQTVDLSMQINMGMYEYN 258
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 313-668 3.79e-94

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain.The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. There are two PI-PLC-gamma isozymes (1-2). They are activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region. Aside from the two PI-PLC-gamma isozymes identified in mammals, some eukaryotic PI-PLC-gamma homologs have been classified with this subfamily.


Pssm-ID: 176534 [Multi-domain]  Cd Length: 229  Bit Score: 300.50  E-value: 3.79e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGkgEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08592      2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQaleshPLEP-GRALPSPNDLKRKILIKNKRLKpevek 471
Cdd:cd08592     80 KEHAFVTSEYPVILSIENHCSLPQQRNMAQAFKEVFGDMLLTQ-----PVDRnADQLPSPNQLKRKIIIKHKKLF----- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08592        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYL-KTHAIEFVNYNKRQMSRIYPKGGRVD 630
Cdd:cd08592    150 --------------------------------------YEMSSFPETKAEKYLnRQKGKIFLKYNRRQLSRVYPKGQRVD 191

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1784638851  631 SSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08592    192 SSNYDPVPMWNCGSQMVALNFQTPDKPMQLNQALFMLN 229
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 313-668 2.31e-90

Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This family corresponds to the catalytic domain present in metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel Inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(previously known as p130 or PLC-1), which is predominantly expressed in the brain, and PRIP-2 (previously known as PLC-2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 176539 [Multi-domain]  Cd Length: 260  Bit Score: 291.25  E-value: 2.31e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGkgEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08597      2 QDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQAleshPLEPGRALPSPNDLKRKILIKNKRLKpevekk 472
Cdd:cd08597     80 NEYAFVASEYPLILCIENHCSEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKKLK------ 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  473 qlealrsmmeagesaspanileddneeeiesadqeeeahpEFKFGNELSadDLghkeavansvkkglvtvedeqawmasy 552
Cdd:cd08597    150 ----------------------------------------RRKLCKELS--DL--------------------------- 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  553 kyvgattnihpylstmINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSS 632
Cdd:cd08597    161 ----------------VSLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSS 224

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1784638851  633 NYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08597    225 NYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 312-665 6.07e-87

Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This family corresponds to the catalytic domain present in a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this CD is protein Plc1p encoded by PLC1 genes from Saccharomyces cerevisiae. Plc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that Plc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like Plc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 176540 [Multi-domain]  Cd Length: 231  Bit Score: 280.67  E-value: 6.07e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08598      1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWD--GDDGEPVVTHGYTLTSSVPFRDVCRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgraLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08598     79 IKKYAFVTSPYPLILSLEVHCDAEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeEEAHPEFKFgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08598    148 ------------------------------------ESKTPNHIF----------------------------------- 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpylstminyaqpvkfqgfhvaeernihynmsSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08598    157 ------------------------------------------SLSERSLLKLLKDKRAALDKHNRRHLMRVYPSGTRISS 194

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKF 665
Cdd:cd08598    195 SNFNPLPFWRAGVQMVALNWQTYDLGMQLNEAMF 228
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 312-668 2.79e-84

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta3 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This family corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus.


Pssm-ID: 176567 [Multi-domain]  Cd Length: 258  Bit Score: 274.59  E-value: 2.79e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGedQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08630      1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPG--GEPVIYHGHTLTSKILFRDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrALPSPNDLKRKILIKNKRLKpevek 471
Cdd:cd08630     79 VRQHAFTASPYPVILSLENHCGLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQ----- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08630        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08630    151 ---------ISPELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNS 221

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08630    222 ANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 313-668 1.62e-81

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-epsilon isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-epsilon represents a class of mammalian PI-PLC that has an N-terminal CDC25 homology domain with a guanyl-nucleotide exchange factor (GFF) activity, a pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and two predicted RA (Ras association) domains that are implicated in the binding of small GTPases, such as Ras or Rap, from the Ras family. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PI-PLC-epsilon isozyme (1). PI-PLC-epsilon is activated by G alpha(12/13), G beta gamma, and activated members of Ras and Rho small GTPases. Aside from PI-PLC-epsilon identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 176538 [Multi-domain]  Cd Length: 254  Bit Score: 266.71  E-value: 1.62e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08596      2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWD--GDDGMPIIYHGHTLTTKIPFKDVVEAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRlkpevekk 472
Cdd:cd08596     80 NRSAFITSDYPVILSIENHCSLQQQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  473 qlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmasy 552
Cdd:cd08596        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  553 kyvgattniHPYLSTMINYAQPVKFQGFHVAEerniHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSS 632
Cdd:cd08596    152 ---------APELSDLVIYCQAVKFPGLSTPK----CYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSS 218

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1784638851  633 NYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08596    219 NPNPLIFWLHGLQLVALNYQTDDLPMHLNAAMFEAN 254
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 312-668 1.75e-79

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta1 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This subfamily corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1and 3 from the cell nucleus. Experiments show PI-PLC-delta1 is essential for normal hair formation.


Pssm-ID: 176566 [Multi-domain]  Cd Length: 258  Bit Score: 261.51  E-value: 1.75e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08629      1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGP--NQEPIIYHGYTFTSKILFCDVLRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgraLPSPNDLKRKILIKNKRLKPEVEk 471
Cdd:cd08629     79 IRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTS----LPSPEQLKGKILLKGKKLKLVPE- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08629        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQGFH-VAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVD 630
Cdd:cd08629    154 -------------LSDMIIYCKSVHFGGFSsPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTD 220

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1784638851  631 SSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08629    221 SSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 312-668 3.49e-79

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are two PI-PLC-eta isozymes (1-2), both neuron-specific enzymes. They function as calcium sensors that are activated by small increases in intracellular calcium concentrations. The PI-PLC-eta isozymes are also activated through GPCR stimulation. Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 176536 [Multi-domain]  Cd Length: 227  Bit Score: 259.35  E-value: 3.49e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08594      1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDGP--DGEPVVHHGYTLTSKILFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLlkqALESHPLEPGRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08594     79 INKYAFIKNEYPVILSIENHCSVQQQKKMAQYLKEILGDKL---DLSSVISGDSKQLPSPQSLKGKILIKGKK------- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmas 551
Cdd:cd08594        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08594    149 --------------------------------------WQVSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDS 190

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08594    191 SNFNPQPYWNAGCQLVALNYQTEGRMLQLNRAKFRAN 227
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 312-668 2.64e-78

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta4 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This CD corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4. Experiments show PI-PLC-delta4 is required for the acrosome reaction in fertilization.


Pssm-ID: 176568 [Multi-domain]  Cd Length: 258  Bit Score: 258.34  E-value: 2.64e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08631      1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDGP--NGEPIVYHGHTFTSKILFKDVVAA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEshplepGRA---LPSPNDLKRKILIKNKRLKpe 468
Cdd:cd08631     79 VAQYAFQVSDYPVILSLENHCGVEQQQTMAQHLTEILGEKLLSTTLD------GVLptqLPSPEELRGKILLKGKKIR-- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  469 vekkqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqaw 548
Cdd:cd08631        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  549 masykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGR 628
Cdd:cd08631    151 ------------LSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLR 218

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1784638851  629 VDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08631    219 TDSSNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 312-668 3.65e-78

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family corresponds to the catalytic domain presenting in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-zeta isozyme. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-zeta represents a class of sperm-specific PI-PLC that has an N-terminal EF-hand domain, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PLC-zeta isozyme (1). PLC-zeta plays a fundamental role in vertebrate fertilization by initiating intracellular calcium oscillations that trigger the embryo development. However, the mechanism of its activation still remains unclear. Aside from PI-PLC-zeta identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 176537 [Multi-domain]  Cd Length: 257  Bit Score: 257.56  E-value: 3.65e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08595      1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGA--DNEPVVYHGYTLTSKILFKEVITT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEsHPlePGRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08595     79 VEKYAFEKSDYPVVLSLENHCSTEQQEIMAHYLVSILGEKLLRAPID-DP--ATGELPSPEALKFKILVKNKK------- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghKEAVAnsvkkglvtvedeqawmas 551
Cdd:cd08595    149 --------------------------------------------------------KIAKA------------------- 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08595    154 -------------LSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASS 220

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08595    221 SNYNPQEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN 257
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 315-462 1.88e-77

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 250.89  E-value: 1.88e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  315 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 394
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWD--GPDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1784638851  395 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgraLPSPNDLKRKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLDDDLTE----LPSPEDLKGKILIKG 142
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 313-668 2.66e-76

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta2 is a neuron-specific enzyme and expressed in the brain. It may in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain.


Pssm-ID: 176570 [Multi-domain]  Cd Length: 254  Bit Score: 252.27  E-value: 2.66e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08633      2 QDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGP--DGEPIVHHGYTLTSKILFKDVIETI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDlllKQALESHPLEPGRALPSPNDLKRKILIKNKRLKpevekk 472
Cdd:cd08633     80 NKYAFIKNEYPVILSIENHCSVPQQKKMAQYLTEILGD---KLDLSSVISNDCTRLPSPEILKGKILVKGKKLS------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  473 qlealRSmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmasy 552
Cdd:cd08633    151 -----RA------------------------------------------------------------------------- 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  553 kyvgattnihpyLSTMINYAQPVkfqGFHVAE-ERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08633    153 ------------LSDLVKYTKSV---RVHDIEtEATSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDS 217

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08633    218 SNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 312-668 2.45e-73

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta1 is a neuron-specific enzyme and expressed in only nerve tissues such as the brain and spinal cord. It may perform a fundamental role in the brain.


Pssm-ID: 176569 [Multi-domain]  Cd Length: 253  Bit Score: 244.17  E-value: 2.45e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08632      1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDGP--DGEPVVHHGYTLTSKITFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLL-LKQALESHPlepgRALPSPNDLKRKILIKNKRLkpeve 470
Cdd:cd08632     79 INKYAFVKNEFPVILSIENHCSIQQQKKIAQYLKEIFGDKLdLSSVLTGDP----KQLPSPQLLKGKILVKGKKL----- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  471 kkqLEALRSMMEAGESASPANILEDdneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawma 550
Cdd:cd08632    150 ---CRDLSDLVVYTNSVAAQDIVDD------------------------------------------------------- 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  551 sykyvGATTNIhpylstminyaqpvkfqgfhvaeernihynmSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVD 630
Cdd:cd08632    172 -----GSTGNV-------------------------------LSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRID 215

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1784638851  631 SSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08632    216 SSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 313-668 1.19e-72

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma1, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. PI-PLC-gamma1 is ubiquitously expressed. It is activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region.


Pssm-ID: 176564 [Multi-domain]  Cd Length: 229  Bit Score: 241.09  E-value: 1.19e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08627      2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGP--DGMPVIYHGHTLTTKIKFSDVLHTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHplepGRALPSPNDLKRKILIKNKRLkpevekk 472
Cdd:cd08627     80 KEHAFVTSEYPIILSIEDHCSIVQQRNMAQHFKKVFGDMLLTKPVDIN----ADGLPSPNQLKRKILIKHKKL------- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  473 qlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkglvtvedeqawmasy 552
Cdd:cd08627        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  553 kyvgattnihpylstminyaqpvkfqgfhvaeerniHYNMSSFNESVGLGYL-KTHAIEFVNYNKRQMSRIYPKGGRVDS 631
Cdd:cd08627    149 ------------------------------------YRDMSSFPETKAEKYVnRSKGKKFLQYNRRQLSRIYPKGQRLDS 192

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08627    193 SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
PLN02228 PLN02228
Phosphoinositide phospholipase C
 218-807 2.17e-72

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 252.26  E-value: 2.17e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  218 PRTDIEDLFKKINGDktDYLTVDQLVSFLNEHQ--RDPRLNEILFPFYDAKRAmqiiEMYEPdedlkkKGLISSDGFCRY 295
Cdd:PLN02228    22 PPVSIKRLFEAYSRN--GKMSFDELLRFVSEVQgeRHAGLDYVQDIFHSVKHH----NVFHH------HGLVHLNAFYRY 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  296 LMSDENAPVFLDRlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCW-DGKGEDQEpiIT 374
Cdd:PLN02228    90 LFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWpNPSGNAAE--VR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  375 HGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShplepGRALPSPNDL 454
Cdd:PLN02228   167 HGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHLPPNLQAQVAKMLTKTFRGMLFRCTSES-----TKHFPSPEEL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  455 KRKILIKNKRLKPEVEKKQLEALRSMMEagESASPANILEDDNEEEIESADQEEEAhpefkfgnelsaddLGHKEAVAns 534
Cdd:PLN02228   242 KNKILISTKPPKEYLESKTVQTTRTPTV--KETSWKRVADAENKILEEYKDEESEA--------------VGYRDLIA-- 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  535 vkkglvtvedeqawmasykyvgattnIHPylstmINYAQPVKfQGFHVAEERNIHYNMS-SFNESVglgyLKTHAIEFVN 613
Cdd:PLN02228   304 --------------------------IHA-----ANCKDPLK-DCLSDDPEKPIRVSMDeQWLETM----VRTRGTDLVR 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  614 YNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSET 693
Cdd:PLN02228   348 FTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILLDEHTLFDPCKRL 427

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  694 PvdgvIAATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIrkEFRTRMVMNNGLnPVYNEESFVFrKVI 763
Cdd:PLN02228   428 P----IKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV--SYRTETAVDQWF-PIWGNDEFLF-QLR 499

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1784638851  764 LPDLAVLRIAV--YDDN--NKLIGQRILPLDGLQAGYRHISLRNEGNK 807
Cdd:PLN02228   500 VPELALLWFKVqdYDNDtqNDFAGQTCLPLPELKSGVRAVRLHDRAGK 547
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 148-300 1.65e-71

EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta isozymes; PI-PLC-beta isozymes represent a class of metazoan PI-PLCs that hydrolyze the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) to propagate diverse intracellular responses that underlie the physiological action of many hormones, neurotransmitters, and growth factors (EC 3.1.4.11). They have been implicated in numerous processes relevant to central nervous system (CNS), including chemotaxis, cardiovascular function, neuronal signaling, and opioid sensitivity. Like other PI-PLC isozymes, PI-PLC-beta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, they have a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PI-PLC-beta isozymes (1-4). PI-PLC-beta1 and PI-PLC-beta3 are expressed in a wide range of tissues and cell types, whereas PI-PLC-beta2 and PI-PLC-beta4 have been found only in hematopoietic and neuronal tissues, respectively. All PI-PLC-beta isozymes are activated by the heterotrimeric G protein alpha subunits of the Gq class through their C2 domain and long C-terminal extension. They are GTPase-activating proteins (GAPs) for these G alpha(q) proteins. PI-PLC-beta2 and PI-PLC-beta3 can also be activated by beta-gamma subunits of the G alpha(i/o) family of heterotrimeric G proteins and the small GTPases such as Rac and Cdc42. This family also includes two invertebrate homologs of PI-PLC-beta, PLC21 from cephalopod retina and No receptor potential A protein (NorpA) from Drosophila melanogaster.


Pssm-ID: 320030 [Multi-domain]  Cd Length: 153  Bit Score: 234.83  E-value: 1.65e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  148 KKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16200      1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDKKRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16200     81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 313-668 1.29e-70

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozyme 2. PI-PLC is a signaling enzyme that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma2, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. PI-PLC-gamma2 is highly expressed in cells of hematopoietic origin. It is activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region. Unlike PI-PLC-gamma1, the activation of PI-PLC-gamma2 may require concurrent stimulation of PI 3-kinase.


Pssm-ID: 176565 [Multi-domain]  Cd Length: 254  Bit Score: 236.49  E-value: 1.29e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08628      2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDGP--DGKPIIYHGWTRTTKIKFDDVVQAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQaleshPLEP-GRALPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08628     80 KDHAFVTSEYPVILSIEEHCSVEQQRHMAKVFKEVFGDKLLMK-----PLEAsADQLPSPTQLKEKIIIKHKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddlghkeavansvkkgLVTVEdeqawmas 551
Cdd:cd08628    148 -------------------------------------------------------------------LIAIE-------- 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpyLSTMINYAQPVKFQ--GFHVAEERNIHynmsSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRV 629
Cdd:cd08628    153 -------------LSDLVVYCKPTSKTkdNLENPDFKEIR----SFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRV 215

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1784638851  630 DSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08628    216 DSSNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN 254
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 148-300 1.88e-70

EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and similar proteins; NorpA, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase, is an eye-specific phosphoinositide phospholipase C (PI-PLC) encoded by norpA gene in Drosophila. It is expressed predominantly in photoreceptors and plays an essential role in the phototransduction pathway of Drosophila. A mutation within the norpA gene can render the fly blind without affecting any of the obvious structures of the eye. Like beta-class of vertebrate PI-PLCs, NorpA contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320042 [Multi-domain]  Cd Length: 153  Bit Score: 232.05  E-value: 1.88e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  148 KKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16212      1 KKHWMRLGFMVDSGGKIPVKHIARTFASGKTEKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16212     81 SITKGKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 566-680 4.61e-66

Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 128454 [Multi-domain]  Cd Length: 115  Bit Score: 217.88  E-value: 4.61e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   566 STMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQ 645
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1784638851   646 MVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFM 680
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 312-668 1.70e-64

Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This subfamily corresponds to the catalytic domain present in prokaryotic and eukaryotic phosphoinositide-specific phospholipase C (PI-PLC), which is a ubiquitous enzyme catalyzing the cleavage of the sn3-phosphodiester bond in the membrane phosphoinositides (phosphatidylinositol, PI; Phosphatidylinositol-4-phosphate, PIP; phosphatidylinositol 4,5-bisphosphate, PIP2) to yield inositol phosphates (inositol monosphosphate, InsP; inositol diphosphate, InsP2; inositol trisphosphate, InsP3) and diacylglycerol (DAG). The higher eukaryotic PI-PLCs (EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. They play a critical role in most signal transduction pathways, controlling numerous cellular events, such as cell growth, proliferation, excitation and secretion. These PI-PLCs strictly require Ca2+ for their catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated PI-analogues, PIP2 and PIP, to generate two important second messengers, InsP3 and DAG. InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. In contrast, bacterial PI-PLCs contain a single catalytic domain. Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. They participate in Ca2+-independent PI metabolism. They are characterized as phosphatidylinositol-specific phospholipase C (EC 4.6.1.13) that selectively hydrolyze PI, not PIP or PIP2. The TIM-barrel type catalytic domain in bacterial PI-PLCs is very similar to the one in eukaryotic PI-PLCs, in which the catalytic domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. The catalytic mechanism of both prokaryotic and eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host#s immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.


Pssm-ID: 176497 [Multi-domain]  Cd Length: 274  Bit Score: 219.83  E-value: 1.70e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQF-----GGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMcTDILFK 386
Cdd:cd00137      1 HHPDTQPLAHYSIPGTHDTYLTAGQFtikqvWGLTQTEMYRQQLLSGCRCVDIRCWDGK--PEEPIIYHGPTF-LDIFLK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  387 DVIQAIKETAFVTSEYPVILSFENHCSKY--QQYKMSKYCEDLFGDLLLkqaleSHPLEPGRALPSPNDLKRKILIKNKR 464
Cdd:cd00137     78 EVIEAIAQFLKKNPPETIIMSLKNEVDSMdsFQAKMAEYCRTIFGDMLL-----TPPLKPTVPLPSLEDLRGKILLLNKK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  465 lkpevekkqlealrsmmeagesaspanileddneeeiesadqeeeahpefkfgnelsaddLGHKEAVANSVKKGLVTVEd 544
Cdd:cd00137    153 ------------------------------------------------------------NGFSGPTGSSNDTGFVSFE- 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  545 eqawmasykyvgattnihpyLSTMINYAqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIE----FVNYNKRQMS 620
Cdd:cd00137    172 --------------------FSTQKNRS-----------------YNISSQDEYKAYDDEKVKLIKatvqFVDYNKNQLS 214

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  621 RIYPKGGRV---------DSSNYMPQIFWN---AGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd00137    215 RNYPSGTSGgtawyyyamDSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 315-463 3.68e-63

Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 210.99  E-value: 3.68e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   315 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 394
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWD--GPDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1784638851   395 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgraLPSPNDLKRKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHCSPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 204-804 7.47e-63

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 225.29  E-value: 7.47e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  204 FSYEKFYELTQKICPRtDIEDLFKKINgdKTDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEmyEPDEDLKK 283
Cdd:PLN02222    10 FCFRRRFRYTASEAPR-EIKTIFEKYS--ENGVMTVDHLHRFLIDVQKQDKATR--------EDAQSIIN--SASSLLHR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  284 KGLiSSDGFCRYLMSDENAPVFLDrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWD 363
Cdd:PLN02222    77 NGL-HLDAFFKYLFGDNNPPLALH--EVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWP 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  364 GKGEDQEPIItHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEshplE 443
Cdd:PLN02222   154 NSDKDDIDVL-HGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVG----E 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  444 PGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSMMEAGES-----ASPANILEDDNEEEIESAdqeeeahpefkfGN 518
Cdd:PLN02222   229 SLKEFPSPNSLKKRIIISTKPPKEYKEGKDDEVVQKGKDLGDEevwgrEVPSFIQRNKSVDKNDSN------------GD 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  519 ELSADDLGHKEAVANSVK--KGLVTVEdeqawmASYKYVGATTNIHpylstminyAQPVKFQGFHVAEERnihynMSSFN 596
Cdd:PLN02222   297 DDDDDDDGEDKSKKNAPPqyKHLIAIH------AGKPKGGITECLK---------VDPDKVRRLSLSEEQ-----LEKAA 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  597 ESvglgylktHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLK 676
Cdd:PLN02222   357 EK--------YAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKK 428

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  677 PDFMRRPD---RTFDPFSETPVDgviaATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIRKefRTRMV 743
Cdd:PLN02222   429 PDLLLKSGsdsDIFDPKATLPVK----TTLRVTIYMGEgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK--KTKTL 502

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1784638851  744 MNNGLnPVYnEESFVFrKVILPDLAVLRIAV--YDDNNK--LIGQRILPLDGLQAGYRHISLRNE 804
Cdd:PLN02222   503 EDNWI-PAW-DEVFEF-PLTVPELALLRLEVheYDMSEKddFGGQTCLPVWELSQGIRAFPLHSR 564
PLN02952 PLN02952
phosphoinositide phospholipase C
 218-809 1.46e-62

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 224.88  E-value: 1.46e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  218 PRTDIEDLFKKINgDKTDYLTVDQLVSFLNEHQrdprlNEILFPFYDAKRAM-QIIEMYEPDEDLKKKGLISSDGFCRYL 296
Cdd:PLN02952    36 PPDDVKDVFCKFS-VGGGHMGADQLRRFLVLHQ-----DELDCTLAEAQRIVeEVINRRHHVTRYTRHGLNLDDFFHFLL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  297 MSDENAPVFLdrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDqEPIITHG 376
Cdd:PLN02952   110 YDDLNGPITP---QVHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKD-EILVLHG 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  377 KAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQalESHPLepgRALPSPNDLKR 456
Cdd:PLN02952   186 RTLTTPVPLIKCLKSIRDYAFSSSPYPVIITLEDHLTPDLQAKVAEMATQIFGQMLYYP--ESDSL---VQFPSPESLKH 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  457 KILIKNKRLKPEVEKKQLealrSMMEAGESASPANileddneeeIESADQEEEAHPEFKFGNELSADDLGHKEAVANsvk 536
Cdd:PLN02952   261 RIIISTKPPKEYLESSGP----IVIKKKNNVSPSG---------RNSSEETEEAQTLESMLFEQEADSRSDSDQDDN--- 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  537 kglvtvEDEQAWMASYKYVgattnihpylsTMINYAQP---VKfQGFHVAEERnihYNMSSFNESVGLGYLKTHAIEFVN 613
Cdd:PLN02952   325 ------KSGELQKPAYKRL-----------ITIHAGKPkgtLK-DAMKVAVDK---VRRLSLSEQELEKAATTNGQDVVR 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  614 YNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRP---DRTFDPF 690
Cdd:PLN02952   384 FTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKgfhDEVFDPK 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  691 SETPVdgviAATCSVQVISG----------QFLSDKKIGTYVEVDMYGLPTDTIRKefRTRMVMNNgLNPVYNEEsFVFr 760
Cdd:PLN02952   464 KKLPV----KKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK--KTKIIEDN-WYPAWNEE-FSF- 534

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  761 KVILPDLAVLRIAV--YD--DNNKLIGQRILPLDGLQAGYRHISLRNEGNKPL 809
Cdd:PLN02952   535 PLTVPELALLRIEVreYDmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-143 6.15e-62

Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 270167  Cd Length: 127  Bit Score: 206.65  E-value: 6.15e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   17 LQEGAVFDRYEEESfVFEPNCLFKVDEFGFFLTWRSEGKEGQVLECSLINSIRSGAIPKDPKILAALE-AVGKSENDLEG 95
Cdd:cd13361      1 LLKGSKFDKWDEDS-SLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREvNVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1784638851   96 RIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSP 143
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 565-679 7.87e-62

Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to form a single structural unit.


Pssm-ID: 459794  Cd Length: 114  Bit Score: 205.77  E-value: 7.87e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  565 LSTMINYAQPVKFQGFHvAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGC 644
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1784638851  645 QMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDF 679
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-140 3.42e-58

PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C enzymes.


Pssm-ID: 465506  Cd Length: 131  Bit Score: 196.44  E-value: 3.42e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   12 EVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVLECSLINSIRSGA---IPKDPKILAALeAVGK 88
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPNVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKfakIPKDPKLREVL-SMGG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1784638851   89 SENDLEGRIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANN 140
Cdd:pfam17787   80 SDNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 148-300 1.57e-54

EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family includes invertebrate homologs of phosphoinositide phospholipase C beta (PI-PLC-beta) named PLC21 from cephalopod retina. It also includes PLC21 encoded by plc-21 gene, which is expressed in the central nervous system of Drosophila. Like beta-class of vertebrate PI-PLCs, PLC21 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320043  Cd Length: 154  Bit Score: 186.74  E-value: 1.57e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  148 KKHWMKLAFMTNTNGKIPVRSITRTFASGKTE-KVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLF 226
Cdd:cd16213      1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQHKDDrKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1784638851  227 KKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16213     81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYLMSED 154
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 312-668 7.89e-54

Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family corresponds to the catalytic domain present in a group of phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11) encoded by PLC genes from higher plants, which are homologs of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The domain arrangement of plant PI-PLCs is structurally similar to the mammalian PLC-zeta isoform, which lacks the N-terminal pleckstrin homology (PH) domain, but contains EF-hand like motifs (which are absent in a few plant PLCs), a PLC catalytic core domain with X- and Y- highly conserved regions split by a linker sequence, and a C2 domain. However, at the sequence level, the plant PI-PLCs are closely related to the mammalian PLC-delta isoform. Experiments show that plant PLCs display calcium dependent PLC catalytic properties, although they lack some of the N-terminal motifs found in their mammalian counterparts. A putative calcium binding site may be located at the region spanning the X- and Y- domains.


Pssm-ID: 176541 [Multi-domain]  Cd Length: 228  Bit Score: 187.58  E-value: 7.89e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDqePIITHGKAMCTDILFKDVIQA 391
Cdd:cd08599      1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQalesHPLEPGRALPSPNDLKRKILIknkRLKPEVek 471
Cdd:cd08599     79 IKENAFTASEYPVIITLENHLSPELQAKAAQILRETLGDKLFYP----DSEDLPEEFPSPEELKGKILI---SDKPPV-- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  472 kqlealrsmmeagesaspanileddneeeiesadqeeeahpefkFGNELSAddlghkeavansvkkglvTVEDEQAWMAS 551
Cdd:cd08599    150 --------------------------------------------IRNSLSE------------------TQLKKVIEGEH 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  552 ykyvgattnihpylstminyaqpvkfqgfhvaeernihynmssfnesvglgylKTHAIEFvnyNKRQMSRIYPKGGRVDS 631
Cdd:cd08599    168 -----------------------------------------------------PTDLIEF---TQKNLLRVYPAGLRITS 191

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1784638851  632 SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 668
Cdd:cd08599    192 SNYDPMLAWMHGAQMVALNMQGYDRPLWLNRGKFRAN 228
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 218-803 4.03e-53

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 197.23  E-value: 4.03e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  218 PRTDIEDLFKKInGDKTDYLTVDQLVSFLNEHQRDPRLNEIlfpfydaKRAMQIIemyepDEDLKKKGLISS-------- 289
Cdd:PLN02230    27 PVADVRDLFEKY-ADGDAHMSPEQLQKLMAEEGGGEGETSL-------EEAERIV-----DEVLRRKHHIAKftrrnltl 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  290 DGFCRYLMSDENAPVFLDrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgKGEDq 369
Cdd:PLN02230    94 DDFNYYLFSTDLNPPIAD--QVHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWP-RGTD- 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  370 EPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLkqaleSHPLEPGRALP 449
Cdd:PLN02230   170 DVCVKHGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHLTPKLQFKVAKMITQTFGDMLY-----YHDSEGCQEFP 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  450 SPNDLKRKILIKNKRLKPEVEKKQLEAlrsmMEAGESASpaniledDNEEEIESADQEEEAHPEFKFGNELSA-DDLGHK 528
Cdd:PLN02230   245 SPEELKEKILISTKPPKEYLEANDAKE----KDNGEKGK-------DSDEDVWGKEPEDLISTQSDLDKVTSSvNDLNQD 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  529 EAVANSVKKGLVTvedeQAWMASYKYVGATTNIHPYLS-TMINYAQPVKFQGFHVAEERnIHYNMSSFNESVglgylkth 607
Cdd:PLN02230   314 DEERGSCESDTSC----QLQAPEYKRLIAIHAGKPKGGlRMALKVDPNKIRRLSLSEQL-LEKAVASYGADV-------- 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  608 aiefVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTF 687
Cdd:PLN02230   381 ----IRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNG 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  688 DPFseTPVDGVI-AATCSVQVISG----------QFLSDKKIGTYVEVDMYGLPTDTIRKEFRtrmVMNNGLNPVYNEEs 756
Cdd:PLN02230   457 QDF--YPKDNSCpKKTLKVKVCMGdgwlldfkktHFDSYSPPDFFVRVGIAGAPVDEVMEKTK---IEYDTWTPIWNKE- 530

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1784638851  757 FVFrKVILPDLAVLRIAVYD----DNNKLIGQRILPLDGLQAGYRHISLRN 803
Cdd:PLN02230   531 FIF-PLAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFN 580
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 702-818 3.79e-42

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 150.38  E-value: 3.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  702 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 775
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1784638851  776 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 818
Cdd:cd00275     80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
PLN02223 PLN02223
phosphoinositide phospholipase C
 295-810 7.51e-37

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 147.09  E-value: 7.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  295 YLMSDENAPVFLDRLElYQEMDHPLAHYFISSSHNTYLTGRQ-FGGKSSVEMYRQVLLAGCRCVELDCW-DGKGedqepi 372
Cdd:PLN02223    89 FLFSTELNPPIGDQVR-HHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLLpDGKD------ 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  373 ithgkAMCT--------DILFKDVIQAIKETAFV-TSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQAlESHPLE 443
Cdd:PLN02223   162 -----GICVrpkwnfekPLELQECLDAIKEHAFTkCRSYPLIITFKDGLKPDLQSKATQMIDQTFGDMVYHED-PQHSLE 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  444 pgrALPSPNDLKRKILIKNKRLKPEVEKKQLEalrsmmeagesaspaNILEDDNEEEIesadQEEEAHPefkfgnelsad 523
Cdd:PLN02223   236 ---EFPSPAELQNKILISRRPPKELLYAKADD---------------GGVGVRNELEI----QEGPADK----------- 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  524 dlghkeavansvkkglvtvedeqawmasykyvgattnihpylstmiNYAQPVkfqGFHVAEERNIHYNM--SSFNESVGL 601
Cdd:PLN02223   283 ----------------------------------------------NYQSLV---GFHAVEPRGMLQKAltGKADDIQQP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  602 GYLKTHAIEFVnynKRQMSRIYPKGGRVDS-SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFM 680
Cdd:PLN02223   314 GWYERDIISFT---QKKFLRTRPKKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFL 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  681 RR--PDRTFDPfSETPvdgVIAATCSVQVISGQ-FLSD--KKIGT------YVEVDMYGLPTDtirKEFRTRMVMNNGLN 749
Cdd:PLN02223   391 LNagPSGVFYP-TENP---VVVKILKVKIYMGDgWIVDfkKRIGRlskpdlYVRISIAGVPHD---EKIMKTTVKNNEWK 463

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1784638851  750 PVYNEEsFVFrKVILPDLAVLRIAVYD----DNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLS 810
Cdd:PLN02223   464 PTWGEE-FTF-PLTYPDLALISFEVYDyevsTADAFCGQTCLPVSELIEGIRAVPLYDERGKACS 526
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 149-300 1.37e-36

EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1, or PLC-154, or phospholipase C-I (PLC-I), or phospholipase C-beta-1 (PLC-beta1), is expressed at highest levels in specific regions of the brain, as well as in the cardiovascular system. It has two splice variants, PI-PLC-beta1a and PI-PLC-beta1b, both of which are present within the nucleus. Nuclear PI-PLC-beta1 is a key molecule for nuclear inositide signaling, where it plays a role in cell cycle progression, proliferation and differentiation. It also contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta1 acts as an effector and a GTPase activating protein (GAP) specifically activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It regulates neuronal activity in the cerebral cortex and hippocampus, and has been implicated for participations in diverse critical functions related to forebrain diseases such as schizophrenia. It may play an important role in maintenance of the status epilepticus, and in osteosarcoma-related signal transduction pathways. PI-PLC-beta1 also functions as a regulator of erythropoiesis in kinamycin F, a potent inducer of gamma-globin production in K562 cells. The G protein activation and the degradation of PI-PLC-beta1 can be regulated by the interaction of alpha-synuclein. As a result, it may reduce cell damage under oxidative stress. Moreover, PI-PLC-beta1 works as a new intermediate in the HIV-1 gp120-triggered phosphatidylcholine-specific phospholipase C (PC-PLC)-driven signal transduction pathway leading to cytoplasmic CCL2 secretion in macrophages. PI-PLC-beta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320038  Cd Length: 151  Bit Score: 135.39  E-value: 1.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  149 KHWMKLAFMTNTNGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKK 228
Cdd:cd16208      2 KAYTKLKLQVNPEGRIPVKNIYRLFSADR--KRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSE 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1784638851  229 INGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16208     80 FGAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
 148-300 2.07e-32

EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, or phospholipase C-beta-3 (PLC-beta3), is widely expressed at highest levels in brain, liver, and parotid gland. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta3 associates with CXC chemokine receptor 2 (CXCR2) and Na+/H+ exchanger regulatory factor-1 (NHERF1) to form macromolecular complexes at the plasma membrane of pancreatic cancer cells, which functionally couple chemokine signaling to PI-PLC-beta3-mediated signaling cascade. Moreover, PI-PLC-beta3 directly interacts with the M3 muscarinic receptor (M3R), a prototypical G alpha-q-coupled receptor that promotes PI-PLC-beta3 localization to the plasma membrane. This binding can alter G alpha-q-dependent PLC activation. Furthermore, PI-PLC-beta3 inhibits the proliferation of hematopoietic stem cells (HSCs) and myeloid cells through the interaction of SH2-domain-containing protein phosphatase 1 (SHP-1) and signal transducer and activator of transcription 5 (Stat5), and the augment of the dephosphorylating activity of SHP-1 toward Stat5, leading to the inactivation of Stat5. It is also involved in atopic dermatitis (AD) pathogenesis via regulating the expression of periostin in fibroblasts and thymic stromal lymphopoietin (TSLP) in keratinocytes. In addition, PI-PLC-beta3 mediates the thrombin-induced Ca2+ response in glial cells. PI-PLC-beta3 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320040  Cd Length: 151  Bit Score: 123.49  E-value: 2.07e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  148 KKHWMKLAFMTNTNGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16210      1 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILL 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16210     79 EIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-300 3.45e-27

EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, or phospholipase C-beta-2 (PLC-beta2), is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits (G alpha(q)) through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta2 has two cellular binding partners, alpha- and gamma-synuclein. The binding of either alpha- and gamma-synuclein inhibits PI-PLC-beta2 activity through preventing the binding of its activator G alpha(q). However, the binding of gamma-synuclein to PI-PLC-beta2 does not affect its binding to G beta(gamma) subunits or small G proteins, but enhances these signals. Meanwhile, gamma-synuclein may protect PI-PLC-beta2 from protease degradation and contribute to its over-expression in breast cancer. In leukocytes, the G beta(gamma)-mediated activation of PI-PLC-beta2 can be promoted by a scaffolding protein WDR26, which is also required for the translocation of PI-PLC-beta2 from the cytosol to the membrane in polarized leukocytes. PI-PLC-beta2 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320039  Cd Length: 151  Bit Score: 108.43  E-value: 3.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  149 KHWMKLAFMTNTNGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKK 228
Cdd:cd16209      2 KIYVKLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTS 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1784638851  229 INGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16209     80 YHAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 913-955 1.32e-17

Protein of unknown function (DUF1154); This family represents a small conserved region of unknown function within eukaryotic phospholipase C (EC:3.1.4.3). All members also contain pfam00387 and pfam00388.


Pssm-ID: 461969  Cd Length: 45  Bit Score: 77.30  E-value: 1.32e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1784638851  913 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 955
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 326-434 3.71e-17

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 80.56  E-value: 3.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  326 SSHNTYLtgrQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHG------KAMCTDILFKDVIQAIKETAFvT 399
Cdd:cd08555      2 LSHRGYS---QNGQENTLEAFYRALDAGARGLELDVRLTK--DGELVVYHGptldrtTAGILPPTLEEVLELIADYLK-N 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1784638851  400 SEYPVILSFENHCS----KYQQYKMSKYCEDLFGDLLLK 434
Cdd:cd08555     76 PDYTIILSLEIKQDspeyDEFLAKVLKELRVYFDYDLRG 114
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 177-300 2.82e-15

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 73.80  E-value: 2.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  177 KTEKVIFQALKELGlpsgkNDEIEPTAFsyEKFYE-LTQkicpRTDIEDLFKKINGDKtDYLTVDQLVSFLNEHQRDPRL 255
Cdd:cd16202     36 DYAKKLFQEADTSG-----EDVLDEEEF--VQFYNrLTK----RPEIEELFKKYSGDD-EALTVEELRRFLQEEQKVKDV 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1784638851  256 neilfpfyDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16202    104 --------TLEWAEQLIETYEPSEDLKAQGLMSLDGFTLFLLSPD 140
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 705-801 5.50e-14

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 69.05  E-value: 5.50e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   705 VQVISGQFLSDKKIGT----YVEVDMYGLPtdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN-- 778
Cdd:smart00239    4 VKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVKNT-LNPVWNET-FEF-EVPPPELAELEIEVYDKDrf 76

                            90       100
                    ....*....|....*....|....*
gi 1784638851   779 --NKLIGQRILPLDGLQAGYRHISL 801
Cdd:smart00239   77 grDDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 209-300 5.79e-14

Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are predominantly found in phosphoinositide-specific phospholipase C. They adopt a structure consisting of a core of four alpha helices, in an EF like fold, and are required for functioning of the enzyme.


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 68.43  E-value: 5.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  209 FY-ELTQkicpRTDIEDLFKKINGDkTDYLTVDQLVSFLNEHQRDPRlneilfpfYDAKRAMQIIEMYEPDEDLKKKGLI 287
Cdd:pfam09279    1 FYkMLTQ----REEIDEIFQEYSGD-GQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAM 67

                           90
                   ....*....|...
gi 1784638851  288 SSDGFCRYLMSDE 300
Cdd:pfam09279   68 TKDGFLMYLCSPD 80
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 151-300 2.73e-12

EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 65.31  E-value: 2.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  151 WMKLAFM---TNTNGKIP---VRSITRTFASGKTEKVIFQALKELglpSGKNDEiEPTAFSYEKFYELTQKICPRTDIED 224
Cdd:cd16206      1 WLESVFEeadTNKSGFLDeeeAVQLIKQLNPGLSTSRIKQKLKEL---QKKKDG-ARGRVSSDEFVELFKELATRPEIYF 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1784638851  225 LFKKINGDKtDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16206     77 LLVRYASNK-DYLTVDDLMLFLEAEQGMTGVTK--------EKCLEIINKYEPSEEGREKGQLGIDGFTRYLLSEE 143
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 206-298 1.18e-09

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 57.78  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  206 YEKFYELTQKICPRTDIEDLFKKInGDKTDYLTVDQLVSFLNEHQRdprLNEIlfpfyDAKRAMQIIEMYEPDEDLKKKG 285
Cdd:cd16205     56 FEEFCAFYKMMSTRRELYLLLLSY-SNKKDYLTLEDLARFLEVEQK---MTNV-----TLEYCLDIIEKFEPSEENKKNG 126

                           90
                   ....*....|...
gi 1784638851  286 LISSDGFCRYLMS 298
Cdd:cd16205    127 LLGIDGFTNYMRS 139
C2 pfam00168
C2 domain;
704-798 2.25e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.79  E-value: 2.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  704 SVQVISGQFLSDKKIG----TYVEVDMYGLptdtiRKEFRTRmVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 778
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNgtsdPYVKVYLLDG-----KQKKKTK-VVKNTLNPVWNET-FTF-SVPDPENAVLEIEVYDYDr 75

                           90       100
                   ....*....|....*....|...
gi 1784638851  779 ---NKLIGQRILPLDGLQAGYRH 798
Cdd:pfam00168   76 fgrDDFIGEVRIPLSELDSGEGL 98
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 205-300 1.08e-08

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 54.98  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  205 SYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEdlkKK 284
Cdd:cd15898     54 TFDEFEELYKSLTERPELEPIFKKYAGTNRDYMTLEEFIRFLREEQGEN---------VSEEECEELIEKYEPER---EN 121

                           90
                   ....*....|....*.
gi 1784638851  285 GLISSDGFCRYLMSDE 300
Cdd:cd15898    122 RQLSFEGFTNFLLSPE 137
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 207-300 1.89e-08

EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus.


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 54.36  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  207 EKFY-ELTQkicpRTDIEDLFKKINGdKTDYLTVDQLVSFLNEHQRDPRLNEIlfpfydakrAMQIIEMYEPDEDLKKKG 285
Cdd:cd16217     59 EEFYkLLTK----REEIDVIFGEYAK-SDGTMSRNNLLNFLQEEQREEVAPAY---------ALSLIEKYEPDETAKAQR 124

                           90
                   ....*....|....*
gi 1784638851  286 LISSDGFCRYLMSDE 300
Cdd:cd16217    125 QMTKDGFLMYLLSPE 139
PTZ00121 PTZ00121
MAEBL; Provisional
 839-1170 2.54e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  839 KKFLSITEKRADQMRAMGIETSDIADVP-SDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASGVEAKKGIELipQV 917
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KK 1398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  918 RIEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEMKKE 997
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-----EAKKA 1472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  998 TEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQ--EIRDLHLSQQCELLKKllinAHE-QQTQQLKLSHD-RES 1073
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKK----AEEaKKADEAKKAEEkKKA 1548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1074 KEMRAHQAKISMENSKAISQdksiKNKAERE-----RRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHL--EF 1146
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEE----AKKAEEDknmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEE 1624

                          330       340
                   ....*....|....*....|....
gi 1784638851 1147 LEKQNEQAKEMQQMVKLEAEMDRR 1170
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKK 1648
PTZ00121 PTZ00121
MAEBL; Provisional
 847-1164 5.20e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 5.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  847 KRADQMRAMGIETSDIADvpSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASgvEAKKGIElipQVRIEDLKQMK 926
Cdd:PTZ00121  1483 KKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEE---KKKADELKKAE 1555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  927 aylkHLKKQQKELNSLKKKHAKEHSTMQkLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKggsnclEMKKETEIKIQTLT 1006
Cdd:PTZ00121  1556 ----ELKKAEEKKKAEEAKKAEEDKNMA-LRKAEEAKKAEEARIEEVMKLYEEEKKMKAE------EAKKAEEAKIKAEE 1624

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1007 SDHKSKVKEIVAQHTKEWSEMINT-----HSAEEQEIRDLHLSQQCELLKKlliNAHEQQTQQLKLSHDRESKEMRAHQA 1081
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKKaeelkKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEA 1701

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1082 KISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMV 1161
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781


                   ...
gi 1784638851 1162 KLE 1164
Cdd:PTZ00121  1782 EEE 1784
EFh_PRIP2 cd16223
EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); ...
 177-300 6.30e-08

EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); PRIP-2, also termed phospholipase C-L2, or phospholipase C-epsilon-2 (PLC-epsilon-2), or inactive phospholipase C-like protein 2 (PLC-L2), is a novel inositol 1,4,5-trisphosphate (InsP3) binding protein that exhibits a relatively ubiquitous expression. It functions as a novel negative regulator of B-cell receptor (BCR) signaling and immune responses. PRIP-2 has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP-2 does not have PLC enzymatic activity.


Pssm-ID: 320053 [Multi-domain]  Cd Length: 144  Bit Score: 52.99  E-value: 6.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  177 KTEKVIFQaLKELGlpsgKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKtDYLTVDQLVSFLNEHQRDPRLN 256
Cdd:cd16223     34 KTSKIELK-FKELH----KSKEKGGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSNK-EFLDTKDLMMFLEAEQGMAHVT 107

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1784638851  257 EilfpfydaKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16223    108 E--------EISLDIIHKYEPSKEGQEKGWLSLDGFTNYLMSPE 143
PH_PLC_ELMO1 cd01248
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ...
 17-133 1.32e-07

Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The C-terminal region of ELMO1, the PH domain and Pro-rich sequences, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle allowing for DOCK mediated Rac1 activation. ELMO1, a mammalian homolog of C. elegans CED-12, contains an N-terminal RhoG-binding region, a ELMO domain, a PH domain, and a C-terminal sequence with three PxxP motifs. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). All PLCs, except for PLCzeta, have a PH domain which is for most part N-terminally located, though lipid binding specificity is not conserved between them. In addition PLC gamma contains a split PH domain within its catalytic domain that is separated by 2 SH2 domains and a single SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269952  Cd Length: 108  Bit Score: 50.78  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851   17 LQEGAVFDRYEEESFVFEpnCLFKVDEFGFFLTWRSEGK--EGQVLECSLINSIRSGAIPKDPKilaaleAVGKSENDLE 94
Cdd:cd01248      1 LQQGTLLLKYREGSKPKE--RTFYLDPDGTRITWESSKKksEKKSIDISDIKEIRPGKDTDGFK------RKKKSNKPKE 72

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1784638851   95 GRIVCVCSGTDLVNISFtymVAENPEVTKQWVEGLRSII 133
Cdd:cd01248     73 ERCFSIIYGSNNKTLDL---VAPSEDEANLWVEGLRALL 108
PTZ00121 PTZ00121
MAEBL; Provisional
 836-1170 1.41e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  836 SDPKKFLSITEKRADQMRAMGiETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAAlASGVEAKKGIELip 915
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK-KKAEEAKKADEA-- 1449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  916 QVRIEDLKQMKAyLKHLKKQQKELNSLKKK--------HAKEHSTMQKLHCTQVDKivAQYDKEKSTHEKILEKAMKKKG 987
Cdd:PTZ00121  1450 KKKAEEAKKAEE-AKKKAEEAKKADEAKKKaeeakkadEAKKKAEEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADE 1526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  988 GSNCLEMKKETEIKiqtlTSDHKSKVKEI-VAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKL------LINAHEQ 1060
Cdd:PTZ00121  1527 AKKAEEAKKADEAK----KAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeearieEVMKLYE 1602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1061 QTQQLKLSHDRESKEMR--AHQAKISMENSKAISQDKSI----KNKAERERRVRELN---SSNTKKFLEERKRLAMKQSK 1131
Cdd:PTZ00121  1603 EEKKMKAEEAKKAEEAKikAEELKKAEEEKKKVEQLKKKeaeeKKKAEELKKAEEENkikAAEEAKKAEEDKKKAEEAKK 1682

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1784638851 1132 EMDQLKKVQlehlEFLEKQNEQAKEMQQMVKLEAEMDRR 1170
Cdd:PTZ00121  1683 AEEDEKKAA----EALKKEAEEAKKAEELKKKEAEEKKK 1717
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 704-784 1.77e-07

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 50.53  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  704 SVQVISGQFLSDKKIG----TYVEVDMYGlptdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 778
Cdd:cd00030      2 RVTVIEARNLPAKDLNgksdPYVKVSLGG------KQKFKTKVVKNT-LNPVWNET-FEF-PVLDPESDTLTVEVWDKDr 72


                   ....*....
gi 1784638851  779 ---NKLIGQ 784
Cdd:cd00030     73 fskDDFLGE 81
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 1035-1174 2.13e-07

PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 51.99  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1035 EQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMrahQAKISMENSKAISQ-DKSIKNKAERERRVRELNSS 1113
Cdd:pfam08703   25 EKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEM---KKKLERKRLESIQEaKKRTSDKAAQERLKKEINNS 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1784638851 1114 NTKKFLEERKRLAMKQSKEMDQLKKVQ---LEHLEFLEKQNEQakemQQMVKLEAEMDRRPATV 1174
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQaecLQQIKEEEPQLQA----ELNAEYEEKLKGLPAEV 161
PTZ00121 PTZ00121
MAEBL; Provisional
 847-1166 2.58e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  847 KRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANvTPQSSSELRPTTTAALASGVEAKKGIELIPQVRIEDLKQMK 926
Cdd:PTZ00121  1302 KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  927 AYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKK-KGGSNCLEMKKETEIKIQTL 1005
Cdd:PTZ00121  1381 DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAE 1460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1006 TSDHKSKVKEIVAQHTKEWSEminTHSAEEQEIRDLHLSQQCELLKKLLiNAHEQQTQQLKLSHDRESKEMR-AHQAKIS 1084
Cdd:PTZ00121  1461 EAKKKAEEAKKADEAKKKAEE---AKKADEAKKKAEEAKKKADEAKKAA-EAKKKADEAKKAEEAKKADEAKkAEEAKKA 1536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1085 MENSKAISQDKSIK-NKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEmQQMVKL 1163
Cdd:PTZ00121  1537 DEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA-EEAKKA 1615


                   ...
gi 1784638851 1164 EAE 1166
Cdd:PTZ00121  1616 EEA 1618
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 880-1169 3.95e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 51.27  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  880 TAKaNVTPQSSSELRPTTTAALAsgvEAKKGIEL----IPQVR------IEDLKQMKAYLKHLKKQQKELNSLKKKHAKE 949
Cdd:pfam15921  485 TAK-KMTLESSERTVSDLTASLQ---EKERAIEAtnaeITKLRsrvdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEK 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  950 HSTMQKLHcTQVD---KIVAQYDKEKSTHEkiLEKA-MKKKGGSNCLEMKketEIKIqtLTSDHKSKVKEIVAQHTK--- 1022
Cdd:pfam15921  561 DKVIEILR-QQIEnmtQLVGQHGRTAGAMQ--VEKAqLEKEINDRRLELQ---EFKI--LKDKKDAKIRELEARVSDlel 632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1023 EWSEMINTHSAEEQEIRDL-------------------HLSQQCELLKKLLINAHEQQ---TQQLKL---SHDRESKEMR 1077
Cdd:pfam15921  633 EKVKLVNAGSERLRAVKDIkqerdqllnevktsrnelnSLSEDYEVLKRNFRNKSEEMettTNKLKMqlkSAQSELEQTR 712

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1078 ----------AHQAKISMENSKAISQDKSIKNKAERERRVRE---LNSSNTKKFL-EERKRLAMKQSKEMDQLKKVQLEh 1143
Cdd:pfam15921  713 ntlksmegsdGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamTNANKEKHFLkEEKNKLSQELSTVATEKNKMAGE- 791

                          330       340
                   ....*....|....*....|....*.
gi 1784638851 1144 LEFLEKQNEQAKEmqQMVKLEAEMDR 1169
Cdd:pfam15921  792 LEVLRSQERRLKE--KVANMEVALDK 815
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 207-300 4.62e-06

EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (PLCD4), or phospholipase C-delta-4 (PLC-delta-4), is expressed in various tissues with the highest levels detected selectively in the brain, skeletal muscle, testis and kidney. It plays a significant role in cell growth, cell proliferation, tumorigenesis, and in an early stage of fertilization. PI-PLC-delta4 may function as a key enzyme in the regulation of PtdIns(4,5)P2 levels and Ca2+ metabolism in nuclei in response to growth factors, and its expression may be partially regulated by an increase in cytoplasmic Ca2+. Moreover, PI-PLC-delta4 binds glutamate receptor-interacting protein1 (GRIP1) in testis and is required for calcium mobilization essential for the zona pellucida-induced acrosome reaction in sperm. Overexpression or dysregulated expression of PLCdelta4 may initiate oncogenesis in certain tissues through upregulating erbB1/2 expression, extracellular signal-regulated kinase (ERK) signaling pathway, and proliferation in MCF-7 cells. PI-PLC-delta4 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4.


Pssm-ID: 320049 [Multi-domain]  Cd Length: 140  Bit Score: 47.53  E-value: 4.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  207 EKFYELTQKICPRTDIEDLFKKINGDKTDyLTVDQLVSFLNEHQRDPRLNEILfpfydakrAMQIIEMYEPDEDLKKKGL 286
Cdd:cd16219     56 EEFVLFYKALTQREDVLKIFQDFSADGQK-LTLLEFVDFLQQEQLERENTEEL--------AMELIDRYEPSDTAKKLHA 126

                           90
                   ....*....|....
gi 1784638851  287 ISSDGFCRYLMSDE 300
Cdd:cd16219    127 LSIDGFLMYLCSPE 140
EFh_PRIP1 cd16222
EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1); ...
 195-300 7.73e-06

EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1); PRIP-1, also termed phospholipase C-deleted in lung carcinoma, or inactive phospholipase C-like protein 1 (PLC-L1), or p130, is a novel inositol 1,4,5-trisphosphate (InsP3) binding protein that is predominantly expressed in the brain. It is involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. It interacts with the catalytic subunits of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A), and functions as a scaffold to regulate the activities and subcellular localizations of both PP1 and PP2A in phospho-dependent cellular signaling. It also promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of hormone-sensitive lipase (HSL) and perilipin A, thus reducing protein kinase A (PKA)-mediated lipolysis. Moreover, PRIP-1 plays an important role in insulin granule exocytosis through the association with GABAA-receptor-associated protein (GABARAP) to form a complex to regulate KIF5B-mediated insulin secretion. It also inhibits regulated exocytosis through direct interactions with syntaxin 1 and synaptosomal-associated protein 25 (SNAP-25) via its C2 domain. Furthermore, PRIP-1 has been implicated in the negative regulation of bone formation. PRIP-1 has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP-1 does not have PLC enzymatic activity.


Pssm-ID: 320052 [Multi-domain]  Cd Length: 143  Bit Score: 46.78  E-value: 7.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  195 KNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKtDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEM 274
Cdd:cd16222     47 KSKEKLTTRVTEEEFCEAYSELCTRPEVYFLLVQISKNK-EYLDAKDLMLFLEAEQGMTHITE--------EMCLDIIRR 117

                           90       100
                   ....*....|....*....|....*.
gi 1784638851  275 YEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16222    118 YEPSQEGRLKGFLGIDGFTQYLLSSE 143
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 1048-1169 4.84e-05

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 44.47  E-value: 4.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1048 ELLKKLLINAHEQQTQQLKLSHDRESKEM-RAHQAKIS-MENSKAISQDKSIKN-KAERERRvrelnssnTKKFLEERKR 1124
Cdd:pfam12474    2 QLQKEQQKDRFEQERQQLKKRYEKELEQLeRQQKQQIEkLEQRQTQELRRLPKRiRAEQKKR--------LKMFRESLKQ 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1784638851 1125 LAMKQSKEMDQLKKVQL--------EHLEFLEKQNEQAKEMQQMVKLEAEMDR 1169
Cdd:pfam12474   74 EKKELKQEVEKLPKFQRkeakrqrkEELELEQKHEELEFLQAQSEALERELQQ 126
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 912-1156 5.15e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.51  E-value: 5.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  912 ELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHcTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNC 991
Cdd:pfam10174  264 LLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQ-TKLETLTNQNSDCKQHIEVLKESLTAKEQRAAI 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  992 LEmkkeTEIKIQTLTSDHKskvKEIVAQHTKEWSEMINTHSAEEQEIRDLhlsqqcellKKLLinaheqqtqqlklshDR 1071
Cdd:pfam10174  343 LQ----TEVDALRLRLEEK---ESFLNKKTKQLQDLTEEKSTLAGEIRDL---------KDML---------------DV 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1072 ESKEMRAHQAKIsmENSKAISQDKSiKNKAERERRVREL--NSSNT-------KKFLEERKRLAMKQSKEMDQLKKVQLE 1142
Cdd:pfam10174  392 KERKINVLQKKI--ENLQEQLRDKD-KQLAGLKERVKSLqtDSSNTdtalttlEEALSEKERIIERLKEQREREDRERLE 468

                          250
                   ....*....|....
gi 1784638851 1143 HLEFLEKQNEQAKE 1156
Cdd:pfam10174  469 ELESLKKENKDLKE 482
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 932-1173 6.21e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 6.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  932 LKKQQKELNSLKKKH-AKEHSTMQKLHCTQVDKivaQYDKEKSTHEkiLEKAMKKKggsnCLEMKKETEIKIQTLTSDHK 1010
Cdd:pfam17380  355 QEERKRELERIRQEEiAMEISRMRELERLQMER---QQKNERVRQE--LEAARKVK----ILEEERQRKIQQQKVEMEQI 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1011 SKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKllinaHEQQTQQLKLSHDRESKEmrahQAKISMENSKA 1090
Cdd:pfam17380  426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ-----QEEERKRKKLELEKEKRD----RKRAEEQRRKI 496

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1091 ISQDKSIKNKA----ERERRV--RELNSSNTKKFLEERKR---------LAMKQSKEM-DQLKKVQLE--HLEFLEKQNE 1152
Cdd:pfam17380  497 LEKELEERKQAmieeERKRKLleKEMEERQKAIYEEERRReaeeerrkqQEMEERRRIqEQMRKATEErsRLEAMERERE 576

                          250       260
                   ....*....|....*....|.
gi 1784638851 1153 QakeMQQMVKLEAEMDRRPAT 1173
Cdd:pfam17380  577 M---MRQIVESEKARAEYEAT 594
EFh_PI-PLCepsilon cd16203
EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1); ...
 237-297 7.25e-05

EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1); PI-PLC-epsilon1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1, or pancreas-enriched phospholipase C, or phospholipase C-epsilon-1 (PLC-epsilon-1), is dominant in connective tissues and brain. It has been implicated in carcinogenesis, such as in bladder and intestinal tumor, oesophageal squamous cell carcinoma, gastric adenocarcinoma, murine skin cancer, head and neck cancer. PI-PLC-epsilon1 contains an N-terminal CDC25 homology domain with a guanyl-nucleotide exchange factor (GFF) activity, a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and at least one and perhaps two C-terminal predicted RA (Ras association) domains that are implicated in the binding of small GTPases, such as Ras or Rap, from the Ras family. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is only one PI-PLC-epsilon isozyme. It is directly activated by G alpha(12/13), G beta gamma, and activated members of Ras and Rho small GTPases.


Pssm-ID: 320033  Cd Length: 174  Bit Score: 44.62  E-value: 7.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1784638851  237 LTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLM 297
Cdd:cd16203    120 LTISQLKDFLENHQMEH---------ITEEEAIKIIQRHEPDPILRSKNCLSFEGFARYLM 171
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 316-465 1.32e-04

Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins; This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.


Pssm-ID: 176500 [Multi-domain]  Cd Length: 271  Bit Score: 45.16  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  316 DHPLAHYFISSSHNTY---LTGRQFGGKSSVE-----MYRQvLLAGCRCVELDCWDgKGEDQEPIITHGKAMCTDILFKD 387
Cdd:cd08557      6 DLPLSQLSIPGTHNSYaytIDGNSPIVSKWSKtqdlsITDQ-LDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQTLED 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  388 VIQAIKetAFVT---SEyPVILSFENHcskyqqYKMSKYCEDLFGDLLLKQALESHPLEPgrALPSPNDLKRKILIKNKR 464
Cdd:cd08557     84 VLNEVK--DFLDahpSE-VVILDLEHE------YGGDNGEDHDELDALLRDVLGDPLYRP--PVRAGGWPTLGELRAGKR 152


                   .
gi 1784638851  465 L 465
Cdd:cd08557    153 V 153
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
 211-300 3.02e-04

EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (PLCD3), phospholipase C-delta-3 (PLC-delta-3), is expressed abundantly in brain, skeletal muscle and heart. PI-PLC-delta3 gene expression is down-regulation by cAMP and calcium. PI-PLC-delta3 acts as anchoring of myosin VI on plasma membrane, and further modulates Myosin IV expression and microvilli formation in enterocytes. It negatively regulates RhoA expression, inhibits RhoA/Rho kinase signaling, and plays an essential role in normal neuronal migration by promoting neuronal outgrowth in the developing brain. Moreover, PI-PLC-delta3 is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta3 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta3 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. In addition, PI-PLC-delta3 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, which may be responsible transporting PI-PLC-delta3 from the cell nucleus.


Pssm-ID: 320048 [Multi-domain]  Cd Length: 138  Bit Score: 42.04  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  211 ELTQKICPRTDIEDLFKKINGdKTDYLTVDQLVSFLNEHQRDPRLneilfpfydaKRAMQIIEMYEPDEDLKKKGLISSD 290
Cdd:cd16218     60 EFCRRLMQRPELEEIFHQYSG-EDCVLSAEELREFLKDQGEDASL----------VHAKELIQTYELNEKAKQHQLMTLD 128

                           90
                   ....*....|
gi 1784638851  291 GFCRYLMSDE 300
Cdd:cd16218    129 GFTMYMLSKD 138
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 798-1162 3.22e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  798 HISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSiteKRADQMRAmgiETSDIAdvPSDTSKNDKKGK 877
Cdd:TIGR00618  354 EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC---KELDILQR---EQATID--TRTSAFRDLQGQ 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  878 ANTAKANVTPQssseLRPTTTAALASGVEAKKGIELIP-----QVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHST 952
Cdd:TIGR00618  426 LAHAKKQQELQ----QRYAELCAAAITCTAQCEKLEKIhlqesAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  953 MQKLHCTQV----DKIVAQYDKEKST--------HEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSkvkEIVAQH 1020
Cdd:TIGR00618  502 EPCPLCGSCihpnPARQDIDNPGPLTrrmqrgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF---SILTQC 578

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1021 TKEWSEMINTHSAEEQEIRDLhLSQQCELLKKLLInahEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQ-DKSIKN 1099
Cdd:TIGR00618  579 DNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLAC---EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlHALQLT 654

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851 1100 KAERERRVRELNSSNTKKFLEERKRLAMkqsKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMVK 1162
Cdd:TIGR00618  655 LTQERVREHALSIRVLPKELLASRQLAL---QKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1022-1170 3.77e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1022 KEWSEMINTHSAEEQEIRDLHLSQQCELLKKLL-------------INAHEQQTQQLKLSHDRESKEMRAHQAKISMENS 1088
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELeeleaeleeleaeLAELEAELEELRLELEELELELEEAQAEEYELLA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1089 KAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMD 1168
Cdd:COG1196    296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                   ..
gi 1784638851 1169 RR 1170
Cdd:COG1196    376 EA 377
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 219-298 5.80e-04

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 41.47  E-value: 5.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  219 RTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMS 298
Cdd:cd16207     70 RKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKED---------VDRETWEKIFEKFARRIDDSDSLTMTLEGFTSFLLS 140
EFh_PI-PLCzeta cd16204
EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, ...
 195-300 6.12e-04

EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1, or phospholipase C-zeta-1 (PLC-zeta-1), or testis-development protein NYD-SP27, is only found in the testis. The sperm-specific PI-PLC plays a fundamental role in vertebrate fertilization by initiating intracellular calcium oscillations that trigger the embryo development. However, the mechanism of its activation still remains unclear. PI-PLC-zeta1 contains an N-terminal four atypical EF-hand motifs, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unlike other PI-PLCs, PI-PLC-zeta is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. There is only one PLC-zeta isozyme. Aside from PI-PLC-zeta identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 320034 [Multi-domain]  Cd Length: 142  Bit Score: 41.33  E-value: 6.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  195 KNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKkINGDKTDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEM 274
Cdd:cd16204     46 KNDSFKAGNITIEDFRAIYRAIAHRCEIHEIFN-TYSENRKILSAPNLVGFLKKEQFQDEADE--------TIASELIAK 116

                           90       100
                   ....*....|....*....|....*.
gi 1784638851  275 YEPDEDLKKKGLISSDGFCRYLMSDE 300
Cdd:cd16204    117 YEPIEEVRKRKQMSFEGFIRYMTSED 142
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 831-1161 7.77e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.59  E-value: 7.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  831 IVDALSDPKKFLSITEKRADQmramgiETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASGVEAKKG 910
Cdd:pfam09731  158 AVKAHTDSLKEASDTAEISRE------KATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNV 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  911 IE----------LIPQV-------RIEDLKQMKAYLKHLKKQQKELNSLKKkhAKEHSTMQKLHcTQVDKIVAQYDKEKS 973
Cdd:pfam09731  232 EEkvekaqslakLVDQYkelvaseRIVFQQELVSIFPDIIPVLKEDNLLSN--DDLNSLIAHAH-REIDQLSKKLAELKK 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  974 THEKILEKAMKKKggsnclemKKETEIKIQTLTSDHKSKVKEIVAQHTKEW-SEMINTHSAEEQEIRdLHLSQQCELLKK 1052
Cdd:pfam09731  309 REEKHIERALEKQ--------KEELDKLAEELSARLEEVRAADEAQLRLEFeREREEIRESYEEKLR-TELERQAEAHEE 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1053 LLINAHEQQTQQLKLSHDREskemrahqakismenskaisqdksIKNKAERERRVRelnssnTKKFLEERKRLAmkqske 1132
Cdd:pfam09731  380 HLKDVLVEQEIELQREFLQD------------------------IKEKVEEERAGR------LLKLNELLANLK------ 423

                          330       340
                   ....*....|....*....|....*....
gi 1784638851 1133 mdQLKKVQLEHLEfLEKQNEQAKEMQQMV 1161
Cdd:pfam09731  424 --GLEKATSSHSE-VEDENRKAQQLWLAV 449
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 909-1169 8.83e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.50  E-value: 8.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  909 KGIELIPQVRIEDLKQMKAYlkHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKE----KSTHEKILEKAMK 984
Cdd:TIGR00606  186 KALETLRQVRQTQGQKVQEH--QMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEldplKNRLKEIEHNLSK 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  985 KKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAE----EQEIRDLH-----LSQQCELLK---- 1051
Cdd:TIGR00606  264 IMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvrekERELVDCQrelekLNKERRLLNqekt 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1052 -------KLLINAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKfLEERKR 1124
Cdd:TIGR00606  344 ellveqgRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCAD-LQSKER 422

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1125 LAMKQSKEMDQLKK-----VQLEHLEFLEKQNEQAKEMQQMVKLEAEMDR 1169
Cdd:TIGR00606  423 LKQEQADEIRDEKKglgrtIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 704-778 9.46e-04

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 40.32  E-value: 9.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  704 SVQVISGQFLSDKKIGT----YVEVDmygLPTDTIRKeFRTRmVMNNGLNPVYNeESFVFRkvILPDLA-VLRIAVYDDN 778
Cdd:cd04036      3 TVRVLRATNITKGDLLStpdcYVELW---LPTASDEK-KRTK-TIKNSINPVWN-ETFEFR--IQSQVKnVLELTVMDED 74
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 721-789 1.43e-03

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 39.94  E-value: 1.43e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1784638851  721 YVEVdmYGLPtDTiRKEFRTRmVMNNGLNPVYNeESFVFrKVILPDLA--VLRIAVYDDN----NKLIGQRILPL 789
Cdd:cd08385     40 YVKV--YLLP-DK-KKKFETK-VHRKTLNPVFN-ETFTF-KVPYSELGnkTLVFSVYDFDrfskHDLIGEVRVPL 107
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 156-298 1.71e-03

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 40.01  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  156 FMTNTNGKIPVRSITRTFASGKTekvifqalkelglpsgknDEIEPTaFSYEKFYELTQKICPRTDIEDLFKKINgDKTD 235
Cdd:cd16220     25 LMHKLNVNLPRRKVRQMFQEADT------------------DENQGT-LTFEEFCVFYKMMSLRRDLYLLLLSYS-DKKD 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784638851  236 YLTVDQLVSFLNEHQrdpRLNEILFPFydakrAMQIIEMYEPDEDLKKKGLISSDGFCRYLMS 298
Cdd:cd16220     85 HLTVEELAQFLKVEQ---KMNNVTTEY-----CLDIIKKFEVSEENKEQNVLGIEGFTNFMRS 139
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 923-1095 2.81e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.02  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  923 KQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKlhctqvdkivaQYDKEKSTHEKILEKAMKKKGGSN-CLEMKKETEIK 1001
Cdd:pfam05483  629 KQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-----------EIEDKKISEEKLLEEVEKAKAIADeAVKLQKEIDKR 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1002 IQ-------TLTSDHKSKVKEIVAQHTKEwsemINTHSAEEQEIRDLHLSQQCEL--LKKLLINAHEQqtqqlkLSHDRE 1072
Cdd:pfam05483  698 CQhkiaemvALMEKHKHQYDKIIEERDSE----LGLYKNKEQEQSSAKAALEIELsnIKAELLSLKKQ------LEIEKE 767

                          170       180
                   ....*....|....*....|...
gi 1784638851 1073 SKEMRAHQAKismENSKAISQDK 1095
Cdd:pfam05483  768 EKEKLKMEAK---ENTAILKDKK 787
PTZ00121 PTZ00121
MAEBL; Provisional
 920-1142 4.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  920 EDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLH-CTQVDKIVAQYDKEKSTHEKILEKAMKKKggsnclemkKET 998
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKkAEEENKIKAEEAKKEAEEDKKKAEEAKKD---------EEE 1755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  999 EIKIQTLTSDHKSKVKEIvaqhTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQ------QLKLSHDRE 1072
Cdd:PTZ00121  1756 KKKIAHLKKEEEKKAEEI----RKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgnlvinDSKEMEDSA 1831

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1073 SKEMrAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRlAMKQSKEMDQLKKVQLE 1142
Cdd:PTZ00121  1832 IKEV-ADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE-EIEEADEIEKIDKDDIE 1899
PTZ00121 PTZ00121
MAEBL; Provisional
 875-1164 4.78e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  875 KGKANTAKANVTPQSSSELRPTTTAALASGVEAKKGIELIPQVRIEDLKQMKAYLK--HLKK--QQKELNSLKKKHAKEH 950
Cdd:PTZ00121  1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadEAKKaeEKKKADEAKKKAEEAK 1315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  951 STMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIK--IQTLTSDHKSKvkeivAQHTKEWSEmi 1028
Cdd:PTZ00121  1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaAEKKKEEAKKK-----ADAAKKKAE-- 1388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1029 NTHSAEEQEIRDLHLSQQCELLKKllinAHEQQTQQLKLSHDRESKEmRAHQAKISMENSKAISQdksIKNKAERERRVR 1108
Cdd:PTZ00121  1389 EKKKADEAKKKAEEDKKKADELKK----AAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKKADE---AKKKAEEAKKAE 1460

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1109 ELN-SSNTKKFLEERKRLAmKQSKEMDQLKKVQLEH---LEFLEKQNEQAKEMQQMVKLE 1164
Cdd:PTZ00121  1461 EAKkKAEEAKKADEAKKKA-EEAKKADEAKKKAEEAkkkADEAKKAAEAKKKADEAKKAE 1519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
908-1167 5.09e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  908 KKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKIvAQYDKEKSTHE---KILEKAMK 984
Cdd:PRK03918   254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDEL-REIEKRLSRLEeeiNGIEERIK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  985 KkggsncLEMKKETEIKIQTLTSDHKSKVKEIvaqhtKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQ 1064
Cdd:PRK03918   332 E------LEEKEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1065 LKLSHD-RESKEMRAHQAKISMENSKAISQDKSIKNKAERERrvRELNSsntkkflEERKRLAMKQSKEMDQLKKVQLEH 1143
Cdd:PRK03918   401 EEIEEEiSKITARIGELKKEIKELKKAIEELKKAKGKCPVCG--RELTE-------EHRKELLEEYTAELKRIEKELKEI 471

                          250       260
                   ....*....|....*....|....
gi 1784638851 1144 LEFLEKQNEQAKEMQQMVKLEAEM 1167
Cdd:PRK03918   472 EEKERKLRKELRELEKVLKKESEL 495
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 933-1155 5.15e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 5.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  933 KKQQKELNSLKKKHAKEHSTMQKLhctQVDKIVAQyDKEKSTHEKIL-----------EKAMKKKGGSNCLEMKKETEIK 1001
Cdd:pfam01576   99 KKMQQHIQDLEEQLDEEEAARQKL---QLEKVTTE-AKIKKLEEDILlledqnsklskERKLLEERISEFTSNLAEEEEK 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1002 IQTLT---SDHKSKVKEIVAQHTKE---WSEMINTHSAEEQEIRDLH-----LSQQ-CELLKKLLINAHEQQTQQLKLsh 1069
Cdd:pfam01576  175 AKSLSklkNKHEAMISDLEERLKKEekgRQELEKAKRKLEGESTDLQeqiaeLQAQiAELRAQLAKKEEELQAALARL-- 252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1070 DRES-------KEMRAHQAKISmENSKAISQDKSIKNKAERERR----------------------------VRELNSSN 1114
Cdd:pfam01576  253 EEETaqknnalKKIRELEAQIS-ELQEDLESERAARNKAEKQRRdlgeelealkteledtldttaaqqelrsKREQEVTE 331

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1784638851 1115 TKKFLEERKRLAMKQSKEMDQLKKVQLEHlefLEKQNEQAK 1155
Cdd:pfam01576  332 LKKALEEETRSHEAQLQEMRQKHTQALEE---LTEQLEQAK 369
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 915-1165 5.54e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  915 PQVRIEDLKQMKAYLKHLKKQQKELNSLKKKH---AKEHSTMQKLHCTQVDKIVAQYD-KEKSTHEKILEKAMKKKGGSN 990
Cdd:TIGR00618  364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLqslCKELDILQREQATIDTRTSAFRDlQGQLAHAKKQQELQQRYAELC 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  991 CLEMKKETEIKIQTLT----SDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLL-INAHEQQTQQL 1065
Cdd:TIGR00618  444 AAAITCTAQCEKLEKIhlqeSAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhPNPARQDIDNP 523

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1066 KLSHDR-ESKEMRAHQAKISMENSKAI-----SQDKSIKNKAERERRVRELNSS----------NTKKFLEERKRLAMKQ 1129
Cdd:TIGR00618  524 GPLTRRmQRGEQTYAQLETSEEDVYHQltserKQRASLKEQMQEIQQSFSILTQcdnrskedipNLQNITVRLQDLTEKL 603

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1784638851 1130 SKEMDQLKKVQLEHLEFLE-KQNEQ--AKEMQQMVKLEA 1165
Cdd:TIGR00618  604 SEAEDMLACEQHALLRKLQpEQDLQdvRLHLQQCSQELA 642
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 704-798 5.59e-03

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 38.33  E-value: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  704 SVQVISGQFLSDKKIG----TYVEVDMYGlpTDTIRKEFRTRMVMNNgLNPVYNeESFVFrKVILPDL--AVLRIAVYDD 777
Cdd:cd00276     17 TVVVLKARNLPPSDGKglsdPYVKVSLLQ--GGKKLKKKKTSVKKGT-LNPVFN-EAFSF-DVPAEQLeeVSLVITVVDK 91

                           90       100
                   ....*....|....*....|....*
gi 1784638851  778 ----NNKLIGQRILPLDGLQAGYRH 798
Cdd:cd00276     92 dsvgRNEVIGQVVLGPDSGGEELEH 116
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 930-1166 5.78e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  930 KHLKKQQKELNSLKKKHAKEHSTMQKLhctqvdkivaqyDKEKSTHEKILEKAMKKKggsnclemkKETEIKIQTLTSDH 1009
Cdd:TIGR04523  363 RELEEKQNEIEKLKKENQSYKQEIKNL------------ESQINDLESKIQNQEKLN---------QQKDEQIKKLQQEK 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1010 KSKVKEI------VAQHTKEWSEMINTHSAEEQEIRDL-----HLSQQCELLKKLLINAH---EQQTQQLKlSHDRESKE 1075
Cdd:TIGR04523  422 ELLEKEIerlketIIKNNSEIKDLTNQDSVKELIIKNLdntreSLETQLKVLSRSINKIKqnlEQKQKELK-SKEKELKK 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1076 MRAHQAKISMENSKAISQDKSIKNKaererrVRELNSSNTKKFLE----ERKRLAMKQSKEMDQLKKV---------QLE 1142
Cdd:TIGR04523  501 LNEEKKELEEKVKDLTKKISSLKEK------IEKLESEKKEKESKisdlEDELNKDDFELKKENLEKEideknkeieELK 574

                          250       260
                   ....*....|....*....|....*
gi 1784638851 1143 H-LEFLEKQNEQAKEMQQmvKLEAE 1166
Cdd:TIGR04523  575 QtQKSLKKKQEEKQELID--QKEKE 597
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 920-1170 6.51e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  920 EDLKQMKAYLKHLKKqqkELNSLKKKHAKEHSTMQKLH--CTQVDKIVAQYDKEKSTHEKILEKA--------MKKKGGS 989
Cdd:pfam05483  282 ENLKELIEKKDHLTK---ELEDIKMSLQRSMSTQKALEedLQIATKTICQLTEEKEAQMEELNKAkaahsfvvTEFEATT 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  990 NCLEMKKETEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLH--LSQQCELL---KKLLINAHEQQTQQ 1064
Cdd:pfam05483  359 CSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkiLAEDEKLLdekKQFEKIAEELKGKE 438

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1065 LKLSHDRESKEMRAHQAKISMENSKA-----ISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKV 1139
Cdd:pfam05483  439 QELIFLLQAREKEIHDLEIQLTAIKTseehyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1784638851 1140 QlEHLEFLEKQNEqaKEMQQMVKL-EAEMDRR 1170
Cdd:pfam05483  519 Q-EDIINCKKQEE--RMLKQIENLeEKEMNLR 547
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 918-1169 7.97e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 7.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  918 RIEDL-KQMKAYLKHLKKQ----------QKELNSLKKKHAKehstmqkLHCTQVDKIVAQYDKEKSTHEKILEKAMKKK 986
Cdd:COG1196    190 RLEDIlGELERQLEPLERQaekaeryrelKEELKELEAELLL-------LKLRELEAELEELEAELEELEAELEELEAEL 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  987 ggsnclemkKETEIKIQTLTSDHKSKVKEI------VAQHTKEWSEMINTHSAEEQEIRDLH-----LSQQCELLKKLLI 1055
Cdd:COG1196    263 ---------AELEAELEELRLELEELELELeeaqaeEYELLAELARLEQDIARLEERRRELEerleeLEEELAELEEELE 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1056 nAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIknkAERERRVRELNssntKKFLEERKRLAMKQSKEMDQ 1135
Cdd:COG1196    334 -ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELA----EELLEALRAAAELAAQLEEL 405

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1784638851 1136 LKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMDR 1169
Cdd:COG1196    406 EEAEEALLERLERLEEELEELEEALAELEEEEEE 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 918-1162 9.70e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 9.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  918 RIEDLK-QMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKL--HCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEM 994
Cdd:TIGR04523  167 QKEELEnELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851  995 K-KETEIKIQTLTSDH-------KSKVKEIVaQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLlinaHEQQTQQlk 1066
Cdd:TIGR04523  247 EiSNTQTQLNQLKDEQnkikkqlSEKQKELE-QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL----KSELKNQ-- 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638851 1067 lshdreSKEMRAHQAKISmENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQlKKVQLEHLEF 1146
Cdd:TIGR04523  320 ------EKKLEEIQNQIS-QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLES 391

                          250       260
                   ....*....|....*....|....
gi 1784638851 1147 --------LEKQNEQAKEMQQMVK 1162
Cdd:TIGR04523  392 qindleskIQNQEKLNQQKDEQIK 415
 
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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