NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568915847|ref|XP_006499010|]
View 

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 isoform X8 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
169-538 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: 553.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08591       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08591   154 --------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQ 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08591   208 LSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
5-157 2.76e-103

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: 320.14  E-value: 2.76e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    5 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 84
Cdd:cd16211     1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915847   85 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16211    81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
572-688 2.67e-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: 150.77  E-value: 2.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  572 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 645
Cdd:cd00275     3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568915847  646 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 688
Cdd:cd00275    80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
783-825 3.62e-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: 75.76  E-value: 3.62e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568915847   783 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 825
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PTZ00121 super family cl31754
MAEBL; Provisional
717-1064 1.45e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  717 KRADQMRAMGIETSDIADvpSDTSKNDKKGKANPAKANVTPQSSSELRPTTTA----ALGSGQEAKKGIELipqVRIEDL 792
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkadEAKKAEEKKKADEL---KKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  793 KQMKAYLK-HLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEIKKETEIK 871
Cdd:PTZ00121 1558 KKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-----ELKKAEEEK 1632
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  872 IQTLTTDHKSKVKEIVAQHTKEwseminthSAEEQEIRDLHLSQQCELLRKlliNAHEQQTQQLKLSHDRESKEMRAHQA 951
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEA 1701
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  952 KISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQLLKSCHAV 1031
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
                         330       340       350
                  ....*....|....*....|....*....|...
gi 568915847 1032 SQTQGEGDAADGEIGSRDGPQTSNSSMKLQSAN 1064
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFDNFANIIEGG 1814
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
169-538 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: 553.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08591       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08591   154 --------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQ 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08591   208 LSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
5-157 2.76e-103

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: 320.14  E-value: 2.76e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    5 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 84
Cdd:cd16211     1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915847   85 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16211    81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
172-319 1.93e-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: 250.11  E-value: 1.93e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   172 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 251
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWD--GPDGEPVVYHGYTLTSKIPFRDVLEAIKD 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915847   252 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPlepgRPLPSPNDLKRKILIKN 319
Cdd:pfam00388   79 YAFVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLDDDL----TELPSPEDLKGKILIKG 142
PLN02228 PLN02228
Phosphoinositide phospholipase C
75-677 5.46e-72

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 250.34  E-value: 5.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   75 PRTDIEDLFKKINGDktDYLTVDQLVSFLNEHQ--RDPRLNEILFPFYDAKRAmqiiEMYEPdeelkkKGLISSDGFCRY 152
Cdd:PLN02228   22 PPVSIKRLFEAYSRN--GKMSFDELLRFVSEVQgeRHAGLDYVQDIFHSVKHH----NVFHH------HGLVHLNAFYRY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  153 LMSDENAPVFLDRlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCW-DGKGEDQEpiIT 231
Cdd:PLN02228   90 LFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWpNPSGNAAE--VR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  232 HGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShplepGRPLPSPNDL 311
Cdd:PLN02228  167 HGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHLPPNLQAQVAKMLTKTFRGMLFRCTSES-----TKHFPSPEEL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  312 KRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASiledDNEEEIESAADQEEEAHPEYKFGNELSAddyshkeavAN 391
Cdd:PLN02228  242 KNKILISTKPPKEYLESKTVQTTRTPTVKETSWKRVA----DAENKILEEYKDEESEAVGYRDLIAIHA---------AN 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  392 SVKKTSDDLEHENNKKGLVTVeDEQawmasykyvgattnihpYLSTMInyaqpvkfqgfhvaeernihynmssfnesvgl 471
Cdd:PLN02228  309 CKDPLKDCLSDDPEKPIRVSM-DEQ-----------------WLETMV-------------------------------- 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  472 gylKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMR 551
Cdd:PLN02228  339 ---RTRGTDLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILL 415
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  552 RPDRTFDPFSETPvdgvIAATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIrkEFRTRMVMNNGLnPV 621
Cdd:PLN02228  416 DEHTLFDPCKRLP----IKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV--SYRTETAVDQWF-PI 488
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  622 YNEESFVFrKVILPDLAVLRIAV--YDDN--NKLIGQRILPLDGLQAGYRHISLRNEGNK 677
Cdd:PLN02228  489 WGNDEFLF-QLRVPELALLWFKVqdYDNDtqNDFAGQTCLPLPELKSGVRAVRLHDRAGK 547
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
436-550 2.52e-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: 218.26  E-value: 2.52e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    436 STMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQ 515
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 568915847    516 MVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFM 550
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
572-688 2.67e-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: 150.77  E-value: 2.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  572 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 645
Cdd:cd00275     3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568915847  646 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 688
Cdd:cd00275    80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
783-825 3.62e-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: 75.76  E-value: 3.62e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568915847   783 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 825
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
575-671 2.85e-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: 69.44  E-value: 2.85e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    575 VQVISGQFLSDKKIGT----YVEVDMYGLPtdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN-- 648
Cdd:smart00239    4 VKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVKNT-LNPVWNET-FEF-EVPPPELAELEIEVYDKDrf 76
                            90       100
                    ....*....|....*....|....*
gi 568915847    649 --NKLIGQRILPLDGLQAGYRHISL 671
Cdd:smart00239   77 grDDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
66-157 6.42e-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: 68.04  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    66 FY-ELTQkicpRTDIEDLFKKINGDkTDYLTVDQLVSFLNEHQRDPRlneilfpfYDAKRAMQIIEMYEPDEELKKKGLI 144
Cdd:pfam09279    1 FYkMLTQ----REEIDEIFQEYSGD-GQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAM 67
                           90
                   ....*....|...
gi 568915847   145 SSDGFCRYLMSDE 157
Cdd:pfam09279   68 TKDGFLMYLCSPD 80
C2 pfam00168
C2 domain;
574-668 1.31e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.56  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   574 SVQVISGQFLSDKKIG----TYVEVDMYGLptdtiRKEFRTRmVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 648
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNgtsdPYVKVYLLDG-----KQKKKTK-VVKNTLNPVWNET-FTF-SVPDPENAVLEIEVYDYDr 75
                           90       100
                   ....*....|....*....|...
gi 568915847   649 ---NKLIGQRILPLDGLQAGYRH 668
Cdd:pfam00168   76 fgrDDFIGEVRIPLSELDSGEGL 98
PTZ00121 PTZ00121
MAEBL; Provisional
717-1064 1.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  717 KRADQMRAMGIETSDIADvpSDTSKNDKKGKANPAKANVTPQSSSELRPTTTA----ALGSGQEAKKGIELipqVRIEDL 792
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkadEAKKAEEKKKADEL---KKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  793 KQMKAYLK-HLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEIKKETEIK 871
Cdd:PTZ00121 1558 KKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-----ELKKAEEEK 1632
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  872 IQTLTTDHKSKVKEIVAQHTKEwseminthSAEEQEIRDLHLSQQCELLRKlliNAHEQQTQQLKLSHDRESKEMRAHQA 951
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEA 1701
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  952 KISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQLLKSCHAV 1031
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
                         330       340       350
                  ....*....|....*....|....*....|...
gi 568915847 1032 SQTQGEGDAADGEIGSRDGPQTSNSSMKLQSAN 1064
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFDNFANIIEGG 1814
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
905-1026 1.36e-05

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: 46.60  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   905 EQEIRDLHLSQQCELLRKLLINAHEQQTQQLKLSHDRESKEMrahQAKISMENSKAISQ-DKSIKNKAERERRVRELNSS 983
Cdd:pfam08703   25 EKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEM---KKKLERKRLESIQEaKKRTSDKAAQERLKKEINNS 101
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568915847   984 NTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQLLK 1026
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQA 144
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
169-538 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: 553.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08591       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08591   154 --------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQ 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08591   208 LSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
169-538 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: 526.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08626     1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08626    81 IKDTAFVTSDYPVILSFENHCSKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08626       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08626   154 --------------------------LSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQ 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08626   208 MSRIYPKGTRVDSSNYMPQIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
169-538 1.10e-132

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: 400.67  E-value: 1.10e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08558     1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGP--DGEPVVYHGHTLTSKILFKDVIEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08558    79 IKEYAFVTSPYPVILSLENHCSLEQQKKMAQILKEIFGDKLLTPPLDENPVQ----LPSPEQLKGKILIKGKK------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08558       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08558   148 ---------------------------------------------------YHMSSFSETKALKLLKESPEEFVKYNKRQ 176
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08558   177 LSRVYPKGTRVDSSNYNPQPFWNAGCQMVALNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
169-538 2.96e-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: 358.99  E-value: 2.96e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRLkpeve 327
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKKY----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  328 kkqlealksmmeagesaapasileddnEEeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkk 407
Cdd:cd08624   156 ---------------------------EE--------------------------------------------------- 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  408 glvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKR 487
Cdd:cd08624   158 ---------------------------MSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKR 210
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915847  488 QMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08624   211 QMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
171-538 2.34e-113

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: 351.28  E-value: 2.34e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  171 EMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIK 250
Cdd:cd08625     3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  251 ETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevekk 329
Cdd:cd08625    83 ESAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  330 qlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 409
Cdd:cd08625       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  410 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 489
Cdd:cd08625   155 -------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQL 209
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568915847  490 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08625   210 SRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
169-538 4.03e-107

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: 334.69  E-value: 4.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08593     1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWD--GPDGEPIIYHGHTLTSKILFKDVIQA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRLKpevek 328
Cdd:cd08593    79 IREYAFKVSPYPVILSLENHCSVEQQKVMAQHLKSILGDKLLTQPLDGVLTA----LPSPEELKGKILVKGKKLK----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08593       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08593   150 ----------------------LAKELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQ 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08593   208 LSRIYPAGLRTDSSNYDPQEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
5-157 2.76e-103

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: 320.14  E-value: 2.76e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    5 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 84
Cdd:cd16211     1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915847   85 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16211    81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
170-538 2.32e-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: 311.25  E-value: 2.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  170 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAI 249
Cdd:cd08623     2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  250 KETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08623    82 AECAFKTSPFPILLSFENHVdSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08623       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08623   155 --------------------------MSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQ 208
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08623   209 LSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLSMQINMGMYEYN 258
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
170-538 4.50e-92

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: 293.18  E-value: 4.50e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  170 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGkgEDQEPIITHGKAMCTDILFKDVIQAI 249
Cdd:cd08592     2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  250 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQaleshPLEP-GRPLPSPNDLKRKILIKNKRLKpevek 328
Cdd:cd08592    80 KEHAFVTSEYPVILSIENHCSLPQQRNMAQAFKEVFGDMLLTQ-----PVDRnADQLPSPNQLKRKIIIKHKKLF----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08592       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYL-KTHAIEFVNYNKR 487
Cdd:cd08592   150 ---------------------------------------------------YEMSSFPETKAEKYLnRQKGKIFLKYNRR 178
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915847  488 QMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08592   179 QLSRVYPKGQRVDSSNYDPVPMWNCGSQMVALNFQTPDKPMQLNQALFMLN 229
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
170-538 1.09e-88

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: 285.47  E-value: 1.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  170 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGkgEDQEPIITHGKAMCTDILFKDVIQAI 249
Cdd:cd08597     2 QDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  250 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQAleshPLEPGRPLPSPNDLKRKILIKNKRLKpeveKK 329
Cdd:cd08597    80 NEYAFVASEYPLILCIENHCSEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKKLK----RR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  330 QLealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansVKKTSDdlehennkkgL 409
Cdd:cd08597   152 KL-------------------------------------------------------------CKELSD----------L 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  410 VTVedeqawmasykyvgattnihpylstminyAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 489
Cdd:cd08597   161 VSL-----------------------------CKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFL 211
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568915847  490 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08597   212 SRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
169-535 1.41e-85

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: 275.66  E-value: 1.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08598     1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWD--GDDGEPVVTHGYTLTSSVPFRDVCRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKnkrlkpevek 328
Cdd:cd08598    79 IKKYAFVTSPYPLILSLEVHCDAEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIK---------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansVKKTSDDLEHennkkg 408
Cdd:cd08598   145 ----------------------------------------------------------------VKKESKTPNH------ 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihynMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08598   155 -----------------------------------------------------IFSLSERSLLKLLKDKRAALDKHNRRH 181
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKF 535
Cdd:cd08598   182 LMRVYPSGTRISSSNFNPLPFWRAGVQMVALNWQTYDLGMQLNEAMF 228
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
169-538 7.62e-83

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: 269.58  E-value: 7.62e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGedQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08630     1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPG--GEPVIYHGHTLTSKILFRDVIQA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrPLPSPNDLKRKILIKNKRLKpevek 328
Cdd:cd08630    79 VRQHAFTASPYPVILSLENHCGLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQ----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08630       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08630   151 ----------------------ISPELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQ 208
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08630   209 LTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
170-538 2.65e-79

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: 259.78  E-value: 2.65e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  170 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAI 249
Cdd:cd08596     2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWD--GDDGMPIIYHGHTLTTKIPFKDVVEAI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  250 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevekk 329
Cdd:cd08596    80 NRSAFITSDYPVILSIENHCSLQQQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  330 qlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 409
Cdd:cd08596       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  410 vtvedeqawmasykyvgattniHPYLSTMINYAQPVKFQGFHVAEerniHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 489
Cdd:cd08596   152 ----------------------APELSDLVIYCQAVKFPGLSTPK----CYHISSLNENAAKRLCRRYPQKLVQHTRCQL 205
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568915847  490 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08596   206 LRTYPAATRIDSSNPNPLIFWLHGLQLVALNYQTDDLPMHLNAAMFEAN 254
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
169-538 4.75e-78

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: 256.50  E-value: 4.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08629     1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGP--NQEPIIYHGYTFTSKILFCDVLRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRLKPEVEk 328
Cdd:cd08629    79 IRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTS----LPSPEQLKGKILLKGKKLKLVPE- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08629       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFH-VAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKR 487
Cdd:cd08629   154 --------------------------LSDMIIYCKSVHFGGFSsPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVS 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915847  488 QMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08629   208 CLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
172-319 1.93e-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: 250.11  E-value: 1.93e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   172 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 251
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWD--GPDGEPVVYHGYTLTSKIPFRDVLEAIKD 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915847   252 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPlepgRPLPSPNDLKRKILIKN 319
Cdd:pfam00388   79 YAFVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLDDDL----TELPSPEDLKGKILIKG 142
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
169-538 4.38e-77

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: 252.42  E-value: 4.38e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08594     1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDGP--DGEPVVHHGYTLTSKILFRDVIET 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLlkqALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08594    79 INKYAFIKNEYPVILSIENHCSVQQQKKMAQYLKEILGDKL---DLSSVISGDSKQLPSPQSLKGKILIKGKK------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08594       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08594   149 ---------------------------------------------------WQVSSFSETRAHQIVQQKAAQFLRFNQRQ 177
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08594   178 LSRIYPSAYRIDSSNFNPQPYWNAGCQLVALNYQTEGRMLQLNRAKFRAN 227
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
169-538 1.28e-76

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: 252.56  E-value: 1.28e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08631     1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDGP--NGEPIVYHGHTFTSKILFKDVVAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShpLEPGRpLPSPNDLKRKILIKNKRLKpevek 328
Cdd:cd08631    79 VAQYAFQVSDYPVILSLENHCGVEQQQTMAQHLTEILGEKLLSTTLDG--VLPTQ-LPSPEELRGKILLKGKKIR----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 408
Cdd:cd08631       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08631   151 ----------------------LSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQ 208
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08631   209 LSRVYPSGLRTDSSNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
169-538 5.83e-76

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: 250.62  E-value: 5.83e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08595     1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGA--DNEPVVYHGYTLTSKILFKEVITT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEsHPlePGRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08595    79 VEKYAFEKSDYPVVLSLENHCSTEQQEIMAHYLVSILGEKLLRAPID-DP--ATGELPSPEALKFKILVKNKK------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshKEAVAnsvkktsddlehennkkg 408
Cdd:cd08595   149 ---------------------------------------------------------KIAKA------------------ 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08595   154 --------------------------LSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRF 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08595   208 ITRIYPKGTRASSSNYNPQEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN 257
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
170-538 1.28e-74

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: 246.88  E-value: 1.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  170 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 249
Cdd:cd08633     2 QDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGP--DGEPIVHHGYTLTSKILFKDVIETI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  250 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDlllKQALESHPLEPGRPLPSPNDLKRKILIKNKRLkpevekk 329
Cdd:cd08633    80 NKYAFIKNEYPVILSIENHCSVPQQKKMAQYLTEILGD---KLDLSSVISNDCTRLPSPEILKGKILVKGKKL------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  330 qlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshKEAVANSVKKTSDDLEHEnnkkgl 409
Cdd:cd08633   150 --------------------------------------------------------SRALSDLVKYTKSVRVHD------ 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  410 VTVEDEQAWmasykyvgattnihpylstminyaqpvkfqgfhvaeernihyNMSSFNESVGLGYLKTHAIEFVNYNKRQM 489
Cdd:cd08633   168 IETEATSSW------------------------------------------QVSSFSETKAHQILQQKPAQYLRFNQRQL 205
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568915847  490 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08633   206 SRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
PLN02228 PLN02228
Phosphoinositide phospholipase C
75-677 5.46e-72

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 250.34  E-value: 5.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   75 PRTDIEDLFKKINGDktDYLTVDQLVSFLNEHQ--RDPRLNEILFPFYDAKRAmqiiEMYEPdeelkkKGLISSDGFCRY 152
Cdd:PLN02228   22 PPVSIKRLFEAYSRN--GKMSFDELLRFVSEVQgeRHAGLDYVQDIFHSVKHH----NVFHH------HGLVHLNAFYRY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  153 LMSDENAPVFLDRlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCW-DGKGEDQEpiIT 231
Cdd:PLN02228   90 LFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWpNPSGNAAE--VR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  232 HGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShplepGRPLPSPNDL 311
Cdd:PLN02228  167 HGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHLPPNLQAQVAKMLTKTFRGMLFRCTSES-----TKHFPSPEEL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  312 KRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASiledDNEEEIESAADQEEEAHPEYKFGNELSAddyshkeavAN 391
Cdd:PLN02228  242 KNKILISTKPPKEYLESKTVQTTRTPTVKETSWKRVA----DAENKILEEYKDEESEAVGYRDLIAIHA---------AN 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  392 SVKKTSDDLEHENNKKGLVTVeDEQawmasykyvgattnihpYLSTMInyaqpvkfqgfhvaeernihynmssfnesvgl 471
Cdd:PLN02228  309 CKDPLKDCLSDDPEKPIRVSM-DEQ-----------------WLETMV-------------------------------- 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  472 gylKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMR 551
Cdd:PLN02228  339 ---RTRGTDLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILL 415
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  552 RPDRTFDPFSETPvdgvIAATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIrkEFRTRMVMNNGLnPV 621
Cdd:PLN02228  416 DEHTLFDPCKRLP----IKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV--SYRTETAVDQWF-PI 488
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  622 YNEESFVFrKVILPDLAVLRIAV--YDDN--NKLIGQRILPLDGLQAGYRHISLRNEGNK 677
Cdd:PLN02228  489 WGNDEFLF-QLRVPELALLWFKVqdYDNDtqNDFAGQTCLPLPELKSGVRAVRLHDRAGK 547
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
169-538 1.78e-71

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: 238.01  E-value: 1.78e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 248
Cdd:cd08632     1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDGP--DGEPVVHHGYTLTSKITFRDVIET 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLL-LKQALESHPlepgRPLPSPNDLKRKILIKNKRLkpeve 327
Cdd:cd08632    79 INKYAFVKNEFPVILSIENHCSIQQQKKIAQYLKEIFGDKLdLSSVLTGDP----KQLPSPQLLKGKILVKGKKL----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  328 kkqLEALKSMMEAGESAAPASILEDdneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkk 407
Cdd:cd08632   150 ---CRDLSDLVVYTNSVAAQDIVDD------------------------------------------------------- 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  408 glvtvedeqawmasykyvGATTNIhpylstminyaqpvkfqgfhvaeernihynmSSFNESVGLGYLKTHAIEFVNYNKR 487
Cdd:cd08632   172 ------------------GSTGNV-------------------------------LSFSETRAHQLVQQKAEQFMTYNQK 202
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915847  488 QMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08632   203 QLTRIYPSAYRIDSSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
170-538 5.64e-71

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: 235.69  E-value: 5.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  170 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 249
Cdd:cd08627     2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGP--DGMPVIYHGHTLTTKIKFSDVLHTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  250 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRLkpevekk 329
Cdd:cd08627    80 KEHAFVTSEYPIILSIEDHCSIVQQRNMAQHFKKVFGDMLLTKPVDINADG----LPSPNQLKRKILIKHKKL------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  330 qlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 409
Cdd:cd08627       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  410 vtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeerniHYNMSSFNESVGLGYL-KTHAIEFVNYNKRQ 488
Cdd:cd08627   149 -------------------------------------------------YRDMSSFPETKAEKYVnRSKGKKFLQYNRRQ 179
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08627   180 LSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
5-157 7.97e-71

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: 232.44  E-value: 7.97e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    5 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 84
Cdd:cd16212     1 KKHWMRLGFMVDSGGKIPVKHIARTFASGKTEKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915847   85 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16212    81 SITKGKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
5-157 1.44e-70

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: 231.75  E-value: 1.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    5 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 84
Cdd:cd16200     1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDKKRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915847   85 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16200    81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
170-538 7.20e-69

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: 231.10  E-value: 7.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  170 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 249
Cdd:cd08628     2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDGP--DGKPIIYHGWTRTTKIKFDDVVQAI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  250 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQaleshPLEP-GRPLPSPNDLKRKILIKNKRlkpevek 328
Cdd:cd08628    80 KDHAFVTSEYPVILSIEEHCSVEQQRHMAKVFKEVFGDKLLMK-----PLEAsADQLPSPTQLKEKIIIKHKK------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgneLSADDYSHKEAVANSVKKTSDDLEHENNKKg 408
Cdd:cd08628   148 -------------------------------------------------LIAIELSDLVVYCKPTSKTKDNLENPDFKE- 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihynMSSFNESVGLGYLKTHAIEFVNYNKRQ 488
Cdd:cd08628   178 -----------------------------------------------------IRSFVETKAPSIIRQKPVQLLKYNRKG 204
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08628   205 LTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN 254
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
436-550 2.52e-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: 218.26  E-value: 2.52e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    436 STMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQ 515
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 568915847    516 MVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFM 550
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PLN02222 PLN02222
phosphoinositide phospholipase C 2
61-674 4.87e-63

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 225.29  E-value: 4.87e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   61 FTYEKFYELTQKICPRtDIEDLFKKINgdKTDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEmyEPDEELKK 140
Cdd:PLN02222   10 FCFRRRFRYTASEAPR-EIKTIFEKYS--ENGVMTVDHLHRFLIDVQKQDKATR--------EDAQSIIN--SASSLLHR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  141 KGLiSSDGFCRYLMSDENAPVFLDrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWD 220
Cdd:PLN02222   77 NGL-HLDAFFKYLFGDNNPPLALH--EVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  221 GKGEDQEPIItHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEshplE 300
Cdd:PLN02222  154 NSDKDDIDVL-HGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVG----E 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  301 PGRPLPSPNDLKRKILIKNKRLKPEVEKKQLEALKSMMEAGES-----AAPASILEDDNEEEIESAADQEEEAHPEYKFG 375
Cdd:PLN02222  229 SLKEFPSPNSLKKRIIISTKPPKEYKEGKDDEVVQKGKDLGDEevwgrEVPSFIQRNKSVDKNDSNGDDDDDDDDGEDKS 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  376 NELSADDYSHKEAVANSVKK--TSDDLEHENNKKGLVTVEDEQAWMASYKYvgattnihpylstminyaqpvkfqgfhva 453
Cdd:PLN02222  309 KKNAPPQYKHLIAIHAGKPKggITECLKVDPDKVRRLSLSEEQLEKAAEKY----------------------------- 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  454 eernihynmssfnesvglgylkthAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQG 533
Cdd:PLN02222  360 ------------------------AKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQG 415
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  534 KFEYNGSCGYLLKPDFMRRPD---RTFDPFSETPVDgviaATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLP 600
Cdd:PLN02222  416 MFRANGGCGYIKKPDLLLKSGsdsDIFDPKATLPVK----TTLRVTIYMGEgwyfdfrhthFDQYSPPDFYTRVGIAGVP 491
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915847  601 TDTIRKefRTRMVMNNGLnPVYnEESFVFrKVILPDLAVLRIAV--YDDNNK--LIGQRILPLDGLQAGYRHISLRNE 674
Cdd:PLN02222  492 GDTVMK--KTKTLEDNWI-PAW-DEVFEF-PLTVPELALLRLEVheYDMSEKddFGGQTCLPVWELSQGIRAFPLHSR 564
PLN02952 PLN02952
phosphoinositide phospholipase C
57-679 5.45e-63

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 225.65  E-value: 5.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   57 EPAAFTYEKFYELTQK-----ICPRTDIEDLFKKINgDKTDYLTVDQLVSFLNEHQrdprlNEILFPFYDAKRAM-QIIE 130
Cdd:PLN02952   13 DSGSYNYKMFNLFNRKfkiteAEPPDDVKDVFCKFS-VGGGHMGADQLRRFLVLHQ-----DELDCTLAEAQRIVeEVIN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  131 MYEPDEELKKKGLISSDGFCRYLMSDENAPVFLdrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAG 210
Cdd:PLN02952   87 RRHHVTRYTRHGLNLDDFFHFLLYDDLNGPITP---QVHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  211 CRCVELDCWDGKGEDqEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLL 290
Cdd:PLN02952  164 VRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLKSIRDYAFSSSPYPVIITLEDHLTPDLQAKVAEMATQIFGQMLY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  291 KQalESHPLepgRPLPSPNDLKRKILIKNKRLKpevekkqlealksmmEAGESAAPASILEDDN-EEEIESAADQEEEAH 369
Cdd:PLN02952  243 YP--ESDSL---VQFPSPESLKHRIIISTKPPK---------------EYLESSGPIVIKKKNNvSPSGRNSSEETEEAQ 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  370 PEYKFGNELSADDYShkeavansvkktsdDLEHENNKKGlvtvedeQAWMASYKYVgattnihpylsTMINYAQP---VK 446
Cdd:PLN02952  303 TLESMLFEQEADSRS--------------DSDQDDNKSG-------ELQKPAYKRL-----------ITIHAGKPkgtLK 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  447 fQGFHVAEERnihYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDL 526
Cdd:PLN02952  351 -DAMKVAVDK---VRRLSLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGK 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  527 AMQLNQGKFEYNGSCGYLLKPDFMRRP---DRTFDPFSETPVdgviAATCSVQVISG----------QFLSDKKIGTYVE 593
Cdd:PLN02952  427 SLWLMHGMFRANGGCGYLKKPDFLMKKgfhDEVFDPKKKLPV----KKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTK 502
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  594 VDMYGLPTDTIRKefRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAV--YD--DNNKLIGQRILPLDGLQAGYRHI 669
Cdd:PLN02952  503 MYIVGVPADNAKK--KTKIIEDN-WYPAWNEE-FSF-PLTVPELALLRIEVreYDmsEKDDFGGQTCLPVSELRPGIRSV 577
                         650
                  ....*....|
gi 568915847  670 SLRNEGNKPL 679
Cdd:PLN02952  578 PLHDKKGEKL 587
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
172-320 5.96e-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: 209.83  E-value: 5.96e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    172 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 251
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWD--GPDGEPVIYHGHTFTLPIKLSEVLEAIKD 78
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915847    252 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLepgrPLPSPNDLKRKILIKNK 320
Cdd:smart00148   79 FAFVTSPYPVILSLENHCSPDQQAKMAQMFKEIFGDMLYTPPLTSSLE----VLPSPEQLRGKILLKVR 143
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
169-538 1.92e-62

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: 213.67  E-value: 1.92e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQF-----GGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMcTDILFK 243
Cdd:cd00137     1 HHPDTQPLAHYSIPGTHDTYLTAGQFtikqvWGLTQTEMYRQQLLSGCRCVDIRCWDGK--PEEPIIYHGPTF-LDIFLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  244 DVIQAIKETAFVTSEYPVILSFENHCSKY--QQYKMSKYCEDLFGDLLLkqaleSHPLEPGRPLPSPNDLKRKILIKNKr 321
Cdd:cd00137    78 EVIEAIAQFLKKNPPETIIMSLKNEVDSMdsFQAKMAEYCRTIFGDMLL-----TPPLKPTVPLPSLEDLRGKILLLNK- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  322 lkpevekkqlealksmmeagesaapasileddneeeiesaadqeeeahpeykfgnelsaddyshkeavansvkktsddle 401
Cdd:cd00137       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  402 heNNKKGLVTVEDEQAWMASYKYvgattnihpylSTMINYAqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIE- 480
Cdd:cd00137   152 --KNGFSGPTGSSNDTGFVSFEF-----------STQKNRS-----------------YNISSQDEYKAYDDEKVKLIKa 201
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915847  481 ---FVNYNKRQMSRIYPKGGRV---------DSSNYMPQIFWN---AGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd00137   202 tvqFVDYNKNQLSRNYPSGTSGgtawyyyamDSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
435-549 5.93e-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: 5.93e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   435 LSTMINYAQPVKFQGFHvAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGC 514
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568915847   515 QMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDF 549
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
5-157 1.26e-53

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: 184.04  E-value: 1.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    5 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTE-KVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLF 83
Cdd:cd16213     1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQHKDDrKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915847   84 KKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16213    81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYLMSED 154
PLN02230 PLN02230
phosphoinositide phospholipase C 4
75-673 3.46e-53

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 196.85  E-value: 3.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   75 PRTDIEDLFKKInGDKTDYLTVDQLVSFLNEHQRDPRLNEIlfpfydaKRAMQIIemyepDEELKKKGLISS-------- 146
Cdd:PLN02230   27 PVADVRDLFEKY-ADGDAHMSPEQLQKLMAEEGGGEGETSL-------EEAERIV-----DEVLRRKHHIAKftrrnltl 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  147 DGFCRYLMSDENAPVFLDrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgKGEDq 226
Cdd:PLN02230   94 DDFNYYLFSTDLNPPIAD--QVHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWP-RGTD- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  227 EPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLkqaleSHPLEPGRPLP 306
Cdd:PLN02230  170 DVCVKHGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHLTPKLQFKVAKMITQTFGDMLY-----YHDSEGCQEFP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  307 SPNDLKRKILIKNKrlkpevekkqlealksmmeagesaAPASILEDDNEEEIESAADQEEEahPEYKFGNElsADDYSHK 386
Cdd:PLN02230  245 SPEELKEKILISTK------------------------PPKEYLEANDAKEKDNGEKGKDS--DEDVWGKE--PEDLIST 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  387 EAVANSVKKTSDDLEHENNKKGLVTVEDE-QAWMASYKYVGATTNIHPYLS-TMINYAQPVKFQGFHVAEERnIHYNMSS 464
Cdd:PLN02230  297 QSDLDKVTSSVNDLNQDDEERGSCESDTScQLQAPEYKRLIAIHAGKPKGGlRMALKVDPNKIRRLSLSEQL-LEKAVAS 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  465 FNESVglgylkthaiefVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYL 544
Cdd:PLN02230  376 YGADV------------IRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYV 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  545 LKPDFMRRPDRTFDPFseTPVDGVI-AATCSVQVISG----------QFLSDKKIGTYVEVDMYGLPTDTIRKEFRtrmV 613
Cdd:PLN02230  444 KKPDFLMDAGPNGQDF--YPKDNSCpKKTLKVKVCMGdgwlldfkktHFDSYSPPDFFVRVGIAGAPVDEVMEKTK---I 518
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915847  614 MNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYD----DNNKLIGQRILPLDGLQAGYRHISLRN 673
Cdd:PLN02230  519 EYDTWTPIWNKE-FIF-PLAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFN 580
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
169-538 1.55e-51

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: 181.03  E-value: 1.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  169 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDqePIITHGKAMCTDILFKDVIQA 248
Cdd:cd08599     1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  249 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQalesHPLEPGRPLPSPNDLKRKILIknkRLKPEVek 328
Cdd:cd08599    79 IKENAFTASEYPVIITLENHLSPELQAKAAQILRETLGDKLFYP----DSEDLPEEFPSPEELKGKILI---SDKPPV-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  329 kqlealksmmeagesaapasileddneeeiesaadqeeeahpeykFGNELSaddyshkeavansvkktsddlEHENNKKg 408
Cdd:cd08599   150 ---------------------------------------------IRNSLS---------------------ETQLKKV- 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  409 lvtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihynmssfnesVGLGYlKTHAIEFvnyNKRQ 488
Cdd:cd08599   163 ------------------------------------------------------------IEGEH-PTDLIEF---TQKN 178
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915847  489 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 538
Cdd:cd08599   179 LLRVYPAGLRITSSNYDPMLAWMHGAQMVALNMQGYDRPLWLNRGKFRAN 228
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
572-688 2.67e-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: 150.77  E-value: 2.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  572 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 645
Cdd:cd00275     3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568915847  646 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 688
Cdd:cd00275    80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
6-157 1.95e-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: 134.62  E-value: 1.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    6 KHWMKLAFLTNTTGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKK 85
Cdd:cd16208     2 KAYTKLKLQVNPEGRIPVKNIYRLFSADR--KRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSE 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915847   86 INGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16208    80 FGAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PLN02223 PLN02223
phosphoinositide phospholipase C
152-680 2.54e-35

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 142.47  E-value: 2.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  152 YLMSDENAPVFLDRLElYQEMDHPLAHYFISSSHNTYLTGRQ-FGGKSSVEMYRQVLLAGCRCVELDCW-DGKGedqepi 229
Cdd:PLN02223   89 FLFSTELNPPIGDQVR-HHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLLpDGKD------ 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  230 ithgkAMCT--------DILFKDVIQAIKETAFV-TSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQAlESHPLE 300
Cdd:PLN02223  162 -----GICVrpkwnfekPLELQECLDAIKEHAFTkCRSYPLIITFKDGLKPDLQSKATQMIDQTFGDMVYHED-PQHSLE 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  301 PgrpLPSPNDLKRKILIKnkRLKPeveKKQLEAlksmmeagesaapasileDDNEEEIESAADQEEEAHPEYKfgnelsa 380
Cdd:PLN02223  236 E---FPSPAELQNKILIS--RRPP---KELLYA------------------KADDGGVGVRNELEIQEGPADK------- 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  381 ddyshkeavansvkktsddlehennkkglvtvedeqawmasykyvgattnihpylstmiNYAQPVkfqGFHVAEERNIHY 460
Cdd:PLN02223  283 -----------------------------------------------------------NYQSLV---GFHAVEPRGMLQ 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  461 NM--SSFNESVGLGYLKTHAIEFVnynKRQMSRIYPKGGRVDS-SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEY 537
Cdd:PLN02223  301 KAltGKADDIQQPGWYERDIISFT---QKKFLRTRPKKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRA 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  538 NGSCGYLLKPDFMRR--PDRTFDPfSETPvdgVIAATCSVQVISGQ-FLSD--KKIGT------YVEVDMYGLPTDtirK 606
Cdd:PLN02223  378 NGGCGYVKKPDFLLNagPSGVFYP-TENP---VVVKILKVKIYMGDgWIVDfkKRIGRlskpdlYVRISIAGVPHD---E 450
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915847  607 EFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYD----DNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLS 680
Cdd:PLN02223  451 KIMKTTVKNNEWKPTWGEE-FTF-PLTYPDLALISFEVYDyevsTADAFCGQTCLPVSELIEGIRAVPLYDERGKACS 526
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
5-157 3.05e-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: 122.72  E-value: 3.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    5 KKHWMKLAFLTNTTGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 84
Cdd:cd16210     1 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915847   85 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
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, ...
6-157 1.67e-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: 109.20  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    6 KHWMKLAFLTNTTGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKK 85
Cdd:cd16209     2 KIYVKLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTS 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915847   86 INGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16209    80 YHAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
783-825 3.62e-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: 75.76  E-value: 3.62e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568915847   783 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 825
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
183-291 4.03e-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: 80.17  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  183 SSHNTYLtgrQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHG------KAMCTDILFKDVIQAIKETAFvT 256
Cdd:cd08555     2 LSHRGYS---QNGQENTLEAFYRALDAGARGLELDVRLTK--DGELVVYHGptldrtTAGILPPTLEEVLELIADYLK-N 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568915847  257 SEYPVILSFENHCS----KYQQYKMSKYCEDLFGDLLLK 291
Cdd:cd08555    76 PDYTIILSLEIKQDspeyDEFLAKVLKELRVYFDYDLRG 114
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
34-157 1.37e-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: 74.57  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   34 KTEKVIFQALKELGlpsgkNDEIEPAAFTyeKFYE-LTQkicpRTDIEDLFKKINGDKtDYLTVDQLVSFLNEHQRDPRL 112
Cdd:cd16202    36 DYAKKLFQEADTSG-----EDVLDEEEFV--QFYNrLTK----RPEIEELFKKYSGDD-EALTVEELRRFLQEEQKVKDV 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568915847  113 neilfpfyDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16202   104 --------TLEWAEQLIETYEPSEDLKAQGLMSLDGFTLFLLSPD 140
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
575-671 2.85e-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: 69.44  E-value: 2.85e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    575 VQVISGQFLSDKKIGT----YVEVDMYGLPtdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN-- 648
Cdd:smart00239    4 VKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVKNT-LNPVWNET-FEF-EVPPPELAELEIEVYDKDrf 76
                            90       100
                    ....*....|....*....|....*
gi 568915847    649 --NKLIGQRILPLDGLQAGYRHISL 671
Cdd:smart00239   77 grDDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
66-157 6.42e-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: 68.04  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    66 FY-ELTQkicpRTDIEDLFKKINGDkTDYLTVDQLVSFLNEHQRDPRlneilfpfYDAKRAMQIIEMYEPDEELKKKGLI 144
Cdd:pfam09279    1 FYkMLTQ----REEIDEIFQEYSGD-GQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAM 67
                           90
                   ....*....|...
gi 568915847   145 SSDGFCRYLMSDE 157
Cdd:pfam09279   68 TKDGFLMYLCSPD 80
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
8-157 5.62e-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: 64.54  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847    8 WMKLAFL---TNTTGKIP---VRSITRTFASGKTEKVIFQALKELglpSGKNDEiEPAAFTYEKFYELTQKICPRTDIED 81
Cdd:cd16206     1 WLESVFEeadTNKSGFLDeeeAVQLIKQLNPGLSTSRIKQKLKEL---QKKKDG-ARGRVSSDEFVELFKELATRPEIYF 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915847   82 LFKKINGDKtDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
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 ...
62-155 2.69e-10

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: 59.70  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   62 TYEKFYELTQKICPRTDIEDLFKKInGDKTDYLTVDQLVSFLNEHQRdprLNEIlfpfyDAKRAMQIIEMYEPDEELKKK 141
Cdd:cd16205    55 DFEEFCAFYKMMSTRRELYLLLLSY-SNKKDYLTLEDLARFLEVEQK---MTNV-----TLEYCLDIIEKFEPSEENKKN 125
                          90
                  ....*....|....
gi 568915847  142 GLISSDGFCRYLMS 155
Cdd:cd16205   126 GLLGIDGFTNYMRS 139
C2 pfam00168
C2 domain;
574-668 1.31e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.56  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   574 SVQVISGQFLSDKKIG----TYVEVDMYGLptdtiRKEFRTRmVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 648
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNgtsdPYVKVYLLDG-----KQKKKTK-VVKNTLNPVWNET-FTF-SVPDPENAVLEIEVYDYDr 75
                           90       100
                   ....*....|....*....|...
gi 568915847   649 ---NKLIGQRILPLDGLQAGYRH 668
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. ...
62-157 2.61e-09

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: 56.52  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   62 TYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEElkkK 141
Cdd:cd15898    54 TFDEFEELYKSLTERPELEPIFKKYAGTNRDYMTLEEFIRFLREEQGEN---------VSEEECEELIEKYEPERE---N 121
                          90
                  ....*....|....*.
gi 568915847  142 GLISSDGFCRYLMSDE 157
Cdd:cd15898   122 RQLSFEGFTNFLLSPE 137
EFh_PRIP2 cd16223
EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); ...
15-157 1.49e-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: 54.53  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   15 TNTTGKIP----VRSITRTFASGKTEKVIFQaLKELGlpsgKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKKINGDK 90
Cdd:cd16223    11 TDNVGHITlcraVQFIKNLNPGLKTSKIELK-FKELH----KSKEKGGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSNK 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915847   91 tDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16223    86 -EFLDTKDLMMFLEAEQGMAHVTE--------EISLDIIHKYEPSKEGQEKGWLSLDGFTNYLMSPE 143
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
64-157 2.27e-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: 53.97  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   64 EKFY-ELTQkicpRTDIEDLFKKINGdKTDYLTVDQLVSFLNEHQRDPRLNEIlfpfydakrAMQIIEMYEPDEELKKKG 142
Cdd:cd16217    59 EEFYkLLTK----REEIDVIFGEYAK-SDGTMSRNNLLNFLQEEQREEVAPAY---------ALSLIEKYEPDETAKAQR 124
                          90
                  ....*....|....*
gi 568915847  143 LISSDGFCRYLMSDE 157
Cdd:cd16217   125 QMTKDGFLMYLLSPE 139
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
574-654 1.02e-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: 50.91  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  574 SVQVISGQFLSDKKIG----TYVEVDMYGlptdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 648
Cdd:cd00030     2 RVTVIEARNLPAKDLNgksdPYVKVSLGG------KQKFKTKVVKNT-LNPVWNET-FEF-PVLDPESDTLTVEVWDKDr 72

                  ....*....
gi 568915847  649 ---NKLIGQ 654
Cdd:cd00030    73 fskDDFLGE 81
EFh_PRIP1 cd16222
EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1); ...
62-157 7.80e-07

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: 49.48  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   62 TYEKFYELTQKICPRTDIEDLFKKINGDKtDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEMYEPDEELKKK 141
Cdd:cd16222    57 TEEEFCEAYSELCTRPEVYFLLVQISKNK-EYLDAKDLMLFLEAEQGMTHITE--------EMCLDIIRRYEPSQEGRLK 127
                          90
                  ....*....|....*.
gi 568915847  142 GLISSDGFCRYLMSDE 157
Cdd:cd16222   128 GFLGIDGFTQYLLSSE 143
PTZ00121 PTZ00121
MAEBL; Provisional
717-1064 1.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  717 KRADQMRAMGIETSDIADvpSDTSKNDKKGKANPAKANVTPQSSSELRPTTTA----ALGSGQEAKKGIELipqVRIEDL 792
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkadEAKKAEEKKKADEL---KKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  793 KQMKAYLK-HLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEIKKETEIK 871
Cdd:PTZ00121 1558 KKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-----ELKKAEEEK 1632
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  872 IQTLTTDHKSKVKEIVAQHTKEwseminthSAEEQEIRDLHLSQQCELLRKlliNAHEQQTQQLKLSHDRESKEMRAHQA 951
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEA 1701
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  952 KISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQLLKSCHAV 1031
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
                         330       340       350
                  ....*....|....*....|....*....|...
gi 568915847 1032 SQTQGEGDAADGEIGSRDGPQTSNSSMKLQSAN 1064
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFDNFANIIEGG 1814
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
64-157 4.07e-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: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   64 EKFYELTQKICPRTDIEDLFKKINGDKTDyLTVDQLVSFLNEHQRDPRLNEILfpfydakrAMQIIEMYEPDEELKKKGL 143
Cdd:cd16219    56 EEFVLFYKALTQREDVLKIFQDFSADGQK-LTLLEFVDFLQQEQLERENTEEL--------AMELIDRYEPSDTAKKLHA 126
                          90
                  ....*....|....
gi 568915847  144 ISSDGFCRYLMSDE 157
Cdd:cd16219   127 LSIDGFLMYLCSPE 140
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
905-1026 1.36e-05

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: 46.60  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   905 EQEIRDLHLSQQCELLRKLLINAHEQQTQQLKLSHDRESKEMrahQAKISMENSKAISQ-DKSIKNKAERERRVRELNSS 983
Cdd:pfam08703   25 EKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEM---KKKLERKRLESIQEaKKRTSDKAAQERLKKEINNS 101
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568915847   984 NTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQLLK 1026
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQA 144
EFh_PI-PLCzeta cd16204
EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, ...
52-157 2.21e-05

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: 45.57  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   52 KNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKkINGDKTDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEM 131
Cdd:cd16204    46 KNDSFKAGNITIEDFRAIYRAIAHRCEIHEIFN-TYSENRKILSAPNLVGFLKKEQFQDEADE--------TIASELIAK 116
                          90       100
                  ....*....|....*....|....*.
gi 568915847  132 YEPDEELKKKGLISSDGFCRYLMSDE 157
Cdd:cd16204   117 YEPIEEVRKRKQMSFEGFIRYMTSED 142
PTZ00121 PTZ00121
MAEBL; Provisional
717-1024 2.35e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  717 KRADQMRamgiETSDIADVPSDTSKNDKKGKANPAKanvtpQSSSELRPTTTAALGSGQEAKKGIEL------------- 783
Cdd:PTZ00121 1290 KKADEAK----KAEEKKKADEAKKKAEEAKKADEAK-----KKAEEAKKKADAAKKKAEEAKKAAEAakaeaeaaadeae 1360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  784 -------IPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKK- 855
Cdd:PTZ00121 1361 aaeekaeAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKa 1440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  856 KGGSNCLEIKKETEIKIQTLTTDHKSKVKEIVAQHTKEWSEminTHSAEEQEIRDLHLSQQCELLRKLLiNAHEQQTQQL 935
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE---AKKADEAKKKAEEAKKKADEAKKAA-EAKKKADEAK 1516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  936 KLSHDRESKEMR-AHQAKISMENSKAISQDKSIK-NKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEH 1013
Cdd:PTZ00121 1517 KAEEAKKADEAKkAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
                         330
                  ....*....|.
gi 568915847 1014 LEFLEKQNEQL 1024
Cdd:PTZ00121 1597 VMKLYEEEKKM 1607
EFh_PI-PLCepsilon cd16203
EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1); ...
94-154 3.15e-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: 45.78  E-value: 3.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915847   94 LTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLM 154
Cdd:cd16203   120 LTISQLKDFLENHQMEH---------ITEEEAIKIIQRHEPDPILRSKNCLSFEGFARYLM 171
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
173-322 4.45e-05

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: 46.32  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  173 DHPLAHYFISSSHNTY---LTGRQFGGKSSVE-----MYRQvLLAGCRCVELDCWDgKGEDQEPIITHGKAMCTDILFKD 244
Cdd:cd08557     6 DLPLSQLSIPGTHNSYaytIDGNSPIVSKWSKtqdlsITDQ-LDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQTLED 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  245 VIQAIKetAFVT---SEyPVILSFENHcskyqqYKMSKYCEDLFGDLLLKQALESHPLEPgrPLPSPNDLKRKILIKNKR 321
Cdd:cd08557    84 VLNEVK--DFLDahpSE-VVILDLEHE------YGGDNGEDHDELDALLRDVLGDPLYRP--PVRAGGWPTLGELRAGKR 152

                  .
gi 568915847  322 L 322
Cdd:cd08557   153 V 153
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
61-155 2.17e-04

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: 42.70  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   61 FTYEKFYELTQKICPRTDIEDLFKKINgDKTDYLTVDQLVSFLNEHQrdpRLNEILFPFydakrAMQIIEMYEPDEELKK 140
Cdd:cd16220    54 LTFEEFCVFYKMMSLRRDLYLLLLSYS-DKKDHLTVEELAQFLKVEQ---KMNNVTTEY-----CLDIIKKFEVSEENKE 124
                          90
                  ....*....|....*
gi 568915847  141 KGLISSDGFCRYLMS 155
Cdd:cd16220   125 QNVLGIEGFTNFMRS 139
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
802-1016 2.41e-04

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: 45.11  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   802 LKKQQKELNSLKKKH-AKEHSTMQKLHCTQVDKivaQYDKEKSTHE-------KILEKAMKKKGGSNCLE---IKKETE- 869
Cdd:pfam17380  355 QEERKRELERIRQEEiAMEISRMRELERLQMER---QQKNERVRQEleaarkvKILEEERQRKIQQQKVEmeqIRAEQEe 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   870 ---IKIQTLTtDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLS--------QQCELLRKLLINAHEQQTQQLKLS 938
Cdd:pfam17380  432 arqREVRRLE-EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLElekekrdrKRAEEQRRKILEKELEERKQAMIE 510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   939 HDRE----SKEMRAHQAKISMENSKAISQDKSIKNKA-ERERRVRElnssNTKKFLEERKRL-AMKQSKEM-DQLKKVQL 1011
Cdd:pfam17380  511 EERKrkllEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQE----QMRKATEERSRLeAMEREREMmRQIVESEK 586

                   ....*
gi 568915847  1012 EHLEF 1016
Cdd:pfam17380  587 ARAEY 591
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
68-157 2.67e-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: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   68 ELTQKICPRTDIEDLFKKINGdKTDYLTVDQLVSFLNEHQRDPRLneilfpfydaKRAMQIIEMYEPDEELKKKGLISSD 147
Cdd:cd16218    60 EFCRRLMQRPELEEIFHQYSG-EDCVLSAEELREFLKDQGEDASL----------VHAKELIQTYELNEKAKQHQLMTLD 128
                          90
                  ....*....|
gi 568915847  148 GFCRYLMSDE 157
Cdd:cd16218   129 GFTMYMLSKD 138
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
701-1043 4.18e-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: 44.36  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   701 IVDALSDPKKFLSITEKRADQmramgiETSDIADVPSDTSKNDKKGKANPAKANVTPQSSSELRP----------TTTAA 770
Cdd:pfam09731  158 AVKAHTDSLKEASDTAEISRE------KATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAapetppklpeHLDNV 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   771 LGSGQEAKKGIELIPQV-------RIEDLKQMKAYLKHLKKQQKELNSLKKkhAKEHSTMQKLHcTQVDKIVAQYDKEKS 843
Cdd:pfam09731  232 EEKVEKAQSLAKLVDQYkelvaseRIVFQQELVSIFPDIIPVLKEDNLLSN--DDLNSLIAHAH-REIDQLSKKLAELKK 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   844 THEKILEKAMKKKggsncleiKKETEIKIQTLTTDHKSKVKEIVAQHTKEW-SEMINTHSAEEQEIRdLHLSQQCELLRK 922
Cdd:pfam09731  309 REEKHIERALEKQ--------KEELDKLAEELSARLEEVRAADEAQLRLEFeREREEIRESYEEKLR-TELERQAEAHEE 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   923 LLINAHEQQTQQLKLSHDREskemrahqakismenskaisqdksIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKE 1002
Cdd:pfam09731  380 HLKDVLVEQEIELQREFLQD------------------------IKEKVEEERAGRLLKLNELLANLKGLEKATSSHSEV 435
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 568915847  1003 MDQLKKVQlehleflekqneQLLKSCHAVSQTQGEGDAADG 1043
Cdd:pfam09731  436 EDENRKAQ------------QLWLAVEALRSTLEDGSADSR 464
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
574-648 6.63e-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: 40.71  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  574 SVQVISGQFLSDKKIGT----YVEVDmygLPTDTIRKeFRTRmVMNNGLNPVYNeESFVFRkvILPDLA-VLRIAVYDDN 648
Cdd:cd04036     3 TVRVLRATNITKGDLLStpdcYVELW---LPTASDEK-KRTK-TIKNSINPVWN-ETFEFR--IQSQVKnVLELTVMDED 74
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
790-1035 1.01e-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: 43.17  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   790 EDLKQMKAYLKHLKKqqkELNSLKKKHAKEHSTMQKLH--CTQVDKIVAQYDKEKSTHEKILEKA-------MKKKGGSN 860
Cdd:pfam05483  282 ENLKELIEKKDHLTK---ELEDIKMSLQRSMSTQKALEedLQIATKTICQLTEEKEAQMEELNKAkaahsfvVTEFEATT 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   861 C------------LEiKKETEIKIQTLTTDHKSKVKEivaqhtkEWSEMINTHSAEEQEIRDLHLSQQCELLRKLLIN-- 926
Cdd:pfam05483  359 CsleellrteqqrLE-KNEDQLKIITMELQKKSSELE-------EMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEki 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   927 AHEQQTQQLKLSHDRESKEMRAHQAKISMENSKA-----ISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSK 1001
Cdd:pfam05483  431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTseehyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
                          250       260       270
                   ....*....|....*....|....*....|....
gi 568915847  1002 EMDQLKKVQlEHLEFLEKQNEQLLKSCHAVSQTQ 1035
Cdd:pfam05483  511 MTLELKKHQ-EDIINCKKQEERMLKQIENLEEKE 543
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
775-1024 1.08e-03

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: 42.89  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   775 QEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHcTQVDKIVAQYDKEKSTHEKILEKAMK 854
Cdd:pfam10174  257 QMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQ-TKLETLTNQNSDCKQHIEVLKESLTA 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   855 KKGGSNCLeikkETEIKIQTLTTDHKskvKEIVAQHTKEWSEMINTHSAEEQEIRDLhlsqqcellrKLLINAHEQQTQQ 934
Cdd:pfam10174  336 KEQRAAIL----QTEVDALRLRLEEK---ESFLNKKTKQLQDLTEEKSTLAGEIRDL----------KDMLDVKERKINV 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   935 LklshdreskemrahQAKIsmENSKAISQDKSiKNKAERERRVREL--NSSNT-------KKFLEERKRLAMKQSKEMDQ 1005
Cdd:pfam10174  399 L--------------QKKI--ENLQEQLRDKD-KQLAGLKERVKSLqtDSSNTdtalttlEEALSEKERIIERLKEQRER 461
                          250
                   ....*....|....*....
gi 568915847  1006 LKKVQLEHLEFLEKQNEQL 1024
Cdd:pfam10174  462 EDRERLEELESLKKENKDL 480
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
591-659 1.27e-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: 1.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915847  591 YVEVdmYGLPtDTiRKEFRTRmVMNNGLNPVYNeESFVFrKVILPDLA--VLRIAVYDDN----NKLIGQRILPL 659
Cdd:cd08385    40 YVKV--YLLP-DK-KKKFETK-VHRKTLNPVFN-ETFTF-KVPYSELGnkTLVFSVYDFDrfskHDLIGEVRVPL 107
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
76-155 1.35e-03

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: 40.31  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   76 RTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMS 155
Cdd:cd16207    70 RKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKED---------VDRETWEKIFEKFARRIDDSDSLTMTLEGFTSFLLS 140
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
879-1026 3.93e-03

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: 41.26  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   879 HKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLRKLLINAHEQQT----QQLKLSHDRE-----------S 943
Cdd:pfam17380  280 HQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaEQERMAMERErelerirqeerK 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   944 KEM-RAHQAKISMENSKAISQDKSIKNKAERERRVR-ELNSSNTKKFLE-ERKRLAMKQSKEMDQLKKVQLE----HLEF 1016
Cdd:pfam17380  360 RELeRIRQEEIAMEISRMRELERLQMERQQKNERVRqELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEEarqrEVRR 439
                          170
                   ....*....|
gi 568915847  1017 LEKQNEQLLK 1026
Cdd:pfam17380  440 LEEERAREME 449
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
574-668 4.94e-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: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847  574 SVQVISGQFLSDKKIG----TYVEVDMYGlpTDTIRKEFRTRMVMNNgLNPVYNeESFVFrKVILPDL--AVLRIAVYDD 647
Cdd:cd00276    17 TVVVLKARNLPPSDGKglsdPYVKVSLLQ--GGKKLKKKKTSVKKGT-LNPVFN-EAFSF-DVPAEQLeeVSLVITVVDK 91
                          90       100
                  ....*....|....*....|....*
gi 568915847  648 ----NNKLIGQRILPLDGLQAGYRH 668
Cdd:cd00276    92 dsvgRNEVIGQVVLGPDSGGEELEH 116
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
793-965 6.22e-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: 40.48  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   793 KQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKlhctqvdkivaQYDKEKSTHEKILEKAMKKKGGSN-CLEIKKETEIK 871
Cdd:pfam05483  629 KQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-----------EIEDKKISEEKLLEEVEKAKAIADeAVKLQKEIDKR 697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   872 IQ-------TLTTDHKSKVKEIVAQHTKEwsemINTHSAEEQEIRDLHLSQQCEL--LRKLLINAHEQqtqqlkLSHDRE 942
Cdd:pfam05483  698 CQhkiaemvALMEKHKHQYDKIIEERDSE----LGLYKNKEQEQSSAKAALEIELsnIKAELLSLKKQ------LEIEKE 767
                          170       180
                   ....*....|....*....|...
gi 568915847   943 SKEMRAHQAKismENSKAISQDK 965
Cdd:pfam05483  768 EKEKLKMEAK---ENTAILKDKK 787
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
918-1028 7.47e-03

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: 37.93  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915847   918 ELLRKLLINAHEQQTQQLKLSHDRESKEM-RAHQAKIS-MENSKAISQDKSIKN-KAERERRVRELNSS---NTKKFLEE 991
Cdd:pfam12474    2 QLQKEQQKDRFEQERQQLKKRYEKELEQLeRQQKQQIEkLEQRQTQELRRLPKRiRAEQKKRLKMFRESlkqEKKELKQE 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568915847   992 RKRLAMKQSKEMDQLKKVQLEH------LEFLEKQNEQLLKSC 1028
Cdd:pfam12474   82 VEKLPKFQRKEAKRQRKEELELeqkheeLEFLQAQSEALEREL 124
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH