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Conserved domains on  [gi|1624433999|ref|XP_028857980|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1-like isoform X2 [Denticeps clupeoides]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
316-672 1.89e-177

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: 521.90  E-value: 1.89e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDSpKQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08591        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateeMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08591    154 -------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDS 220
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08591    221 SNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
154-304 8.54e-88

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: 280.23  E-value: 8.54e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSADRKRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFSEV 233
Cdd:cd16208      1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624433999  234 GAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16208     81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
22-149 2.65e-64

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


:

Pssm-ID: 270167  Cd Length: 127  Bit Score: 213.59  E-value: 2.65e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   22 LKKGSKFMKWDDDSTSVTPVTLRVDPQGYFLYWTDQNKETDVLDISTIKDTRNGKYAKLPKDTKLRElLDVGAMVGKMEN 101
Cdd:cd13361      1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKERE-VNVGGSDEDLED 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1624433999  102 RVLTVVFGPDMVNISFLNFVAFQEDLAKEWTGELFSLASNLLAQNMSR 149
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
706-825 2.07e-38

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: 139.60  E-value: 2.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  706 TLSVKIISGQFLSD------RKVGTYVEVDMFGLPVDTKRKaFRTKTSPGNSVNPVWEEEpIVFKkVVLPTLASLRIAVY 779
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAK-FKTKVVKNNGFNPVWNET-FEFD-VTVPELAFLRFVVY 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1624433999  780 EDGG---KFIGHRIIPVSAIRPGYHYVGLRNEKNQSLTLPALFIYIEVK 825
Cdd:cd00275     80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
PLC-beta_C super family cl25592
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
1047-1164 2.36e-31

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


The actual alignment was detected with superfamily member pfam08703:

Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 121.33  E-value: 2.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1047 YYSEKYLKREHVKQLVEKLTAVAEECQNNQMKKLKELCEKEKKDLKKRMDKKRQEKIHEVKTKEKNLTEEEKL--EINRT 1124
Cdd:pfam08703   22 YEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAKKRTSDKAAQERLkkEINNS 101
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1624433999 1125 FVNEVVQYIKRLEDAQNKRQDKLLARHKDIRQQILDEKPK 1164
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQ 141
DUF1154 super family cl05918
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
929-972 3.55e-04

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.


The actual alignment was detected with superfamily member pfam06631:

Pssm-ID: 461969  Cd Length: 45  Bit Score: 39.16  E-value: 3.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1624433999  929 TDLEAQSMEELKQQKVFVREQRRQYKELKELVKRHHKKTTDMIK 972
Cdd:pfam06631    2 IKFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
Activator_LAG-3 super family cl29315
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ...
881-1008 8.54e-04

Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.


The actual alignment was detected with superfamily member pfam11498:

Pssm-ID: 151935 [Multi-domain]  Cd Length: 476  Bit Score: 43.41  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  881 SEPKTDPKPAPTENGMSHAPLIAPKPASLVSHQPQPSVKSEDVIQSVLTDLEAQSMEELKQQKVFVREQRRQYKE--LKE 958
Cdd:pfam11498  290 MEPEGETKKSPMEAGGDRMPQSAPPPAMNPQHIAQLAQQQNKMRLLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEhqQQQ 369
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624433999  959 LVKRHHKKTTDMIKEHT-------ARQNEQHSQHLRHRASMQKSAKRDGKKRSGTEH 1008
Cdd:pfam11498  370 MLLQQQQQMHQLQQHHQmngggqfATQAHQHAAYLQQMQHMRLQEQIQHQQQQAQHH 426
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
316-672 1.89e-177

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: 521.90  E-value: 1.89e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDSpKQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08591        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateeMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08591    154 -------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDS 220
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08591    221 SNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
154-304 8.54e-88

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: 280.23  E-value: 8.54e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSADRKRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFSEV 233
Cdd:cd16208      1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624433999  234 GAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16208     81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
319-467 5.93e-74

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: 241.26  E-value: 5.93e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  319 MTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRttEEEPVITHGFTMTSEISFKEVIEAIAE 398
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGP--DGEPVVYHGYTLTSKIPFRDVLEAIKD 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624433999  399 SAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEkfplEQGVALPSPMDLMGKILIKN 467
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
22-149 2.65e-64

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


Pssm-ID: 270167  Cd Length: 127  Bit Score: 213.59  E-value: 2.65e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   22 LKKGSKFMKWDDDSTSVTPVTLRVDPQGYFLYWTDQNKETDVLDISTIKDTRNGKYAKLPKDTKLRElLDVGAMVGKMEN 101
Cdd:cd13361      1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKERE-VNVGGSDEDLED 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1624433999  102 RVLTVVFGPDMVNISFLNFVAFQEDLAKEWTGELFSLASNLLAQNMSR 149
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
570-684 4.41e-62

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: 206.71  E-value: 4.41e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   570 SNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSSNYMPQVFWNAGCQ 649
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1624433999   650 LVALNFQVIDLSMQLNLGMYEYNGKSGYRLKPEYM 684
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
18-146 1.46e-57

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 194.52  E-value: 1.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   18 VPESLKKGSKFMKWDDDSTSVTP-VTLRVDPQGYFLYWTDQNKETDVLDISTIKDTRNGKYAKLPKDTKLRELLDVGAMV 96
Cdd:pfam17787    2 VPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGSD 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1624433999   97 GKMENRVLTVVFGPDMVNISFLNFVAFQEDLAKEWTGELFSLASNLLAQN 146
Cdd:pfam17787   82 NSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLN02952 PLN02952
phosphoinositide phospholipase C
208-813 4.57e-57

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 208.70  E-value: 4.57e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  208 FTTEIFKAF-----LNSICPRPDIDTIFSEVGAKSRpYLTVEQLTDFINNKQRDprLNEILYPPLKVeqVQTLVEKYEPN 282
Cdd:PLN02952    17 YNYKMFNLFnrkfkITEAEPPDDVKDVFCKFSVGGG-HMGADQLRRFLVLHQDE--LDCTLAEAQRI--VEEVINRRHHV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  283 AMLSQRGqISVEGFTRYLSGEEnsIVPPEKLDQSEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVE 362
Cdd:PLN02952    92 TRYTRHG-LNLDDFFHFLLYDD--LNGPITPQVHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  363 LDCWKGrTTEEEPVITHGFTMTSEISFKEVIEAIAESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLteal 442
Cdd:PLN02952   169 LDLWPG-STKDEILVLHGRTLTTPVPLIKCLKSIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY---- 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  443 ekFPLEQG-VALPSPMDLMGKILIKNK--KKSQKADGSTKKKlteqtsntysdtssMCEPSSPStGSNHQETSDQTNHGP 519
Cdd:PLN02952   243 --YPESDSlVQFPSPESLKHRIIISTKppKEYLESSGPIVIK--------------KKNNVSPS-GRNSSEETEEAQTLE 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  520 GEGGDGKQQGtksngepeaeseedededdecKKSIDEDTAGSETFATEEMSNLVNYI--QP---VKFTSFVAAKETNRsy 594
Cdd:PLN02952   306 SMLFEQEADS---------------------RSDSDQDDNKSGELQKPAYKRLITIHagKPkgtLKDAMKVAVDKVRR-- 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  595 emSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSSNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYNGK 674
Cdd:PLN02952   363 --LSLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGG 440
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  675 SGYRLKPEYMRR---TDKAFDPFTERTvdgiVANTLSVKIISG----------QFLSDRKVGTYVEVDMFGLPVDTKRKa 741
Cdd:PLN02952   441 CGYLKKPDFLMKkgfHDEVFDPKKKLP----VKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK- 515
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624433999  742 fRTKTSPGNSvNPVWEEEpIVFKKVVlPTLASLRIAVYE----DGGKFIGHRIIPVSAIRPGYHYVGLRNEKNQSL 813
Cdd:PLN02952   516 -KTKIIEDNW-YPAWNEE-FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
706-825 2.07e-38

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: 139.60  E-value: 2.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  706 TLSVKIISGQFLSD------RKVGTYVEVDMFGLPVDTKRKaFRTKTSPGNSVNPVWEEEpIVFKkVVLPTLASLRIAVY 779
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAK-FKTKVVKNNGFNPVWNET-FEFD-VTVPELAFLRFVVY 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1624433999  780 EDGG---KFIGHRIIPVSAIRPGYHYVGLRNEKNQSLTLPALFIYIEVK 825
Cdd:cd00275     80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
1047-1164 2.36e-31

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: 121.33  E-value: 2.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1047 YYSEKYLKREHVKQLVEKLTAVAEECQNNQMKKLKELCEKEKKDLKKRMDKKRQEKIHEVKTKEKNLTEEEKL--EINRT 1124
Cdd:pfam08703   22 YEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAKKRTSDKAAQERLkkEINNS 101
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1624433999 1125 FVNEVVQYIKRLEDAQNKRQDKLLARHKDIRQQILDEKPK 1164
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQ 141
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
706-805 5.14e-13

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: 66.36  E-value: 5.14e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   706 TLSVKIISGQFLSDRKVGT----YVEVDMFGLPvdtkRKAFRTKTSPgNSVNPVWEEEpIVFKkVVLPTLASLRIAVYED 781
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVK-NTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73
                            90       100
                    ....*....|....*....|....*...
gi 1624433999   782 GG----KFIGHRIIPVSAIRPGYHYVGL 805
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
705-807 3.70e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.32  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  705 NTLSVKIISGQFLSDRKVG----TYVEVDMfglpvDTKRKAFRTKTSPgNSVNPVWEEEpIVFkKVVLPTLASLRIAVYE 780
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdPYVKVYL-----LDGKQKKKTKVVK-NTLNPVWNET-FTF-SVPDPENAVLEIEVYD 72
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1624433999  781 DGG----KFIGHRIIPVSAIRPGYHYVGLRN 807
Cdd:pfam00168   73 YDRfgrdDFIGEVRIPLSELDSGEGLDGWYP 103
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
223-307 1.30e-05

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: 44.54  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  223 RPDIDTIFSEVgAKSRPYLTVEQLTDFINNKQRdprlnEILYPPlkvEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSG 302
Cdd:pfam09279    8 REEIDEIFQEY-SGDGQKLSLDELVDFLREEQR-----EEDASP---ALALSLIERYEPSETAKKQHAMTKDGFLMYLCS 78

                   ....*
gi 1624433999  303 EENSI 307
Cdd:pfam09279   79 PDGSI 83
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
929-972 3.55e-04

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: 39.16  E-value: 3.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1624433999  929 TDLEAQSMEELKQQKVFVREQRRQYKELKELVKRHHKKTTDMIK 972
Cdd:pfam06631    2 IKFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
914-1165 3.61e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  914 PQPSVKSEDVIQsVLTDLEAQSMEELKQQKV----------FVREQRRQYKELKELVKRhHKKTTDMIKEHT-------- 975
Cdd:TIGR00618  211 PCMPDTYHERKQ-VLEKELKHLREALQQTQQshayltqkreAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEetqerinr 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  976 ARQNEQHSQHLRHRASMQKSAKR-----DGKKRSGTE-----HAHLALEQELKTLDEESSWRLAELKEQQQLQLLTLRQE 1045
Cdd:TIGR00618  289 ARKAAPLAAHIKAVTQIEQQAQRihtelQSKMRSRAKllmkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1046 QYYSEKYLKREHVKQLVEKLTAVAEecQNNQMKKLKELCEKEKKDLKKRMDKKRQEKIHEVKTKEKNLTEEEKLEINRTF 1125
Cdd:TIGR00618  369 EISCQQHTLTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1624433999 1126 VNEVVQYIKRLEDAQNKRQDKLLARHKDIRQ-QILDEKPKE 1165
Cdd:TIGR00618  447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETR 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
927-1177 7.84e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 7.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  927 VLTDLEAQsMEELKQQkvfvREQRRQYKELK-ELVKRHHKKTTDMIKEHTARQNEQHSQHLRHRASMQKSAKRdgkkRSG 1005
Cdd:COG1196    194 ILGELERQ-LEPLERQ----AEKAERYRELKeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE----LAE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1006 TEHAHLALEQELKTLDEESSWRLAELKEqqqlqlLTLRQEQYYSEKYLKREHVKQLVEKLTAVAEECQN-----NQMKKL 1080
Cdd:COG1196    265 LEAELEELRLELEELELELEEAQAEEYE------LLAELARLEQDIARLEERRRELEERLEELEEELAEleeelEELEEE 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1081 KELCEKEKKDLKKRMDKKrQEKIHEVKTKEKNLtEEEKLEINRTFVNEVVQYIKRLEDAQNKRQDKLLARHKDIRQQILD 1160
Cdd:COG1196    339 LEELEEELEEAEEELEEA-EAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
                          250
                   ....*....|....*..
gi 1624433999 1161 EKPKEDCSSEDEAAERA 1177
Cdd:COG1196    417 ERLEEELEELEEALAEL 433
Activator_LAG-3 pfam11498
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ...
881-1008 8.54e-04

Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.


Pssm-ID: 151935 [Multi-domain]  Cd Length: 476  Bit Score: 43.41  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  881 SEPKTDPKPAPTENGMSHAPLIAPKPASLVSHQPQPSVKSEDVIQSVLTDLEAQSMEELKQQKVFVREQRRQYKE--LKE 958
Cdd:pfam11498  290 MEPEGETKKSPMEAGGDRMPQSAPPPAMNPQHIAQLAQQQNKMRLLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEhqQQQ 369
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624433999  959 LVKRHHKKTTDMIKEHT-------ARQNEQHSQHLRHRASMQKSAKRDGKKRSGTEH 1008
Cdd:pfam11498  370 MLLQQQQQMHQLQQHHQmngggqfATQAHQHAAYLQQMQHMRLQEQIQHQQQQAQHH 426
PRK12704 PRK12704
phosphodiesterase; Provisional
1047-1165 2.29e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1047 YYSEKYLKREHVKQLVEKLTAVAEECQN--NQMKKLKELCEKEK-KDLKKRMDKKRQEKIHEVKTKEKNLTE-EEKLEin 1122
Cdd:PRK12704    22 YFVRKKIAEAKIKEAEEEAKRILEEAKKeaEAIKKEALLEAKEEiHKLRNEFEKELRERRNELQKLEKRLLQkEENLD-- 99
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1624433999 1123 rtfvnevvqyiKRLEDAqNKRQDKLLARHKDI--RQQILDEKPKE 1165
Cdd:PRK12704   100 -----------RKLELL-EKREEELEKKEKELeqKQQELEKKEEE 132
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
316-672 1.89e-177

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: 521.90  E-value: 1.89e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDSpKQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08591        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateeMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08591    154 -------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDS 220
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08591    221 SNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
316-672 4.96e-154

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: 461.09  E-value: 4.96e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08623      1 NEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDSPKQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08623     81 IAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08623        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateeMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08623    155 -------------MSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDS 221
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08623    222 SNYMPQLFWNAGCQMVALNFQTVDLSMQINMGMYEYN 258
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
316-672 2.29e-152

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: 456.82  E-value: 2.29e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08625      1 SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDSPKQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08625     81 IAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08625        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateeMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08625    155 -------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDS 221
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08625    222 SNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
316-672 2.31e-147

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: 443.73  E-value: 2.31e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDSPKQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08624        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfaTEEMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08624    155 ----------YEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDS 224
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08624    225 SNYMPQMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
317-672 2.54e-129

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: 394.90  E-value: 2.54e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRttEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08558      2 QDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGP--DGEPVVYHGHTLTSKILFKDVIEAI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEKFPleqgVALPSPMDLMGKILIKNKKksqkadg 476
Cdd:cd08558     80 KEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKK------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08558        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfateemsnlvnyiqpvkftsfvaaketnrsYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSS 636
Cdd:cd08558    148 -------------------------------------YHMSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSS 190
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1624433999  637 NYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08558    191 NYNPQPFWNAGCQMVALNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
318-672 4.67e-121

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: 374.10  E-value: 4.67e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  318 DMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTEEEPVITHGFTMTSEISFKEVIEAIA 397
Cdd:cd08626      3 DMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  398 ESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkadgs 477
Cdd:cd08626     83 DTAFVTSDYPVILSFENHC-SKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR-------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  478 tkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksided 557
Cdd:cd08626        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  558 tagsetfateeMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSSN 637
Cdd:cd08626    154 -----------LSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSN 222
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1624433999  638 YMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08626    223 YMPQIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
317-672 2.32e-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: 337.77  E-value: 2.32e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08593      2 QDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQAI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEkfplEQGVALPSPMDLMGKILIKNKkksqkadg 476
Cdd:cd08593     80 REYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGK-------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stKKKLteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08593    147 --KLKL-------------------------------------------------------------------------- 150
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfaTEEMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSS 636
Cdd:cd08593    151 ---------AKELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSS 221
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1624433999  637 NYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08593    222 NYDPQEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN 257
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
317-672 1.05e-90

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


Pssm-ID: 176539 [Multi-domain]  Cd Length: 260  Bit Score: 292.79  E-value: 1.05e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08597      2 QDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEalekFPLEQGVALPSPMDLMGKILIKNKKksqkadg 476
Cdd:cd08597     80 NEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTE----PPNEGESYLPSPHDLKGKIIIKGKK------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 sTKK-KLteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeCKksid 555
Cdd:cd08597    148 -LKRrKL-------------------------------------------------------------------CK---- 155
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateEMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08597    156 ------------ELSDLVSLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDS 223
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08597    224 SNYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
154-304 8.54e-88

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: 280.23  E-value: 8.54e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSADRKRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFSEV 233
Cdd:cd16208      1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624433999  234 GAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16208     81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
316-669 4.65e-83

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: 270.27  E-value: 4.65e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRttEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08598      1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDGD--DGEPVVTHGYTLTSSVPFRDVCRA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDsPKQQAKMAEYCKSIFGDALLTEALEkfplEQGVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08598     79 IKKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLD----GLEDELPSPEELRGKILIKVKK------ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcEPSSPstgsNHqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08598    148 ----------------------ESKTP----NH----------------------------------------------- 154
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateemsnlvnyiqpvkftsfvaaketnrsyeMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08598    155 ----------------------------------------IFSLSERSLLKLLKDKRAALDKHNRRHLMRVYPSGTRISS 194
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMY 669
Cdd:cd08598    195 SNFNPLPFWRAGVQMVALNWQTYDLGMQLNEAMF 228
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
317-672 2.23e-82

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: 268.53  E-value: 2.23e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08592      2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVDSPkQQAKMAEYCKSIFGDALLTEALEkfPLEQGvaLPSPMDLMGKILIKNKKksqkadg 476
Cdd:cd08592     80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD--RNADQ--LPSPNQLKRKIIIKHKK------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08592        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfateemsnlvnyiqpvkftsfvaaketnRSYEMSSFVETKALEQLTKS-PVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08592    148 -----------------------------------LFYEMSSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDS 192
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08592    193 SNYDPVPMWNCGSQMVALNFQTPDKPMQLNQALFMLN 229
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
317-672 1.78e-80

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: 264.40  E-value: 1.78e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08596      2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDG--DDGMPIIYHGHTLTTKIPFKDVVEAI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVDSPkQQAKMAEYCKSIFGDALLTEALEKFPLEQGVALPSPMDLMGKILIKNKKksqkadg 476
Cdd:cd08596     80 NRSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08596        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfaTEEMSNLVNYIQPVKFTSFVAAKetnrSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSS 636
Cdd:cd08596    152 ---------APELSDLVIYCQAVKFPGLSTPK----CYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSS 218
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1624433999  637 NYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08596    219 NPNPLIFWLHGLQLVALNYQTDDLPMHLNAAMFEAN 254
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
317-672 9.99e-78

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


Pssm-ID: 176537 [Multi-domain]  Cd Length: 257  Bit Score: 256.79  E-value: 9.99e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08595      2 QDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDG--ADNEPVVYHGYTLTSKILFKEVITTV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEKFPLEQgvaLPSPMDLMGKILIKNKKKSQKAdg 476
Cdd:cd08595     80 EKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATGE---LPSPEALKFKILVKNKKKIAKA-- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08595        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfateeMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSS 636
Cdd:cd08595    154 ------------LSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSS 221
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1624433999  637 NYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08595    222 NYNPQEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN 257
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
317-672 1.26e-77

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: 1.26e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08629      2 QDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRAI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEkfplEQGVALPSPMDLMGKILIKNKkksqkadg 476
Cdd:cd08629     80 RDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLD----GVTTSLPSPEQLKGKILLKGK-------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stKKKLteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08629    147 --KLKL-------------------------------------------------------------------------- 150
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfaTEEMSNLVNYIQPVKFTSFVAAKETNRS-YEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08629    151 ---------VPELSDMIIYCKSVHFGGFSSPGTSGQAfYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDS 221
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08629    222 SNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
317-672 6.17e-77

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: 254.49  E-value: 6.17e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTTeeEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08631      2 QDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDGPNG--EPIVYHGHTFTSKILFKDVVAAV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALE-KFPleqgVALPSPMDLMGKILIKNKKksqkad 475
Cdd:cd08631     80 AQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKK------ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08631        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagseTFATEEMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08631    149 -------IRLSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDS 221
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08631    222 SNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
317-672 7.29e-77

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: 254.18  E-value: 7.29e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08630      2 QDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQAV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEKFPLEQgvaLPSPMDLMGKILIKNKkksqkadg 476
Cdd:cd08630     80 RQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPEE---LPSPEELKGRVLVKGK-------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stKKKLteqtsntysdtssmcepsSPstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08630    148 --KLQI------------------SP------------------------------------------------------ 153
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfateEMSNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSS 636
Cdd:cd08630    154 -----------ELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSA 222
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1624433999  637 NYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08630    223 NYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
319-467 5.93e-74

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: 241.26  E-value: 5.93e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  319 MTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRttEEEPVITHGFTMTSEISFKEVIEAIAE 398
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGP--DGEPVVYHGYTLTSKIPFRDVLEAIKD 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624433999  399 SAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEkfplEQGVALPSPMDLMGKILIKN 467
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
318-672 1.73e-72

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: 242.56  E-value: 1.73e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  318 DMTLPLSHYLINSSHNTYLTAGQLA-----GNSSVEMYRQVLLSGCRCVELDCWKGRttEEEPVITHGFTMTsEISFKEV 392
Cdd:cd00137      3 PDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDGK--PEEPIIYHGPTFL-DIFLKEV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  393 IEAIAESAFKTSPFPVILSFENHVDS-PKQQAKMAEYCKSIFGDALLTealekFPLEQGVALPSPMDLMGKILIKNKKks 471
Cdd:cd00137     80 IEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  472 qkadgSTKKKlteqtsntysdtssmcepssPSTGSNHQEtsdqtnhgpgeggdgkqqgtksngepeaeseedededdeck 551
Cdd:cd00137    153 -----NGFSG--------------------PTGSSNDTG----------------------------------------- 166
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  552 ksidedtAGSETFATEEmsnlvnyiqpvkftsfvaaketNRSYEMSSFVETKALE----QLTKSPVEFVEYNKLQLSRIY 627
Cdd:cd00137    167 -------FVSFEFSTQK----------------------NRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNY 217
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624433999  628 PKGTRY---------DSSNYMPQVFWN---AGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd00137    218 PSGTSGgtawyyyamDSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
317-672 2.05e-71

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: 237.78  E-value: 2.05e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRttEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08594      2 QDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDGP--DGEPVVHHGYTLTSKILFRDVIETI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALlteALEKFPLEQGVALPSPMDLMGKILIKNKKksqkadg 476
Cdd:cd08594     80 NKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKL---DLSSVISGDSKQLPSPQSLKGKILIKGKK------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08594        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfateemsnlvnyiqpvkftsfvaaketnrsYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSS 636
Cdd:cd08594    149 -------------------------------------WQVSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSS 191
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1624433999  637 NYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08594    192 NFNPQPYWNAGCQLVALNYQTEGRMLQLNRAKFRAN 227
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
316-672 2.08e-71

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: 238.79  E-value: 2.08e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  316 SEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEA 395
Cdd:cd08633      1 NQDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIET 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAFKTSPFPVILSFENHVDSPkQQAKMAEYCKSIFGDALlteALEKFPLEQGVALPSPMDLMGKILIKNKKKSQKad 475
Cdd:cd08633     79 INKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKKLSRA-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08633        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateeMSNLVNYIQPVKFTSFvaAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08633    153 -------------LSDLVKYTKSVRVHDI--ETEATSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDS 217
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08633    218 SNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
154-304 3.96e-70

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: 230.96  E-value: 3.96e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSADRKRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFSEV 233
Cdd:cd16210      1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624433999  234 GAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16210     81 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
317-672 1.06e-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: 234.18  E-value: 1.06e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08628      2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVDSpKQQAKMAEYCKSIFGDALLTEALEKfPLEQgvaLPSPMDLMGKILIKNKKksqkadg 476
Cdd:cd08628     80 KDHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLEA-SADQ---LPSPTQLKEKIIIKHKK------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08628        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetFATEEMSNLVNYIQPvkfTSFVAAKETNRSY-EMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08628    148 -------LIAIELSDLVVYCKP---TSKTKDNLENPDFkEIRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDS 217
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08628    218 SNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN 254
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
154-304 6.69e-65

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: 216.34  E-value: 6.69e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSAD--RKRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFS 231
Cdd:cd16200      1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624433999  232 EVGAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16200     81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
317-672 7.87e-65

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: 220.29  E-value: 7.87e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08632      2 QDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIETI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDAL-LTEALEKFPLEqgvaLPSPMDLMGKILIKNKKKSQkad 475
Cdd:cd08632     80 NKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKKLCR--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 gstkkklteqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08632        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateEMSNLVNYiqpvkfTSFVAAKET---NRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTR 632
Cdd:cd08632    152 ------------DLSDLVVY------TNSVAAQDIvddGSTGNVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYR 213
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1624433999  633 YDSSNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08632    214 IDSSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
22-149 2.65e-64

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


Pssm-ID: 270167  Cd Length: 127  Bit Score: 213.59  E-value: 2.65e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   22 LKKGSKFMKWDDDSTSVTPVTLRVDPQGYFLYWTDQNKETDVLDISTIKDTRNGKYAKLPKDTKLRElLDVGAMVGKMEN 101
Cdd:cd13361      1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKERE-VNVGGSDEDLED 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1624433999  102 RVLTVVFGPDMVNISFLNFVAFQEDLAKEWTGELFSLASNLLAQNMSR 149
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
154-304 7.07e-63

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: 210.51  E-value: 7.07e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSADRKRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFSEV 233
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624433999  234 GAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
570-684 4.41e-62

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: 206.71  E-value: 4.41e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   570 SNLVNYIQPVKFTSFVAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSSNYMPQVFWNAGCQ 649
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1624433999   650 LVALNFQVIDLSMQLNLGMYEYNGKSGYRLKPEYM 684
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
154-304 3.55e-61

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: 205.61  E-value: 3.55e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSA---DRKRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIF 230
Cdd:cd16213      1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1624433999  231 SEVGAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16213     81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYLMSED 154
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
317-672 3.88e-61

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: 208.73  E-value: 3.88e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  317 EDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGrtTEEEPVITHGFTMTSEISFKEVIEAI 396
Cdd:cd08627      2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  397 AESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEKfpleQGVALPSPMDLMGKILIKNKKksqkadg 476
Cdd:cd08627     80 KEHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVDI----NADGLPSPNQLKRKILIKHKK------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  477 stkkklteqtsnTYSDtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkside 556
Cdd:cd08627    148 ------------LYRD---------------------------------------------------------------- 151
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  557 dtagsetfateemsnlvnyiqpvkftsfvaaketnrsyeMSSFVETKALEQLTKSP-VEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08627    152 ---------------------------------------MSSFPETKAEKYVNRSKgKKFLQYNRRQLSRIYPKGQRLDS 192
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08627    193 SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
319-468 1.07e-59

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: 200.97  E-value: 1.07e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   319 MTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTteEEPVITHGFTMTSEISFKEVIEAIAE 398
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDGPD--GEPVIYHGHTFTLPIKLSEVLEAIKD 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   399 SAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEALEKFPLEqgvaLPSPMDLMGKILIKNK 468
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
18-146 1.46e-57

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 194.52  E-value: 1.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   18 VPESLKKGSKFMKWDDDSTSVTP-VTLRVDPQGYFLYWTDQNKETDVLDISTIKDTRNGKYAKLPKDTKLRELLDVGAMV 96
Cdd:pfam17787    2 VPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGSD 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1624433999   97 GKMENRVLTVVFGPDMVNISFLNFVAFQEDLAKEWTGELFSLASNLLAQN 146
Cdd:pfam17787   82 NSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLN02952 PLN02952
phosphoinositide phospholipase C
208-813 4.57e-57

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 208.70  E-value: 4.57e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  208 FTTEIFKAF-----LNSICPRPDIDTIFSEVGAKSRpYLTVEQLTDFINNKQRDprLNEILYPPLKVeqVQTLVEKYEPN 282
Cdd:PLN02952    17 YNYKMFNLFnrkfkITEAEPPDDVKDVFCKFSVGGG-HMGADQLRRFLVLHQDE--LDCTLAEAQRI--VEEVINRRHHV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  283 AMLSQRGqISVEGFTRYLSGEEnsIVPPEKLDQSEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVE 362
Cdd:PLN02952    92 TRYTRHG-LNLDDFFHFLLYDD--LNGPITPQVHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  363 LDCWKGrTTEEEPVITHGFTMTSEISFKEVIEAIAESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLteal 442
Cdd:PLN02952   169 LDLWPG-STKDEILVLHGRTLTTPVPLIKCLKSIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY---- 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  443 ekFPLEQG-VALPSPMDLMGKILIKNK--KKSQKADGSTKKKlteqtsntysdtssMCEPSSPStGSNHQETSDQTNHGP 519
Cdd:PLN02952   243 --YPESDSlVQFPSPESLKHRIIISTKppKEYLESSGPIVIK--------------KKNNVSPS-GRNSSEETEEAQTLE 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  520 GEGGDGKQQGtksngepeaeseedededdecKKSIDEDTAGSETFATEEMSNLVNYI--QP---VKFTSFVAAKETNRsy 594
Cdd:PLN02952   306 SMLFEQEADS---------------------RSDSDQDDNKSGELQKPAYKRLITIHagKPkgtLKDAMKVAVDKVRR-- 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  595 emSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSSNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYNGK 674
Cdd:PLN02952   363 --LSLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGG 440
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  675 SGYRLKPEYMRR---TDKAFDPFTERTvdgiVANTLSVKIISG----------QFLSDRKVGTYVEVDMFGLPVDTKRKa 741
Cdd:PLN02952   441 CGYLKKPDFLMKkgfHDEVFDPKKKLP----VKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK- 515
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624433999  742 fRTKTSPGNSvNPVWEEEpIVFKKVVlPTLASLRIAVYE----DGGKFIGHRIIPVSAIRPGYHYVGLRNEKNQSL 813
Cdd:PLN02952   516 -KTKIIEDNW-YPAWNEE-FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
569-683 6.50e-57

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 191.91  E-value: 6.50e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  569 MSNLVNYIQPVKFTSFvAAKETNRSYEMSSFVETKALEQLTKSPVEFVEYNKLQLSRIYPKGTRYDSSNYMPQVFWNAGC 648
Cdd:pfam00387    1 LSDLVVYTQSVKFKSF-STPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1624433999  649 QLVALNFQVIDLSMQLNLGMYEYNGKSGYRLKPEY 683
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PLN02222 PLN02222
phosphoinositide phospholipase C 2
219-823 1.40e-56

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 206.80  E-value: 1.40e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  219 SICPrPDIDTIFSEVGAKSrpYLTVEQLTDFINNKQRDPRLNEilypplkvEQVQTLVEKyepNAMLSQRGQISVEGFTR 298
Cdd:PLN02222    21 SEAP-REIKTIFEKYSENG--VMTVDHLHRFLIDVQKQDKATR--------EDAQSIINS---ASSLLHRNGLHLDAFFK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  299 YLSGEENSIVPPEKLDQseDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKgRTTEEEPVIT 378
Cdd:PLN02222    87 YLFGDNNPPLALHEVHH--DMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWP-NSDKDDIDVL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  379 HGFTMTSEISFKEVIEAIAESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLT----EALEKFpleqgvalP 454
Cdd:PLN02222   164 HGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTppvgESLKEF--------P 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  455 SPMDLMGKILIKNKKKSQKADGsTKKKLTEQTSNtYSDTSSMCEPSSPSTGSNHQETSDQTNHGPGEGGDGKQQGTKSNG 534
Cdd:PLN02222   235 SPNSLKKRIIISTKPPKEYKEG-KDDEVVQKGKD-LGDEEVWGREVPSFIQRNKSVDKNDSNGDDDDDDDDGEDKSKKNA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  535 EPEAeseedededdecKKSIDEDTAGSETFATEEMSnlvnyIQPVKFtsfvaaketnRSYEMSSFVETKALEQLTKSPVE 614
Cdd:PLN02222   313 PPQY------------KHLIAIHAGKPKGGITECLK-----VDPDKV----------RRLSLSEEQLEKAAEKYAKQIVR 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  615 FVEYNklqLSRIYPKGTRYDSSNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYNGKSGYRLKPEYMRRTD---KAF 691
Cdd:PLN02222   366 FTQHN---LLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGsdsDIF 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  692 DPftERTVDgiVANTLSVKIISGQ----------FLSDRKVGTYVEVDMFGLPVDTKRKafRTKTSPGNSVnPVWEEepi 761
Cdd:PLN02222   443 DP--KATLP--VKTTLRVTIYMGEgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK--KTKTLEDNWI-PAWDE--- 512
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624433999  762 VFK-KVVLPTLASLRIAVYE----DGGKFIGHRIIPVSAIRPGYHYVGLRNEKNQSLTLPALFIYIE 823
Cdd:PLN02222   513 VFEfPLTVPELALLRLEVHEydmsEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PLN02228 PLN02228
Phosphoinositide phospholipase C
269-807 3.02e-56

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 205.66  E-value: 3.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  269 VEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEENSIVPPEKlDQSEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVE 348
Cdd:PLN02228    59 LDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVE 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  349 MYRQVLLSGCRCVELDCWKGRTTEEEPViTHGFTMTSEISFKEVIEAIAESAFKTSPFPVILSFENHVdSPKQQAKMAEY 428
Cdd:PLN02228   138 PIVQALRKGVKVIELDLWPNPSGNAAEV-RHGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKM 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  429 CKSIFGDALL---TEALEKFpleqgvalPSPMDLMGKILIKNKkksqkadgSTKKKLTEQTSNTysDTSSMCEPSSPSTG 505
Cdd:PLN02228   216 LTKTFRGMLFrctSESTKHF--------PSPEELKNKILISTK--------PPKEYLESKTVQT--TRTPTVKETSWKRV 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  506 SNHQEtsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckkSIDEDTAGSETFATeEMSNLV-----NYIQPVK 580
Cdd:PLN02228   278 ADAEN------------------------------------------KILEEYKDEESEAV-GYRDLIaihaaNCKDPLK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  581 ftsFVAAKETNRSYEMSsfVETKALEQLTKSP-VEFVEYNKLQLSRIYPKGTRYDSSNYMPQVFWNAGCQLVALNFQVID 659
Cdd:PLN02228   315 ---DCLSDDPEKPIRVS--MDEQWLETMVRTRgTDLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  660 LSMQLNLGMYEYNGKSGYRLKPEYMRRTDKAFDPFTERTVDgivaNTLSVKIISGQ----------FLSDRKVGTYVEVD 729
Cdd:PLN02228   390 KQLWIMQGMFRANGGCGYVKKPRILLDEHTLFDPCKRLPIK----TTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIG 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  730 MFGLPVDTkrKAFRTKTSPgNSVNPVWEEEPIVFKKVVlPTLASLRIAV--YEDGGK--FIGHRIIPVSAIRPGYHYVGL 805
Cdd:PLN02228   466 IAGVPRDT--VSYRTETAV-DQWFPIWGNDEFLFQLRV-PELALLWFKVqdYDNDTQndFAGQTCLPLPELKSGVRAVRL 541

                   ..
gi 1624433999  806 RN 807
Cdd:PLN02228   542 HD 543
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
318-672 1.66e-50

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: 178.33  E-value: 1.66e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  318 DMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTteEEPVITHGFTMTSEISFKEVIEAIA 397
Cdd:cd08599      3 DMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGR--GDICVLHGGTLTKPVKFEDCIKAIK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  398 ESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTEAlekfPLEQGVALPSPMDLMGKILIKNKKK--SQKAD 475
Cdd:cd08599     81 ENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILISDKPPviRNSLS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  476 GSTKKKLTEqtsntysdtssmcepsspstgsnhqetsdqtnhgpgeggdgkqqgtksngepeaeseedededdeckksid 555
Cdd:cd08599    156 ETQLKKVIE----------------------------------------------------------------------- 164
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  556 edtagsetfateemsnlvnyiqpvkftsfvaaketnrsyemssfvetkaleqlTKSPVEFVEYNKLQLSRIYPKGTRYDS 635
Cdd:cd08599    165 -----------------------------------------------------GEHPTDLIEFTQKNLLRVYPAGLRITS 191
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1624433999  636 SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYN 672
Cdd:cd08599    192 SNYDPMLAWMHGAQMVALNMQGYDRPLWLNRGKFRAN 228
PLN02230 PLN02230
phosphoinositide phospholipase C 4
288-823 1.21e-48

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 183.75  E-value: 1.21e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  288 RGQISVEGFTRYLSGEEnsIVPPEKLDQSEDMTLPLSHYLINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWK 367
Cdd:PLN02230    88 RRNLTLDDFNYYLFSTD--LNPPIADQVHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWP 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  368 GRTteEEPVITHGFTMTSEISFKEVIEAIAESAFKTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALL---TEALEK 444
Cdd:PLN02230   166 RGT--DDVCVKHGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYyhdSEGCQE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  445 FpleqgvalPSPMDLMGKILIKNK--KKSQKADGSTKKKLTEQTSNTYSDTSSMCEPSSPSTGSNHQETSDQTNHgpgEG 522
Cdd:PLN02230   243 F--------PSPEELKEKILISTKppKEYLEANDAKEKDNGEKGKDSDEDVWGKEPEDLISTQSDLDKVTSSVND---LN 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  523 GDGKQQGtksngepeaeseedededdeckkSIDEDTAGSETFATEEMSNLVNYIQPVKFTSFVAAKETN--RSYEMSSFV 600
Cdd:PLN02230   312 QDDEERG-----------------------SCESDTSCQLQAPEYKRLIAIHAGKPKGGLRMALKVDPNkiRRLSLSEQL 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  601 ETKALEQLTKSPVEFVEYNKLqlsRIYPKGTRYDSSNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYNGKSGYRLK 680
Cdd:PLN02230   369 LEKAVASYGADVIRFTQKNFL---RIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYVKK 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  681 PEYMRRTDKAFDPFTERTvDGIVANTLSVKIISG----------QFLSDRKVGTYVEVDMFGLPVDTKRKAFRTKTspgN 750
Cdd:PLN02230   446 PDFLMDAGPNGQDFYPKD-NSCPKKTLKVKVCMGdgwlldfkktHFDSYSPPDFFVRVGIAGAPVDEVMEKTKIEY---D 521
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624433999  751 SVNPVWEEEPIVfkKVVLPTLASLRIAVYE----DGGKFIGHRIIPVSAIRPGYHYVGLRNEKNQSLTLPALFIYIE 823
Cdd:PLN02230   522 TWTPIWNKEFIF--PLAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFNRKGVKYSSTRLLMRFE 596
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
154-304 2.45e-43

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: 154.89  E-value: 2.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  154 EKIYTRLKLQLNPDGCIPVKNIFRMFSADR--KRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFS 231
Cdd:cd16211      1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624433999  232 EVGAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16211     81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
706-825 2.07e-38

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: 139.60  E-value: 2.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  706 TLSVKIISGQFLSD------RKVGTYVEVDMFGLPVDTKRKaFRTKTSPGNSVNPVWEEEpIVFKkVVLPTLASLRIAVY 779
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAK-FKTKVVKNNGFNPVWNET-FEFD-VTVPELAFLRFVVY 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1624433999  780 EDGG---KFIGHRIIPVSAIRPGYHYVGLRNEKNQSLTLPALFIYIEVK 825
Cdd:cd00275     80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
155-304 9.83e-35

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: 129.98  E-value: 9.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  155 KIYTRLKLQLNPDGCIPVKNIFRMFSADR--KRVETALENCNLSSGRNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFSE 232
Cdd:cd16212      2 KHWMRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTS 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624433999  233 VGAKSRPYLTVEQLTDFINNKQRDPRLNEILYPPLKVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16212     82 ITKGKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
1047-1164 2.36e-31

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: 121.33  E-value: 2.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1047 YYSEKYLKREHVKQLVEKLTAVAEECQNNQMKKLKELCEKEKKDLKKRMDKKRQEKIHEVKTKEKNLTEEEKL--EINRT 1124
Cdd:pfam08703   22 YEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAKKRTSDKAAQERLkkEINNS 101
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1624433999 1125 FVNEVVQYIKRLEDAQNKRQDKLLARHKDIRQQILDEKPK 1164
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQ 141
PLN02223 PLN02223
phosphoinositide phospholipase C
318-812 2.98e-23

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 105.49  E-value: 2.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  318 DMTLPLSHYLINSSHNTYLTAGQLAGNS-SVEMYRQVLLSGCRCVELDCWK-GRtteEEPVITHGFTMTSEISFKEVIEA 395
Cdd:PLN02223   107 DMHAPLSHYFIHTSLKSYFTGNNVFGKLySIEPIIDALEQGVRVVELDLLPdGK---DGICVRPKWNFEKPLELQECLDA 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  396 IAESAF-KTSPFPVILSFENHVdSPKQQAKMAEYCKSIFGDALLTE----ALEKFpleqgvalPSPMDLMGKILIKNKkk 470
Cdd:PLN02223   184 IKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYHEdpqhSLEEF--------PSPAELQNKILISRR-- 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  471 sqkadgSTKKKLTEQTSNTYSDTSSMCEPSSPSTGSNHQetsdqtnhgpgeggdgkqqgtksngepeaeseedededdec 550
Cdd:PLN02223   253 ------PPKELLYAKADDGGVGVRNELEIQEGPADKNYQ----------------------------------------- 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  551 kksidedtagsetfateemsNLVNY--IQPVKFTSFVAAKETNRsYEMSSFVETkaleqltkspvEFVEYNKLQLSRIYP 628
Cdd:PLN02223   286 --------------------SLVGFhaVEPRGMLQKALTGKADD-IQQPGWYER-----------DIISFTQKKFLRTRP 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  629 KGTRYDS-SNYMPQVFWNAGCQLVALNFQVIDLSMQLNLGMYEYNGKSGYRLKPEYMRRTDKA--FDPfterTVDGIVAN 705
Cdd:PLN02223   334 KKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNAGPSgvFYP----TENPVVVK 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  706 TLSVKIISGQ-FLSD--RKVGT------YVEVDMFGLPVDTKrkaFRTKTSPGNSVNPVWEEE---PIVFkkvvlPTLAS 773
Cdd:PLN02223   410 ILKVKIYMGDgWIVDfkKRIGRlskpdlYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEEftfPLTY-----PDLAL 481
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1624433999  774 LRIAVYE----DGGKFIGHRIIPVSAIRPGYHYVGLRNEKNQS 812
Cdd:PLN02223   482 ISFEVYDyevsTADAFCGQTCLPVSELIEGIRAVPLYDERGKA 524
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
329-438 2.83e-22

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: 95.20  E-value: 2.83e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  329 NSSHNTYLTAGQLagnSSVEMYRQVLLSGCRCVELDCWKgrTTEEEPVITHGFTMT------SEISFKEVIEAIAESAFk 402
Cdd:cd08555      1 VLSHRGYSQNGQE---NTLEAFYRALDAGARGLELDVRL--TKDGELVVYHGPTLDrttagiLPPTLEEVLELIADYLK- 74
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1624433999  403 TSPFPVILSFENHVDS---PKQQAKMAEYCKSIFGDALL 438
Cdd:cd08555     75 NPDYTIILSLEIKQDSpeyDEFLAKVLKELRVYFDYDLR 113
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
706-805 5.14e-13

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: 66.36  E-value: 5.14e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   706 TLSVKIISGQFLSDRKVGT----YVEVDMFGLPvdtkRKAFRTKTSPgNSVNPVWEEEpIVFKkVVLPTLASLRIAVYED 781
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVK-NTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73
                            90       100
                    ....*....|....*....|....*...
gi 1624433999   782 GG----KFIGHRIIPVSAIRPGYHYVGL 805
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRHEKL 101
PH_PLC_ELMO1 cd01248
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ...
22-138 1.74e-11

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


Pssm-ID: 269952  Cd Length: 108  Bit Score: 61.95  E-value: 1.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999   22 LKKGSKFMKWDDdSTSVTPVTLRVDPQGYFLYWTDQNK--ETDVLDISTIKDTRNGKYAKLPKDTKLRELLDvgamvgkm 99
Cdd:cd01248      1 LQQGTLLLKYRE-GSKPKERTFYLDPDGTRITWESSKKksEKKSIDISDIKEIRPGKDTDGFKRKKKSNKPK-------- 71
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1624433999  100 ENRVLTVVFGPdmvNISFLNFVAFQEDLAKEWTGELFSL 138
Cdd:cd01248     72 EERCFSIIYGS---NNKTLDLVAPSEDEANLWVEGLRAL 107
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
213-304 1.10e-10

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: 60.76  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  213 FKAFLNSICPRPDIDTIFSEVGAKSRPYLTVEQLTDFINNKQrdprlneilYPPLKVEQVQTLVEKYEPNAmlsQRGQIS 292
Cdd:cd15898     58 FEELYKSLTERPELEPIFKKYAGTNRDYMTLEEFIRFLREEQ---------GENVSEEECEELIEKYEPER---ENRQLS 125
                           90
                   ....*....|..
gi 1624433999  293 VEGFTRYLSGEE 304
Cdd:cd15898    126 FEGFTNFLLSPE 137
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
179-300 5.68e-10

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: 58.78  E-value: 5.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  179 FSADRKRVETALENCNLSsgRNDAIPQDDFTTeifkaFLNSICPRPDIDTIFSEVGAKSRpYLTVEQLTDFINNKQRDPR 258
Cdd:cd16202     31 VKVDKDYAKKLFQEADTS--GEDVLDEEEFVQ-----FYNRLTKRPEIEELFKKYSGDDE-ALTVEELRRFLQEEQKVKD 102
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1624433999  259 LNeilypplkVEQVQTLVEKYEPNAMLSQRGQISVEGFTRYL 300
Cdd:cd16202    103 VT--------LEWAEQLIETYEPSEDLKAQGLMSLDGFTLFL 136
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
202-304 7.84e-09

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: 55.68  E-value: 7.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  202 AIPQDDFTtEIFKaflnSICPRPDIDTIFSEVgAKSRPYLTVEQLTDFINNKQRDPRLNEilypplkvEQVQTLVEKYEP 281
Cdd:cd16206     55 RVSSDEFV-ELFK----ELATRPEIYFLLVRY-ASNKDYLTVDDLMLFLEAEQGMTGVTK--------EKCLEIINKYEP 120
                           90       100
                   ....*....|....*....|...
gi 1624433999  282 NAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16206    121 SEEGREKGQLGIDGFTRYLLSEE 143
C2 pfam00168
C2 domain;
705-807 3.70e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.32  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  705 NTLSVKIISGQFLSDRKVG----TYVEVDMfglpvDTKRKAFRTKTSPgNSVNPVWEEEpIVFkKVVLPTLASLRIAVYE 780
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdPYVKVYL-----LDGKQKKKTKVVK-NTLNPVWNET-FTF-SVPDPENAVLEIEVYD 72
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1624433999  781 DGG----KFIGHRIIPVSAIRPGYHYVGLRN 807
Cdd:pfam00168   73 YDRfgrdDFIGEVRIPLSELDSGEGLDGWYP 103
EFh_PI-PLCzeta cd16204
EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, ...
199-304 4.94e-07

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: 50.19  E-value: 4.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  199 RNDAIPQDDFTTEIFKAFLNSICPRPDIDTIFSeVGAKSRPYLTVEQLTDFINNKQRDPRLNEILypplkveqVQTLVEK 278
Cdd:cd16204     46 KNDSFKAGNITIEDFRAIYRAIAHRCEIHEIFN-TYSENRKILSAPNLVGFLKKEQFQDEADETI--------ASELIAK 116
                           90       100
                   ....*....|....*....|....*.
gi 1624433999  279 YEPNAMLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16204    117 YEPIEEVRKRKQMSFEGFIRYMTSED 142
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
213-301 1.27e-06

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: 49.17  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  213 FKAFLNSICPRPDIDTIFSEVGAKSRPYLTVEQLTDFINNKQRDprlneilypPLKVEQVQTLVEKYEPNAMLSQRGQIS 292
Cdd:cd16207     60 FQEFVKLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKE---------DVDRETWEKIFEKFARRIDDSDSLTMT 130

                   ....*....
gi 1624433999  293 VEGFTRYLS 301
Cdd:cd16207    131 LEGFTSFLL 139
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
211-304 3.00e-06

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: 47.81  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  211 EIfKAFLNSICPRPDIDTIFSEVgAKSRPYLTVEQLTDFINNKQRDPrlneilyppLKVEQVQTLVEKYEPNAMLSQRGQ 290
Cdd:cd16217     57 EI-EEFYKLLTKREEIDVIFGEY-AKSDGTMSRNNLLNFLQEEQREE---------VAPAYALSLIEKYEPDETAKAQRQ 125
                           90
                   ....*....|....
gi 1624433999  291 ISVEGFTRYLSGEE 304
Cdd:cd16217    126 MTKDGFLMYLLSPE 139
EFh_PI-PLCepsilon cd16203
EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1); ...
215-301 3.85e-06

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: 48.48  E-value: 3.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  215 AFLNSICPrpDIDTifsevgakSRPY-LTVEQLTDFINNKQRDPrlneilyppLKVEQVQTLVEKYEPNAMLSQRGQISV 293
Cdd:cd16203    103 ASIVTNGA--GVDS--------SRSSvLTISQLKDFLENHQMEH---------ITEEEAIKIIQRHEPDPILRSKNCLSF 163

                   ....*...
gi 1624433999  294 EGFTRYLS 301
Cdd:cd16203    164 EGFARYLM 171
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
223-307 1.30e-05

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: 44.54  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  223 RPDIDTIFSEVgAKSRPYLTVEQLTDFINNKQRdprlnEILYPPlkvEQVQTLVEKYEPNAMLSQRGQISVEGFTRYLSG 302
Cdd:pfam09279    8 REEIDEIFQEY-SGDGQKLSLDELVDFLREEQR-----EEDASP---ALALSLIERYEPSETAKKQHAMTKDGFLMYLCS 78

                   ....*
gi 1624433999  303 EENSI 307
Cdd:pfam09279   79 PDGSI 83
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
211-300 4.52e-05

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: 44.68  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  211 EIFKAFLNSICPRPDIDTIFSEVGAKsRPYLTVEQLTDFINNKQRdprLNEIlypplKVEQVQTLVEKYEPNAMLSQRGQ 290
Cdd:cd16205     57 EEFCAFYKMMSTRRELYLLLLSYSNK-KDYLTLEDLARFLEVEQK---MTNV-----TLEYCLDIIEKFEPSEENKKNGL 127
                           90
                   ....*....|
gi 1624433999  291 ISVEGFTRYL 300
Cdd:cd16205    128 LGIDGFTNYM 137
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
707-801 9.13e-05

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: 42.82  E-value: 9.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  707 LSVKIISGQFLSDRKVG----TYVEVDMFGlpvdtkRKAFRTKTSPgNSVNPVWEEEpIVFkKVVLPTLASLRIAVYEDG 782
Cdd:cd00030      1 LRVTVIEARNLPAKDLNgksdPYVKVSLGG------KQKFKTKVVK-NTLNPVWNET-FEF-PVLDPESDTLTVEVWDKD 71
                           90       100
                   ....*....|....*....|...
gi 1624433999  783 G----KFIGHRIIPVSAIRPGYH 801
Cdd:cd00030     72 RfskdDFLGEVEIPLSELLDSGK 94
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
929-972 3.55e-04

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: 39.16  E-value: 3.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1624433999  929 TDLEAQSMEELKQQKVFVREQRRQYKELKELVKRHHKKTTDMIK 972
Cdd:pfam06631    2 IKFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
914-1165 3.61e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  914 PQPSVKSEDVIQsVLTDLEAQSMEELKQQKV----------FVREQRRQYKELKELVKRhHKKTTDMIKEHT-------- 975
Cdd:TIGR00618  211 PCMPDTYHERKQ-VLEKELKHLREALQQTQQshayltqkreAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEetqerinr 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  976 ARQNEQHSQHLRHRASMQKSAKR-----DGKKRSGTE-----HAHLALEQELKTLDEESSWRLAELKEQQQLQLLTLRQE 1045
Cdd:TIGR00618  289 ARKAAPLAAHIKAVTQIEQQAQRihtelQSKMRSRAKllmkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1046 QYYSEKYLKREHVKQLVEKLTAVAEecQNNQMKKLKELCEKEKKDLKKRMDKKRQEKIHEVKTKEKNLTEEEKLEINRTF 1125
Cdd:TIGR00618  369 EISCQQHTLTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1624433999 1126 VNEVVQYIKRLEDAQNKRQDKLLARHKDIRQ-QILDEKPKE 1165
Cdd:TIGR00618  447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETR 487
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
211-304 4.36e-04

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: 41.75  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  211 EIFKAFLNSICPRPDIDTIFSEVGAKSRPyLTVEQLTDFINNKQRDPRLNEilypplkvEQVQTLVEKYEPNAMLSQRGQ 290
Cdd:cd16219     56 EEFVLFYKALTQREDVLKIFQDFSADGQK-LTLLEFVDFLQQEQLERENTE--------ELAMELIDRYEPSDTAKKLHA 126
                           90
                   ....*....|....
gi 1624433999  291 ISVEGFTRYLSGEE 304
Cdd:cd16219    127 LSIDGFLMYLCSPE 140
EFh_PRIP1 cd16222
EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1); ...
209-304 4.50e-04

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: 41.77  E-value: 4.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  209 TTEIFKAFLNSICPRPDIDTIFSEVgAKSRPYLTVEQLTDFINNKQRDPRLNEilypplkvEQVQTLVEKYEPNAMLSQR 288
Cdd:cd16222     57 TEEEFCEAYSELCTRPEVYFLLVQI-SKNKEYLDAKDLMLFLEAEQGMTHITE--------EMCLDIIRRYEPSQEGRLK 127
                           90
                   ....*....|....*.
gi 1624433999  289 GQISVEGFTRYLSGEE 304
Cdd:cd16222    128 GFLGIDGFTQYLLSSE 143
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
932-1162 4.91e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.87  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  932 EAQSMEELKQQKVFVRE-QRRQYKELKELVKRHHKKttdMIKEHTARQNEQHSQHLRHRaSMQKSAKRDGKKRSGTEHah 1010
Cdd:pfam15558   19 EEQRMRELQQQAALAWEeLRRRDQKRQETLERERRL---LLQQSQEQWQAEKEQRKARL-GREERRRADRREKQVIEK-- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1011 laleqelktldeESSWRLAELKEQQQLQLLTLRQEqyYSEKYLKREHVKQLVEK---LTAVAEECQNNQMKKLKELCEK- 1086
Cdd:pfam15558   93 ------------ESRWREQAEDQENQRQEKLERAR--QEAEQRKQCQEQRLKEKeeeLQALREQNSLQLQERLEEACHKr 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1087 ---EKKDLKKRMDKKRQEKI-HEVKTKEKNLTEEEKLEINRTFVNevvqyiKRLEDAQNKRQDKLLARHKDIRQQILDEK 1162
Cdd:pfam15558  159 qlkEREEQKKVQENNLSELLnHQARKVLVDCQAKAEELLRRLSLE------QSLQRSQENYEQLVEERHRELREKAQKEE 232
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
862-1166 5.44e-04

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


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.98  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  862 EEGREEVDNKEVEAGGDAPSEPKTDPKPAPTENGMSHAPLIAPKPASlvshqpqPSVKSEDVIQSVLTDLEAQSMEELKQ 941
Cdd:pfam09731  174 EISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPET-------PPKLPEHLDNVEEKVEKAQSLAKLVD 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  942 Q-KVFVREQRRQYKElkELVKRHhKKTTDMIKEHTARQNEQHSQHLRH--RASMQKSAKRDGKKRSGTEHAHLALEQelk 1018
Cdd:pfam09731  247 QyKELVASERIVFQQ--ELVSIF-PDIIPVLKEDNLLSNDDLNSLIAHahREIDQLSKKLAELKKREEKHIERALEK--- 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1019 tldeesswrlaelkeqqqlqlltlrqeqyysekylKREHVKQLVEKLTAVAEECQNNQMKKLKELCEKEKKDLKKRMDKK 1098
Cdd:pfam09731  321 -----------------------------------QKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK 365
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1624433999 1099 ------RQEKIHEVKTkeKNLTEEEKLEINRTFVNEVVQYIKRLEDAQNKRQDKLLARHKDIRQQILDEKPKED 1166
Cdd:pfam09731  366 lrteleRQAEAHEEHL--KDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKATSSHSEVED 437
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
927-1177 7.84e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 7.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  927 VLTDLEAQsMEELKQQkvfvREQRRQYKELK-ELVKRHHKKTTDMIKEHTARQNEQHSQHLRHRASMQKSAKRdgkkRSG 1005
Cdd:COG1196    194 ILGELERQ-LEPLERQ----AEKAERYRELKeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE----LAE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1006 TEHAHLALEQELKTLDEESSWRLAELKEqqqlqlLTLRQEQYYSEKYLKREHVKQLVEKLTAVAEECQN-----NQMKKL 1080
Cdd:COG1196    265 LEAELEELRLELEELELELEEAQAEEYE------LLAELARLEQDIARLEERRRELEERLEELEEELAEleeelEELEEE 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1081 KELCEKEKKDLKKRMDKKrQEKIHEVKTKEKNLtEEEKLEINRTFVNEVVQYIKRLEDAQNKRQDKLLARHKDIRQQILD 1160
Cdd:COG1196    339 LEELEEELEEAEEELEEA-EAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
                          250
                   ....*....|....*..
gi 1624433999 1161 EKPKEDCSSEDEAAERA 1177
Cdd:COG1196    417 ERLEEELEELEEALAEL 433
Activator_LAG-3 pfam11498
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ...
881-1008 8.54e-04

Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.


Pssm-ID: 151935 [Multi-domain]  Cd Length: 476  Bit Score: 43.41  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  881 SEPKTDPKPAPTENGMSHAPLIAPKPASLVSHQPQPSVKSEDVIQSVLTDLEAQSMEELKQQKVFVREQRRQYKE--LKE 958
Cdd:pfam11498  290 MEPEGETKKSPMEAGGDRMPQSAPPPAMNPQHIAQLAQQQNKMRLLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEhqQQQ 369
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624433999  959 LVKRHHKKTTDMIKEHT-------ARQNEQHSQHLRHRASMQKSAKRDGKKRSGTEH 1008
Cdd:pfam11498  370 MLLQQQQQMHQLQQHHQmngggqfATQAHQHAAYLQQMQHMRLQEQIQHQQQQAQHH 426
EFh_PRIP2 cd16223
EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); ...
204-304 1.93e-03

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: 39.89  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  204 PQDDFTTEIFKAFLNSICPRPDIDTIFSEVgAKSRPYLTVEQLTDFINNKQRDPRLNEilypplkvEQVQTLVEKYEPNA 283
Cdd:cd16223     52 GGTEVTKEEFIEVFHELCTRPEIYFLLVQF-SSNKEFLDTKDLMMFLEAEQGMAHVTE--------EISLDIIHKYEPSK 122
                           90       100
                   ....*....|....*....|.
gi 1624433999  284 MLSQRGQISVEGFTRYLSGEE 304
Cdd:cd16223    123 EGQEKGWLSLDGFTNYLMSPE 143
PTZ00121 PTZ00121
MAEBL; Provisional
932-1176 2.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  932 EAQSMEELKQQKvfvrEQRRQYKELKELVKRHHKKTTDMIKEHTARQNEQHSQHLRHRASMQKSAKRDGKKRSgtEHAHL 1011
Cdd:PTZ00121  1468 EAKKADEAKKKA----EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA--DEAKK 1541
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1012 ALE----------QELKTLDEESSWRLAELKEQQQLQLLTLRQEQYYSEKYLKREHVKQLVEKLTAVAEECQNNQMKKLK 1081
Cdd:PTZ00121  1542 AEEkkkadelkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1082 ELCEKEKKDLKKRMDKKRQEKIHEVKTKEKNLTEEEKleinrtfvnevvQYIKRLEDAQNKRQDKLLArhKDIRQQILDE 1161
Cdd:PTZ00121  1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE------------NKIKAAEEAKKAEEDKKKA--EEAKKAEEDE 1687
                          250
                   ....*....|....*
gi 1624433999 1162 KPKEDCSSEDEAAER 1176
Cdd:PTZ00121  1688 KKAAEALKKEAEEAK 1702
PTZ00121 PTZ00121
MAEBL; Provisional
932-1176 2.25e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  932 EAQSMEELKQQkvfvrEQRRQYKELKElvKRHHKKTTDMIKEHTARQNEQHSQHLRHRASMQKSA--KRDGKKRSGTEHA 1009
Cdd:PTZ00121  1532 EAKKADEAKKA-----EEKKKADELKK--AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIEEVMKLYEEE 1604
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1010 HLALEQELKTlDEESSWRLAELKEQQQLQLLTLRQEQYYSEKYLKREHVKQLVEKLTAVAEEC---QNNQMKKLKELCEK 1086
Cdd:PTZ00121  1605 KKMKAEEAKK-AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkAEEDKKKAEEAKKA 1683
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1087 EKKDLKKRMDKKRQE----KIHEVKTKEknltEEEKLEINRTFVNEVVQYIK----RLEDAQNKRQDKLLARHKDIRQQI 1158
Cdd:PTZ00121  1684 EEDEKKAAEALKKEAeeakKAEELKKKE----AEEKKKAEELKKAEEENKIKaeeaKKEAEEDKKKAEEAKKDEEEKKKI 1759
                          250
                   ....*....|....*...
gi 1624433999 1159 LDEKPKEDCSSEDEAAER 1176
Cdd:PTZ00121  1760 AHLKKEEEKKAEEIRKEK 1777
PRK12704 PRK12704
phosphodiesterase; Provisional
1047-1165 2.29e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1047 YYSEKYLKREHVKQLVEKLTAVAEECQN--NQMKKLKELCEKEK-KDLKKRMDKKRQEKIHEVKTKEKNLTE-EEKLEin 1122
Cdd:PRK12704    22 YFVRKKIAEAKIKEAEEEAKRILEEAKKeaEAIKKEALLEAKEEiHKLRNEFEKELRERRNELQKLEKRLLQkEENLD-- 99
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1624433999 1123 rtfvnevvqyiKRLEDAqNKRQDKLLARHKDI--RQQILDEKPKE 1165
Cdd:PRK12704   100 -----------RKLELL-EKREEELEKKEKELeqKQQELEKKEEE 132
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
1060-1120 3.59e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 41.01  E-value: 3.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624433999 1060 QLVEKLTAVAEeCQNNQMKKLKELCEKEKKDLKKRMDKKRQEKIHEVKTKEKNLTEEEKLE 1120
Cdd:pfam07946  243 YLIDKLAKRAK-LRPEALKKAKKTREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA 302
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
216-300 3.83e-03

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: 38.96  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  216 FLNSICPRPDIDTIFSEVGAKSRpYLTVEQLTDFINNKQRDPRLneilypplkvEQVQTLVEKYEPNAMLSQRGQISVEG 295
Cdd:cd16218     61 FCRRLMQRPELEEIFHQYSGEDC-VLSAEELREFLKDQGEDASL----------VHAKELIQTYELNEKAKQHQLMTLDG 129

                   ....*
gi 1624433999  296 FTRYL 300
Cdd:cd16218    130 FTMYM 134
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
879-1176 4.89e-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: 4.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  879 APSEPKTDPKPAPTENGMSHAPLIAPKPASLVSHQPQPSVK-------SEDVIQSVLTDLEAQ-SMEELKQQKVFVREQR 950
Cdd:pfam17380  219 APKEVQGMPHTLAPYEKMERRKESFNLAEDVTTMTPEYTVRyngqtmtENEFLNQLLHIVQHQkAVSERQQQEKFEKMEQ 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  951 RQYKELKELVKRHHKKTTDMIKEHTARQNEQHSQHL----RHRASMQKS-----AKRDGKKRSGTEHAHLALEQELKTLD 1021
Cdd:pfam17380  299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERErelerIRQEERKRELERIRQEEIAMEISRMR 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1022 EESSWRLAELKEQQQLQLLTLRQEQYY---SEKYLKREHVKQLVEKLTAVAEECQNNQMKKLKELCEKEKKDLKKRmDKK 1098
Cdd:pfam17380  379 ELERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE-EQE 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1099 RQEKIHEVKTKE----KNLTEEEKLEINRTFVNEVVQYI--KRLED-----AQNKRQDKLLARHKDIRQQILDE-----K 1162
Cdd:pfam17380  458 RQQQVERLRQQEeerkRKKLELEKEKRDRKRAEEQRRKIleKELEErkqamIEEERKRKLLEKEMEERQKAIYEeerrrE 537
                          330
                   ....*....|....
gi 1624433999 1163 PKEDCSSEDEAAER 1176
Cdd:pfam17380  538 AEEERRKQQEMEER 551
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
933-1190 5.89e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  933 AQSMEELKQQKVFVREQRRQYKELKELVKRHHKKTTDMIKEHTARQNEQhsQHLRHRASMQKSAKRDGKKRSGTEHAhlA 1012
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEKEIA--E 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1013 LEQELKTLDEE------SSWRLAELKEQQQLQLLTLRQEQYYSEKYLKR--EHVKQLVEKLTAVAEEcqnnqMKKLKELC 1084
Cdd:COG4942     95 LRAELEAQKEElaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAE-----LAALRAEL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1085 EKEKKDLKKRMDKKRQEKihevktkeknlteeEKLEINRTFVNEVVQYIKRLEDAQNKRQDKLLARHKDIRQQIlDEKPK 1164
Cdd:COG4942    170 EAERAELEALLAELEEER--------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI-ARLEA 234
                          250       260
                   ....*....|....*....|....*..
gi 1624433999 1165 EDCSSEDEAAERAGPGVPGQIP-PASG 1190
Cdd:COG4942    235 EAAAAAERTPAAGFAALKGKLPwPVSG 261
PTZ00121 PTZ00121
MAEBL; Provisional
861-1177 7.82e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  861 LEEGREEVDNKEVEAGGDApSEPKTDPKPAPTENGMSHAPLIAPKPASLVSH--QPQPSVKSEDV--IQSVLTDLEAQSM 936
Cdd:PTZ00121  1214 AEEARKAEDAKKAEAVKKA-EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfaRRQAAIKAEEArkADELKKAEEKKKA 1292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999  937 EELKQQkvfvrEQRRQYKELKElvKRHHKKTTDMIKEhTARQNEQHSQHLRHRASMQKSAKRDGKKRSGTEHAHLALEQE 1016
Cdd:PTZ00121  1293 DEAKKA-----EEKKKADEAKK--KAEEAKKADEAKK-KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1017 LKTLDEesswrlaelkeqqqlqlltlrqeqyysekyLKREHVKQLVEKLTAVAEECQN-NQMKKLKELCEKEKKDLKKRM 1095
Cdd:PTZ00121  1365 KAEAAE------------------------------KKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAA 1414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624433999 1096 DKKRQEKIHEVKTKEKNLTEEEKleinrtfvnevvqyiKRLEDAqnKRQDKLLARHKDIRQQILDEKPKEDCSSEDEAAE 1175
Cdd:PTZ00121  1415 AAKKKADEAKKKAEEKKKADEAK---------------KKAEEA--KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477

                   ..
gi 1624433999 1176 RA 1177
Cdd:PTZ00121  1478 KA 1479
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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