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Conserved domains on  [gi|148745659|gb|AAI42682|]
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Phospholipase C, beta 3 (phosphatidylinositol-specific) [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
316-693 2.13e-178

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  Cd Length: 258  Bit Score: 529.63  E-value: 2.13e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08625     1 SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08625    81 IAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08625       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08625   155 ----------------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPME 200
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  636 FVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08625   201 FVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
154-304 2.70e-99

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: 314.55  E-value: 2.70e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEI 233
Cdd:cd16210     1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148745659  234 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16210    81 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
1029-1202 1.39e-70

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


:

Pssm-ID: 312287  Cd Length: 176  Bit Score: 235.33  E-value: 1.39e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1029 KRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISE 1108
Cdd:pfam08703    1 KQVAELKEKLEQELLELREEQYESEKKRKEQHLKEQIQKLKELAREKQAAELKKLKESCESEKKEMKKKLERKRLESIQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1109 AKMRDKHK-KEAELT-EINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:pfam08703   81 AKKKTKDKaAQERLKkEINNSHIQEVVQSIKRLEEAQSRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKMKRLPAE 160
                          170
                   ....*....|....*.
gi 148745659  1187 IRRSLLGEMPEGLGDG 1202
Cdd:pfam08703  161 IQESVQNCMKTKFPDE 176
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
22-149 2.70e-61

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: 207.42  E-value: 2.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   22 LRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVlGFGGPDARLEE 101
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 148745659  102 KLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASR 149
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PI-PLC-Y super family cl27705
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
318-833 4.88e-60

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


The actual alignment was detected with superfamily member PLN02952:

Pssm-ID: 332526  Cd Length: 599  Bit Score: 219.10  E-value: 4.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:PLN02952  124 DMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGS-TKDEILVLHGRTLTTPVPLIKCLKSIR 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepldkYPLAPG-VPLPSPQDLMGRILVKNKkrhrPSag 476
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTK----PP-- 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  477 gpdsagrKRPLEQSNSALSESSAATEPSSPQlGSPSSDscpglsngEEVGLEKPSLEPQ---KSLGDEGLNRGPYVLGPA 553
Cdd:PLN02952  270 -------KEYLESSGPIVIKKKNNVSPSGRN-SSEETE--------EAQTLESMLFEQEadsRSDSDQDDNKSGELQKPA 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  554 DRedeeedeeeeeqtdpKKPTTDEGTASSEVNatEEMSTLVNYIEPVkfksfeaarkrnkcfemsSFVETKAMEQLTKSP 633
Cdd:PLN02952  334 YK---------------RLITIHAGKPKGTLK--DAMKVAVDKVRRL------------------SLSEQELEKAATTNG 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  634 MEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRP---DK 710
Cdd:PLN02952  379 QDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKgfhDE 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  711 SFDPFTEVivdgIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDEEp 780
Cdd:PLN02952  459 VFDPKKKL----PVKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK-KTKIIEDN-WYPAWNEE- 531
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  781 FDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEANQPL 833
Cdd:PLN02952  532 FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
DUF812 super family cl25503
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ...
867-1189 6.95e-04

Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.


The actual alignment was detected with superfamily member pfam05667:

Pssm-ID: 310341  Cd Length: 588  Bit Score: 43.48  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   867 SLMDQRARQLAALigeseaqAGQETCQDTQSQQLGSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSS---------PGQ 937
Cdd:pfam05667  129 AIAAAIRSQLAAP-------WLPPECKRPTQRRQGSRAVRAFRTQPLVLPGLGGKTKKNPKELKEFYAkflppvtaqPSR 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   938 RDDLIASILSEVApTPLDELRGHKALVKLRSRQERDLRELRKKHQRKavtltrRLLDGLAQAqaegrcrLRPGALGGAAD 1017
Cdd:pfam05667  202 RADVVPSLLERNA-AELAAAQEWEEEWNEQGLQSRLTPEEYKKRKRE------KLLKRIAEQ-------LRSAALSGGEA 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1018 VEDTKEGEDEAKRYQEFQNRqvqsllelREAQVDAEAQRRLEHlRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKI 1097
Cdd:pfam05667  268 TEKSRSKQDLAELLSSFGEK--------NTTDDGLSKGSRFTH-TEKLQFANEESALPKTETEEELQAKREKELEELQEQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1098 LDRkrhnsiSEAKMrDKHKKEAELTEINRRHITESVNSIRRL---EEAQKQRHDRLVA------GQQQVLQQLAEEEPKL 1168
Cdd:pfam05667  339 LEE------LESSI-EELEEEIKKLTVSIKQVEEELEEQKAEneeLEKEYKVKKKTLDllpdaeENIAKLQKLVEASAQR 411
                          330       340
                   ....*....|....*....|.
gi 148745659  1169 LAQLAQECQEQRARLPQEIRR 1189
Cdd:pfam05667  412 LVELAGQWEKHRVPLIEEYRR 432
 
Name Accession Description Interval E-value
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
316-693 2.13e-178

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  Cd Length: 258  Bit Score: 529.63  E-value: 2.13e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08625     1 SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08625    81 IAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08625       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08625   155 ----------------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPME 200
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  636 FVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08625   201 FVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
154-304 2.70e-99

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: 314.55  E-value: 2.70e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEI 233
Cdd:cd16210     1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148745659  234 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16210    81 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
319-467 3.75e-75

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


Pssm-ID: 306818  Cd Length: 142  Bit Score: 246.64  E-value: 3.75e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   319 MTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIAE 398
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGKSSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSPIPFRDVLEAIKE 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148745659   399 TAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKyplaPGVPLPSPQDLMGRILVKN 467
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLDD----DLTELPSPEDLKGKILIKG 142
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
1029-1202 1.39e-70

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


Pssm-ID: 312287  Cd Length: 176  Bit Score: 235.33  E-value: 1.39e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1029 KRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISE 1108
Cdd:pfam08703    1 KQVAELKEKLEQELLELREEQYESEKKRKEQHLKEQIQKLKELAREKQAAELKKLKESCESEKKEMKKKLERKRLESIQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1109 AKMRDKHK-KEAELT-EINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:pfam08703   81 AKKKTKDKaAQERLKkEINNSHIQEVVQSIKRLEEAQSRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKMKRLPAE 160
                          170
                   ....*....|....*.
gi 148745659  1187 IRRSLLGEMPEGLGDG 1202
Cdd:pfam08703  161 IQESVQNCMKTKFPDE 176
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
591-705 8.43e-65

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  Cd Length: 115  Bit Score: 217.11  E-value: 8.43e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659    591 STLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQ 670
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKDPFYEMSSFSETKAKKLLKKAPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNAGCQ 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 148745659    671 LVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFM 705
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
22-149 2.70e-61

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: 207.42  E-value: 2.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   22 LRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVlGFGGPDARLEE 101
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 148745659  102 KLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASR 149
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PLN02952 PLN02952
phosphoinositide phospholipase C
318-833 4.88e-60

phosphoinositide phospholipase C


Pssm-ID: 178538  Cd Length: 599  Bit Score: 219.10  E-value: 4.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:PLN02952  124 DMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGS-TKDEILVLHGRTLTTPVPLIKCLKSIR 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepldkYPLAPG-VPLPSPQDLMGRILVKNKkrhrPSag 476
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTK----PP-- 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  477 gpdsagrKRPLEQSNSALSESSAATEPSSPQlGSPSSDscpglsngEEVGLEKPSLEPQ---KSLGDEGLNRGPYVLGPA 553
Cdd:PLN02952  270 -------KEYLESSGPIVIKKKNNVSPSGRN-SSEETE--------EAQTLESMLFEQEadsRSDSDQDDNKSGELQKPA 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  554 DRedeeedeeeeeqtdpKKPTTDEGTASSEVNatEEMSTLVNYIEPVkfksfeaarkrnkcfemsSFVETKAMEQLTKSP 633
Cdd:PLN02952  334 YK---------------RLITIHAGKPKGTLK--DAMKVAVDKVRRL------------------SLSEQELEKAATTNG 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  634 MEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRP---DK 710
Cdd:PLN02952  379 QDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKgfhDE 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  711 SFDPFTEVivdgIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDEEp 780
Cdd:PLN02952  459 VFDPKKKL----PVKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK-KTKIIEDN-WYPAWNEE- 531
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  781 FDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEANQPL 833
Cdd:PLN02952  532 FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
728-843 8.04e-36

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  Cd Length: 128  Bit Score: 134.98  E-value: 8.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  728 LRVKVISGQFLSD------RKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEE 801
Cdd:cd00275     4 LTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTKVVKNNGFNPVWNET-FEFD-VTVPELAFLRFVVYDE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 148745659  802 GG---KFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTE 843
Cdd:cd00275    82 DSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHID 126
PLN02223 PLN02223
phosphoinositide phospholipase C
318-828 1.22e-24

phosphoinositide phospholipase C


Pssm-ID: 165867  Cd Length: 537  Bit Score: 109.73  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTS-SVEMYRQALLWGCRCVELDVWkgrpPEEEPFITHGFTMTTEVPLR--DVLE 394
Cdd:PLN02223  107 DMHAPLSHYFIHTSLKSYFTGNNVFGKLySIEPIIDALEQGVRVVELDLL----PDGKDGICVRPKWNFEKPLElqECLD 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  395 AIAETAF-KTSPYPVILSFEnhvDSAKQ--QAKMAEYCRSIFGDALLIEPldkyPLAPGVPLPSPQDLMGRILVKNKkrh 471
Cdd:PLN02223  183 AIKEHAFtKCRSYPLIITFK---DGLKPdlQSKATQMIDQTFGDMVYHED----PQHSLEEFPSPAELQNKILISRR--- 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  472 rpsaggpdsagrkrpleqsnsalsessaatePSSPQLGSPSSDSCPGLSNGEEVglekpslepqkslgdeglNRGPyvlg 551
Cdd:PLN02223  253 -------------------------------PPKELLYAKADDGGVGVRNELEI------------------QEGP---- 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  552 padredeeedeeeeeqTDPkkpttdegtassevnateemstlvNYIEPVKFKSFEAARKRNKCFEMSSfvetKAMEQLTK 631
Cdd:PLN02223  280 ----------------ADK------------------------NYQSLVGFHAVEPRGMLQKALTGKA----DDIQQPGW 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  632 SPMEFVEYNKQQLSRIYPKGTRVDS-SNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRR--P 708
Cdd:PLN02223  316 YERDIISFTQKKFLRTRPKKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagP 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  709 DKSFDPftevIVDGIVANALRVKVISGQ-FLSD--RKVG------IYVEVDMFGLPVDtrRKYRTRTSQGNSFNPVWDEE 779
Cdd:PLN02223  396 SGVFYP----TENPVVVKILKVKIYMGDgWIVDfkKRIGrlskpdLYVRISIAGVPHD--EKIMKTTVKNNEWKPTWGEE 469
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148745659  780 pFDFPkVVLPTLA--SLRIAAFE--EGGKFVGHRILPVSAIRSGYHYVCLRNE 828
Cdd:PLN02223  470 -FTFP-LTYPDLAliSFEVYDYEvsTADAFCGQTCLPVSELIEGIRAVPLYDE 520
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
728-825 1.08e-12

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  Cd Length: 101  Bit Score: 67.51  E-value: 1.08e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659    728 LRVKVISGQFLSDRKVG----IYVEVDMFGlpvDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:smart00239    2 LTVKIISARNLPPKDKGgksdPYVKVSLDG---DPKEKKKTKVVK-NTLNPVWNET-FEFE-VPPPELAELEIEVYDKDR 75
                            90       100
                    ....*....|....*....|....*.
gi 148745659    804 ----KFVGHRILPVSAIRSGYHYVCL 825
Cdd:smart00239   76 fgrdDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
216-308 4.45e-08

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: 312695  Cd Length: 85  Bit Score: 53.41  E-value: 4.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   216 FLNKLCLRPDIDKILLEIGAKGKpYLTLEQLMDFINQKQRDPRLNevlypplrPSQARLLIEKYEPNQQFLERDQMSMEG 295
Cdd:pfam09279    1 FYKMLTQREEIDRIFQEYSGDGQ-KLSLDELVDFLREEQREEDAS--------PALALELIERYEPSETAKKQHAMTKDG 71
                           90
                   ....*....|...
gi 148745659   296 FSRYLGGEENGIL 308
Cdd:pfam09279   72 FLMYLLSPDGSIF 84
C2 pfam00168
C2 domain;
728-822 2.99e-07

C2 domain;


Pssm-ID: 306639  Cd Length: 104  Bit Score: 51.16  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   728 LRVKVISGQFLSDRKVGI----YVEVDMfglpVDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:pfam00168    3 LRVTVIEAKNLPPKDLNGksdpYVKVYL----LDGKQKKKTKVVK-NTLNPVWNET-FTFS-VPDPENAVLEIEVYDYDR 75
                           90       100
                   ....*....|....*....|...
gi 148745659   804 ----KFVGHRILPVSAIRSGYHY 822
Cdd:pfam00168   76 fgrdDFIGEVRIPLSELDSGEVL 98
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1026-1189 5.90e-07

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 53.95  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1026 DEAKRYQEFQNrqvqsllELREAQVdAEAQRRLEHLRQALQRLREVV------LDANTTQFKRLKEMNEREKKELQKIld 1099
Cdd:COG1196   210 EKAERYQELKA-------ELRELEL-ALLLAKLKELRKELEELEEELsrleeeLEELQEELEEAEKEIEELKSELEEL-- 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1100 rKRHNSISEAKMRDKHKKEAEL---TEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVL--QQLAEEEPKLLAQLAQ 1174
Cdd:COG1196   280 -REELEELQEELLELKEEIEELegeISLLRERLEELENELEELEERLEELKEKIEALKEELEerETLLEELEQLLAELEE 358
                         170
                  ....*....|....*
gi 148745659 1175 ECQEQRARLPQEIRR 1189
Cdd:COG1196   359 AKEELEEKLSALLEE 373
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1019-1187 7.85e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 53.53  E-value: 7.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1019 EDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDA-----EAQRRLEHLRQALQRLREVV--LDANTTQFKRLKEMNEREK 1091
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrkigEIEKEIEQLEQEEEKLKERLeeLEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1092 KELQKILDRKRhnsiseakmRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVA---------GQQQVLQQLA 1162
Cdd:TIGR02169  761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreieqklNRLTLEKEYL 831
                          170       180
                   ....*....|....*....|....*
gi 148745659  1163 EEEPKLLAQLAQECQEQRARLPQEI 1187
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEI 856
PTZ00121 PTZ00121
MAEBL; Provisional
955-1189 1.26e-05

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 49.75  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  955 DELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRlrpgalgGAADVEDTKEGeDEAKRYQEF 1034
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-------EAKKAEEKKKA-DELKKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1035 QN-RQVQSLLELREAQVDAE-AQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMR 1112
Cdd:PTZ00121 1558 KKaEEKKKAEEAKKAEEDKNmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659 1113 DKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQqqvLQQLAEEEPKLLAQLAQECQEqrARLPQEIRR 1189
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE---AKKAEEDEKKAAEALKKEAEE--AKKAEELKK 1709
DUF812 pfam05667
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ...
867-1189 6.95e-04

Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.


Pssm-ID: 310341  Cd Length: 588  Bit Score: 43.48  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   867 SLMDQRARQLAALigeseaqAGQETCQDTQSQQLGSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSS---------PGQ 937
Cdd:pfam05667  129 AIAAAIRSQLAAP-------WLPPECKRPTQRRQGSRAVRAFRTQPLVLPGLGGKTKKNPKELKEFYAkflppvtaqPSR 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   938 RDDLIASILSEVApTPLDELRGHKALVKLRSRQERDLRELRKKHQRKavtltrRLLDGLAQAqaegrcrLRPGALGGAAD 1017
Cdd:pfam05667  202 RADVVPSLLERNA-AELAAAQEWEEEWNEQGLQSRLTPEEYKKRKRE------KLLKRIAEQ-------LRSAALSGGEA 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1018 VEDTKEGEDEAKRYQEFQNRqvqsllelREAQVDAEAQRRLEHlRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKI 1097
Cdd:pfam05667  268 TEKSRSKQDLAELLSSFGEK--------NTTDDGLSKGSRFTH-TEKLQFANEESALPKTETEEELQAKREKELEELQEQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1098 LDRkrhnsiSEAKMrDKHKKEAELTEINRRHITESVNSIRRL---EEAQKQRHDRLVA------GQQQVLQQLAEEEPKL 1168
Cdd:pfam05667  339 LEE------LESSI-EELEEEIKKLTVSIKQVEEELEEQKAEneeLEKEYKVKKKTLDllpdaeENIAKLQKLVEASAQR 411
                          330       340
                   ....*....|....*....|.
gi 148745659  1169 LAQLAQECQEQRARLPQEIRR 1189
Cdd:pfam05667  412 LVELAGQWEKHRVPLIEEYRR 432
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
873-1066 4.47e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899  Cd Length: 656  Bit Score: 40.86  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  873 ARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPldASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPT 952
Cdd:PRK06975  256 ERIVRAFLTWADAAAQPATAAPAPSRMTDTNDSKSVTSQP--AAAAAAPAPPPNPPATPPEPPARRGRGSAALWFVVVVL 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  953 PLDELRGHKALVKLRSRQERDLRELRKK---HQRKAVTLTRRLLDGLAQAQAEgrcrlrPGALggaadveDTKEGEDEAK 1029
Cdd:PRK06975  334 ACAAAVGGYALNRKVDRLDQELVQRQQAndaQTAELRVKTEQAQASVHQLDSQ------FAQL-------DGKLADAQSA 400
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 148745659 1030 ryQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQ 1066
Cdd:PRK06975  401 --QQALEQQYQDLSRNRDDWMIAEVEQMLSSASQQLQ 435
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
1084-1189 8.59e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879  Cd Length: 291  Bit Score: 39.48  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1084 KEMNEREKKELQKILDRKRhnsisEAKMRDKHKKEAELTEINRRHITEsvnsIRRLEEAQKQRHDRLVAGQQQVLQQLAE 1163
Cdd:cd16269   196 KEKEIEAERAKAEAAEQER-----KLLEEQQRELEQKLEDQERSYEEH----LRQLKEKMEEERENLLKEQERALESKLK 266
                          90       100
                  ....*....|....*....|....*.
gi 148745659 1164 EEPKLlaqLAQECQEQRARLPQEIRR 1189
Cdd:cd16269   267 EQEAL---LEEGFKEQAELLQEEIRS 289
 
Name Accession Description Interval E-value
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
316-693 2.13e-178

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  Cd Length: 258  Bit Score: 529.63  E-value: 2.13e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08625     1 SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08625    81 IAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08625       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08625   155 ----------------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPME 200
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  636 FVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08625   201 FVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
316-693 1.47e-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  Cd Length: 257  Bit Score: 527.29  E-value: 1.47e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  396 IAETAFKTSPYPVILSFENHVDSaKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08591       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08591   154 ----------------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIE 199
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  636 FVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08591   200 FVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
316-693 1.56e-146

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  Cd Length: 261  Bit Score: 446.04  E-value: 1.56e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08624       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  556 edeeedeeeeeqtdpkkpttdegtassevnaTEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08624   155 -------------------------------YEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQ 203
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  636 FVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08624   204 FVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
316-693 5.90e-137

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  Cd Length: 258  Bit Score: 420.64  E-value: 5.90e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08623     1 NEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08623    81 IAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08623       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08623   155 ----------------------------------MSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVE 200
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  636 FVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08623   201 FVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLSMQINMGMYEYN 258
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
318-693 2.22e-125

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  Cd Length: 226  Bit Score: 388.35  E-value: 2.22e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08558     3 DMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEAIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPlapgVPLPSPQDLMGRILVKNKKRHrpsagg 477
Cdd:cd08558    81 EYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKKYH------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08558       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcfeMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08558   150 -----------------------------------------------------------MSSFSETKALKLLKESPEEFV 170
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08558   171 KYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVALNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
318-693 1.91e-117

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  Cd Length: 257  Bit Score: 368.71  E-value: 1.91e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08626     3 DMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08626    83 DTAFVTSDYPVILSFENHC-SKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR-------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08626       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08626   154 --------------------------------LSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFV 201
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08626   202 NYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
318-693 1.03e-106

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  Cd Length: 257  Bit Score: 339.31  E-value: 1.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08593     3 DMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQAIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKRHrpsagg 477
Cdd:cd08593    81 EYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKKLK------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsaLSessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08593   150 ----------------LA-------------------------------------------------------------- 151
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnatEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08593   152 ------------------------------KELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFV 201
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08593   202 RHNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN 257
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
154-304 2.70e-99

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: 314.55  E-value: 2.70e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEI 233
Cdd:cd16210     1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148745659  234 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16210    81 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
318-693 1.53e-86

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  Cd Length: 260  Bit Score: 283.16  E-value: 1.53e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08597     3 DMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKyplaPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08597    81 EYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEPPNE----GESYLPSPHDLKGKIIIKGKK-------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevgLEKPSLepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08597   148 -------------------------------------------------LKRRKL------------------------- 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnaTEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08597   154 -----------------------------CKELSDLVSLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFV 204
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08597   205 NYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
316-690 5.52e-80

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  Cd Length: 231  Bit Score: 263.72  E-value: 5.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08598     1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  396 IAETAFKTSPYPVILSFENHVDSAkQQAKMAEYCRSIFGDALLIEPLDkyPLAPGvpLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08598    79 IKKYAFVTSPYPLILSLEVHCDAE-QQERMVEIMKETFGDLLVTEPLD--GLEDE--LPSPEELRGKILIKVKK------ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  476 ggpdsagrkrpleqsnsalsessaatEPSSPqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08598   148 --------------------------ESKTP------------------------------------------------- 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  556 edeeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrNKCFemsSFVETKAMEQLTKSPME 635
Cdd:cd08598   153 --------------------------------------------------------NHIF---SLSERSLLKLLKDKRAA 173
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148745659  636 FVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVF 690
Cdd:cd08598   174 LDKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVALNWQTYDLGMQLNEAMF 228
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
318-693 1.18e-78

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  Cd Length: 229  Bit Score: 260.05  E-value: 1.18e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08592     3 DMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKRHRpsagg 477
Cdd:cd08592    81 EHAFVTSEYPVILSIENHC-SLPQQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKKLFY----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08592       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcfEMSSFVETKAMEQLTKS-PMEF 636
Cdd:cd08592   151 ----------------------------------------------------------EMSSFPETKAEKYLNRQkGKIF 172
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08592   173 LKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVALNFQTPDKPMQLNQALFMLN 229
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
318-693 2.90e-75

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  Cd Length: 257  Bit Score: 251.78  E-value: 2.90e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08595     3 DMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDG--ADNEPVVYHGYTLTSKILFKEVITTVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLApgvPLPSPQDLMGRILVKNKKRhrpsagg 477
Cdd:cd08595    81 KYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKKK------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpYVLGpadred 557
Cdd:cd08595   150 ----------------------------------------------------------------------IAKA------ 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08595   154 --------------------------------LSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFV 201
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08595   202 GHTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN 257
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
318-693 3.09e-75

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  Cd Length: 258  Bit Score: 251.79  E-value: 3.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08631     3 DMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAAVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLD-KYPlapgVPLPSPQDLMGRILVKNKKrhrpsag 476
Cdd:cd08631    81 QYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKK------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  477 gpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadre 556
Cdd:cd08631       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  557 deeedeeeeeqtdpkkpttdegtasseVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEF 636
Cdd:cd08631   149 ---------------------------IRLSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEF 201
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08631   202 VQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
319-467 3.75e-75

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


Pssm-ID: 306818  Cd Length: 142  Bit Score: 246.64  E-value: 3.75e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   319 MTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIAE 398
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGKSSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSPIPFRDVLEAIKE 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148745659   399 TAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKyplaPGVPLPSPQDLMGRILVKN 467
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLDD----DLTELPSPEDLKGKILIKG 142
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
318-693 4.71e-75

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  Cd Length: 258  Bit Score: 251.11  E-value: 4.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08629     3 DMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRAIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08629    81 DYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLD----GVTTSLPSPEQLKGKILLKGKK-------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08629       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtasseVNATEEMSTLVNYIEPVKFKSFEAARKRNKCF-EMSSFVETKAMEQLTKSPMEF 636
Cdd:cd08629   148 --------------------------LKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFyEMASFSESRALRLLQESGNGF 201
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08629   202 VRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
318-693 9.92e-73

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  Cd Length: 258  Bit Score: 244.55  E-value: 9.92e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08630     3 DMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQAVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLApgvPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08630    81 QHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKK-------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08630       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeEQTDPkkpttdegtassevnateEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08630   149 --------LQISP------------------ELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFV 202
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08630   203 RHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
318-693 3.24e-72

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  Cd Length: 254  Bit Score: 243.22  E-value: 3.24e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRppEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08596     3 DLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08596    81 RSAFITSDYPVILSIENHC-SLQQQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08596       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnaTEEMSTLVNYIEPVKFKSFEAArkrnKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08596   152 -----------------------------APELSDLVIYCQAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLV 198
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08596   199 QHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLVALNYQTDDLPMHLNAAMFEAN 254
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
1029-1202 1.39e-70

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


Pssm-ID: 312287  Cd Length: 176  Bit Score: 235.33  E-value: 1.39e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1029 KRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISE 1108
Cdd:pfam08703    1 KQVAELKEKLEQELLELREEQYESEKKRKEQHLKEQIQKLKELAREKQAAELKKLKESCESEKKEMKKKLERKRLESIQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1109 AKMRDKHK-KEAELT-EINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:pfam08703   81 AKKKTKDKaAQERLKkEINNSHIQEVVQSIKRLEEAQSRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKMKRLPAE 160
                          170
                   ....*....|....*.
gi 148745659  1187 IRRSLLGEMPEGLGDG 1202
Cdd:pfam08703  161 IQESVQNCMKTKFPDE 176
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
154-304 3.14e-70

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


Pssm-ID: 320030  Cd Length: 153  Bit Score: 233.68  E-value: 3.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILL 231
Cdd:cd16200     1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDKkrKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148745659  232 EIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16200    81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
155-304 2.47e-68

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: 228.22  E-value: 2.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  155 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIG 234
Cdd:cd16208     2 KAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEFG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  235 AKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16208    82 AKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
318-693 5.81e-67

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  Cd Length: 227  Bit Score: 227.38  E-value: 5.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08594     3 DMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIETIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08594    81 KYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKK-------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08594       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08594   149 ---------------------------------------------------------WQVSSFSETRAHQIVQQKAAQFL 171
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08594   172 RFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVALNYQTEGRMLQLNRAKFRAN 227
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
318-693 5.53e-66

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  Cd Length: 254  Bit Score: 225.70  E-value: 5.53e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08628     3 DMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVDsAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKRhrpsagg 477
Cdd:cd08628    81 DHAFVTSEYPVILSIEEHCS-VEQQRHMAKVFKEVFGDKLLMKPLE----ASADQLPSPTQLKEKIIIKHKKL------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08628       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnATEEMSTLVNYIEPvkfKSFEAARKRNKCF-EMSSFVETKAMEQLTKSPMEF 636
Cdd:cd08628   149 ----------------------------IAIELSDLVVYCKP---TSKTKDNLENPDFkEIRSFVETKAPSIIRQKPVQL 197
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08628   198 LKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN 254
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
591-705 8.43e-65

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  Cd Length: 115  Bit Score: 217.11  E-value: 8.43e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659    591 STLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQ 670
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKDPFYEMSSFSETKAKKLLKKAPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNAGCQ 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 148745659    671 LVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFM 705
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
318-693 9.66e-65

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  Cd Length: 254  Bit Score: 222.22  E-value: 9.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08633     3 DMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIETIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALliePLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRpsagg 477
Cdd:cd08633    81 KYAFIKNEYPVILSIENHC-SVPQQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKKLSR----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsALSEssaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08633   152 ---------------ALSD------------------------------------------------------------- 155
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnateemstLVNYIEPVKFKSFEAarKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08633   156 -----------------------------------LVKYTKSVRVHDIET--EATSSWQVSSFSETKAHQILQQKPAQYL 198
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08633   199 RFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
318-693 1.24e-64

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


Pssm-ID: 176497  Cd Length: 274  Bit Score: 222.52  E-value: 1.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLA-----GTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTtEVPLRDV 392
Cdd:cd00137     3 PDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLKEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  393 LEAIAETAFKTSPYPVILSFENHVDSA-KQQAKMAEYCRSIFGDALLIEPLDkyplaPGVPLPSPQDLMGRILVKNKKrh 471
Cdd:cd00137    80 IEAIAQFLKKNPPETIIMSLKNEVDSMdSFQAKMAEYCRTIFGDMLLTPPLK-----PTVPLPSLEDLRGKILLLNKK-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  472 rpsaggpdsagrkrpleqsnsalsesSAATEPSspqlgspssdscpGLSNGEEVGLEKPSLEPQKSlgdeglnrgpyvlg 551
Cdd:cd00137   153 --------------------------NGFSGPT-------------GSSNDTGFVSFEFSTQKNRS-------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  552 padredeeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcFEMSSFVETKAME---- 627
Cdd:cd00137   180 ---------------------------------------------------------------YNISSQDEYKAYDdekv 196
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  628 QLTKSPMEFVEYNKQQLSRIYPKGTRV---------DSSNYMPQLFWN---VGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd00137   197 KLIKATVQFVDYNKNQLSRNYPSGTSGgtawyyyamDSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
22-149 2.70e-61

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: 207.42  E-value: 2.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   22 LRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVlGFGGPDARLEE 101
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 148745659  102 KLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASR 149
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
154-304 8.32e-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: 207.15  E-value: 8.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSA---DKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKIL 230
Cdd:cd16213     1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148745659  231 LEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16213    81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYLMSED 154
PLN02952 PLN02952
phosphoinositide phospholipase C
318-833 4.88e-60

phosphoinositide phospholipase C


Pssm-ID: 178538  Cd Length: 599  Bit Score: 219.10  E-value: 4.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:PLN02952  124 DMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGS-TKDEILVLHGRTLTTPVPLIKCLKSIR 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepldkYPLAPG-VPLPSPQDLMGRILVKNKkrhrPSag 476
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTK----PP-- 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  477 gpdsagrKRPLEQSNSALSESSAATEPSSPQlGSPSSDscpglsngEEVGLEKPSLEPQ---KSLGDEGLNRGPYVLGPA 553
Cdd:PLN02952  270 -------KEYLESSGPIVIKKKNNVSPSGRN-SSEETE--------EAQTLESMLFEQEadsRSDSDQDDNKSGELQKPA 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  554 DRedeeedeeeeeqtdpKKPTTDEGTASSEVNatEEMSTLVNYIEPVkfksfeaarkrnkcfemsSFVETKAMEQLTKSP 633
Cdd:PLN02952  334 YK---------------RLITIHAGKPKGTLK--DAMKVAVDKVRRL------------------SLSEQELEKAATTNG 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  634 MEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRP---DK 710
Cdd:PLN02952  379 QDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKgfhDE 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  711 SFDPFTEVivdgIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDEEp 780
Cdd:PLN02952  459 VFDPKKKL----PVKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK-KTKIIEDN-WYPAWNEE- 531
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  781 FDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEANQPL 833
Cdd:PLN02952  532 FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
318-693 7.16e-60

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  Cd Length: 253  Bit Score: 208.35  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08632     3 DMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIETIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDAL-LIEPLDKYPLApgvpLPSPQDLMGRILVKNKKRHRpsag 476
Cdd:cd08632    81 KYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKKLCR---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  477 gpdsagrkrpleqsnsALSESSAATEpsspqlgSPSSDSCpglsngeevglekpslepqkslgdeglnrgpyvlgpadre 556
Cdd:cd08632   152 ----------------DLSDLVVYTN-------SVAAQDI---------------------------------------- 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  557 deeedeeeeeqtdpkkptTDEGTASSEVnateemstlvnyiepvkfksfeaarkrnkcfemsSFVETKAMEQLTKSPMEF 636
Cdd:cd08632   169 ------------------VDDGSTGNVL----------------------------------SFSETRAHQLVQQKAEQF 196
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08632   197 MTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
319-468 1.67e-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  Cd Length: 143  Bit Score: 202.90  E-value: 1.67e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659    319 MTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIAE 398
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659    399 TAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLapgvPLPSPQDLMGRILVKNK 468
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLE----VLPSPEQLRGKILLKVR 143
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
590-704 1.18e-57

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


Pssm-ID: 306817  Cd Length: 115  Bit Score: 196.58  E-value: 1.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   590 MSTLVNYIEPVKFKSFEAARK--RNKCFEMSSFVETKAMEqLTKSpMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNV 667
Cdd:pfam00387    1 LSDLVVYTQSVKFKGFGFSTKtpNNTFYHMFSFSESKALK-LLKA-EDFVNHNRRHLSRVYPKGTRVDSSNYNPQPFWNA 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 148745659   668 GCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEF 704
Cdd:pfam00387   79 GCQMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 115
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
318-693 3.66e-57

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  Cd Length: 229  Bit Score: 199.87  E-value: 3.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08627     3 EMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYplAPGvpLPSPQDLMGRILVKNKKRHRpsagg 477
Cdd:cd08627    81 EHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVDIN--ADG--LPSPNQLKRKILIKHKKLYR----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08627       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcfEMSSFVETKAMEQLTKSP-MEF 636
Cdd:cd08627   151 ----------------------------------------------------------DMSSFPETKAEKYVNRSKgKKF 172
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08627   173 LQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
PLN02222 PLN02222
phosphoinositide phospholipase C 2
285-828 1.04e-55

phosphoinositide phospholipase C 2


Pssm-ID: 177868  Cd Length: 581  Bit Score: 206.03  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  285 FLERDQMSMEGFSRYLGGEENGilPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELD 364
Cdd:PLN02222   73 LLHRNGLHLDAFFKYLFGDNNP--PLALHEVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELD 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  365 VWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDK 444
Cdd:PLN02222  151 IWPNS-DKDDIDVLHGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  445 YPLApgvpLPSPQDLMGRILVKNKKRHRPSAGGPDSAGRKrpleqsnsalsessaatepsspqlgspssdsCPGLSNGEE 524
Cdd:PLN02222  229 SLKE----FPSPNSLKKRIIISTKPPKEYKEGKDDEVVQK-------------------------------GKDLGDEEV 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  525 VGLEKPS-LEPQKSLGDEGLNrgpyvlGPADredeeedeeeeeqtdpkkPTTDEGTASSEVNATEEMSTLVNyIEPVKFK 603
Cdd:PLN02222  274 WGREVPSfIQRNKSVDKNDSN------GDDD------------------DDDDDGEDKSKKNAPPQYKHLIA-IHAGKPK 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  604 S-----FEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNkqqLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQT 678
Cdd:PLN02222  329 GgitecLKVDPDKVRRLSLSEEQLEKAAEKYAKQIVRFTQHN---LLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  679 LDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKS---FDPFTEVIVDgivaNALRVKVISGQ----------FLSDRKVGI 745
Cdd:PLN02222  406 YGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDsdiFDPKATLPVK----TTLRVTIYMGEgwyfdfrhthFDQYSPPDF 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  746 YVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDeEPFDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYH 821
Cdd:PLN02222  482 YTRVGIAGVPGDTVMK-KTKTLEDN-WIPAWD-EVFEFPLTV-PELALLRLEVHEydmsEKDDFGGQTCLPVWELSQGIR 557

                  ....*..
gi 148745659  822 YVCLRNE 828
Cdd:PLN02222  558 AFPLHSR 564
PLN02228 PLN02228
Phosphoinositide phospholipase C
285-831 7.14e-54

Phosphoinositide phospholipase C


Pssm-ID: 177873  Cd Length: 567  Bit Score: 200.26  E-value: 7.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  285 FLERDQMSMEGFSRYLGGEENGILPLEAlDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELD 364
Cdd:PLN02228   75 FHHHGLVHLNAFYRYLFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  365 VWKGrPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDK 444
Cdd:PLN02228  154 LWPN-PSGNAAEVRHGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFRCTSES 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  445 YPLapgvpLPSPQDLMGRILVKNKKrhrpsaggpdsagrkrPLEQSNSALSESSaatepSSPQLGSPSSDScpgLSNGEE 524
Cdd:PLN02228  232 TKH-----FPSPEELKNKILISTKP----------------PKEYLESKTVQTT-----RTPTVKETSWKR---VADAEN 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  525 VGLEKPSLEPQKSLGDEGLnrgpYVLGPADRedeEEDEEEEEQTDPKKPTtdegtassEVNATEEmstlvnyiepvkfks 604
Cdd:PLN02228  283 KILEEYKDEESEAVGYRDL----IAIHAANC---KDPLKDCLSDDPEKPI--------RVSMDEQ--------------- 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  605 feaarkrnkcfemssFVETKAMeqlTKSPmEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQ 684
Cdd:PLN02228  333 ---------------WLETMVR---TRGT-DLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLW 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  685 LNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDgivaNALRVKVISGQ----------FLSDRKVGIYVEVDMFGL 754
Cdd:PLN02228  394 IMQGMFRANGGCGYVKKPRILLDEHTLFDPCKRLPIK----TTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGV 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  755 PVDTrRKYRTRTSQGNSFnPVWDEEPFDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEAN 830
Cdd:PLN02228  470 PRDT-VSYRTETAVDQWF-PIWGNDEFLFQLRV-PELALLWFKVQDydndTQNDFAGQTCLPLPELKSGVRAVRLHDRAG 546

                  .
gi 148745659  831 Q 831
Cdd:PLN02228  547 K 547
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
318-693 2.03e-51

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


Pssm-ID: 176541  Cd Length: 228  Bit Score: 183.34  E-value: 2.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRppEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08599     3 DMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGG--RGDICVLHGGTLTKPVKFEDCIKAIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPldkyPLAPGVPLPSPQDLMGRILVknkkrhrpsagg 477
Cdd:cd08599    81 ENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILI------------ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  478 pdsagrkrpleqsnsalsessaatepsspqlgspsSDSCPGLSNgeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08599   144 -----------------------------------SDKPPVIRN------------------------------------ 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  558 eeedeeeeeqtdpkkpttdegtassevNATEemSTLVNYIEpvkfksfeaarkrnkcfemssfvetkameqlTKSPMEFV 637
Cdd:cd08599   153 ---------------------------SLSE--TQLKKVIE-------------------------------GEHPTDLI 172
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148745659  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08599   173 EFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVALNMQGYDRPLWLNRGKFRAN 228
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
155-304 4.10e-51

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: 179.69  E-value: 4.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  155 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIG 234
Cdd:cd16209     2 KIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSYH 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  235 AKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16209    82 AKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLN02230 PLN02230
phosphoinositide phospholipase C 4
288-827 1.35e-43

phosphoinositide phospholipase C 4


Pssm-ID: 177875  Cd Length: 598  Bit Score: 169.50  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  288 RDQMSMEGFSRYLGGEEngILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVW- 366
Cdd:PLN02230   88 RRNLTLDDFNYYLFSTD--LNPPIADQVHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWp 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  367 KGrppEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYP 446
Cdd:PLN02230  166 RG---TDDVCVKHGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYYHDSEGCQ 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  447 lapgvPLPSPQDLMGRILVKNKKrhrpsaggpdsagrkrPLEqsnsaLSESSAATEPSSPQLGSPSSDSCPGLSNGEEVG 526
Cdd:PLN02230  242 -----EFPSPEELKEKILISTKP----------------PKE-----YLEANDAKEKDNGEKGKDSDEDVWGKEPEDLIS 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  527 LEKPSLEPQKSLGDeglnrgpyvlgpadredeeedeeeeEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKFKSFE 606
Cdd:PLN02230  296 TQSDLDKVTSSVND-------------------------LNQDDEERGSCESDTSCQLQAPEYKRLIAIHAGKPKGGLRM 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  607 AARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLN 686
Cdd:PLN02230  351 ALKVDPNKIRRLSLSEQLLEKAVASYGADVIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLM 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  687 AGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIvDGIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPV 756
Cdd:PLN02230  431 EGMFRANGGCGYVKKPDFLMDAGPNGQDFYPKD-NSCPKKTLKVKVCMGdgwlldfkktHFDSYSPPDFFVRVGIAGAPV 509
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  757 D-----TRRKYRTRTsqgnsfnPVWDEEpFDFPkVVLPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRN 827
Cdd:PLN02230  510 DevmekTKIEYDTWT-------PIWNKE-FIFP-LAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFN 580
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
154-304 1.33e-39

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: 146.80  E-value: 1.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILL 231
Cdd:cd16211     1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148745659  232 EIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16211    81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
728-843 8.04e-36

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  Cd Length: 128  Bit Score: 134.98  E-value: 8.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  728 LRVKVISGQFLSD------RKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEE 801
Cdd:cd00275     4 LTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTKVVKNNGFNPVWNET-FEFD-VTVPELAFLRFVVYDE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 148745659  802 GG---KFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTE 843
Cdd:cd00275    82 DSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHID 126
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
154-304 7.51e-33

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  Cd Length: 153  Bit Score: 127.28  E-value: 7.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILL 231
Cdd:cd16212     1 KKHWMRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148745659  232 EIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16212    81 SITKGKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PLN02223 PLN02223
phosphoinositide phospholipase C
318-828 1.22e-24

phosphoinositide phospholipase C


Pssm-ID: 165867  Cd Length: 537  Bit Score: 109.73  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  318 DMTQPLSAYFINSSHNTYLTAGQLAGTS-SVEMYRQALLWGCRCVELDVWkgrpPEEEPFITHGFTMTTEVPLR--DVLE 394
Cdd:PLN02223  107 DMHAPLSHYFIHTSLKSYFTGNNVFGKLySIEPIIDALEQGVRVVELDLL----PDGKDGICVRPKWNFEKPLElqECLD 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  395 AIAETAF-KTSPYPVILSFEnhvDSAKQ--QAKMAEYCRSIFGDALLIEPldkyPLAPGVPLPSPQDLMGRILVKNKkrh 471
Cdd:PLN02223  183 AIKEHAFtKCRSYPLIITFK---DGLKPdlQSKATQMIDQTFGDMVYHED----PQHSLEEFPSPAELQNKILISRR--- 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  472 rpsaggpdsagrkrpleqsnsalsessaatePSSPQLGSPSSDSCPGLSNGEEVglekpslepqkslgdeglNRGPyvlg 551
Cdd:PLN02223  253 -------------------------------PPKELLYAKADDGGVGVRNELEI------------------QEGP---- 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  552 padredeeedeeeeeqTDPkkpttdegtassevnateemstlvNYIEPVKFKSFEAARKRNKCFEMSSfvetKAMEQLTK 631
Cdd:PLN02223  280 ----------------ADK------------------------NYQSLVGFHAVEPRGMLQKALTGKA----DDIQQPGW 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  632 SPMEFVEYNKQQLSRIYPKGTRVDS-SNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRR--P 708
Cdd:PLN02223  316 YERDIISFTQKKFLRTRPKKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagP 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  709 DKSFDPftevIVDGIVANALRVKVISGQ-FLSD--RKVG------IYVEVDMFGLPVDtrRKYRTRTSQGNSFNPVWDEE 779
Cdd:PLN02223  396 SGVFYP----TENPVVVKILKVKIYMGDgWIVDfkKRIGrlskpdLYVRISIAGVPHD--EKIMKTTVKNNEWKPTWGEE 469
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148745659  780 pFDFPkVVLPTLA--SLRIAAFE--EGGKFVGHRILPVSAIRSGYHYVCLRNE 828
Cdd:PLN02223  470 -FTFP-LTYPDLAliSFEVYDYEvsTADAFCGQTCLPVSELIEGIRAVPLYDE 520
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
154-304 1.74e-20

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  Cd Length: 137  Bit Score: 91.19  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRV---ETALESCGLKFNRSESIRPDEFsleifERFLNKLCLRPDIDKIL 230
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVsekELKKLFKEVDTNGDGTLTFDEF-----EELYKSLTERPELEPIF 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148745659  231 LEIGAKGKPYLTLEQLMDFINQKQrdprlnevlYPPLRPSQARLLIEKYEPNqqfLERDQMSMEGFSRYLGGEE 304
Cdd:cd15898    76 KKYAGTNRDYMTLEEFIRFLREEQ---------GENVSEEECEELIEKYEPE---RENRQLSFEGFTNFLLSPE 137
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
329-438 8.71e-19

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  Cd Length: 179  Bit Score: 87.11  E-value: 8.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  329 NSSHNTYLTAGQlagTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVP------LRDVLEAIAETAFk 402
Cdd:cd08555     1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLT--KDGELVVYHGPTLDRTTAgilpptLEEVLELIADYLK- 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 148745659  403 TSPYPVILSFENHVDSA---KQQAKMAEYCRSIFGDALL 438
Cdd:cd08555    75 NPDYTIILSLEIKQDSPeydEFLAKVLKELRVYFDYDLR 113
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
164-300 4.98e-13

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  Cd Length: 140  Bit Score: 69.18  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  164 VNQDGRI---PVKNILKM--FSADKKRVETAlescglkFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIgAKGK 238
Cdd:cd16202    11 KNGDGKLsfkECKKLLKKlnVKVDKDYAKKL-------FQEADTSGEDVLDEEEFVQFYNRLTKRPEIEELFKKY-SGDD 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148745659  239 PYLTLEQLMDFINQKQRDPRLNevlypplrPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16202    83 EALTVEELRRFLQEEQKVKDVT--------LEWAEQLIETYEPSEDLKAQGLMSLDGFTLFL 136
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
728-825 1.08e-12

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  Cd Length: 101  Bit Score: 67.51  E-value: 1.08e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659    728 LRVKVISGQFLSDRKVG----IYVEVDMFGlpvDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:smart00239    2 LTVKIISARNLPPKDKGgksdPYVKVSLDG---DPKEKKKTKVVK-NTLNPVWNET-FEFE-VPPPELAELEIEVYDKDR 75
                            90       100
                    ....*....|....*....|....*.
gi 148745659    804 ----KFVGHRILPVSAIRSGYHYVCL 825
Cdd:smart00239   76 fgrdDFIGQVTIPLSDLLLGGRHEKL 101
PH_PLC_ELMO1 cd01248
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ...
22-138 6.97e-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: 62.34  E-value: 6.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   22 LRRGSKFIKWDEEtSSRNLVTLRVDPNGFFLYWTGP--NMEVDTLDISSIRDTRTGRYARLPKDpkirevlgFGGPDARL 99
Cdd:cd01248     1 LQQGTLLLKYREG-SKPKERTFYLDPDGTRITWESSkkKSEKKSIDISDIKEIRPGKDTDGFKR--------KKKSNKPK 71
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 148745659  100 EEKLMTVVSGPdpvNTVFLNFMAVQDDTAKVWSEELFKL 138
Cdd:cd01248    72 EERCFSIIYGS---NNKTLDLVAPSEDEANLWVEGLRAL 107
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
165-304 1.80e-08

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  Cd Length: 140  Bit Score: 55.24  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  165 NQDGRI---PVKNILKMFSADKKRvETALEScglkFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPyL 241
Cdd:cd16219    12 NKDGRMnfkEVRDLLKMMNVDMNE-EHALRL----FQMADKSESGTLEGEEFVLFYKALTQREDVLKIFQDFSADGQK-L 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148745659  242 TLEQLMDFINQKQRDPRLNEVLypplrpsqARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16219    86 TLLEFVDFLQQEQLERENTEEL--------AMELIDRYEPSDTAKKLHALSIDGFLMYLCSPE 140
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
216-308 4.45e-08

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: 312695  Cd Length: 85  Bit Score: 53.41  E-value: 4.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   216 FLNKLCLRPDIDKILLEIGAKGKpYLTLEQLMDFINQKQRDPRLNevlypplrPSQARLLIEKYEPNQQFLERDQMSMEG 295
Cdd:pfam09279    1 FYKMLTQREEIDRIFQEYSGDGQ-KLSLDELVDFLREEQREEDAS--------PALALELIERYEPSETAKKQHAMTKDG 71
                           90
                   ....*....|...
gi 148745659   296 FSRYLGGEENGIL 308
Cdd:pfam09279   72 FLMYLLSPDGSIF 84
C2 pfam00168
C2 domain;
728-822 2.99e-07

C2 domain;


Pssm-ID: 306639  Cd Length: 104  Bit Score: 51.16  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   728 LRVKVISGQFLSDRKVGI----YVEVDMfglpVDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:pfam00168    3 LRVTVIEAKNLPPKDLNGksdpYVKVYL----LDGKQKKKTKVVK-NTLNPVWNET-FTFS-VPDPENAVLEIEVYDYDR 75
                           90       100
                   ....*....|....*....|...
gi 148745659   804 ----KFVGHRILPVSAIRSGYHY 822
Cdd:pfam00168   76 fgrdDFIGEVRIPLSELDSGEVL 98
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1026-1189 5.90e-07

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 53.95  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1026 DEAKRYQEFQNrqvqsllELREAQVdAEAQRRLEHLRQALQRLREVV------LDANTTQFKRLKEMNEREKKELQKIld 1099
Cdd:COG1196   210 EKAERYQELKA-------ELRELEL-ALLLAKLKELRKELEELEEELsrleeeLEELQEELEEAEKEIEELKSELEEL-- 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1100 rKRHNSISEAKMRDKHKKEAEL---TEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVL--QQLAEEEPKLLAQLAQ 1174
Cdd:COG1196   280 -REELEELQEELLELKEEIEELegeISLLRERLEELENELEELEERLEELKEKIEALKEELEerETLLEELEQLLAELEE 358
                         170
                  ....*....|....*
gi 148745659 1175 ECQEQRARLPQEIRR 1189
Cdd:COG1196   359 AKEELEEKLSALLEE 373
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
197-300 7.11e-07

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  Cd Length: 142  Bit Score: 50.33  E-value: 7.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  197 FNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDprlnevlypPLRPSQARLLI 276
Cdd:cd16207    44 FDKADTDKKGYLNFEEFQEFVKLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKE---------DVDRETWEKIF 114
                          90       100
                  ....*....|....*....|....
gi 148745659  277 EKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16207   115 EKFARRIDDSDSLTMTLEGFTSFL 138
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1019-1187 7.85e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 53.53  E-value: 7.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1019 EDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDA-----EAQRRLEHLRQALQRLREVV--LDANTTQFKRLKEMNEREK 1091
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrkigEIEKEIEQLEQEEEKLKERLeeLEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1092 KELQKILDRKRhnsiseakmRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVA---------GQQQVLQQLA 1162
Cdd:TIGR02169  761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreieqklNRLTLEKEYL 831
                          170       180
                   ....*....|....*....|....*
gi 148745659  1163 EEEPKLLAQLAQECQEQRARLPQEI 1187
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEI 856
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
211-304 1.14e-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  Cd Length: 139  Bit Score: 49.74  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  211 EIfERFLNKLCLRPDIDKILLEIgAKGKPYLTLEQLMDFINQKQRDPrlnevlyppLRPSQARLLIEKYEPNQQFLERDQ 290
Cdd:cd16217    57 EI-EEFYKLLTKREEIDVIFGEY-AKSDGTMSRNNLLNFLQEEQREE---------VAPAYALSLIEKYEPDETAKAQRQ 125
                          90
                  ....*....|....
gi 148745659  291 MSMEGFSRYLGGEE 304
Cdd:cd16217   126 MTKDGFLMYLLSPE 139
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
1025-1187 2.32e-06

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 317717  Cd Length: 142  Bit Score: 48.81  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1025 EDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDAnttqfKRLKEMNEREKKElqkildrkrhn 1104
Cdd:pfam15346   10 EETARRVEEAVRKRVEEELNKRSEEIEAEIERRVEEARKAMEKQVLEELER-----EREAELEEARRKE----------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1105 sisEAKMRDKHKKEAELTEINrrhitesvnsiRRLEEAQ-KQRHDRLVAGQQQvlQQLAEEEPKLLAQlaqecQEQRARL 1183
Cdd:pfam15346   74 ---EEERKKREELERILEENN-----------RKVEEAQrKLAEERLAELEEQ--QRQKEERQRRKKE-----EEEEEKA 132

                   ....
gi 148745659  1184 PQEI 1187
Cdd:pfam15346  133 EQEK 136
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
960-1182 2.55e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 316391  Cd Length: 352  Bit Score: 51.05  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   960 HKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRpgalggaADVEDTKEGEDEAKRYQEFQNRQV 1039
Cdd:pfam13868   31 KKRIKAEEKEEERRLDEMMEEERLKALEEEEEKERERKEKRKEYRQELQ-------EQIEEREQKRQLEYEEKLQEKEQI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1040 QSLLElreaQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILdrkrhnsiseAKMRDKHKKEA 1119
Cdd:pfam13868  104 DEIVE----RIQEEDQAEAEEKLEKQKELREEIDEFNEEQKERKEQEKEEEREEDERIL----------EYLREKEEREE 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148745659  1120 ELTEinrrhitesvnSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEpKLLAQLAQECQEQRAR 1182
Cdd:pfam13868  170 EREA-----------ERREIEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEAERKWR 220
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1019-1197 3.83e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 51.30  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1019 EDTKEGEDEAKRYQEFQN---------RQVQSLLELREAQVDaEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNER 1089
Cdd:COG0419   488 EELSREKEEAELREEIEElekelreleEELIELLELEEALKE-ELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLED 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1090 EKKELQKILDRKRHNSISEAKMRDKHKKEAEL---------------TEINRRHITESVNSIRRLEE---AQKQRHDrlv 1151
Cdd:COG0419   567 RLQELKELLEELRLLRTRKEELEELRERLKELkkklkeleerlsqleELLQSLELSEAENELEEAEEeleSELEKLN--- 643
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 148745659 1152 agQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEI--RRSLLGEMPE 1197
Cdd:COG0419   644 --LQAELEELLQAALEELEEKVEELEAEIRRELQRIenEEQLEEKLEE 689
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
1029-1189 4.50e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 318010  Cd Length: 520  Bit Score: 50.77  E-value: 4.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1029 KRYQEFQNRQVQSLLEL---REAQVDAEAQRRLEHLRQALQRLREvvldanttqfkrlkEMNEREKKElqkildRKRHNS 1105
Cdd:pfam15709  352 RREQEEQRRLQQEQLERaekMKEELELEQQRRAEEIRLRKQRLEE--------------EQQRQEEEE------RKQRLQ 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1106 ISEAKMRDKHKKEA---ELTEINRRHITESVNSirrlEEAQKQRHDRL---VAGQQQVLQQLAEEEpKLLAQLAQECQEQ 1179
Cdd:pfam15709  412 LQAAQERARQQQEEfrrKLQELQRKKQQEEAER----AEAEKQRQKELemqLAEEQKRLMEMAEEE-RLEYQRQKQEAEE 486
                          170
                   ....*....|
gi 148745659  1180 RARLPQEIRR 1189
Cdd:pfam15709  487 KAQLEAEERR 496
EFh_PI-PLCzeta cd16204
EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, ...
197-304 5.20e-06

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  Cd Length: 142  Bit Score: 47.50  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  197 FNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILlEIGAKGKPYLTLEQLMDFINQKQRDPRLNEvlypplrpSQARLLI 276
Cdd:cd16204    44 FKKNDSFKAGNITIEDFRAIYRAIAHRCEIHEIF-NTYSENRKILSAPNLVGFLKKEQFQDEADE--------TIASELI 114
                          90       100
                  ....*....|....*....|....*...
gi 148745659  277 EKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16204   115 AKYEPIEEVRKRKQMSFEGFIRYMTSED 142
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
968-1199 5.23e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 50.83  E-value: 5.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   968 SRQERDLRELRKKHQRKAVTLTRRlldGLAQAQAEGRCRLRPGALGGAAdvEDTKEGEDEAKRYQEFQNRQVQSLLELRE 1047
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQL---SKELTELEAEIEELEERLEEAE--EELAEAEAEIEELEAQIEQLKEELKALRE 803
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1048 AQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRR 1127
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148745659  1128 HITESVNSIR-RLEEAQKQRHDrlVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRR-----SLLGEMPEGL 1199
Cdd:TIGR02168  884 SLEEALALLRsELEELSEELRE--LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEAL 959
EFh_PRIP2 cd16223
EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); ...
161-300 7.06e-06

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  Cd Length: 144  Bit Score: 47.21  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  161 KLQVNQDGRIPVKNILKMFSADKKRVETAleSCGLKF---NRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKg 237
Cdd:cd16223     8 EADTDNVGHITLCRAVQFIKNLNPGLKTS--KIELKFkelHKSKEKGGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSN- 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148745659  238 KPYLTLEQLMDFINQKQRDPRLNEvlypplrpsQARL-LIEKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16223    85 KEFLDTKDLMMFLEAEQGMAHVTE---------EISLdIIHKYEPSKEGQEKGWLSLDGFTNYL 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
954-1195 8.20e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 50.06  E-value: 8.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   954 LDELRGHKALVKlrsRQERDLRELRKKHQRKAVTLTRRLLD-GLAQAQAEGRCRLRPGALGGAADVEDTKEGEdeaKRYQ 1032
Cdd:TIGR02168  234 LEELREELEELQ---EELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRLEQQ---KQIL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1033 EFQNRQVQSLLELREAQVDaEAQRRLEHLRQALQRLREVVLDANTtQFKRLKEMNEREKKELQkilDRKRHNSISEAKMR 1112
Cdd:TIGR02168  308 RERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEELKE-ELESLEAELEELEAELE---ELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1113 DKHKKEAELT----------EINRRHITESVNSIRRL-----------EEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQ 1171
Cdd:TIGR02168  383 TLRSKVAQLElqiaslnneiERLEARLERLEDRRERLqqeieellkklEEAELKELQAELEELEEELEELQEELERLEEA 462
                          250       260
                   ....*....|....*....|....
gi 148745659  1172 LAQecQEQRARLPQEIRRSLLGEM 1195
Cdd:TIGR02168  463 LEE--LREELEEAEQALDAAEREL 484
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
209-304 1.00e-05

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  Cd Length: 143  Bit Score: 46.82  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  209 SLEIFERFLNKLCLRPDIDKILLEIgAKGKPYLTLEQLMDFINQKQRDPRLNEvlypplrpSQARLLIEKYEPNQQFLER 288
Cdd:cd16206    57 SSDEFVELFKELATRPEIYFLLVRY-ASNKDYLTVDDLMLFLEAEQGMTGVTK--------EKCLEIINKYEPSEEGREK 127
                          90
                  ....*....|....*.
gi 148745659  289 DQMSMEGFSRYLGGEE 304
Cdd:cd16206   128 GQLGIDGFTRYLLSEE 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
728-796 1.03e-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  Cd Length: 102  Bit Score: 46.29  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148745659  728 LRVKVISGQFLSDRKVGI----YVEVDmfglpVDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRI 796
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGksdpYVKVS-----LGGKQKFKTKVVK-NTLNPVWNET-FEFP-VLDPESDTLTV 65
PTZ00121 PTZ00121
MAEBL; Provisional
955-1189 1.26e-05

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 49.75  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  955 DELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRlrpgalgGAADVEDTKEGeDEAKRYQEF 1034
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-------EAKKAEEKKKA-DELKKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1035 QN-RQVQSLLELREAQVDAE-AQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMR 1112
Cdd:PTZ00121 1558 KKaEEKKKAEEAKKAEEDKNmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148745659 1113 DKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQqqvLQQLAEEEPKLLAQLAQECQEqrARLPQEIRR 1189
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE---AKKAEEDEKKAAEALKKEAEE--AKKAEELKK 1709
PTZ00121 PTZ00121
MAEBL; Provisional
955-1189 1.40e-05

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 49.37  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  955 DELRghKALVKLRSRQERDLRELRKKHQRKAVTLTRRlldglaqaqAEGRcrlRPGALGGAADVEDTKEG--EDEAKRYQ 1032
Cdd:PTZ00121 1537 DEAK--KAEEKKKADELKKAEELKKAEEKKKAEEAKK---------AEED---KNMALRKAEEAKKAEEAriEEVMKLYE 1602
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1033 EFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQrlrevvldanttQFKRLKEMNEREKKELQKILDRKRHNSISEAKMR 1112
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE------------QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659 1113 DKHKKEAE---LTEINRRHITESVNsiRRLEEAQK-QRHDRLVAGQQQVLQQL--AEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:PTZ00121 1671 EEDKKKAEeakKAEEDEKKAAEALK--KEAEEAKKaEELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEEDKKKAEE 1748

                  ...
gi 148745659 1187 IRR 1189
Cdd:PTZ00121 1749 AKK 1751
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
165-300 1.45e-05

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  Cd Length: 138  Bit Score: 46.28  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  165 NQDGRIP---VKNILKMFSADKKRVETAL--ESCglkfNRSESIRPDEfsLEIfERFLNKLCLRPDIDKILLEIGAKGKp 239
Cdd:cd16218    12 NKDGKMSfeeIKDLLQMINIDLNEQYAYQlfKEC----DRSNDDRLEE--HEI-EEFCRRLMQRPELEEIFHQYSGEDC- 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148745659  240 YLTLEQLMDFINQKQRDPRLnevlypplrpSQARLLIEKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16218    84 VLSAEELREFLKDQGEDASL----------VHAKELIQTYELNEKAKQHQLMTLDGFTMYM 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
965-1194 1.47e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 49.28  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   965 KLRSRQERDLRELRKKHQRKAVTLTRRL-LDGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEA-KRYQEFQNR--QVQ 1040
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELrAELTLLNEEaaNLR 823
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1041 SLLELREAQVdAEAQRRLEHLRQALQRLREVVLDANTtQFKRLKEMNEREKKELQKILDRK--------RHNSISEAKMR 1112
Cdd:TIGR02168  824 ERLESLERRI-AATERRLEDLEEQIEELSEDIESLAA-EIEELEELIEELESELEALLNERasleealaLLRSELEELSE 901
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1113 DKHKKEAELTEINR--RHITESVNSIRRLEEAQKQRHDRL---VAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEI 1187
Cdd:TIGR02168  902 ELRELESKRSELRRelEELREKLAQLELRLEGLEVRIDNLqerLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981

                   ....*..
gi 148745659  1188 RRslLGE 1194
Cdd:TIGR02168  982 KE--LGP 986
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
967-1191 3.11e-05

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  Cd Length: 1042  Bit Score: 48.43  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659   967 RSRQERDLRELRKKHQrKAVTLTRRLldGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFQNRQVQSLLELR 1046
Cdd:TIGR00618  255 QLKKQQLLKQLRARIE-ELRAQEAVL--EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1047 EAQVDAEAQRRLEHLRQALQRLREVVLDANTTQfKRLKEMNEREKKELQKIldRKRHNSISEAKMRDKHKKEAELTEINR 1126
Cdd:TIGR00618  332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTLTQHI--HTLQQQKTTLTQKLQSLCKELDILQRE 408
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148745659  1127 RHITESVNSIRRLEEAQKqrhdrLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSL 1191
Cdd:TIGR00618  409 QATIDTRTSAFRDLQGQL-----AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
1019-1175 3.12e-05

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011  Cd Length: 489  Bit Score: 47.69  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1019 EDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRleHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKil 1098
Cdd:pfam05262  210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRD--EVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEK-- 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148745659  1099 drkrhnSISEAKMRD---KHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDrlVAGQQQVLQQLAEEEPKLLAQLAQE 1175
Cdd:pfam05262  286 ------AQIEIKKNDeeaLKAKDHKAFDLKQESKASEKEAEDKELEAQKKREP--VAEDLQKTKPQVEAQPTSLNEDAID 357
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
161-300 4.66e-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  Cd Length: 141  Bit Score: 44.68  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|