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Conserved domains on  [gi|11386139|ref|NP_000923|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 isoform 1 [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 4.65e-180

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


:

Pssm-ID: 176562 [Multi-domain]  Cd Length: 258  Bit Score: 529.63  E-value: 4.65e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08625    1 SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08625   81 IAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08625      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08625  155 ----------------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPME 200

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139  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 2.95e-100

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: 2.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEI 233
Cdd:cd16210    1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386139  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 6.77e-72

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


:

Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 237.27  E-value: 6.77e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1029 KRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISE 1108
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1109 AKMRDKHK-KEAELT-EINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:pfam08703   81 AKKRTSDKaAQERLKkEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 11386139   1187 IRRSLLGEMPEGLGDG 1202
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 22-149 3.72e-62

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


:

Pssm-ID: 270167  Cd Length: 127  Bit Score: 207.42  E-value: 3.72e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   22 LRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVlGFGGPDARLEE 101
Cdd:cd13361    1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 11386139  102 KLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASR 149
Cdd:cd13361   80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PLN02952 super family cl31960
phosphoinositide phospholipase C
 318-833 1.67e-60

phosphoinositide phospholipase C


The actual alignment was detected with superfamily member PLN02952:

Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 219.10  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:PLN02952  124 DMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGS-TKDEILVLHGRTLTTPVPLIKCLKSIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepldkYPLAPG-VPLPSPQDLMGRILVKNKkrhrPSag 476
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTK----PP-- 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   477 gpdsagrKRPLEQSNSALSESSAATEPSSPQlGSPSSDscpglsngEEVGLEKPSLEPQ---KSLGDEGLNRGPYVLGPA 553
Cdd:PLN02952  270 -------KEYLESSGPIVIKKKNNVSPSGRN-SSEETE--------EAQTLESMLFEQEadsRSDSDQDDNKSGELQKPA 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   554 DRedeeedeeeeeqtdpKKPTTDEGTASSEVNatEEMSTLVNYIEPVkfksfeaarkrnkcfemsSFVETKAMEQLTKSP 633
Cdd:PLN02952  334 YK---------------RLITIHAGKPKGTLK--DAMKVAVDKVRRL------------------SLSEQELEKAATTNG 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   634 MEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRP---DK 710
Cdd:PLN02952  379 QDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKgfhDE 458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   711 SFDPFTEVivdgIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDEEp 780
Cdd:PLN02952  459 VFDPKKKL----PVKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK-KTKIIEDN-WYPAWNEE- 531

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139   781 FDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEANQPL 833
Cdd:PLN02952  532 FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
DUF1154 super family cl05918
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 951-990 1.83e-03

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


The actual alignment was detected with superfamily member pfam06631:

Pssm-ID: 461969  Cd Length: 45  Bit Score: 37.24  E-value: 1.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 11386139    951 PTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTR 990
Cdd:pfam06631    6 PITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PRK06975 super family cl35524
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 873-1066 5.24e-03

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


The actual alignment was detected with superfamily member PRK06975:

Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.86  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   873 ARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPldASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPT 952
Cdd:PRK06975  256 ERIVRAFLTWADAAAQPATAAPAPSRMTDTNDSKSVTSQP--AAAAAAPAPPPNPPATPPEPPARRGRGSAALWFVVVVL 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   953 PLDELRGHKALVKLRSRQERDLRELRKK---HQRKAVTLTRRLLDGLAQAQAEgrcrlrPGALggaadveDTKEGEDEAK 1029
Cdd:PRK06975  334 ACAAAVGGYALNRKVDRLDQELVQRQQAndaQTAELRVKTEQAQASVHQLDSQ------FAQL-------DGKLADAQSA 400

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 11386139  1030 ryQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQ 1066
Cdd:PRK06975  401 --QQALEQQYQDLSRNRDDWMIAEVEQMLSSASQQLQ 435
 
Name Accession Description Interval E-value
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 316-693 4.65e-180

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


Pssm-ID: 176562 [Multi-domain]  Cd Length: 258  Bit Score: 529.63  E-value: 4.65e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08625    1 SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08625   81 IAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08625      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08625  155 ----------------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPME 200

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139  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 2.95e-100

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: 2.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEI 233
Cdd:cd16210    1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386139  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 1.39e-74

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 243.18  E-value: 1.39e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    319 MTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIAE 398
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11386139    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 6.77e-72

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 237.27  E-value: 6.77e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1029 KRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISE 1108
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1109 AKMRDKHK-KEAELT-EINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:pfam08703   81 AKKRTSDKaAQERLKkEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 11386139   1187 IRRSLLGEMPEGLGDG 1202
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 591-705 1.23e-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 [Multi-domain]  Cd Length: 115  Bit Score: 217.11  E-value: 1.23e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     591 STLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQ 670
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 11386139     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 3.72e-62

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


Pssm-ID: 270167  Cd Length: 127  Bit Score: 207.42  E-value: 3.72e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   22 LRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVlGFGGPDARLEE 101
Cdd:cd13361    1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 11386139  102 KLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASR 149
Cdd:cd13361   80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PLN02952 PLN02952
phosphoinositide phospholipase C
 318-833 1.67e-60

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 219.10  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:PLN02952  124 DMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGS-TKDEILVLHGRTLTTPVPLIKCLKSIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepldkYPLAPG-VPLPSPQDLMGRILVKNKkrhrPSag 476
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTK----PP-- 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   477 gpdsagrKRPLEQSNSALSESSAATEPSSPQlGSPSSDscpglsngEEVGLEKPSLEPQ---KSLGDEGLNRGPYVLGPA 553
Cdd:PLN02952  270 -------KEYLESSGPIVIKKKNNVSPSGRN-SSEETE--------EAQTLESMLFEQEadsRSDSDQDDNKSGELQKPA 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   554 DRedeeedeeeeeqtdpKKPTTDEGTASSEVNatEEMSTLVNYIEPVkfksfeaarkrnkcfemsSFVETKAMEQLTKSP 633
Cdd:PLN02952  334 YK---------------RLITIHAGKPKGTLK--DAMKVAVDKVRRL------------------SLSEQELEKAATTNG 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   634 MEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRP---DK 710
Cdd:PLN02952  379 QDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKgfhDE 458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   711 SFDPFTEVivdgIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDEEp 780
Cdd:PLN02952  459 VFDPKKKL----PVKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK-KTKIIEDN-WYPAWNEE- 531

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139   781 FDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEANQPL 833
Cdd:PLN02952  532 FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 17-146 5.35e-48

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 167.17  E-value: 5.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     17 TVVETLRRGSKFIKWDEETSSRN-LVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGP 95
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEpNVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 11386139     96 DARLEEKLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQN 146
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 728-843 8.71e-37

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


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 134.98  E-value: 8.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  728 LRVKVISGQFLSD------RKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEE 801
Cdd:cd00275    4 LTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTKVVKNNGFNPVWNET-FEFD-VTVPELAFLRFVVYDE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 11386139  802 GG---KFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTE 843
Cdd:cd00275   82 DSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHID 126
PLN02223 PLN02223
phosphoinositide phospholipase C
 318-828 1.37e-24

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 109.73  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   318 DMTQPLSAYFINSSHNTYLTAGQLAGTS-SVEMYRQALLWGCRCVELDVWkgrpPEEEPFITHGFTMTTEVPLR--DVLE 394
Cdd:PLN02223  107 DMHAPLSHYFIHTSLKSYFTGNNVFGKLySIEPIIDALEQGVRVVELDLL----PDGKDGICVRPKWNFEKPLElqECLD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   395 AIAETAF-KTSPYPVILSFEnhvDSAKQ--QAKMAEYCRSIFGDALLIEPldkyPLAPGVPLPSPQDLMGRILVKNKkrh 471
Cdd:PLN02223  183 AIKEHAFtKCRSYPLIITFK---DGLKPdlQSKATQMIDQTFGDMVYHED----PQHSLEEFPSPAELQNKILISRR--- 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   472 rpsaggpdsagrkrpleqsnsalsessaatePSSPQLGSPSSDSCPGLSNGEEVglekpslepqkslgdeglNRGPyvlg 551
Cdd:PLN02223  253 -------------------------------PPKELLYAKADDGGVGVRNELEI------------------QEGP---- 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   552 padredeeedeeeeeqTDPkkpttdegtassevnateemstlvNYIEPVKFKSFEAARKRNKCFEMSSfvetKAMEQLTK 631
Cdd:PLN02223  280 ----------------ADK------------------------NYQSLVGFHAVEPRGMLQKALTGKA----DDIQQPGW 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   632 SPMEFVEYNKQQLSRIYPKGTRVDS-SNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRR--P 708
Cdd:PLN02223  316 YERDIISFTQKKFLRTRPKKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagP 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   709 DKSFDPftevIVDGIVANALRVKVISGQ-FLSD--RKVG------IYVEVDMFGLPVDtrRKYRTRTSQGNSFNPVWDEE 779
Cdd:PLN02223  396 SGVFYP----TENPVVVKILKVKIYMGDgWIVDfkKRIGrlskpdLYVRISIAGVPHD--EKIMKTTVKNNEWKPTWGEE 469

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 11386139   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 2.05e-13

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


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 67.51  E-value: 2.05e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     728 LRVKVISGQFLSDRKVG----IYVEVDMFGlpvDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:smart00239    2 LTVKIISARNLPPKDKGgksdPYVKVSLDG---DPKEKKKTKVVK-NTLNPVWNET-FEFE-VPPPELAELEIEVYDKDR 75

                            90       100
                    ....*....|....*....|....*.
gi 11386139     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 7.11e-09

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


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 53.79  E-value: 7.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    216 FLNKLCLRPDIDKILLEIGAKGKpYLTLEQLMDFINQKQRDPRLNevlypplrPSQARLLIEKYEPNQQFLERDQMSMEG 295
Cdd:pfam09279    1 FYKMLTQREEIDEIFQEYSGDGQ-KLSLDELVDFLREEQREEDAS--------PALALSLIERYEPSETAKKQHAMTKDG 71

                           90
                   ....*....|...
gi 11386139    296 FSRYLGGEENGIL 308
Cdd:pfam09279   72 FLMYLCSPDGSIF 84
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
955-1184 5.80e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  955 DELRG-HKALVKLRsRQERDLRELRKKHQRkavtlTRRLLDGLAQAQAEGRcRLRPgalggaadvedtkegEDEAKRYQE 1033
Cdd:COG4913  235 DDLERaHEALEDAR-EQIELLEPIRELAER-----YAAARERLAELEYLRA-ALRL---------------WFAQRRLEL 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1034 FQNRQVQSLLELREAQVD-AEAQRRLEHLRQALQRLREVVLDANTTQFKRLkemnEREKKELQKILDRKRHNS------I 1106
Cdd:COG4913  293 LEAELEELRAELARLEAElERLEARLDALREELDELEAQIRGNGGDRLEQL----EREIERLERELEERERRRarlealL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1107 SEAKMRDKHkKEAELTEiNRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEE-------------P----KLL 1169
Cdd:COG4913  369 AALGLPLPA-SAEEFAA-LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeiaslerrksniParllALR 446

                        250
                 ....*....|....*
gi 11386139 1170 AQLAQECQEQRARLP 1184
Cdd:COG4913  447 DALAEALGLDEAELP 461
C2 pfam00168
C2 domain;
728-822 7.15e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 51.55  E-value: 7.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    728 LRVKVISGQFLSDRKVGI----YVEVDMfglpVDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:pfam00168    3 LTVTVIEAKNLPPKDGNGtsdpYVKVYL----LDGKQKKKTKVVK-NTLNPVWNET-FTFS-VPDPENAVLEIEVYDYDR 75

                           90       100
                   ....*....|....*....|...
gi 11386139    804 ----KFVGHRILPVSAIRSGYHY 822
Cdd:pfam00168   76 fgrdDFIGEVRIPLSELDSGEGL 98
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1019-1187 9.20e-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 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 9.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1019 EDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDA-----EAQRRLEHLRQALQRLREVV--LDANTTQFKRLKEMNEREK 1091
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrkigEIEKEIEQLEQEEEKLKERLeeLEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1092 KELQKILDRKRhnsiseakmRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVA---------GQQQVLQQLA 1162
Cdd:TIGR02169  761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreieqklNRLTLEKEYL 831

                          170       180
                   ....*....|....*....|....*
gi 11386139   1163 EEEPKLLAQLAQECQEQRARLPQEI 1187
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEI 856
PTZ00121 PTZ00121
MAEBL; Provisional
 955-1189 1.48e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   955 DELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRlrpgalgGAADVEDTKEGeDEAKRYQEF 1034
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-------EAKKAEEKKKA-DELKKAEEL 1557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1035 QN-RQVQSLLELREAQVDAE-AQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMR 1112
Cdd:PTZ00121 1558 KKaEEKKKAEEAKKAEEDKNmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  1113 DKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQqqvLQQLAEEEPKLLAQLAQECQEqrARLPQEIRR 1189
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE---AKKAEEDEKKAAEALKKEAEE--AKKAEELKK 1709
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 951-990 1.83e-03

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


Pssm-ID: 461969  Cd Length: 45  Bit Score: 37.24  E-value: 1.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 11386139    951 PTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTR 990
Cdd:pfam06631    6 PITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 873-1066 5.24e-03

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


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.86  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   873 ARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPldASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPT 952
Cdd:PRK06975  256 ERIVRAFLTWADAAAQPATAAPAPSRMTDTNDSKSVTSQP--AAAAAAPAPPPNPPATPPEPPARRGRGSAALWFVVVVL 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   953 PLDELRGHKALVKLRSRQERDLRELRKK---HQRKAVTLTRRLLDGLAQAQAEgrcrlrPGALggaadveDTKEGEDEAK 1029
Cdd:PRK06975  334 ACAAAVGGYALNRKVDRLDQELVQRQQAndaQTAELRVKTEQAQASVHQLDSQ------FAQL-------DGKLADAQSA 400

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 11386139  1030 ryQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQ 1066
Cdd:PRK06975  401 --QQALEQQYQDLSRNRDDWMIAEVEQMLSSASQQLQ 435
 
Name Accession Description Interval E-value
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 316-693 4.65e-180

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


Pssm-ID: 176562 [Multi-domain]  Cd Length: 258  Bit Score: 529.63  E-value: 4.65e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08625    1 SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08625   81 IAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08625      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08625  155 ----------------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPME 200

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139  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 3.23e-179

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


Pssm-ID: 176533 [Multi-domain]  Cd Length: 257  Bit Score: 527.29  E-value: 3.23e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08591    1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  396 IAETAFKTSPYPVILSFENHVDSaKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08591   81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08591      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08591  154 ----------------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIE 199

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139  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 4.96e-148

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


Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 446.04  E-value: 4.96e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08624    1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08624   81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08624      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  556 edeeedeeeeeqtdpkkpttdegtassevnaTEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08624  155 -------------------------------YEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQ 203

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139  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 2.17e-138

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


Pssm-ID: 176560 [Multi-domain]  Cd Length: 258  Bit Score: 420.64  E-value: 2.17e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08623    1 NEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  396 IAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08623   81 IAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  476 ggpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08623      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  556 edeeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPME 635
Cdd:cd08623  155 ----------------------------------MSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVE 200

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139  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 9.91e-127

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


Pssm-ID: 176501 [Multi-domain]  Cd Length: 226  Bit Score: 388.35  E-value: 9.91e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08558    3 DMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEAIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPlapgVPLPSPQDLMGRILVKNKKRHrpsagg 477
Cdd:cd08558   81 EYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKKYH------ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08558      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcfeMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08558  150 -----------------------------------------------------------MSSFSETKALKLLKESPEEFV 170

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 1.03e-118

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


Pssm-ID: 176563 [Multi-domain]  Cd Length: 257  Bit Score: 368.71  E-value: 1.03e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08626    3 DMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08626   83 DTAFVTSDYPVILSFENHC-SKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR-------- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08626      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08626  154 --------------------------------LSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFV 201

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 7.79e-108

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


Pssm-ID: 176535 [Multi-domain]  Cd Length: 257  Bit Score: 339.31  E-value: 7.79e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08593    3 DMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQAIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKRHrpsagg 477
Cdd:cd08593   81 EYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKKLK------ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsaLSessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08593  150 ----------------LA-------------------------------------------------------------- 151

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnatEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08593  152 ------------------------------KELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFV 201

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 2.95e-100

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: 2.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEI 233
Cdd:cd16210    1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386139  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 3.81e-87

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


Pssm-ID: 176539 [Multi-domain]  Cd Length: 260  Bit Score: 283.16  E-value: 3.81e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08597    3 DMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKyplaPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08597   81 EYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEPPNE----GESYLPSPHDLKGKIIIKGKK-------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevgLEKPSLepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08597  148 -------------------------------------------------LKRRKL------------------------- 153

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnaTEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08597  154 -----------------------------CKELSDLVSLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFV 204

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08597  205 NYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 316-690 1.54e-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 [Multi-domain]  Cd Length: 231  Bit Score: 263.72  E-value: 1.54e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEA 395
Cdd:cd08598    1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  396 IAETAFKTSPYPVILSFENHVDSAkQQAKMAEYCRSIFGDALLIEPLDkyPLAPGvpLPSPQDLMGRILVKNKKrhrpsa 475
Cdd:cd08598   79 IKKYAFVTSPYPLILSLEVHCDAE-QQERMVEIMKETFGDLLVTEPLD--GLEDE--LPSPEELRGKILIKVKK------ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  476 ggpdsagrkrpleqsnsalsessaatEPSSPqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadr 555
Cdd:cd08598  148 --------------------------ESKTP------------------------------------------------- 152

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  556 edeeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrNKCFemsSFVETKAMEQLTKSPME 635
Cdd:cd08598  153 --------------------------------------------------------NHIF---SLSERSLLKLLKDKRAA 173

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 11386139  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 3.22e-79

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


Pssm-ID: 176534 [Multi-domain]  Cd Length: 229  Bit Score: 260.05  E-value: 3.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08592    3 DMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKRHRpsagg 477
Cdd:cd08592   81 EHAFVTSEYPVILSIENHC-SLPQQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKKLFY----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08592      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcfEMSSFVETKAMEQLTKS-PMEF 636
Cdd:cd08592  151 ----------------------------------------------------------EMSSFPETKAEKYLNRQkGKIF 172

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  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 7.39e-76

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


Pssm-ID: 176537 [Multi-domain]  Cd Length: 257  Bit Score: 251.78  E-value: 7.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08595    3 DMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDG--ADNEPVVYHGYTLTSKILFKEVITTVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLApgvPLPSPQDLMGRILVKNKKRhrpsagg 477
Cdd:cd08595   81 KYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKKK------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpYVLGpadred 557
Cdd:cd08595  150 ----------------------------------------------------------------------IAKA------ 153

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnateeMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08595  154 --------------------------------LSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFV 201

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 7.89e-76

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


Pssm-ID: 176568 [Multi-domain]  Cd Length: 258  Bit Score: 251.79  E-value: 7.89e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08631    3 DMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLD-KYPlapgVPLPSPQDLMGRILVKNKKrhrpsag 476
Cdd:cd08631   81 QYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKK------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  477 gpdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadre 556
Cdd:cd08631      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  557 deeedeeeeeqtdpkkpttdegtasseVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEF 636
Cdd:cd08631  149 ---------------------------IRLSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEF 201

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08631  202 VQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 318-693 1.19e-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 [Multi-domain]  Cd Length: 258  Bit Score: 251.11  E-value: 1.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08629    3 DMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRAIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08629   81 DYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLD----GVTTSLPSPEQLKGKILLKGKK-------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08629      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtasseVNATEEMSTLVNYIEPVKFKSFEAARKRNKCF-EMSSFVETKAMEQLTKSPMEF 636
Cdd:cd08629  148 --------------------------LKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFyEMASFSESRALRLLQESGNGF 201

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08629  202 VRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 319-467 1.39e-74

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 243.18  E-value: 1.39e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    319 MTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIAE 398
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11386139    399 TAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKyplaPGVPLPSPQDLMGRILVKN 467
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLDD----DLTELPSPEDLKGKILIKG 142
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 318-693 2.31e-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 [Multi-domain]  Cd Length: 258  Bit Score: 244.55  E-value: 2.31e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08630    3 DMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLApgvPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08630   81 QHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKK-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08630      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeEQTDPkkpttdegtassevnateEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08630  149 --------LQISP------------------ELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFV 202

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 7.35e-73

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


Pssm-ID: 176538 [Multi-domain]  Cd Length: 254  Bit Score: 243.22  E-value: 7.35e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRppEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08596    3 DLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08596   81 RSAFITSDYPVILSIENHC-SLQQQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08596      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnaTEEMSTLVNYIEPVKFKSFEAArkrnKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08596  152 -----------------------------APELSDLVIYCQAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLV 198

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 6.77e-72

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 237.27  E-value: 6.77e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1029 KRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISE 1108
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1109 AKMRDKHK-KEAELT-EINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:pfam08703   81 AKKRTSDKaAQERLKkEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 11386139   1187 IRRSLLGEMPEGLGDG 1202
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 154-304 5.65e-71

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


Pssm-ID: 320030 [Multi-domain]  Cd Length: 153  Bit Score: 233.68  E-value: 5.65e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILL 231
Cdd:cd16200    1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDKkrKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139  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 4.17e-69

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: 4.17e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  155 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIG 234
Cdd:cd16208    2 KAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEFG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  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 1.07e-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 [Multi-domain]  Cd Length: 227  Bit Score: 227.38  E-value: 1.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08594    3 DMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIETIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepLDKYPLAPGVPLPSPQDLMGRILVKNKKrhrpsagg 477
Cdd:cd08594   81 KYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKK-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08594      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08594  149 ---------------------------------------------------------WQVSSFSETRAHQIVQQKAAQFL 171

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 1.04e-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 [Multi-domain]  Cd Length: 254  Bit Score: 225.70  E-value: 1.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08628    3 DMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVDsAKQQAKMAEYCRSIFGDALLIEPLDkyplAPGVPLPSPQDLMGRILVKNKKRhrpsagg 477
Cdd:cd08628   81 DHAFVTSEYPVILSIEEHCS-VEQQRHMAKVFKEVFGDKLLMKPLE----ASADQLPSPTQLKEKIIIKHKKL------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08628      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnATEEMSTLVNYIEPvkfKSFEAARKRNKCF-EMSSFVETKAMEQLTKSPMEF 636
Cdd:cd08628  149 ----------------------------IAIELSDLVVYCKP---TSKTKDNLENPDFkEIRSFVETKAPSIIRQKPVQL 197

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08628  198 LKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN 254
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 591-705 1.23e-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 [Multi-domain]  Cd Length: 115  Bit Score: 217.11  E-value: 1.23e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     591 STLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQ 670
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 11386139     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 1.76e-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 [Multi-domain]  Cd Length: 254  Bit Score: 222.22  E-value: 1.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08633    3 DMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIETIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALliePLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRpsagg 477
Cdd:cd08633   81 KYAFIKNEYPVILSIENHC-SVPQQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKKLSR----- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsALSEssaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08633  152 ---------------ALSD------------------------------------------------------------- 155

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnateemstLVNYIEPVKFKSFEAarKRNKCFEMSSFVETKAMEQLTKSPMEFV 637
Cdd:cd08633  156 -----------------------------------LVKYTKSVRVHDIET--EATSSWQVSSFSETKAHQILQQKPAQYL 198

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  638 EYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08633  199 RFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 318-693 2.33e-65

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


Pssm-ID: 176497 [Multi-domain]  Cd Length: 274  Bit Score: 222.52  E-value: 2.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLA-----GTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTtEVPLRDV 392
Cdd:cd00137    3 PDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLKEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  393 LEAIAETAFKTSPYPVILSFENHVDSA-KQQAKMAEYCRSIFGDALLIEPLDkyplaPGVPLPSPQDLMGRILVKNKKrh 471
Cdd:cd00137   80 IEAIAQFLKKNPPETIIMSLKNEVDSMdSFQAKMAEYCRTIFGDMLLTPPLK-----PTVPLPSLEDLRGKILLLNKK-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  472 rpsaggpdsagrkrpleqsnsalsesSAATEPSspqlgspssdscpGLSNGEEVGLEKPSLEPQKSlgdeglnrgpyvlg 551
Cdd:cd00137  153 --------------------------NGFSGPT-------------GSSNDTGFVSFEFSTQKNRS-------------- 179

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  552 padredeeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcFEMSSFVETKAME---- 627
Cdd:cd00137  180 ---------------------------------------------------------------YNISSQDEYKAYDdekv 196

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139  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 3.72e-62

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


Pssm-ID: 270167  Cd Length: 127  Bit Score: 207.42  E-value: 3.72e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   22 LRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVlGFGGPDARLEE 101
Cdd:cd13361    1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 11386139  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 1.19e-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: 1.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSA---DKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKIL 230
Cdd:cd16213    1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11386139  231 LEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16213   81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYLMSED 154
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 318-693 1.19e-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 [Multi-domain]  Cd Length: 253  Bit Score: 208.35  E-value: 1.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08632    3 DMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIETIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDAL-LIEPLDKYPLApgvpLPSPQDLMGRILVKNKKRHRpsag 476
Cdd:cd08632   81 KYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKKLCR---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  477 gpdsagrkrpleqsnsALSESSAATEpsspqlgSPSSDSCpglsngeevglekpslepqkslgdeglnrgpyvlgpadre 556
Cdd:cd08632  152 ----------------DLSDLVVYTN-------SVAAQDI---------------------------------------- 168

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  557 deeedeeeeeqtdpkkptTDEGTASSEVnateemstlvnyiepvkfksfeaarkrnkcfemsSFVETKAMEQLTKSPMEF 636
Cdd:cd08632  169 ------------------VDDGSTGNVL----------------------------------SFSETRAHQLVQQKAEQF 196

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08632  197 MTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PLN02952 PLN02952
phosphoinositide phospholipase C
 318-833 1.67e-60

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 219.10  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:PLN02952  124 DMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGS-TKDEILVLHGRTLTTPVPLIKCLKSIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLiepldkYPLAPG-VPLPSPQDLMGRILVKNKkrhrPSag 476
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTK----PP-- 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   477 gpdsagrKRPLEQSNSALSESSAATEPSSPQlGSPSSDscpglsngEEVGLEKPSLEPQ---KSLGDEGLNRGPYVLGPA 553
Cdd:PLN02952  270 -------KEYLESSGPIVIKKKNNVSPSGRN-SSEETE--------EAQTLESMLFEQEadsRSDSDQDDNKSGELQKPA 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   554 DRedeeedeeeeeqtdpKKPTTDEGTASSEVNatEEMSTLVNYIEPVkfksfeaarkrnkcfemsSFVETKAMEQLTKSP 633
Cdd:PLN02952  334 YK---------------RLITIHAGKPKGTLK--DAMKVAVDKVRRL------------------SLSEQELEKAATTNG 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   634 MEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRP---DK 710
Cdd:PLN02952  379 QDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKgfhDE 458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   711 SFDPFTEVivdgIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDEEp 780
Cdd:PLN02952  459 VFDPKKKL----PVKKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK-KTKIIEDN-WYPAWNEE- 531

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139   781 FDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEANQPL 833
Cdd:PLN02952  532 FSFPLTV-PELALLRIEVREydmsEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKL 587
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 319-468 2.28e-60

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


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 202.90  E-value: 2.28e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     319 MTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIAE 398
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     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 1.71e-59

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 199.22  E-value: 1.71e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    590 MSTLVNYIEPVKFKSFEAArKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGC 669
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFSTP-ESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 11386139    670 QLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEF 704
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 318-693 5.56e-58

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


Pssm-ID: 176564 [Multi-domain]  Cd Length: 229  Bit Score: 199.87  E-value: 5.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08627    3 EMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYplAPGvpLPSPQDLMGRILVKNKKRHRpsagg 477
Cdd:cd08627   81 EHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVDIN--ADG--LPSPNQLKRKILIKHKKLYR----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspssdscpglsngeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08627      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevnateemstlvnyiepvkfksfeaarkrnkcfEMSSFVETKAMEQLTKSP-MEF 636
Cdd:cd08627  151 ----------------------------------------------------------DMSSFPETKAEKYVNRSKgKKF 172

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  637 VEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYN 693
Cdd:cd08627  173 LQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 285-828 3.44e-56

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 206.03  E-value: 3.44e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   285 FLERDQMSMEGFSRYLGGEENGilPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELD 364
Cdd:PLN02222   73 LLHRNGLHLDAFFKYLFGDNNP--PLALHEVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELD 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   365 VWKGRpPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDK 444
Cdd:PLN02222  151 IWPNS-DKDDIDVLHGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   445 YPLApgvpLPSPQDLMGRILVKNKKRHRPSAGGPDSAGRKrpleqsnsalsessaatepsspqlgspssdsCPGLSNGEE 524
Cdd:PLN02222  229 SLKE----FPSPNSLKKRIIISTKPPKEYKEGKDDEVVQK-------------------------------GKDLGDEEV 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   525 VGLEKPS-LEPQKSLGDEGLNrgpyvlGPADredeeedeeeeeqtdpkkPTTDEGTASSEVNATEEMSTLVNyIEPVKFK 603
Cdd:PLN02222  274 WGREVPSfIQRNKSVDKNDSN------GDDD------------------DDDDDGEDKSKKNAPPQYKHLIA-IHAGKPK 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   604 S-----FEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNkqqLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQT 678
Cdd:PLN02222  329 GgitecLKVDPDKVRRLSLSEEQLEKAAEKYAKQIVRFTQHN---LLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQG 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   679 LDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKS---FDPFTEVIVDgivaNALRVKVISGQ----------FLSDRKVGI 745
Cdd:PLN02222  406 YGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDsdiFDPKATLPVK----TTLRVTIYMGEgwyfdfrhthFDQYSPPDF 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   746 YVEVDMFGLPVDTRRKyRTRTSQGNsFNPVWDeEPFDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYH 821
Cdd:PLN02222  482 YTRVGIAGVPGDTVMK-KTKTLEDN-WIPAWD-EVFEFPLTV-PELALLRLEVHEydmsEKDDFGGQTCLPVWELSQGIR 557


                  ....*..
gi 11386139   822 YVCLRNE 828
Cdd:PLN02222  558 AFPLHSR 564
PLN02228 PLN02228
Phosphoinositide phospholipase C
 285-831 2.32e-54

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 200.26  E-value: 2.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   285 FLERDQMSMEGFSRYLGGEENGILPLEAlDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELD 364
Cdd:PLN02228   75 FHHHGLVHLNAFYRYLFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELD 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   365 VWKGrPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDK 444
Cdd:PLN02228  154 LWPN-PSGNAAEVRHGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFRCTSES 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   445 YPLapgvpLPSPQDLMGRILVKNKKrhrpsaggpdsagrkrPLEQSNSALSESSaatepSSPQLGSPSSDScpgLSNGEE 524
Cdd:PLN02228  232 TKH-----FPSPEELKNKILISTKP----------------PKEYLESKTVQTT-----RTPTVKETSWKR---VADAEN 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   525 VGLEKPSLEPQKSLGDEGLnrgpYVLGPADRedeEEDEEEEEQTDPKKPTtdegtassEVNATEEmstlvnyiepvkfks 604
Cdd:PLN02228  283 KILEEYKDEESEAVGYRDL----IAIHAANC---KDPLKDCLSDDPEKPI--------RVSMDEQ--------------- 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   605 feaarkrnkcfemssFVETKAMeqlTKSPmEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQ 684
Cdd:PLN02228  333 ---------------WLETMVR---TRGT-DLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLW 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   685 LNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDgivaNALRVKVISGQ----------FLSDRKVGIYVEVDMFGL 754
Cdd:PLN02228  394 IMQGMFRANGGCGYVKKPRILLDEHTLFDPCKRLPIK----TTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGV 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   755 PVDTrRKYRTRTSQGNSFnPVWDEEPFDFPKVVlPTLASLRIAAFE----EGGKFVGHRILPVSAIRSGYHYVCLRNEAN 830
Cdd:PLN02228  470 PRDT-VSYRTETAVDQWF-PIWGNDEFLFQLRV-PELALLWFKVQDydndTQNDFAGQTCLPLPELKSGVRAVRLHDRAG 546


                  .
gi 11386139   831 Q 831
Cdd:PLN02228  547 K 547
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 318-693 2.85e-52

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


Pssm-ID: 176541 [Multi-domain]  Cd Length: 228  Bit Score: 183.34  E-value: 2.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  318 DMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRppEEEPFITHGFTMTTEVPLRDVLEAIA 397
Cdd:cd08599    3 DMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGG--RGDICVLHGGTLTKPVKFEDCIKAIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  398 ETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPldkyPLAPGVPLPSPQDLMGRILVknkkrhrpsagg 477
Cdd:cd08599   81 ENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILI------------ 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  478 pdsagrkrpleqsnsalsessaatepsspqlgspsSDSCPGLSNgeevglekpslepqkslgdeglnrgpyvlgpadred 557
Cdd:cd08599  144 -----------------------------------SDKPPVIRN------------------------------------ 152

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  558 eeedeeeeeqtdpkkpttdegtassevNATEemSTLVNYIEpvkfksfeaarkrnkcfemssfvetkameqlTKSPMEFV 637
Cdd:cd08599  153 ---------------------------SLSE--TQLKKVIE-------------------------------GEHPTDLI 172

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139  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 4.91e-52

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: 4.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  155 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIG 234
Cdd:cd16209    2 KIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSYH 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  235 AKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16209   82 AKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 17-146 5.35e-48

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 167.17  E-value: 5.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     17 TVVETLRRGSKFIKWDEETSSRN-LVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGP 95
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEpNVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 11386139     96 DARLEEKLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQN 146
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 288-827 7.55e-44

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 169.50  E-value: 7.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   288 RDQMSMEGFSRYLGGEEngILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVW- 366
Cdd:PLN02230   88 RRNLTLDDFNYYLFSTD--LNPPIADQVHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWp 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   367 KGrppEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIEPLDKYP 446
Cdd:PLN02230  166 RG---TDDVCVKHGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYYHDSEGCQ 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   447 lapgvPLPSPQDLMGRILVKNKKrhrpsaggpdsagrkrPLEqsnsaLSESSAATEPSSPQLGSPSSDSCPGLSNGEEVG 526
Cdd:PLN02230  242 -----EFPSPEELKEKILISTKP----------------PKE-----YLEANDAKEKDNGEKGKDSDEDVWGKEPEDLIS 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   527 LEKPSLEPQKSLGDeglnrgpyvlgpadredeeedeeeeEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKFKSFE 606
Cdd:PLN02230  296 TQSDLDKVTSSVND-------------------------LNQDDEERGSCESDTSCQLQAPEYKRLIAIHAGKPKGGLRM 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   607 AARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLN 686
Cdd:PLN02230  351 ALKVDPNKIRRLSLSEQLLEKAVASYGADVIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLM 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   687 AGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIvDGIVANALRVKVISG----------QFLSDRKVGIYVEVDMFGLPV 756
Cdd:PLN02230  431 EGMFRANGGCGYVKKPDFLMDAGPNGQDFYPKD-NSCPKKTLKVKVCMGdgwlldfkktHFDSYSPPDFFVRVGIAGAPV 509

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   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 1.51e-40

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: 1.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILL 231
Cdd:cd16211    1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139  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 8.71e-37

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


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 134.98  E-value: 8.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  728 LRVKVISGQFLSD------RKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEE 801
Cdd:cd00275    4 LTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTKVVKNNGFNPVWNET-FEFD-VTVPELAFLRFVVYDE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 11386139  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 9.01e-34

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


Pssm-ID: 320042 [Multi-domain]  Cd Length: 153  Bit Score: 127.28  E-value: 9.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILL 231
Cdd:cd16212    1 KKHWMRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139  232 EIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16212   81 SITKGKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PLN02223 PLN02223
phosphoinositide phospholipase C
 318-828 1.37e-24

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 109.73  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   318 DMTQPLSAYFINSSHNTYLTAGQLAGTS-SVEMYRQALLWGCRCVELDVWkgrpPEEEPFITHGFTMTTEVPLR--DVLE 394
Cdd:PLN02223  107 DMHAPLSHYFIHTSLKSYFTGNNVFGKLySIEPIIDALEQGVRVVELDLL----PDGKDGICVRPKWNFEKPLElqECLD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   395 AIAETAF-KTSPYPVILSFEnhvDSAKQ--QAKMAEYCRSIFGDALLIEPldkyPLAPGVPLPSPQDLMGRILVKNKkrh 471
Cdd:PLN02223  183 AIKEHAFtKCRSYPLIITFK---DGLKPdlQSKATQMIDQTFGDMVYHED----PQHSLEEFPSPAELQNKILISRR--- 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   472 rpsaggpdsagrkrpleqsnsalsessaatePSSPQLGSPSSDSCPGLSNGEEVglekpslepqkslgdeglNRGPyvlg 551
Cdd:PLN02223  253 -------------------------------PPKELLYAKADDGGVGVRNELEI------------------QEGP---- 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   552 padredeeedeeeeeqTDPkkpttdegtassevnateemstlvNYIEPVKFKSFEAARKRNKCFEMSSfvetKAMEQLTK 631
Cdd:PLN02223  280 ----------------ADK------------------------NYQSLVGFHAVEPRGMLQKALTGKA----DDIQQPGW 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   632 SPMEFVEYNKQQLSRIYPKGTRVDS-SNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRR--P 708
Cdd:PLN02223  316 YERDIISFTQKKFLRTRPKKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagP 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   709 DKSFDPftevIVDGIVANALRVKVISGQ-FLSD--RKVG------IYVEVDMFGLPVDtrRKYRTRTSQGNSFNPVWDEE 779
Cdd:PLN02223  396 SGVFYP----TENPVVVKILKVKIYMGDgWIVDfkKRIGrlskpdLYVRISIAGVPHD--EKIMKTTVKNNEWKPTWGEE 469

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 11386139   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 2.68e-21

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 91.19  E-value: 2.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  154 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRV---ETALESCGLKFNRSESIRPDEFsleifERFLNKLCLRPDIDKIL 230
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVsekELKKLFKEVDTNGDGTLTFDEF-----EELYKSLTERPELEPIF 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11386139  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 1.88e-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 [Multi-domain]  Cd Length: 179  Bit Score: 87.11  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  329 NSSHNTYLTAGQlagTSSVEMYRQALLWGCRCVELDVWKGrpPEEEPFITHGFTMTTEVP------LRDVLEAIAETAFk 402
Cdd:cd08555    1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLT--KDGELVVYHGPTLDRTTAgilpptLEEVLELIADYLK- 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 11386139  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 1.27e-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 [Multi-domain]  Cd Length: 140  Bit Score: 69.18  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  164 VNQDGRI---PVKNILKM--FSADKKRVETAlescglkFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIgAKGK 238
Cdd:cd16202   11 KNGDGKLsfkECKKLLKKlnVKVDKDYAKKL-------FQEADTSGEDVLDEEEFVQFYNRLTKRPEIEELFKKY-SGDD 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11386139  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 2.05e-13

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


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 67.51  E-value: 2.05e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139     728 LRVKVISGQFLSDRKVG----IYVEVDMFGlpvDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:smart00239    2 LTVKIISARNLPPKDKGgksdPYVKVSLDG---DPKEKKKTKVVK-NTLNPVWNET-FEFE-VPPPELAELEIEVYDKDR 75

                            90       100
                    ....*....|....*....|....*.
gi 11386139     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 1.62e-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: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   22 LRRGSKFIKWDEEtSSRNLVTLRVDPNGFFLYWTGP--NMEVDTLDISSIRDTRTGRYARLPKDpkirevlgFGGPDARL 99
Cdd:cd01248    1 LQQGTLLLKYREG-SKPKERTFYLDPDGTRITWESSkkKSEKKSIDISDIKEIRPGKDTDGFKR--------KKKSNKPK 71

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 11386139  100 EEKLMTVVSGPdpvNTVFLNFMAVQDDTAKVWSEELFKL 138
Cdd:cd01248   72 EERCFSIIYGS---NNKTLDLVAPSEDEANLWVEGLRAL 107
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 216-308 7.11e-09

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


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 53.79  E-value: 7.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    216 FLNKLCLRPDIDKILLEIGAKGKpYLTLEQLMDFINQKQRDPRLNevlypplrPSQARLLIEKYEPNQQFLERDQMSMEG 295
Cdd:pfam09279    1 FYKMLTQREEIDEIFQEYSGDGQ-KLSLDELVDFLREEQREEDAS--------PALALSLIERYEPSETAKKQHAMTKDG 71

                           90
                   ....*....|...
gi 11386139    296 FSRYLGGEENGIL 308
Cdd:pfam09279   72 FLMYLCSPDGSIF 84
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 165-304 8.91e-09

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


Pssm-ID: 320049 [Multi-domain]  Cd Length: 140  Bit Score: 55.24  E-value: 8.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  165 NQDGRI---PVKNILKMFSADKKRvETALEScglkFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPyL 241
Cdd:cd16219   12 NKDGRMnfkEVRDLLKMMNVDMNE-EHALRL----FQMADKSESGTLEGEEFVLFYKALTQREDVLKIFQDFSADGQK-L 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139  242 TLEQLMDFINQKQRDPRLNEVLypplrpsqARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16219   86 TLLEFVDFLQQEQLERENTEEL--------AMELIDRYEPSDTAKKLHALSIDGFLMYLCSPE 140
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
955-1184 5.80e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  955 DELRG-HKALVKLRsRQERDLRELRKKHQRkavtlTRRLLDGLAQAQAEGRcRLRPgalggaadvedtkegEDEAKRYQE 1033
Cdd:COG4913  235 DDLERaHEALEDAR-EQIELLEPIRELAER-----YAAARERLAELEYLRA-ALRL---------------WFAQRRLEL 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1034 FQNRQVQSLLELREAQVD-AEAQRRLEHLRQALQRLREVVLDANTTQFKRLkemnEREKKELQKILDRKRHNS------I 1106
Cdd:COG4913  293 LEAELEELRAELARLEAElERLEARLDALREELDELEAQIRGNGGDRLEQL----EREIERLERELEERERRRarlealL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1107 SEAKMRDKHkKEAELTEiNRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEE-------------P----KLL 1169
Cdd:COG4913  369 AALGLPLPA-SAEEFAA-LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeiaslerrksniParllALR 446

                        250
                 ....*....|....*
gi 11386139 1170 AQLAQECQEQRARLP 1184
Cdd:COG4913  447 DALAEALGLDEAELP 461
C2 pfam00168
C2 domain;
728-822 7.15e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 51.55  E-value: 7.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    728 LRVKVISGQFLSDRKVGI----YVEVDMfglpVDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRIAAFEEGG 803
Cdd:pfam00168    3 LTVTVIEAKNLPPKDGNGtsdpYVKVYL----LDGKQKKKTKVVK-NTLNPVWNET-FTFS-VPDPENAVLEIEVYDYDR 75

                           90       100
                   ....*....|....*....|...
gi 11386139    804 ----KFVGHRILPVSAIRSGYHY 822
Cdd:pfam00168   76 fgrdDFIGEVRIPLSELDSGEGL 98
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 197-300 4.94e-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 [Multi-domain]  Cd Length: 142  Bit Score: 50.33  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  197 FNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDprlnevlypPLRPSQARLLI 276
Cdd:cd16207   44 FDKADTDKKGYLNFEEFQEFVKLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKE---------DVDRETWEKIF 114

                         90       100
                 ....*....|....*....|....
gi 11386139  277 EKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16207  115 EKFARRIDDSDSLTMTLEGFTSFL 138
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 211-304 7.95e-07

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


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 49.74  E-value: 7.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  211 EIfERFLNKLCLRPDIDKILLEIgAKGKPYLTLEQLMDFINQKQRDPrlnevlyppLRPSQARLLIEKYEPNQQFLERDQ 290
Cdd:cd16217   57 EI-EEFYKLLTKREEIDVIFGEY-AKSDGTMSRNNLLNFLQEEQREE---------VAPAYALSLIEKYEPDETAKAQRQ 125

                         90
                 ....*....|....
gi 11386139  291 MSMEGFSRYLGGEE 304
Cdd:cd16217  126 MTKDGFLMYLLSPE 139
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1019-1187 9.20e-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 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 9.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1019 EDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDA-----EAQRRLEHLRQALQRLREVV--LDANTTQFKRLKEMNEREK 1091
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrkigEIEKEIEQLEQEEEKLKERLeeLEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1092 KELQKILDRKRhnsiseakmRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVA---------GQQQVLQQLA 1162
Cdd:TIGR02169  761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreieqklNRLTLEKEYL 831

                          170       180
                   ....*....|....*....|....*
gi 11386139   1163 EEEPKLLAQLAQECQEQRARLPQEI 1187
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEI 856
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 960-1182 1.03e-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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 52.23  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    960 HKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRpgalggaADVEDTKEGEDEAKRYQEFQNRQV 1039
Cdd:pfam13868   31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELE-------EQIEEREQKRQEEYEEKLQEREQM 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1040 QSLLElreaQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILdrkrhnsiseAKMRDKHKKEA 1119
Cdd:pfam13868  104 DEIVE----RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL----------EYLKEKAEREE 169

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139   1120 ELTEinrrhitesvnSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEpKLLAQLAQECQEQRAR 1182
Cdd:pfam13868  170 EREA-----------EREEIEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKER 220
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 946-1189 1.92e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  946 LSEVAPTPLDELRGHKALVKLRSRQERDLRELRKKHQRkavtLTRRLLDGLAQAQAEGRcRLRPGALGGAADVEDTKEGE 1025
Cdd:COG1196  536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR----ATFLPLDKIRARAALAA-ALARGAIGAAVDLVASDLRE 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1026 DEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLD-ANTTQFKRLKEMNEREKKELQKILDRKrhn 1104
Cdd:COG1196  611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAER--- 687

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1105 sisEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLA---------QE 1175
Cdd:COG1196  688 ---LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppdlEE 764

                        250
                 ....*....|....
gi 11386139 1176 CQEQRARLPQEIRR 1189
Cdd:COG1196  765 LERELERLEREIEA 778
EFh_PI-PLCzeta cd16204
EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, ...
 197-304 4.40e-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 [Multi-domain]  Cd Length: 142  Bit Score: 47.50  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  197 FNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILlEIGAKGKPYLTLEQLMDFINQKQRDPRLNEvlypplrpSQARLLI 276
Cdd:cd16204   44 FKKNDSFKAGNITIEDFRAIYRAIAHRCEIHEIF-NTYSENRKILSAPNLVGFLKKEQFQDEADE--------TIASELI 114

                         90       100
                 ....*....|....*....|....*...
gi 11386139  277 EKYEPNQQFLERDQMSMEGFSRYLGGEE 304
Cdd:cd16204  115 AKYEPIEEVRKRKQMSFEGFIRYMTSED 142
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 728-796 4.67e-06

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


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 46.29  E-value: 4.67e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139  728 LRVKVISGQFLSDRKVGI----YVEVDmfglpVDTRRKYRTRTSQgNSFNPVWDEEpFDFPkVVLPTLASLRI 796
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGksdpYVKVS-----LGGKQKFKTKVVK-NTLNPVWNET-FEFP-VLDPESDTLTV 65
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1025-1168 5.47e-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: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 47.74  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1025 EDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF---KRLKEMNER-EKKELQKILdR 1100
Cdd:pfam15346   10 EETARRVEEAVAKRVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAEleeERRKEEEERkKREELERIL-E 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11386139   1101 KRHNSISEAKMRDKHKKEAELTEINRRHitesvNSIRRLEEAQKQRHDRlvagQQQVLQQLAEEEPKL 1168
Cdd:pfam15346   89 ENNRKIEEAQRKEAEERLAMLEEQRRMK-----EERQRREKEEEEREKR----EQQKILNKKNSRPKL 147
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 954-1189 5.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 5.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  954 LDELRGHkaLVKLR--SRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRpgALGGAADVEDTKEGEDEAKRy 1031
Cdd:COG1196  195 LGELERQ--LEPLErqAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELE--ELEAELEELEAELAELEAEL- 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1032 QEFQNRQVQSLLELREAQVD-AEAQRRLEHLRQALQRLREVvLDANTTQFKRLKEMNEREKKELQKILDRKrhnsISEAK 1110
Cdd:COG1196  270 EELRLELEELELELEEAQAEeYELLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEEL----EELEE 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1111 MRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKL--LAQLAQECQEQRARLPQEIR 1188
Cdd:COG1196  345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLeeLEEAEEALLERLERLEEELE 424


                 .
gi 11386139 1189 R 1189
Cdd:COG1196  425 E 425
EFh_PRIP2 cd16223
EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); ...
 161-300 6.35e-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 [Multi-domain]  Cd Length: 144  Bit Score: 47.21  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  161 KLQVNQDGRIPVKNILKMFSADKKRVETAleSCGLKF---NRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKg 237
Cdd:cd16223    8 EADTDNVGHITLCRAVQFIKNLNPGLKTS--KIELKFkelHKSKEKGGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSN- 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11386139  238 KPYLTLEQLMDFINQKQRDPRLNEvlypplrpsQARL-LIEKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16223   85 KEFLDTKDLMMFLEAEQGMAHVTE---------EISLdIIHKYEPSKEGQEKGWLSLDGFTNYL 139
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
966-1180 7.40e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  966 LRSRQERDLRELRKKHQRKavtlTRRLLDGLAQAQAEgrcrlrpgalggaadvedTKEGEDEAKRYQEFQNRQVQSLLEL 1045
Cdd:COG4717   47 LLERLEKEADELFKPQGRK----PELNLKELKELEEE------------------LKEAEEKEEEYAELQEELEELEEEL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1046 REAQVD-AEAQRRLEHLRQALQRLR--------EVVLDANTTQFKRLKEmNEREKKELQKILDRKRhNSISEAKmRDKHK 1116
Cdd:COG4717  105 EELEAElEELREELEKLEKLLQLLPlyqelealEAELAELPERLEELEE-RLEELRELEEELEELE-AELAELQ-EELEE 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11386139 1117 KEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQvLQQLAEEEPKLLAQLAQECQEQR 1180
Cdd:COG4717  182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE-LEELEEELEQLENELEAAALEER 244
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 209-304 8.97e-06

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


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 46.82  E-value: 8.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  209 SLEIFERFLNKLCLRPDIDKILLEIgAKGKPYLTLEQLMDFINQKQRDPRLNEvlypplrpSQARLLIEKYEPNQQFLER 288
Cdd:cd16206   57 SSDEFVELFKELATRPEIYFLLVRY-ASNKDYLTVDDLMLFLEAEQGMTGVTK--------EKCLEIINKYEPSEEGREK 127

                         90
                 ....*....|....*.
gi 11386139  289 DQMSMEGFSRYLGGEE 304
Cdd:cd16206  128 GQLGIDGFTRYLLSEE 143
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
 165-300 1.26e-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 [Multi-domain]  Cd Length: 138  Bit Score: 46.28  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  165 NQDGRIP---VKNILKMFSADKKRVETAL--ESCglkfNRSESIRPDEfsLEIfERFLNKLCLRPDIDKILLEIGAKGKp 239
Cdd:cd16218   12 NKDGKMSfeeIKDLLQMINIDLNEQYAYQlfKEC----DRSNDDRLEE--HEI-EEFCRRLMQRPELEEIFHQYSGEDC- 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386139  240 YLTLEQLMDFINQKQRDPRLnevlypplrpSQARLLIEKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16218   84 VLSAEELREFLKDQGEDASL----------VHAKELIQTYELNEKAKQHQLMTLDGFTMYM 134
PTZ00121 PTZ00121
MAEBL; Provisional
 955-1189 1.48e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   955 DELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRlrpgalgGAADVEDTKEGeDEAKRYQEF 1034
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-------EAKKAEEKKKA-DELKKAEEL 1557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1035 QN-RQVQSLLELREAQVDAE-AQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMR 1112
Cdd:PTZ00121 1558 KKaEEKKKAEEAKKAEEDKNmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  1113 DKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQqqvLQQLAEEEPKLLAQLAQECQEqrARLPQEIRR 1189
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE---AKKAEEDEKKAAEALKKEAEE--AKKAEELKK 1709
PTZ00121 PTZ00121
MAEBL; Provisional
 955-1189 1.64e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   955 DELRghKALVKLRSRQERDLRELRKKHQRKAVTLTRRlldglaqaqAEGRcrlRPGALGGAADVEDTKEG--EDEAKRYQ 1032
Cdd:PTZ00121 1537 DEAK--KAEEKKKADELKKAEELKKAEEKKKAEEAKK---------AEED---KNMALRKAEEAKKAEEAriEEVMKLYE 1602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1033 EFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQrlrevvldanttQFKRLKEMNEREKKELQKILDRKRHNSISEAKMR 1112
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE------------QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1113 DKHKKEAE---LTEINRRHITESVNsiRRLEEAQK-QRHDRLVAGQQQVLQQL--AEEEPKLLAQLAQECQEQRARLPQE 1186
Cdd:PTZ00121 1671 EEDKKKAEeakKAEEDEKKAAEALK--KEAEEAKKaEELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEEDKKKAEE 1748


                  ...
gi 11386139  1187 IRR 1189
Cdd:PTZ00121 1749 AKK 1751
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1015-1190 2.09e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1015 AADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQV-DAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNER---- 1089
Cdd:pfam17380  371 AMEISRMRELERLQMERQQKNERVRQELEAARKVKIlEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARemer 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1090 ---EKKELQKILDRKRHNSISEAKMR---DKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQ-LA 1162
Cdd:pfam17380  451 vrlEEQERQQQVERLRQQEEERKRKKlelEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKaIY 530

                          170       180       190
                   ....*....|....*....|....*....|.
gi 11386139   1163 EEEPKLLAQLAQECQ---EQRARLPQEIRRS 1190
Cdd:pfam17380  531 EEERRREAEEERRKQqemEERRRIQEQMRKA 561
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1025-1197 2.98e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.20  E-value: 2.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1025 EDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLRE---------------VVLDANTTQFKRLKEM--- 1086
Cdd:pfam17380  304 EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERElerirqeerkrelerIRQEEIAMEISRMRELerl 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1087 -------NEREKKEL-----QKILDRKRHNSISEaKMRDKHKKEAELTEINRRHitesvnsIRRLEEAQKQRHDRL---- 1150
Cdd:pfam17380  384 qmerqqkNERVRQELeaarkVKILEEERQRKIQQ-QKVEMEQIRAEQEEARQRE-------VRRLEEERAREMERVrlee 455

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 11386139   1151 VAGQQQV--LQQLAEEEPKLLAQLAQEcQEQRARLPQEIRRSLLGEMPE 1197
Cdd:pfam17380  456 QERQQQVerLRQQEEERKRKKLELEKE-KRDRKRAEEQRRKILEKELEE 503
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 965-1194 3.63e-05

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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.22  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    965 KLRSRQERDLRELRKKHQRKavtltRRLLDGLAQAQAEgrcrlrpgalggaadVEDTKEGEDEAKRYQEFQNRQVQSLLE 1044
Cdd:pfam13868  106 IVERIQEEDQAEAEEKLEKQ-----RQLREEIDEFNEE---------------QAEWKELEKEEEREEDERILEYLKEKA 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1045 LREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQ-------FKRLKEMNERE--KKELQKILDRKR-HNSISEA---KM 1111
Cdd:pfam13868  166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKaerdelrAKLYQEEQERKerQKEREEAEKKARqRQELQQAreeQI 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1112 RDKHK---KEAELTEINRRHITESVNSIRRLEEAQKQ-RHDRLVAGQQQVLQQLAE----------EEPKLLAQLAQECQ 1177
Cdd:pfam13868  246 ELKERrlaEEAEREEEEFERMLRKQAEDEEIEQEEAEkRRMKRLEHRRELEKQIEEreeqraaereEELEEGERLREEEA 325

                          250
                   ....*....|....*..
gi 11386139   1178 EQRARLpQEIRRSLLGE 1194
Cdd:pfam13868  326 ERRERI-EEERQKKLKE 341
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 967-1191 3.65e-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 [Multi-domain]  Cd Length: 1042  Bit Score: 48.43  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    967 RSRQERDLRELRKKHQrKAVTLTRRLldGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFQNRQVQSLLELR 1046
Cdd:TIGR00618  255 QLKKQQLLKQLRARIE-ELRAQEAVL--EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1047 EAQVDAEAQRRLEHLRQALQRLREVVLDANTTQfKRLKEMNEREKKELQKIldRKRHNSISEAKMRDKHKKEAELTEINR 1126
Cdd:TIGR00618  332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTLTQHI--HTLQQQKTTLTQKLQSLCKELDILQRE 408

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11386139   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 3.65e-05

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 47.69  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1019 EDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRleHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKil 1098
Cdd:pfam05262  210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRD--EVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEK-- 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   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 4.60e-05

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


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 44.68  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  161 KLQVNqdgrIPVKNILKMFsadkKRVETALESCGLKFnrsesirpDEFSleifeRFLNKLCLRPDIDKILLEIGAKgKPY 240
Cdd:cd16205   28 KLNVN----LPRRKVRQMF----KEADTDDNQGTLDF--------EEFC-----AFYKMMSTRRELYLLLLSYSNK-KDY 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  241 LTLEQLMDFINQKQRdprLNEVlypPLRPSQArlLIEKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16205   86 LTLEDLARFLEVEQK---MTNV---TLEYCLD--IIEKFEPSEENKKNGLLGIDGFTNYM 137
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 1042-1191 6.84e-05

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 46.57  E-value: 6.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1042 LLELREAQVDAEaQRRLEHLRQALQRLREvvldanttqfKRLKEMNEREKKELQKiLDRKRHNSISEAKMRDKHKKEAEL 1121
Cdd:pfam15558   14 LARHKEEQRMRE-LQQQAALAWEELRRRD----------QKRQETLERERRLLLQ-QSQEQWQAEKEQRKARLGREERRR 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386139   1122 TEINRRHITESVNSIRRLEEAQ-KQRHDRLvagqqqvlqqlaeEEPKLLAQLAQECQEQRARLPQEIRRSL 1191
Cdd:pfam15558   82 ADRREKQVIEKESRWREQAEDQeNQRQEKL-------------ERARQEAEQRKQCQEQRLKEKEEELQAL 139
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1038-1189 7.12e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1038 QVQSLLELREAQVDAEAQRR-LEHLRQALQRLREVVLDANttQFKRLKEM-----NEREKKELQKILDRKRHN------S 1105
Cdd:COG4913  233 HFDDLERAHEALEDAREQIElLEPIRELAERYAAARERLA--ELEYLRAAlrlwfAQRRLELLEAELEELRAElarleaE 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1106 ISEAKmRDKHKKEAELTEINRRHITESVNSIRRLE------EAQKQRHDRLVAGQQQVLQQLAEEEP---KLLAQLAQEC 1176
Cdd:COG4913  311 LERLE-ARLDALREELDELEAQIRGNGGDRLEQLEreierlERELEERERRRARLEALLAALGLPLPasaEEFAALRAEA 389

                        170
                 ....*....|...
gi 11386139 1177 QEQRARLPQEIRR 1189
Cdd:COG4913  390 AALLEALEEELEA 402
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1029-1189 9.10e-05

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: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.48  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1029 KRYQEFQNRQVQSLLELRE---AQVDAEAQRRLEHLRQALQRLREvvldanttqfKRLKEMNEREKKELQKILDRKRHNS 1105
Cdd:pfam15709  354 RREQEEQRRLQQEQLERAEkmrEELELEQQRRFEEIRLRKQRLEE----------ERQRQEEEERKQRLQLQAAQERARQ 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1106 ISEAKMRdkhkkeaELTEINRRHITESVNSIRRLEEAQKQRHDRLvAGQQQVLQQLAEEEpKLLAQLAQECQEQRARLPQ 1185
Cdd:pfam15709  424 QQEEFRR-------KLQELQRKKQQEEAERAEAEKQRQKELEMQL-AEEQKRLMEMAEEE-RLEYQRQKQEAEEKARLEA 494


                   ....
gi 11386139   1186 EIRR 1189
Cdd:pfam15709  495 EERR 498
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1048-1189 9.99e-05

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 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 9.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1048 AQVDAEAQRRLEHLRQALQRLREV--VLDANTTQFKRLKEmnEREKKELQKILDRKrhnsiseakmrdkhKKEAELTEIn 1125
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLdlIIDEKRQQLERLRR--EREKAERYQALLKE--------------KREYEGYEL- 228

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11386139   1126 rrhitesVNSIRRLeEAQKQRHDRLVAGQQQVLQQLAEEepklLAQLAQECQEQRARLPQEIRR 1189
Cdd:TIGR02169  229 -------LKEKEAL-ERQKEAIERQLASLEEELEKLTEE----ISELEKRLEEIEQLLEELNKK 280
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1042-1189 1.36e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1042 LLELREAQVD-AEAQRRLEHLRQALQRLREVvldanttqfKRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAE 1120
Cdd:COG4717   70 LKELKELEEElKEAEEKEEEYAELQEELEEL---------EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139 1121 LTEINRR--HITESVNSIRRLEEAQKQRHDRLVAGQQQV---LQQLAEEEPKLLAQLA---QECQEQRARLPQEIRR 1189
Cdd:COG4717  141 LAELPERleELEERLEELRELEEELEELEAELAELQEELeelLEQLSLATEEELQDLAeelEELQQRLAELEEELEE 217
EFh_PRIP1 cd16222
EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1); ...
 211-304 1.94e-04

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


Pssm-ID: 320052 [Multi-domain]  Cd Length: 143  Bit Score: 42.93  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  211 EIFERFLNKLCLRPDIDKILLEIgAKGKPYLTLEQLMDFINQKQRDPRLNEvlypplrpSQARLLIEKYEPNQQFLERDQ 290
Cdd:cd16222   59 EEFCEAYSELCTRPEVYFLLVQI-SKNKEYLDAKDLMLFLEAEQGMTHITE--------EMCLDIIRRYEPSQEGRLKGF 129

                         90
                 ....*....|....
gi 11386139  291 MSMEGFSRYLGGEE 304
Cdd:cd16222  130 LGIDGFTQYLLSSE 143
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 963-1186 3.28e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    963 LVKLRSRQ---ERDLRELRKKHQRkaVTLTRRLLDGLAQAQA-------EGRCRLrpgalggAADVEDTKE--------G 1024
Cdd:pfam01576   14 LQKVKERQqkaESELKELEKKHQQ--LCEEKNALQEQLQAETelcaeaeEMRARL-------AARKQELEEilhelesrL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1025 EDEAKRYQEFQN--RQVQSLLELREAQVDAEaqrrlEHLRQALQrLREVVLDAnttqfkRLKEMNE-------------R 1089
Cdd:pfam01576   85 EEEEERSQQLQNekKKMQQHIQDLEEQLDEE-----EAARQKLQ-LEKVTTEA------KIKKLEEdillledqnsklsK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1090 EKKELQKILDRKRHNSISE---AKM--RDKHKKEAELTEINRRHITESvNSIRRLEEAQKQRHDRLVAGQQQV--LQQLA 1162
Cdd:pfam01576  153 ERKLLEERISEFTSNLAEEeekAKSlsKLKNKHEAMISDLEERLKKEE-KGRQELEKAKRKLEGESTDLQEQIaeLQAQI 231

                          250       260
                   ....*....|....*....|....*..
gi 11386139   1163 EEepkLLAQLAQ---ECQEQRARLPQE 1186
Cdd:pfam01576  232 AE---LRAQLAKkeeELQAALARLEEE 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 992-1189 3.79e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  992 LLDGLAQAQAEGRCRLRpgalggaADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVD--AEAQRRLEHLRQALQRLR 1069
Cdd:COG4942   10 LLALAAAAQADAAAEAE-------AELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1070 EVvLDANTTQFKRLKEMNEREKKELQKILD--------------------------RKRHNSISEAKMRDKHKKEAELTE 1123
Cdd:COG4942   83 AE-LAELEKEIAELRAELEAQKEELAELLRalyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386139 1124 IN--RRHITESVNSIRRLEEAQKQRHDRL---VAGQQQVLQQLAEEEPKLLAQLAQEcQEQRARLPQEIRR 1189
Cdd:COG4942  162 LAalRAELEAERAELEALLAELEEERAALealKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIAR 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 958-1189 4.39e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  958 RGHKALVKLRSRQER-----DLR-ELRK-----KHQRKAVTLTRRLLDGLAQAQAEGRCRLRpgalggaADVEDTKEGED 1026
Cdd:COG1196  173 RKEEAERKLEATEENlerleDILgELERqleplERQAEKAERYRELKEELKELEAELLLLKL-------RELEAELEELE 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1027 EAKRYQEFQNRQVQSLLELREAQVdAEAQRRLEHLRQALQRLREVVLDANTT------QFKRLKEMNEREKKELQKILDR 1100
Cdd:COG1196  246 AELEELEAELEELEAELAELEAEL-EELRLELEELELELEEAQAEEYELLAElarleqDIARLEERRRELEERLEELEEE 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1101 KRHNsisEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRhDRLVAGQQQVLQQLAEEEpKLLAQLAQECQEQR 1180
Cdd:COG1196  325 LAEL---EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL-LEAEAELAEAEEELEELA-EELLEALRAAAELA 399


                 ....*....
gi 11386139 1181 ARLPQEIRR 1189
Cdd:COG1196  400 AQLEELEEA 408
PDCD7 pfam16021
Programmed cell death protein 7;
983-1182 5.53e-04

Programmed cell death protein 7;


Pssm-ID: 464979 [Multi-domain]  Cd Length: 305  Bit Score: 43.56  E-value: 5.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    983 RKAVTLTRRLLDGLAQAQAEgrcrLRpgalggaADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEhlR 1062
Cdd:pfam16021    7 RQALYSAARLVSRLETLCLE----LR-------ENVEDDSVWSESYSRAAELKHELQEKLLLLEDPELLESLKRKLE--R 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1063 QALQRLREvvldanttqfKRLKEMNEREKK-------ELQKILD---RKRHNSISEAKMRDKHKKEAE--LTEINRRH-- 1128
Cdd:pfam16021   74 RQKKRLRR----------KRRKEERKEEKKeeqerraEREAKIDkwrRKQIQEVEEKKRERELKLAADavLSEVRKKQad 143

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11386139   1129 ITESVNSIRRLEEAQKQRH----------------------DRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRAR 1182
Cdd:pfam16021  144 AKRMLDILRSLEKLRKLRKeaarrkgikpesecdeafeshlEKLRSVWKKRTEEYSAEEKALKVMLEGEQEEERKR 219
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 316-441 6.10e-04

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


Pssm-ID: 176500 [Multi-domain]  Cd Length: 271  Bit Score: 43.24  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  316 STDMTQPLSAYFINSSHN--TYLTAGQLAGTSSVEMY-----RQALLWGCRCVELDVWKgRPPEEEPFITHGFTMTTEVP 388
Cdd:cd08557    2 ALLDDLPLSQLSIPGTHNsyAYTIDGNSPIVSKWSKTqdlsiTDQLDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11386139  389 LRDVLEAIAetAF-KTSPY-PVILSFENHV--DSAKQQAKMAEYCRSIFGDALLIEP 441
Cdd:cd08557   81 LEDVLNEVK--DFlDAHPSeVVILDLEHEYggDNGEDHDELDALLRDVLGDPLYRPP 135
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1053-1189 7.30e-04

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 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1053 EAQRRLEHLRQALQRLREVV--LDAN----------TTQFKRLKEmnerEKKELQKILDRKRHNSIsEAKMRDKHKKEAE 1120
Cdd:TIGR02168  176 ETERKLERTRENLDRLEDILneLERQlkslerqaekAERYKELKA----ELRELELALLVLRLEEL-REELEELQEELKE 250

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11386139   1121 LTEINRRHITESVNSIRRLEEAQKQRH--DRLVAGQQQVLQQLAEEEPKLLAQLaQECQEQRARLPQEIRR 1189
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSelEEEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEE 320
PRK12704 PRK12704
phosphodiesterase; Provisional
 1022-1187 8.73e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1022 KEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRL--REVVLDanttqfkRLKEMNEREKKELQKild 1099
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLlqKEENLD-------RKLELLEKREEELEK--- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1100 rkrHNSISEAKMRDKHKKEAELTEINRRHITEsvnsirrLEEaqkqrhdrlVAGqqqvlqqLAEEEPK--LLAQLAQECQ 1177
Cdd:PRK12704  115 ---KEKELEQKQQELEKKEEELEELIEEQLQE-------LER---------ISG-------LTAEEAKeiLLEKVEEEAR 168

                         170
                  ....*....|
gi 11386139  1178 EQRARLPQEI 1187
Cdd:PRK12704  169 HEAAVLIKEI 178
PTZ00121 PTZ00121
MAEBL; Provisional
 964-1190 1.15e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   964 VKLRSRQERDLRELRKK--HQRKAVTLTRRLLDGLAQAQAEGRCRLRPGAlggaadvEDTKEGEDEAKRYQEFQNRQVQS 1041
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA-------DEAKKKAEEAKKADEAKKKAEEA 1495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1042 LLELREAQVDAEAQRRLEHLRQALQRlrevvldanttqfkrlkemneREKKELQKILDRKRHNSISEAKmrdkHKKEAEl 1121
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEA---------------------KKADEAKKAEEAKKADEAKKAE----EKKKAD- 1549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1122 tEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQ------------QVLQQLAEEEPKLLAQLAQECQEQRARlPQEIRR 1189
Cdd:PTZ00121 1550 -ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKK 1627


                  .
gi 11386139  1190 S 1190
Cdd:PTZ00121 1628 A 1628
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 957-1192 1.33e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    957 LRGHkaLVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADV--EDTKEGEDEAKRYQEF 1034
Cdd:TIGR00618  422 LQGQ--LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIhlQETRKKAVVLARLLEL 499

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1035 QNRQ---VQSLLELREAQVDAE----AQRRLEHLRQALQRLREVV------LDANTTQFKRLKEMNEREKKELQKILDRK 1101
Cdd:TIGR00618  500 QEEPcplCGSCIHPNPARQDIDnpgpLTRRMQRGEQTYAQLETSEedvyhqLTSERKQRASLKEQMQEIQQSFSILTQCD 579

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1102 RHNSISEAKMRDKHKKEAELTEINRRH-ITESVNSIRRLEEAQKQRHDRLVAgqqQVLQQLAEEEPKLLAQLAQECQEqr 1180
Cdd:TIGR00618  580 NRSKEDIPNLQNITVRLQDLTEKLSEAeDMLACEQHALLRKLQPEQDLQDVR---LHLQQCSQELALKLTALHALQLT-- 654

                          250
                   ....*....|...
gi 11386139   1181 arLPQE-IRRSLL 1192
Cdd:TIGR00618  655 --LTQErVREHAL 665
PTZ00121 PTZ00121
MAEBL; Provisional
 997-1190 1.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   997 AQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFqnRQVQSLLELREAQvDAEAQRRLEHLRQAlQRLREVVLDAN 1076
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEA--RKAEDARKAEEAR-KAEDAKRVEIARKA-EDARKAEEARK 1171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  1077 TTQFKRLKEmnEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQ 1156
Cdd:PTZ00121 1172 AEDAKKAEA--ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 11386139  1157 VLQQLAEEEPKLLAQLAQECQEQRA---RLPQEIRRS 1190
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAeeaRKADELKKA 1286
Hmw_CFAP97 pfam13879
Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm ...
 1065-1169 1.49e-03

Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm flagella assembly. The human orthologue, known as cilia- and flagella-associated protein 97 (CFAP97) or KIAA1430, localizes to the primary cilium. Another member of this family is the uncharacterized protein CFAP97D1/2 (CFAP97 domain-containing protein 1/2).


Pssm-ID: 464014  Cd Length: 100  Bit Score: 39.26  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1065 LQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMrdkhkkeaelTEINRRHITESVNSIRRLEEAQK 1144
Cdd:pfam13879    1 LNKLKNAKPTVDNKAPPHLSLKLKKLQFEEERLAEIERENQILLEKI----------SRIMRRKGKVDKNSLSTQSYSSK 70

                           90       100
                   ....*....|....*....|....*.
gi 11386139   1145 QRHDRLVAGQQQV-LQQLAEEEPKLL 1169
Cdd:pfam13879   71 TRPKSLNAENRKReLLRIEEENQKLL 96
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 951-990 1.83e-03

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


Pssm-ID: 461969  Cd Length: 45  Bit Score: 37.24  E-value: 1.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 11386139    951 PTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTR 990
Cdd:pfam06631    6 PITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 997-1186 2.35e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  997 AQAQAEGRCRLRPGALGGAADvedtkegedeakRYQEFQNRQ---VQSLLELREAQVDAEAQRRlEHlRQALQRLREVVL 1073
Cdd:COG3096  421 ALEKARALCGLPDLTPENAED------------YLAAFRAKEqqaTEEVLELEQKLSVADAARR-QF-EKAYELVCKIAG 486

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1074 DANTTQ-FKRLKEMnEREKKELQKILDRKrhNSIseakmrdkhkkEAELTEINRRhiTESVNSIRRLEEAQKQRHDRLVA 1152
Cdd:COG3096  487 EVERSQaWQTAREL-LRRYRSQQALAQRL--QQL-----------RAQLAELEQR--LRQQQNAERLLEEFCQRIGQQLD 550

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 11386139 1153 GQQQVLQQLAEEEPKL--LAQLAQECQEQRARLPQE 1186
Cdd:COG3096  551 AAEELEELLAELEAQLeeLEEQAAEAVEQRSELRQQ 586
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 973-1111 2.44e-03

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 39.69  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    973 DLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLrpgalggaADVEDTKEGEdEAKRYQEFQNRQV---------QSLL 1043
Cdd:pfam07321    6 RVKHLREDRAEKAVKRQEQALAAARAAHQQAQASL--------QDYRAWRPQE-EQRLYAEIQGKLVllkelekvkQQVA 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139   1044 ELREAQVD-----AEAQRRLEHLRQALQRLREVVLDANTTQFKrLKEMNEREKKELQKILDRKRHNSISEAKM 1111
Cdd:pfam07321   77 LLRENEADlekqvAEARQQLEAEREALRQARQALAEARRAVEK-FAELVRLVQAEELRQQERQEEQELEEFAE 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 970-1194 3.10e-03

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 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    970 QERDLRELRKKHQRkavtltrrlLDGLAQAQAEGRCRLRpgalggaADVEDTKEGEDEAKRYQEFQNRQVQSL-LELREA 1048
Cdd:TIGR02168  801 LREALDELRAELTL---------LNEEAANLRERLESLE-------RRIAATERRLEDLEEQIEELSEDIESLaAEIEEL 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1049 QVD-AEAQRRLEHL---RQALQRLREVVLDANTTQFKRLKEMnEREKKELQKILDRKRHnSISEAKMRdkhkkEAELtEI 1124
Cdd:TIGR02168  865 EELiEELESELEALlneRASLEEALALLRSELEELSEELREL-ESKRSELRRELEELRE-KLAQLELR-----LEGL-EV 936

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1125 NRRHITESVNSirrleeaqkqrhdrlvagQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRslLGE 1194
Cdd:TIGR02168  937 RIDNLQERLSE------------------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE--LGP 986
EFh_PI-PLCepsilon cd16203
EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1); ...
 241-300 3.19e-03

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


Pssm-ID: 320033  Cd Length: 174  Bit Score: 40.00  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  241 LTLEQLMDFINQKQRDPRLNEvlypplrpsQARLLIEKYEPNQQFLERDQMSMEGFSRYL 300
Cdd:cd16203  120 LTISQLKDFLENHQMEHITEE---------EAIKIIQRHEPDPILRSKNCLSFEGFARYL 170
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1027-1191 3.88e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1027 EAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVvLDANTTQFKRLKEMNEREKKELQKILDR--KRHN 1104
Cdd:COG4372    9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEEleELNE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1105 SISEAKMRDKhKKEAELTEIN------RRHITESVNSIRRLE------EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQL 1172
Cdd:COG4372   88 QLQAAQAELA-QAQEELESLQeeaeelQEELEELQKERQDLEqqrkqlEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                        170
                 ....*....|....*....
gi 11386139 1173 AQECQEQRARLPQEIRRSL 1191
Cdd:COG4372  167 AALEQELQALSEAEAEQAL 185
C2C_MCTP_PRT_plant cd04019
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 728-816 4.87e-03

C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175986 [Multi-domain]  Cd Length: 150  Bit Score: 38.80  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  728 LRVKVISGQ--FLSD--RKVGIYVEVDMfGLPVdtrrkYRTRTSQGNSFNPVWDE-------EPFDFPKVVlptlaSL-- 794
Cdd:cd04019    2 LRVTVIEAQdlVPSDknRVPEVFVKAQL-GNQV-----LRTRPSQTRNGNPSWNEelmfvaaEPFEDHLIL-----SVed 70

                         90       100
                 ....*....|....*....|..
gi 11386139  795 RIAAFEEGgkFVGHRILPVSAI 816
Cdd:cd04019   71 RVGPNKDE--PLGRAVIPLNDI 90
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1025-1186 5.12e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1025 EDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEH-LRQALQRLREVvldanTTQFKRLKEMNERekkelqkiLDRKRH 1103
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQlLKQLRARIEEL-----RAQEAVLEETQER--------INRARK 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1104 NS----ISEAKMRDKHKKEAELTEINRRhITESVNSIRRLEEAQKQRHDrlVAGQQQVLQQLAEEEpKLLAQLAQECQEQ 1179
Cdd:TIGR00618  292 AAplaaHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSS--IEEQRRLLQTLHSQE-IHIRDAHEVATSI 367


                   ....*..
gi 11386139   1180 RARLPQE 1186
Cdd:TIGR00618  368 REISCQQ 374
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 873-1066 5.24e-03

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


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.86  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   873 ARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPldASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPT 952
Cdd:PRK06975  256 ERIVRAFLTWADAAAQPATAAPAPSRMTDTNDSKSVTSQP--AAAAAAPAPPPNPPATPPEPPARRGRGSAALWFVVVVL 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   953 PLDELRGHKALVKLRSRQERDLRELRKK---HQRKAVTLTRRLLDGLAQAQAEgrcrlrPGALggaadveDTKEGEDEAK 1029
Cdd:PRK06975  334 ACAAAVGGYALNRKVDRLDQELVQRQQAndaQTAELRVKTEQAQASVHQLDSQ------FAQL-------DGKLADAQSA 400

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 11386139  1030 ryQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQ 1066
Cdd:PRK06975  401 --QQALEQQYQDLSRNRDDWMIAEVEQMLSSASQQLQ 435
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
948-1189 5.67e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  948 EVAPTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAegrcrlrpgALGGAADVEDTKEGED- 1026
Cdd:COG4717  298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE---------LLREAEELEEELQLEEl 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1027 EAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQR-----LREVVLDANTTQFKRLKEMNEREKKELQKIldrk 1101
Cdd:COG4717  369 EQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEqleelLGELEELLEALDEEELEEELEELEEELEEL---- 444

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1102 rhnsisEAKMRDKHKKEAELteinrRHITESVNSIRRLEEAQKQRHDrlvagQQQVLQQLAEE--EPKLLAQLAQECQE- 1178
Cdd:COG4717  445 ------EEELEELREELAEL-----EAELEQLEEDGELAELLQELEE-----LKAELRELAEEwaALKLALELLEEAREe 508

                        250
                 ....*....|..
gi 11386139 1179 -QRARLPQEIRR 1189
Cdd:COG4717  509 yREERLPPVLER 520
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 1017-1167 5.88e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 39.53  E-value: 5.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1017 DVEDTKEgedEAKRYQEfQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDAnttqfkrlkEMNEREKKEL-- 1094
Cdd:pfam06391   62 DVEETEK---KIEQYEK-ENKDLILKNKMKLSQEEEELEELLELEKREKEERRKEEKQE---------EEEEKEKKEKak 128

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386139   1095 QKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNsiRRLEEAQKQRHDRLVAGQQQVLQQlaEEEPK 1167
Cdd:pfam06391  129 QELIDELMTSNKDAEEIIAQHKKTAKKRKSERRRKLEELN--RVLEQKPTQFSTGIKFGQLPVPKI--EEGPL 197
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
955-1189 6.93e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139  955 DELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRL-LDGLAQAQAEGRCRLRpGALGGAADVEDTKEGEDEAKRYQE 1033
Cdd:COG4913  624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELE 702

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1034 fQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNERE-KKELQKILDRKRHNSISEAKmR 1112
Cdd:COG4913  703 -ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlGDAVERELRENLEERIDALR-A 780

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139 1113 DKHKKEAELTEINRRHITE----------SVNSIRR-LEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRA 1181
Cdd:COG4913  781 RLNRAEEELERAMRAFNREwpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIR 860


                 ....*...
gi 11386139 1182 RLPQEIRR 1189
Cdd:COG4913  861 EIKERIDP 868
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1015-1182 9.04e-03

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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 9.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1015 AADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDaNTTQFKRLKEMNEREKKEL 1094
Cdd:pfam13868   25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEE-REQKRQEEYEEKLQEREQM 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1095 QKILDRKRHNSISEAKMRDKHKKEA--ELTEINRRHIT-------ESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEE 1165
Cdd:pfam13868  104 DEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEwkelekeEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183

                          170
                   ....*....|....*..
gi 11386139   1166 pKLLAQLAQECQEQRAR 1182
Cdd:pfam13868  184 -REIARLRAQQEKAQDE 199
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 967-1189 9.87e-03

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 39.63  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139    967 RSRQERDLRELRKKHQRKAVTLTRRLLdglAQAQAEGRCRLRpgalggaaDVEDTKEGEDEAKRYQEfQNRQVQS--LLE 1044
Cdd:pfam15558   71 KARLGREERRRADRREKQVIEKESRWR---EQAEDQENQRQE--------KLERARQEAEQRKQCQE-QRLKEKEeeLQA 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386139   1045 LREaQVDAEAQRRLE------HLRQALQRLREVVLD----ANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMRDK 1114
Cdd:pfam15558  139 LRE-QNSLQLQERLEeachkrQLKEREEQKKVQENNlselLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLV 217

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11386139   1115 HKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLvagqqQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRR 1189
Cdd:pfam15558  218 EERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHK-----EALAELADRKIQQARQVAHKTVQDKAQRARELNL 287
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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