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Conserved domains on  [gi|442628536|ref|NP_001260618|]
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uncharacterized protein Dmel_CG10747, isoform B [Drosophila melanogaster]

Protein Classification

PI-PLC X domain-containing protein( domain architecture ID 10171267)

PI-PLC (phosphatidylinositol-specific phospholipase C) X domain-containing protein belongs to a small family of receptor-regulated phosphodiesterases that control many cellular processes by the regulation of cytosolic calcium and/or the activity of several protein kinases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 10-302 4.00e-130

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1), 2 (PI-PLCXD2) and 3 (PI-PLCXD3), which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, members in this group contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


:

Pssm-ID: 176555  Cd Length: 290  Bit Score: 372.73  E-value: 4.00e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  10 LPSELRDLSIINLAIPGSHNSMTYGINSKSELSPDAEIS-IRRWHRFFP-CFVRRWSKTQSSGTLDQLELGVRYFDLRIA 87
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSVQnLVKVFPCIFkKIVKKWSKTQSLTITEQLEAGIRYFDLRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  88 QK--DDKFYYCHGLFAMEIFEPLLEIRQFVDTHPEEVVILDLQHFYAMTVAHHQKLHKDLIQFFAHRLYSTVDgSLKDCT 165
Cdd:cd08616   81 TKpkDNDLYFVHGLYGILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDP-DLLNVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 166 LNRCLEMQRSVVIIYRRCPIPLPLRFWPSYAWPTPWPNKASVKKLQSFLEDSLLSRQPQQGYVSQCLITPTGRYIAFRLF 245
Cdd:cd08616  160 LEYLWEKGYQVIVFYHDPVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTILRHLT 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442628536 246 FTLKST-AKRVDKKLQPWIQEQIPGPFEPkdeprVNVFLADFVSLkgGQFCDWVVDLN 302
Cdd:cd08616  240 SGLLKTlTLRALPKLLEWLRKQEPGSGQG-----VNIIIADFVDL--DEFIDTVIALN 290
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 10-302 4.00e-130

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1), 2 (PI-PLCXD2) and 3 (PI-PLCXD3), which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, members in this group contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176555  Cd Length: 290  Bit Score: 372.73  E-value: 4.00e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  10 LPSELRDLSIINLAIPGSHNSMTYGINSKSELSPDAEIS-IRRWHRFFP-CFVRRWSKTQSSGTLDQLELGVRYFDLRIA 87
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSVQnLVKVFPCIFkKIVKKWSKTQSLTITEQLEAGIRYFDLRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  88 QK--DDKFYYCHGLFAMEIFEPLLEIRQFVDTHPEEVVILDLQHFYAMTVAHHQKLHKDLIQFFAHRLYSTVDgSLKDCT 165
Cdd:cd08616   81 TKpkDNDLYFVHGLYGILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDP-DLLNVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 166 LNRCLEMQRSVVIIYRRCPIPLPLRFWPSYAWPTPWPNKASVKKLQSFLEDSLLSRQPQQGYVSQCLITPTGRYIAFRLF 245
Cdd:cd08616  160 LEYLWEKGYQVIVFYHDPVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTILRHLT 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442628536 246 FTLKST-AKRVDKKLQPWIQEQIPGPFEPkdeprVNVFLADFVSLkgGQFCDWVVDLN 302
Cdd:cd08616  240 SGLLKTlTLRALPKLLEWLRKQEPGSGQG-----VNIIIADFVDL--DEFIDTVIALN 290
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 6-262 1.18e-20

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 91.49  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536   6 WMRDLPSELRDLSIINLAIPGSHNSMTYGINSKSELSPDAEISIRR------WHRFFpcFVR---RWSKTQSSGTLDQLE 76
Cdd:PTZ00268  18 WMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADAPGFLLGdsvvasLSRFL--FRGisaSWSKCQGMSVRAQLD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  77 LGVRYFDLRIA---QKDDKFYYCHGLFAMEIFEPLLEIRQFVDT--HPEEVVILDLQHFYAMTVAHHQKLHKDLIQFFAH 151
Cdd:PTZ00268  96 HGVRYLDLRVAtnpEDANRLYISHTQISVPLADVLEDVKAFLNDpsSANEFIVLDFQHLYLTDDSDGKGKFFRELDRLSD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 152 RlYSTVDGSLKD--CTLNRCLEMQRS-VVIIYRRCPIPLPLRFWPSYAWPTPWPNKASVKKLQSFLEDSLLS--RQPQQG 226
Cdd:PTZ00268 176 R-FIPVDVPLTTplEILWRVSRRRRIfLVVASGRNYVPYPAARIRSKCMVSRWVNQMSLRKLLQALENLLLDdlKYPQTG 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442628536 227 -----YVSQCLITPTGRYIAFRLF--------FTLKSTAKRVDKKLQPW 262
Cdd:PTZ00268 255 vpsklYVTQAVYTPRNSDIFRGIFpkisrkvvSSIYDVAKRKNPSLLEW 303
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 62-156 2.65e-05

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: 43.42  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536    62 RWSKTQSSGTLDQLELGVRYFDLRI-AQKDDKFYYCHG-LFAMEIF--EPLLEIRQFVDTHPEEVVILDLQHFYAMTVAH 137
Cdd:smart00148  23 LWGESSVEGYIQALDAGCRCVELDCwDGPDGEPVIYHGhTFTLPIKlsEVLEAIKDFAFVTSPYPVILSLENHCSPDQQA 102

                           90
                   ....*....|....*....
gi 442628536   138 HQKLHkdLIQFFAHRLYST 156
Cdd:smart00148 103 KMAQM--FKEIFGDMLYTP 119
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 10-302 4.00e-130

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1), 2 (PI-PLCXD2) and 3 (PI-PLCXD3), which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, members in this group contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176555  Cd Length: 290  Bit Score: 372.73  E-value: 4.00e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  10 LPSELRDLSIINLAIPGSHNSMTYGINSKSELSPDAEIS-IRRWHRFFP-CFVRRWSKTQSSGTLDQLELGVRYFDLRIA 87
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSVQnLVKVFPCIFkKIVKKWSKTQSLTITEQLEAGIRYFDLRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  88 QK--DDKFYYCHGLFAMEIFEPLLEIRQFVDTHPEEVVILDLQHFYAMTVAHHQKLHKDLIQFFAHRLYSTVDgSLKDCT 165
Cdd:cd08616   81 TKpkDNDLYFVHGLYGILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDP-DLLNVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 166 LNRCLEMQRSVVIIYRRCPIPLPLRFWPSYAWPTPWPNKASVKKLQSFLEDSLLSRQPQQGYVSQCLITPTGRYIAFRLF 245
Cdd:cd08616  160 LEYLWEKGYQVIVFYHDPVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTILRHLT 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442628536 246 FTLKST-AKRVDKKLQPWIQEQIPGPFEPkdeprVNVFLADFVSLkgGQFCDWVVDLN 302
Cdd:cd08616  240 SGLLKTlTLRALPKLLEWLRKQEPGSGQG-----VNIIIADFVDL--DEFIDTVIALN 290
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 11-302 2.36e-97

Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins; This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) 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 and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more 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.


Pssm-ID: 176529  Cd Length: 288  Bit Score: 289.24  E-value: 2.36e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  11 PSELRDLSIINLAIPGSHNSMTYGINSKSELSPDAEisirRWHRFFPCFVRRWSKTQSSGTLDQLELGVRYFDLRIAQK- 89
Cdd:cd08587    1 PSAIGDLPLRDLVIPGSHDSGMYTINGDSPVGPDQP----EFGKIAKGIVRKWSVTQSLSIYDQLEAGIRYFDLRVAYKp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  90 --DDKFYYCHGLFA-MEIFEPLLEIRQFVDTHPEEVVILDLQHFYAMT---VAHHQKLHKDLIQFFAHRLYSTvDGSLKD 163
Cdd:cd08587   77 dsENKLYFVHGLYSgEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDdksPEDHEKLVELLEDIFGDKLCPR-DSDLLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 164 CTLNRCLEMQRSVVIIYRRCPIPLPLRFWPSYAWPTPWPNKASVKKLQSFLEDSLLSRQ-PQQGYVSQCLITPTGRYIAF 242
Cdd:cd08587  156 VTLADLWESGKRVIVFYDDDLASEGPYLWPSPYIPDPWANTDDPQKLIDFLENKLKERRrPDKFFVLQWILTPQASTIVL 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442628536 243 RLFFT-LKSTAKRVDKKLQPWIQEQIPGPfepkdePRVNVFLADFVSlkGGQFCDWVVDLN 302
Cdd:cd08587  236 GLFSGlLKKLALRANPALLEWLREQLPGQ------DGPNIILNDFVD--LGEFIDLAIALN 288
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 11-302 5.96e-55

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: 180.37  E-value: 5.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  11 PSELRDLSIINLAIPGSHNSMTYGINSKSELspdaeisirrwhrffpcfVRRWSKTQSSGTLDQLELGVRYFDLRIAQK- 89
Cdd:cd08557    1 PALLDDLPLSQLSIPGTHNSYAYTIDGNSPI------------------VSKWSKTQDLSITDQLDAGVRYLDLRVAYDp 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  90 -DDKFYYCHGLF---AMEIFEPLLEIRQFVDTHPEEVVILDLQHFYAM-TVAHHQKLHKDLIQFFAHRLYSTVDGSLKDC 164
Cdd:cd08557   63 dDGDLYVCHGLFllnGQTLEDVLNEVKDFLDAHPSEVVILDLEHEYGGdNGEDHDELDALLRDVLGDPLYRPPVRAGGWP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 165 TLNRCLEMQRsVVIIYRRCPIPLPLRFWPSYAWPTPWPNKA-SVKKLQSFLEDSLLSRQ-PQQGYVSQCLITPTGRYIAF 242
Cdd:cd08557  143 TLGELRAGKR-VLLFYFGGDDSSGGYDWGSLNIQDPYANGTdKLESLKAFLNSALASPRsADFFYVNQASLTPGRITIAV 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 243 RlfFTLKSTAKRVDKKLQPWIQEQIPGpfepkdEPRVNVFLADFVSlkGGQFCDWVVDLN 302
Cdd:cd08557  222 A--GSLYTVATRANPALYEWLKEDGSG------ASGPNIVATDFVD--VGDLIDAVIRLN 271
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 17-288 7.23e-21

Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to phosphatidylinositol-specific phospholipase C, X domain containing; This subfamily corresponds to the catalytic domain present in uncharacterized metazoan Drosophila melanogaster CG14945-like proteins, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176559  Cd Length: 276  Bit Score: 90.47  E-value: 7.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  17 LSIINLAIPGSHNSMTYGINSkselspDAEISIrrwhrffpcfVRRWSKTQSSGTLDQLELGVRYFDLRIAQK---DDKF 93
Cdd:cd08622    7 LRIKDLFIPGTHNSAAYDTNS------NANESL----------VDKYLLTQDLDIWTQLVHGIRYLDLRVGYYpdsPDNF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  94 YYCHGLFAM-EIFEPLLEIRQFVDThPEEVVILDLQHFY---AMTVAHHQKLHKDLIQFFAHRLYSTVDGSLKDCTLNRC 169
Cdd:cd08622   71 WINHDLVRIvPLLTVLNDVRNFVQN-TGEIVVLDFHRFPvgfHSHPEVHDELISLLRQELGDLILRRSRNYGWGPTLSEI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 170 LEMQRSVVIIYR-RCPIPLPLRFWPSyaWPTPWPNKASVKKLQSFLeDSLLSRQPQQG---YVSQCLITPTGRYIAFRLF 245
Cdd:cd08622  150 WARRKRVIICYDhEYFVRESDWLWPP--VQQKWGNVQTLDDLKSYL-RKLISQPHRFTnppVSLMAELTPVPWDIISDRL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442628536 246 FTLKSTAKRVDKKLQPWIQEQIpgpfepkdEPRVNVFLADFVS 288
Cdd:cd08622  227 GNLRKLADIVNRKLTRWYRDEW--------GYNANIVATDFFL 261
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 6-262 1.18e-20

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 91.49  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536   6 WMRDLPSELRDLSIINLAIPGSHNSMTYGINSKSELSPDAEISIRR------WHRFFpcFVR---RWSKTQSSGTLDQLE 76
Cdd:PTZ00268  18 WMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADAPGFLLGdsvvasLSRFL--FRGisaSWSKCQGMSVRAQLD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  77 LGVRYFDLRIA---QKDDKFYYCHGLFAMEIFEPLLEIRQFVDT--HPEEVVILDLQHFYAMTVAHHQKLHKDLIQFFAH 151
Cdd:PTZ00268  96 HGVRYLDLRVAtnpEDANRLYISHTQISVPLADVLEDVKAFLNDpsSANEFIVLDFQHLYLTDDSDGKGKFFRELDRLSD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 152 RlYSTVDGSLKD--CTLNRCLEMQRS-VVIIYRRCPIPLPLRFWPSYAWPTPWPNKASVKKLQSFLEDSLLS--RQPQQG 226
Cdd:PTZ00268 176 R-FIPVDVPLTTplEILWRVSRRRRIfLVVASGRNYVPYPAARIRSKCMVSRWVNQMSLRKLLQALENLLLDdlKYPQTG 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442628536 227 -----YVSQCLITPTGRYIAFRLF--------FTLKSTAKRVDKKLQPW 262
Cdd:PTZ00268 255 vpsklYVTQAVYTPRNSDIFRGIFpkisrkvvSSIYDVAKRKNPSLLEW 303
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 7-156 1.58e-15

Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins; This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and its sequence homologs found in bacteria and 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. Their 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. This family also includes some uncharacterized eukaryotic homologs, which contains a single TIM-barrel type catalytic domain, X domain. They are similar to bacterial PI-PLCs, and distinct from typical eukaryotic PI-PLCs, which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC, which has a moderate thermal stability and is active as a monomer.


Pssm-ID: 176528  Cd Length: 279  Bit Score: 75.40  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536   7 MRDLPSelrDLSIINLAIPGSHNSMTYGINSKSelspdaeisirrwhrffpcfvrrWSKTQSSGTLDQLELGVRYFDLRI 86
Cdd:cd08586    1 MSALPD---DTPLSELSIPGTHDSGALHGGLSS-----------------------SVQCQDWSIAEQLNAGIRFLDIRL 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442628536  87 A-QKDDKFYYCHGLFAMEI-FEPLL-EIRQFVDTHPEEVVILDLQHFYAMTVAHH---QKLHKDLIQFFAHRLYST 156
Cdd:cd08586   55 RlIDNNDLAIHHGPFYQGLtFGDVLnECYSFLDANPSETIIMSLKQEGSGDGNTDsfaEIFKEYLDNYPSYFYYTE 130
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 14-292 3.54e-12

Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins; This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176558  Cd Length: 300  Bit Score: 65.86  E-value: 3.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  14 LRDLSIINLAIPGSHNSmtyGINSKS-ELSPDaeisirrwhrfFPcfVRRWSKTQSSGTLDQLELGVRYFDLRIAQKDD- 91
Cdd:cd08621    4 IKDRPLRHIVMPGTHDS---GMSSLTgGLWPV-----------DG--NDSNTQTQGLSIYDQLRAGARYFDIRPVITHGg 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  92 KFYYCHGLFAM---------EIFEPLLEIRQFVDTHPEEVVILDLQHFYAMTVAHHQKLHKDLIqffaHRLYSTVDGSLK 162
Cdd:cd08621   68 ELWTGHYNGEDasaqgangeSLDDILDEVNRFTDENPGELVILNFSHILNTDNGDGRPFSAEEW----EKIFDELEGINN 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 163 DCTlNRCLEMQ---------------RSVVIIYRRCPIPLPLR--------FWPSYAWPTPWPNKASVKKLQSF-LEDSL 218
Cdd:cd08621  144 RCG-NIDEEGDlytqklsdfidasgkACVVFIYDGTISSNQGStpakggiyDGPQFTVYDSYSNTDDTNYMAEDqLAKLR 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536 219 LSRQPQQG----YVSQCLITPTgryiafRLFFT---LKSTAKRVDKKLQPWIQEQIpgpfepKDEPRVNVFLADFVSLKG 291
Cdd:cd08621  223 SHRRPSFGddifFLLSWTLTPQ------ALTVTgssIKKLAEEANPALFWKLVDAM------SPWSFPNVVYVDYLGNFG 290


                 .
gi 442628536 292 G 292
Cdd:cd08621  291 E 291
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 1-127 1.27e-09

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing proteins found in plants; The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, plant PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of plant PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176556  Cd Length: 285  Bit Score: 58.33  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536   1 MSKDH--WMRDLPSEL--RDLSIINLAIPGSHNSMTyginskselspdAEISIrrwhrffPCFVRRWSKTQSSGTLDQLE 76
Cdd:cd08619    7 HTDDHkeWMSLSQLKAmdSSLKLRDIVWPGTHDSAT------------NKIGI-------PKVSRPFARCQSLSIYNQLC 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442628536  77 LGVRYFDLRIAqkdDKFYYCHGLFAMEIFEPLL-EIRQFVDTHPEEVVILDL 127
Cdd:cd08619   68 SGARVLDIRVQ---EDRRVCHGCLKTYPVDVVLnDIKRFLSETKSEFVILEI 116
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 12-201 1.32e-06

Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs; This subfamily corresponds to the catalytic domain present in Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. Members in this family show high sequence similarity to bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participates in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG).


Pssm-ID: 176530  Cd Length: 270  Bit Score: 48.87  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  12 SELRDLSIINLAIPGSHNSMTYGiNSKSELSPDAEISIRrwhrffpcfvrrwsktqssgtlDQLELGVRYFDLRIAQKDD 91
Cdd:cd08588    5 PALCDRTYDEYTFLTTHNSFANS-EDAFFLAPNQEDDIT----------------------KQLDDGVRGLMLDIHDANG 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  92 KFYYCHGLFAMEIFEPLL----EIRQFVDTHPEEVVILDLQHfyamTVAHHQKLHKDLIQF--FAHRLYsTVDGSLKDC- 164
Cdd:cd08588   62 GLRLCHSVCGLGDGGPLSdvlrEVVDFLDANPNEVVTLFLED----YVSPGPLLRSKLFRVagLTDLVY-VPDAMPWAGs 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 442628536 165 ---TLNrclEM----QRSVVIIYR--RCPIPLPLRFWPSYAWPTPW 201
Cdd:cd08588  137 dwpTLG---EMidanKRLLVFTDNedVSTEPPGVMYQFDYTVENPF 179
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 20-131 2.01e-05

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: 45.33  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  20 INLA---IPGSHNSMTYginskselspDAEISIRRwhrffpcfvrRWSKTQSSGTLDQLELGVRYFDLRIAQKDDK---F 93
Cdd:cd00137    6 QPLAhysIPGTHDTYLT----------AGQFTIKQ----------VWGLTQTEMYRQQLLSGCRCVDIRCWDGKPEepiI 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 442628536  94 YycHGLFAMEIF--EPLLEIRQFVDTHPEEVVILDLQHFY 131
Cdd:cd00137   66 Y--HGPTFLDIFlkEVIEAIAQFLKKNPPETIIMSLKNEV 103
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 62-156 2.65e-05

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: 43.42  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536    62 RWSKTQSSGTLDQLELGVRYFDLRI-AQKDDKFYYCHG-LFAMEIF--EPLLEIRQFVDTHPEEVVILDLQHFYAMTVAH 137
Cdd:smart00148  23 LWGESSVEGYIQALDAGCRCVELDCwDGPDGEPVIYHGhTFTLPIKlsEVLEAIKDFAFVTSPYPVILSLENHCSPDQQA 102

                           90
                   ....*....|....*....
gi 442628536   138 HQKLHkdLIQFFAHRLYST 156
Cdd:smart00148 103 KMAQM--FKEIFGDMLYTP 119
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 22-125 5.01e-05

Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins; This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176557  Cd Length: 281  Bit Score: 44.31  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  22 LAIPGSHNSMTYGINSkselspdaeisirrwhrffpcfvrrWSKTQSSGTLDQLELGVRYFDLRIAQKD---------DK 92
Cdd:cd08620   12 FVLPGAHDAGMNGMTN-------------------------LSVTQKDNVSTQLALGARYFDFRPGYLWpqtrvlvllND 66

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442628536  93 FYYCHGLFAMEIFEPLL-EIRQFVDTHPEEVVIL 125
Cdd:cd08620   67 LYHQHNMIPGQGFDTFLqDVVTFLKANPTEIVVV 100
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 24-125 1.02e-04

Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This subfamily corresponds to the catalytic domain present in uncharacterized Mycobacterium tuberculosis Rv2075c and its homologs. Members in this family are more closely related to the Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1(SaPLC1)-like proteins rather than the typical bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). In contrast, SaPLC1-like proteins have two Ca2+-chelating amino acid substitutions which convert them to metal-dependent bacterial PI-PLC. Rv2075c and its homologs have the same amino acid substitutions as well, which might suggest they have metal-dependent PI-PLC activity.


Pssm-ID: 176532  Cd Length: 267  Bit Score: 43.16  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628536  24 IPGSHNSmtygINSKSelspDAEISIRRWhrffpcfVRRWSKTQSSGTLDQLELGVRYFDLRIAQKDDKFYYCHG----- 98
Cdd:cd08590   15 ILGTHNS----YNSRA----YGYGNRYHG-------VRYLDPNQELSITDQLDLGARFLELDVHWTTGDLRLCHGgdhgy 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442628536  99 LFAMEIFEPLL-----EIRQFVDTHPEEVVIL 125
Cdd:cd08590   80 LGVCSSEDRLFedglnEIADWLNANPDEVVIL 111
 
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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