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Conserved domains on  [gi|197333713|ref|NP_001127953|]
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PI-PLC X domain-containing protein 2 [Rattus norvegicus]

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 ...
 39-329 1.89e-163

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: 457.47  E-value: 1.89e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  39 LPPHLHNVPLSNLAIPGSHDSFSYWVDEKSPVGPDQTQAVKRLARISLVKKLMKKWSVTQNLTFREQLEAGIRYFDLRVS 118
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSVQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 119 SKPGdtDQEIYFIHGLFGIKVWDGLMEIDAFLTQHPQEIIFLDFNHFYAMDEAHHKCLVLRIQEAFGNKLCPAC-SVESM 197
Cdd:cd08616   81 TKPK--DNDLYFVHGLYGILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDpDLLNV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 198 TLRTLWEKKYQVLIFYHCPFYKQYPFLWPGKKIPAPWANTTSVQKLILFLETTLSERAPRGaFHVSQAILTPRVKTIARG 277
Cdd:cd08616  159 TLEYLWEKGYQVIVFYHDPVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPG-FHVSQGILTPDVKTILRH 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 197333713 278 LVGGLKNTLVHRNLPAILDWVKTQKPGAM-GVNIITSDFVDLIDFATTVIELN 329
Cdd:cd08616  238 LTSGLLKTLTLRALPKLLEWLRKQEPGSGqGVNIIIADFVDLDEFIDTVIALN 290
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 39-329 1.89e-163

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: 457.47  E-value: 1.89e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  39 LPPHLHNVPLSNLAIPGSHDSFSYWVDEKSPVGPDQTQAVKRLARISLVKKLMKKWSVTQNLTFREQLEAGIRYFDLRVS 118
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSVQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 119 SKPGdtDQEIYFIHGLFGIKVWDGLMEIDAFLTQHPQEIIFLDFNHFYAMDEAHHKCLVLRIQEAFGNKLCPAC-SVESM 197
Cdd:cd08616   81 TKPK--DNDLYFVHGLYGILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDpDLLNV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 198 TLRTLWEKKYQVLIFYHCPFYKQYPFLWPGKKIPAPWANTTSVQKLILFLETTLSERAPRGaFHVSQAILTPRVKTIARG 277
Cdd:cd08616  159 TLEYLWEKGYQVIVFYHDPVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPG-FHVSQGILTPDVKTILRH 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 197333713 278 LVGGLKNTLVHRNLPAILDWVKTQKPGAM-GVNIITSDFVDLIDFATTVIELN 329
Cdd:cd08616  238 LTSGLLKTLTLRALPKLLEWLRKQEPGSGqGVNIIIADFVDLDEFIDTVIALN 290
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 35-297 1.10e-25

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 105.74  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  35 WMASLPPHLHNVPLSNLAIPGSHDSFSYWVDEKSPVGPD------QTQAVKRLARIsLVKKLMKKWSVTQNLTFREQLEA 108
Cdd:PTZ00268  18 WMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADapgfllGDSVVASLSRF-LFRGISASWSKCQGMSVRAQLDH 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 109 GIRYFDLRVSSKPGDTDQeIYFIHGLFGIKVWDGLMEIDAFLTQ--HPQEIIFLDFNHFYAMDEAHHKCLVLRIQEAFGN 186
Cdd:PTZ00268  97 GVRYLDLRVATNPEDANR-LYISHTQISVPLADVLEDVKAFLNDpsSANEFIVLDFQHLYLTDDSDGKGKFFRELDRLSD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 187 KLCPACSVESMTLRTLWEKKYQVLIFYHCPF---YKQYPFL-WPGKKIPAPWANTTSVQKLILFLETTLS---ERAPRGA 259
Cdd:PTZ00268 176 RFIPVDVPLTTPLEILWRVSRRRRIFLVVASgrnYVPYPAArIRSKCMVSRWVNQMSLRKLLQALENLLLddlKYPQTGV 255

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 197333713 260 ---FHVSQAILTPRVKTIARGLVGGLKNTLV--------HRNlPAILDW 297
Cdd:PTZ00268 256 pskLYVTQAVYTPRNSDIFRGIFPKISRKVVssiydvakRKN-PSLLEW 303
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 45-212 4.56e-09

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: 54.21  E-value: 4.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713    45 NVPLSNLAIPGSHDSFsywvdekspvgpdqtqavkrlariSLVKKLmkkWSVTQNLTFREQLEAGIRYFDLRVssKPGDt 124
Cdd:smart00148   2 DKPLSHYFIPSSHNTY------------------------LTGKQL---WGESSVEGYIQALDAGCRCVELDC--WDGP- 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713   125 DQEIYFIHG-LFGIKVW--DGLMEIDAFLTQHPQEIIFLDFNHFYAMDEAHHkcLVLRIQEAFGNKL-CPACSVESMTLR 200
Cdd:smart00148  52 DGEPVIYHGhTFTLPIKlsEVLEAIKDFAFVTSPYPVILSLENHCSPDQQAK--MAQMFKEIFGDMLyTPPLTSSLEVLP 129

                          170
                   ....*....|..
gi 197333713   201 TLWEKKYQVLIF 212
Cdd:smart00148 130 SPEQLRGKILLK 141
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 39-329 1.89e-163

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: 457.47  E-value: 1.89e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  39 LPPHLHNVPLSNLAIPGSHDSFSYWVDEKSPVGPDQTQAVKRLARISLVKKLMKKWSVTQNLTFREQLEAGIRYFDLRVS 118
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSVQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 119 SKPGdtDQEIYFIHGLFGIKVWDGLMEIDAFLTQHPQEIIFLDFNHFYAMDEAHHKCLVLRIQEAFGNKLCPAC-SVESM 197
Cdd:cd08616   81 TKPK--DNDLYFVHGLYGILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDpDLLNV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 198 TLRTLWEKKYQVLIFYHCPFYKQYPFLWPGKKIPAPWANTTSVQKLILFLETTLSERAPRGaFHVSQAILTPRVKTIARG 277
Cdd:cd08616  159 TLEYLWEKGYQVIVFYHDPVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPG-FHVSQGILTPDVKTILRH 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 197333713 278 LVGGLKNTLVHRNLPAILDWVKTQKPGAM-GVNIITSDFVDLIDFATTVIELN 329
Cdd:cd08616  238 LTSGLLKTLTLRALPKLLEWLRKQEPGSGqGVNIIIADFVDLDEFIDTVIALN 290
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 40-329 2.15e-126

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: 363.59  E-value: 2.15e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  40 PPHLHNVPLSNLAIPGSHDSFSYWVDEKSPVGPDQTQAvkrlarISLVKKLMKKWSVTQNLTFREQLEAGIRYFDLRVSS 119
Cdd:cd08587    1 PSAIGDLPLRDLVIPGSHDSGMYTINGDSPVGPDQPEF------GKIAKGIVRKWSVTQSLSIYDQLEAGIRYFDLRVAY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 120 KPGDTDqEIYFIHGLFGI-KVWDGLMEIDAFLTQHPQEIIFLDFNHFYAMDE---AHHKCLVLRIQEAFGNKLCP-ACSV 194
Cdd:cd08587   75 KPDSEN-KLYFVHGLYSGePVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDDkspEDHEKLVELLEDIFGDKLCPrDSDL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 195 ESMTLRTLWEKKYQVLIFYHCPFYKQYPFLWPGKKIPAPWANTTSVQKLILFLETTLSERAPRGAFHVSQAILTPRVKTI 274
Cdd:cd08587  154 LDVTLADLWESGKRVIVFYDDDLASEGPYLWPSPYIPDPWANTDDPQKLIDFLENKLKERRRPDKFFVLQWILTPQASTI 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 197333713 275 ARGLVGGLKNTLVHRNLPAILDWVKTQKPGAMGVNIITSDFVDLIDFATTVIELN 329
Cdd:cd08587  234 VLGLFSGLLKKLALRANPALLEWLREQLPGQDGPNIILNDFVDLGEFIDLAIALN 288
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 40-329 6.86e-77

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: 236.99  E-value: 6.86e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  40 PPHLHNVPLSNLAIPGSHDSFSYWVDEKSPVgpdqtqavkrlarislvkklMKKWSVTQNLTFREQLEAGIRYFDLRVSS 119
Cdd:cd08557    1 PALLDDLPLSQLSIPGTHNSYAYTIDGNSPI--------------------VSKWSKTQDLSITDQLDAGVRYLDLRVAY 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 120 KPGDTDqeIYFIHGLF---GIKVWDGLMEIDAFLTQHPQEIIFLDFNHFYAMDE-AHHKCLVLRIQEAFGNKLCPACSVE 195
Cdd:cd08557   61 DPDDGD--LYVCHGLFllnGQTLEDVLNEVKDFLDAHPSEVVILDLEHEYGGDNgEDHDELDALLRDVLGDPLYRPPVRA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 196 S--MTLRTLWEKKyQVLIFYHCPFYKQYPFLWPGKKIPAPWAN-TTSVQKLILFLETTLSERAPRGAFHVSQAILTPRVK 272
Cdd:cd08557  139 GgwPTLGELRAGK-RVLLFYFGGDDSSGGYDWGSLNIQDPYANgTDKLESLKAFLNSALASPRSADFFYVNQASLTPGRI 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 197333713 273 TIArglVGGLKNTLVHRNLPAILDWVKTQKPGAMGVNIITSDFVDLIDFATTVIELN 329
Cdd:cd08557  218 TIA---VAGSLYTVATRANPALYEWLKEDGSGASGPNIVATDFVDVGDLIDAVIRLN 271
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 42-329 4.39e-30

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: 115.50  E-value: 4.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  42 HLHNVPLSNLAIPGSHDSFSYwvdekspvgpdqtqAVKRLARISLVKKLmkkwSVTQNLTFREQLEAGIRYFDLRVSSKP 121
Cdd:cd08622    3 SIGNLRIKDLFIPGTHNSAAY--------------DTNSNANESLVDKY----LLTQDLDIWTQLVHGIRYLDLRVGYYP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 122 GDTDQeIYFIHGLFGI-KVWDGLMEIDAFLtQHPQEIIFLDFNHFY---AMDEAHHKCLVLRIQEAFGNKLCPACSVES- 196
Cdd:cd08622   65 DSPDN-FWINHDLVRIvPLLTVLNDVRNFV-QNTGEIVVLDFHRFPvgfHSHPEVHDELISLLRQELGDLILRRSRNYGw 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 197 -MTLRTLWEKKYQVLIFY-HCPFYKQYPFLWPGkkIPAPWANTTSVQKLILFLETTLSERAPRGAFHVS-QAILTPRVKT 273
Cdd:cd08622  143 gPTLSEIWARRKRVIICYdHEYFVRESDWLWPP--VQQKWGNVQTLDDLKSYLRKLISQPHRFTNPPVSlMAELTPVPWD 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197333713 274 IARGLVGGLKN--TLVHRNLpaiLDWVKTqkPGAMGVNIITSDFV---DLIDFAttvIELN 329
Cdd:cd08622  221 IISDRLGNLRKlaDIVNRKL---TRWYRD--EWGYNANIVATDFFlgtNIIDVA---IETN 273
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 35-297 1.10e-25

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 105.74  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  35 WMASLPPHLHNVPLSNLAIPGSHDSFSYWVDEKSPVGPD------QTQAVKRLARIsLVKKLMKKWSVTQNLTFREQLEA 108
Cdd:PTZ00268  18 WMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADapgfllGDSVVASLSRF-LFRGISASWSKCQGMSVRAQLDH 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 109 GIRYFDLRVSSKPGDTDQeIYFIHGLFGIKVWDGLMEIDAFLTQ--HPQEIIFLDFNHFYAMDEAHHKCLVLRIQEAFGN 186
Cdd:PTZ00268  97 GVRYLDLRVATNPEDANR-LYISHTQISVPLADVLEDVKAFLNDpsSANEFIVLDFQHLYLTDDSDGKGKFFRELDRLSD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 187 KLCPACSVESMTLRTLWEKKYQVLIFYHCPF---YKQYPFL-WPGKKIPAPWANTTSVQKLILFLETTLS---ERAPRGA 259
Cdd:PTZ00268 176 RFIPVDVPLTTPLEILWRVSRRRRIFLVVASgrnYVPYPAArIRSKCMVSRWVNQMSLRKLLQALENLLLddlKYPQTGV 255

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 197333713 260 ---FHVSQAILTPRVKTIARGLVGGLKNTLV--------HRNlPAILDW 297
Cdd:PTZ00268 256 pskLYVTQAVYTPRNSDIFRGIFPKISRKVVssiydvakRKN-PSLLEW 303
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 47-329 1.31e-19

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: 87.43  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  47 PLSNLAIPGSHDS-FSYWVDEKSPVGPDQTqavkrlarislvkklmkkWSVTQNLTFREQLEAGIRYFDLRVSSkpgDTD 125
Cdd:cd08621    8 PLRHIVMPGTHDSgMSSLTGGLWPVDGNDS------------------NTQTQGLSIYDQLRAGARYFDIRPVI---THG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 126 QEIYFIHGLFGIKVWDG---------LMEIDAFLTQHPQEIIFLDFNHFYAMDEAHHKCLVLRIQEAFGNKL------CP 190
Cdd:cd08621   67 GELWTGHYNGEDASAQGangeslddiLDEVNRFTDENPGELVILNFSHILNTDNGDGRPFSAEEWEKIFDELeginnrCG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 191 ACSVE----SMTLRTLWEK--KYQVLIFY--------HCPFYKQYPFLWPGKKIPAPWANTTSVQKLILFLETTLSERAP 256
Cdd:cd08621  147 NIDEEgdlyTQKLSDFIDAsgKACVVFIYdgtissnqGSTPAKGGIYDGPQFTVYDSYSNTDDTNYMAEDQLAKLRSHRR 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713 257 R----GAFHVSQAILTPRVKTIARGLVGGL----KNTLVHRNLPAILDWvktQKPgamgvNIITSDFVDLI-DFATTVIE 327
Cdd:cd08621  227 PsfgdDIFFLLSWTLTPQALTVTGSSIKKLaeeaNPALFWKLVDAMSPW---SFP-----NVVYVDYLGNFgEVLALAIG 298


                 ..
gi 197333713 328 LN 329
Cdd:cd08621  299 LN 300
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 36-160 2.47e-18

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: 83.49  E-value: 2.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  36 MASLPPhlhNVPLSNLAIPGSHDSFSYWVDEKSpvgpdqtqavkrlarislvkklmkkWSVTQNLTFREQLEAGIRYFDL 115
Cdd:cd08586    1 MSALPD---DTPLSELSIPGTHDSGALHGGLSS-------------------------SVQCQDWSIAEQLNAGIRFLDI 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 197333713 116 RVSskpGDTDQEIYFIHGLFGIKVWDG--LMEIDAFLTQHPQEIIFL 160
Cdd:cd08586   53 RLR---LIDNNDLAIHHGPFYQGLTFGdvLNECYSFLDANPSETIIM 96
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 41-170 3.52e-10

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: 59.97  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  41 PHLHNVPLSNLAIPGSHDSFSYwvdekspvgpdqtqavkrlariSLVKKLMKKWSVTQNLTFREQLEAGIRYFDLRvsSK 120
Cdd:cd00137    1 HHPDTQPLAHYSIPGTHDTYLT----------------------AGQFTIKQVWGLTQTEMYRQQLLSGCRCVDIR--CW 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 197333713 121 PGDtDQEIYFIHGLFGIKVW--DGLMEIDAFLTQHPQEIIFLDF-NHFYAMDE 170
Cdd:cd00137   57 DGK-PEEPIIYHGPTFLDIFlkEVIEAIAQFLKKNPPETIIMSLkNEVDSMDS 108
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 45-212 4.56e-09

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: 54.21  E-value: 4.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713    45 NVPLSNLAIPGSHDSFsywvdekspvgpdqtqavkrlariSLVKKLmkkWSVTQNLTFREQLEAGIRYFDLRVssKPGDt 124
Cdd:smart00148   2 DKPLSHYFIPSSHNTY------------------------LTGKQL---WGESSVEGYIQALDAGCRCVELDC--WDGP- 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713   125 DQEIYFIHG-LFGIKVW--DGLMEIDAFLTQHPQEIIFLDFNHFYAMDEAHHkcLVLRIQEAFGNKL-CPACSVESMTLR 200
Cdd:smart00148  52 DGEPVIYHGhTFTLPIKlsEVLEAIKDFAFVTSPYPVILSLENHCSPDQQAK--MAQMFKEIFGDMLyTPPLTSSLEVLP 129

                          170
                   ....*....|..
gi 197333713   201 TLWEKKYQVLIF 212
Cdd:smart00148 130 SPEQLRGKILLK 141
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 45-163 2.06e-08

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: 54.71  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  45 NVPLSNLAIPGSHDSFSYwvdekspvgpdqtqavkrlarislvkkLMKKWSVTQNLTFREQLEAGIRYFDLRVSSKP--- 121
Cdd:cd08620    6 QQPFNRFVLPGAHDAGMN---------------------------GMTNLSVTQKDNVSTQLALGARYFDFRPGYLWpqt 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 197333713 122 ---GDTDQeIYFIHGLFGIKVWDG-LMEIDAFLTQHPQEIIFLDFN 163
Cdd:cd08620   59 rvlVLLND-LYHQHNMIPGQGFDTfLQDVVTFLKANPTEIVVVHIT 103
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 47-162 1.58e-05

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: 45.78  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  47 PLSNLAIPGSHDSFSywvdekspvgpdqTQAVKRLArislvkklmkkwSVTQNLTFREQLEAGIRYFDLRVsskpGDTDQ 126
Cdd:cd08588   11 TYDEYTFLTTHNSFA-------------NSEDAFFL------------APNQEDDITKQLDDGVRGLMLDI----HDANG 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 197333713 127 EIYFIHG----LFGIKVWDGLMEIDAFLTQHPQEIIFLDF 162
Cdd:cd08588   62 GLRLCHSvcglGDGGPLSDVLREVVDFLDANPNEVVTLFL 101
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 45-190 1.28e-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: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  45 NVPLSNLAIPGSHDSFsywvdekspvgpdQTQAVKRLARISLVKKlmkkWSVTQNLTFREQLEAGIRYFDLRVSSKPGDT 124
Cdd:cd08590    7 NAPLCQAQILGTHNSY-------------NSRAYGYGNRYHGVRY----LDPNQELSITDQLDLGARFLELDVHWTTGDL 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 197333713 125 DQEIYFIHGLFGIK------VWDGLMEIDAFLTQHPQEIIFLDFNHfyAMDEAHHKCLVLRIQEAFGNKLCP 190
Cdd:cd08590   70 RLCHGGDHGYLGVCssedrlFEDGLNEIADWLNANPDEVVILYLED--HGDGGKDDELNALLNDAFGDLLYT 139
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 34-164 1.35e-04

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: 42.92  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333713  34 DWMASLPPHL--HNVPLSNLAIPGSHDSFSywvdekspvgpdqtqavkrlARISlVKKLMKKWSVTQNLTFREQLEAGIR 111
Cdd:cd08619   13 EWMSLSQLKAmdSSLKLRDIVWPGTHDSAT--------------------NKIG-IPKVSRPFARCQSLSIYNQLCSGAR 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 197333713 112 YFDLRVSskpgdtdQEIYFIHG-LFGIKVWDGLMEIDAFLTQHPQEIIFL----DFNH 164
Cdd:cd08619   72 VLDIRVQ-------EDRRVCHGcLKTYPVDVVLNDIKRFLSETKSEFVILeirtEYGH 122
 
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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