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Conserved domains on  [gi|283436112|ref|NP_694566|]
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phospholipase B1, membrane-associated isoform 1 precursor [Homo sapiens]

Protein Classification

phospholipase B family protein( domain architecture ID 10110727)

phospholipase B family protein is part of the SGNH-family of lipolytic enzymes that may have both esterase and phospholipase-A/lysophospholipase activity; it may be a membrane protein involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 382-677 8.23e-146

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


:

Pssm-ID: 238862  Cd Length: 288  Bit Score: 446.02  E-value: 8.23e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  382 SVHRLKPADINVIGALGDSLTAGNGAGSTpgNVLDVLTQYRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKE 461
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSA--NNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  462 TSPNAFLNQAVAGGRAEDLPVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDIL 541
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  542 HAEVPRAFVNLVTVLEIVNLRELYQeKKVYCPRMiLRSLCPCVLKFDDNSTelATLIEFNKKFQEKTHQLIESGRYDtRE 621
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTK-KPLQCETL-LAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 283436112  622 DFTVVVQPFFENVDMPKTSEGlPDNSFFAPDCFHFSSKSHSRAASALWNNMLEPVG 677
Cdd:cd01824   234 DFAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 1085-1371 2.77e-134

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


:

Pssm-ID: 238862  Cd Length: 288  Bit Score: 415.20  E-value: 2.77e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1085 SVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTTLPNILKKFNPYLLGFSTSTWEGT- 1163
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1164 --AGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKDWKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSE 1241
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1242 ELPRAFVNVVEVMELASLYQGQGGK--CAMLAAQnNCTCLRHSQSSlEKQELKKVNWNLQHGISSFSYWHQYTqREDFAV 1319
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLAP-ECPCLLGPTEN-SYQDLKKFYKEYQNEVEEIVESGEFD-REDFAV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 283436112 1320 VVQPFFQNTLTPLNERGdTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVG 1371
Cdd:cd01824   238 VVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 729-1024 4.33e-133

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


:

Pssm-ID: 238862  Cd Length: 288  Bit Score: 412.12  E-value: 4.33e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  729 SVHALRPADIQVVAALGDSLTAGNGIGSKPddLPDVTTQYRGLSYSAGGDGSLENVTTLPNILREFNRNLTGYAVGTGDA 808
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSAN--NLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  809 NDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKDDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVL 888
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  889 HREVPRVLVNLVDFLNPTIMRQVFlGNPDKCPVQQASVlCNCVLTLRENSQelARLEAFSRAYRSSMRELVGSGRYDtQE 968
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLT-KKPLQCETLLAPE-CPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 283436112  969 DFSVVLQPFFQNIQLPVLADGlPDTSFFAPDCIHPNQKFHSQLARALWTNMLEPLG 1024
Cdd:cd01824   234 DFAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 61-317 7.09e-84

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


:

Pssm-ID: 238862  Cd Length: 288  Bit Score: 276.53  E-value: 7.09e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   61 SVHSLKPSDIKFVAAIGNLEIPPDP----GTGDLEKQdwtERPQQVCMGVM------TVLSDIIRYFSPSVPMPVCHTG- 129
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGagsaNNLDLLTE---YRGLSWSIGGDstlrglTTLPNILREFNPSLYGYSVGTGd 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  130 -------KRVIPHDGAEDLWI-QAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLCPSAQQnGLAAGGVDELMGVLD 201
Cdd:cd01824    78 etlpdsgFNVAEPGAKSEDLPqQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANP-GSPQTFVKNLRKALD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  202 YLQQEVPRAFVNLVDLSEVAEVSR-----QYHGTWLSPapePCNCSEETTRLAKVVMQWSYQEAWNSLLASSRYSE--QE 274
Cdd:cd01824   157 ILRDEVPRAFVNLVGLLNVASLRSltkkpLQCETLLAP---ECPCLLGPTENSYQDLKKFYKEYQNEVEEIVESGEfdRE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 283436112  275 SFTVVFQPFFYETTP------------SLHSEDPRLQDSTTLAWHLWNRMMEPAG 317
Cdd:cd01824   234 DFAVVVQPFFEDTSLpplpdgpdlsffSPDCFHFSQRGHAIAANALWNNLLEPVG 288
 
Name Accession Description Interval E-value
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 382-677 8.23e-146

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 446.02  E-value: 8.23e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  382 SVHRLKPADINVIGALGDSLTAGNGAGSTpgNVLDVLTQYRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKE 461
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSA--NNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  462 TSPNAFLNQAVAGGRAEDLPVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDIL 541
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  542 HAEVPRAFVNLVTVLEIVNLRELYQeKKVYCPRMiLRSLCPCVLKFDDNSTelATLIEFNKKFQEKTHQLIESGRYDtRE 621
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTK-KPLQCETL-LAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 283436112  622 DFTVVVQPFFENVDMPKTSEGlPDNSFFAPDCFHFSSKSHSRAASALWNNMLEPVG 677
Cdd:cd01824   234 DFAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 1085-1371 2.77e-134

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 415.20  E-value: 2.77e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1085 SVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTTLPNILKKFNPYLLGFSTSTWEGT- 1163
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1164 --AGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKDWKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSE 1241
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1242 ELPRAFVNVVEVMELASLYQGQGGK--CAMLAAQnNCTCLRHSQSSlEKQELKKVNWNLQHGISSFSYWHQYTqREDFAV 1319
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLAP-ECPCLLGPTEN-SYQDLKKFYKEYQNEVEEIVESGEFD-REDFAV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 283436112 1320 VVQPFFQNTLTPLNERGdTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVG 1371
Cdd:cd01824   238 VVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 729-1024 4.33e-133

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 412.12  E-value: 4.33e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  729 SVHALRPADIQVVAALGDSLTAGNGIGSKPddLPDVTTQYRGLSYSAGGDGSLENVTTLPNILREFNRNLTGYAVGTGDA 808
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSAN--NLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  809 NDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKDDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVL 888
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  889 HREVPRVLVNLVDFLNPTIMRQVFlGNPDKCPVQQASVlCNCVLTLRENSQelARLEAFSRAYRSSMRELVGSGRYDtQE 968
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLT-KKPLQCETLLAPE-CPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 283436112  969 DFSVVLQPFFQNIQLPVLADGlPDTSFFAPDCIHPNQKFHSQLARALWTNMLEPLG 1024
Cdd:cd01824   234 DFAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 61-317 7.09e-84

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 276.53  E-value: 7.09e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   61 SVHSLKPSDIKFVAAIGNLEIPPDP----GTGDLEKQdwtERPQQVCMGVM------TVLSDIIRYFSPSVPMPVCHTG- 129
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGagsaNNLDLLTE---YRGLSWSIGGDstlrglTTLPNILREFNPSLYGYSVGTGd 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  130 -------KRVIPHDGAEDLWI-QAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLCPSAQQnGLAAGGVDELMGVLD 201
Cdd:cd01824    78 etlpdsgFNVAEPGAKSEDLPqQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANP-GSPQTFVKNLRKALD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  202 YLQQEVPRAFVNLVDLSEVAEVSR-----QYHGTWLSPapePCNCSEETTRLAKVVMQWSYQEAWNSLLASSRYSE--QE 274
Cdd:cd01824   157 ILRDEVPRAFVNLVGLLNVASLRSltkkpLQCETLLAP---ECPCLLGPTENSYQDLKKFYKEYQNEVEEIVESGEfdRE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 283436112  275 SFTVVFQPFFYETTP------------SLHSEDPRLQDSTTLAWHLWNRMMEPAG 317
Cdd:cd01824   234 DFAVVVQPFFEDTSLpplpdgpdlsffSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
394-668 6.99e-28

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 112.67  E-value: 6.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   394 IGALGDSLTAGNGAGStpgnvldvltqyrglswsvggdeniGTVTTLANILREFNPSLKGFSVGTgketsPNAFLNQAVA 473
Cdd:pfam00657    1 IVAFGDSLTDGGGDGP-------------------------GGRFSWGDLLADFLARKLGVPGSG-----YNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   474 GGRAEDLPVQARRLVDLMKNDTRihfQEDWKIITLFIGGNDLCDFCNdlvhySPQNFTDNIGKALDILHAEVPRAFVNLV 553
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISDVKD---QAKPDLVTIFIGANDLCNFLS-----SPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   554 TVleivnlrelyqekKVYCPRMILRslCPcvlkfddNSTELATLIEFNKKFQEKTHQLIESGRYDtREDFTVVVQPF--F 631
Cdd:pfam00657  123 KF-------------WVHGLGPLGC--TP-------PKGCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 283436112   632 ENVDMPKTSEGLPdnsffaPDCFHFSSKSHSRAASAL 668
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1097-1362 4.83e-27

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 110.35  E-value: 4.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1097 VAALGDSLTTAVGARPNnssdlptswrglswsiggdgnleTHTTLPNILKKFNPYLLGFSTSTWEGtaGLNVAAEGARAR 1176
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-----------------------GRFSWGDLLADFLARKLGVPGSGYNH--GANFAIGGATIE 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1177 DMPAQAWDLVERMKNSPDInleKDWKLVTLFIGVNDLCHYCENPEahlatEYVQHIQQALDILSEELPRAFVNVVEVMel 1256
Cdd:pfam00657   56 DLPIQLEQLLRLISDVKDQ---AKPDLVTIFIGANDLCNFLSSPA-----RSKKRVPDLLDELRANLPQLGLGARKFW-- 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1257 aslyqgqggkcAMLAAQNNCTclrhsqssLEKQELKKVNWNLQHGISSFSYWHQY--TQREDFAVVVQPF--FQNTLTPL 1332
Cdd:pfam00657  126 -----------VHGLGPLGCT--------PPKGCYELYNALAEEYNERLNELVNSlaAAAEDANVVYVDIygFEDPTDPC 186

                          250       260       270
                   ....*....|....*....|....*....|
gi 283436112  1333 NERGDTDltffseDCFHFSDRGHAEMAIAL 1362
Cdd:pfam00657  187 CGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
741-1015 2.31e-22

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 96.87  E-value: 2.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   741 VAALGDSLTAGngigskpddlpdvttqyrglsysaGGDGSLENvTTLPNILREFNRNLTGYavgtgDANDTNAFLNQAVP 820
Cdd:pfam00657    1 IVAFGDSLTDG------------------------GGDGPGGR-FSWGDLLADFLARKLGV-----PGSGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   821 GAKAEDLMSQVQTLMQKMKDdhrVNFHEDWKVITVLIGGSDLCDYCtdsnlYSAANFVHHLRNALDVLHREVPRVLVNLV 900
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   901 DFLNPTImrqVFLGNpdkCPvqqasvLCNCVLTLRENSQElarleafsraYRSSMRELVGSGRYDtQEDFSVVLQPF--F 978
Cdd:pfam00657  123 KFWVHGL---GPLGC---TP------PKGCYELYNALAEE----------YNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 283436112   979 QNIQLPVLADGLPdtsffaPDCIHPNQKFHSQLARAL 1015
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 385-556 9.84e-06

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 47.72  E-value: 9.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  385 RLKPADINVIGALGDSLTAGNGAGstpgnvldvltqyRGLSWsvggdenigtVTTLANILREFNPslkgfsvgtgketsp 464
Cdd:COG2755     2 KAAAGKPLRIVALGDSITAGYGAS-------------RERGW----------PALLARRLAAADV--------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  465 nAFLNQAVAGGRAEDLPVQARRLVDlmkndtrihfQEDWKIITLFIGGNDLcdfcNDLVHYSPQNFTDNIGKALDILHAE 544
Cdd:COG2755    44 -RVVNAGISGATTADLLARLDRDLL----------ALKPDLVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAA 108

                         170
                  ....*....|..
gi 283436112  545 VPRAFVNLVTVL 556
Cdd:COG2755   109 GPGARVVLVTPP 120
 
Name Accession Description Interval E-value
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 382-677 8.23e-146

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 446.02  E-value: 8.23e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  382 SVHRLKPADINVIGALGDSLTAGNGAGSTpgNVLDVLTQYRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKE 461
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSA--NNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  462 TSPNAFLNQAVAGGRAEDLPVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDIL 541
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  542 HAEVPRAFVNLVTVLEIVNLRELYQeKKVYCPRMiLRSLCPCVLKFDDNSTelATLIEFNKKFQEKTHQLIESGRYDtRE 621
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTK-KPLQCETL-LAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 283436112  622 DFTVVVQPFFENVDMPKTSEGlPDNSFFAPDCFHFSSKSHSRAASALWNNMLEPVG 677
Cdd:cd01824   234 DFAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 1085-1371 2.77e-134

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 415.20  E-value: 2.77e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1085 SVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTTLPNILKKFNPYLLGFSTSTWEGT- 1163
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1164 --AGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKDWKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSE 1241
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1242 ELPRAFVNVVEVMELASLYQGQGGK--CAMLAAQnNCTCLRHSQSSlEKQELKKVNWNLQHGISSFSYWHQYTqREDFAV 1319
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLAP-ECPCLLGPTEN-SYQDLKKFYKEYQNEVEEIVESGEFD-REDFAV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 283436112 1320 VVQPFFQNTLTPLNERGdTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVG 1371
Cdd:cd01824   238 VVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 729-1024 4.33e-133

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 412.12  E-value: 4.33e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  729 SVHALRPADIQVVAALGDSLTAGNGIGSKPddLPDVTTQYRGLSYSAGGDGSLENVTTLPNILREFNRNLTGYAVGTGDA 808
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSAN--NLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  809 NDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKDDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVL 888
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  889 HREVPRVLVNLVDFLNPTIMRQVFlGNPDKCPVQQASVlCNCVLTLRENSQelARLEAFSRAYRSSMRELVGSGRYDtQE 968
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLT-KKPLQCETLLAPE-CPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 283436112  969 DFSVVLQPFFQNIQLPVLADGlPDTSFFAPDCIHPNQKFHSQLARALWTNMLEPLG 1024
Cdd:cd01824   234 DFAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 61-317 7.09e-84

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 276.53  E-value: 7.09e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   61 SVHSLKPSDIKFVAAIGNLEIPPDP----GTGDLEKQdwtERPQQVCMGVM------TVLSDIIRYFSPSVPMPVCHTG- 129
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGagsaNNLDLLTE---YRGLSWSIGGDstlrglTTLPNILREFNPSLYGYSVGTGd 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  130 -------KRVIPHDGAEDLWI-QAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLCPSAQQnGLAAGGVDELMGVLD 201
Cdd:cd01824    78 etlpdsgFNVAEPGAKSEDLPqQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANP-GSPQTFVKNLRKALD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  202 YLQQEVPRAFVNLVDLSEVAEVSR-----QYHGTWLSPapePCNCSEETTRLAKVVMQWSYQEAWNSLLASSRYSE--QE 274
Cdd:cd01824   157 ILRDEVPRAFVNLVGLLNVASLRSltkkpLQCETLLAP---ECPCLLGPTENSYQDLKKFYKEYQNEVEEIVESGEfdRE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 283436112  275 SFTVVFQPFFYETTP------------SLHSEDPRLQDSTTLAWHLWNRMMEPAG 317
Cdd:cd01824   234 DFAVVVQPFFEDTSLpplpdgpdlsffSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
394-668 6.99e-28

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 112.67  E-value: 6.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   394 IGALGDSLTAGNGAGStpgnvldvltqyrglswsvggdeniGTVTTLANILREFNPSLKGFSVGTgketsPNAFLNQAVA 473
Cdd:pfam00657    1 IVAFGDSLTDGGGDGP-------------------------GGRFSWGDLLADFLARKLGVPGSG-----YNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   474 GGRAEDLPVQARRLVDLMKNDTRihfQEDWKIITLFIGGNDLCDFCNdlvhySPQNFTDNIGKALDILHAEVPRAFVNLV 553
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISDVKD---QAKPDLVTIFIGANDLCNFLS-----SPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   554 TVleivnlrelyqekKVYCPRMILRslCPcvlkfddNSTELATLIEFNKKFQEKTHQLIESGRYDtREDFTVVVQPF--F 631
Cdd:pfam00657  123 KF-------------WVHGLGPLGC--TP-------PKGCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 283436112   632 ENVDMPKTSEGLPdnsffaPDCFHFSSKSHSRAASAL 668
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1097-1362 4.83e-27

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 110.35  E-value: 4.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1097 VAALGDSLTTAVGARPNnssdlptswrglswsiggdgnleTHTTLPNILKKFNPYLLGFSTSTWEGtaGLNVAAEGARAR 1176
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-----------------------GRFSWGDLLADFLARKLGVPGSGYNH--GANFAIGGATIE 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1177 DMPAQAWDLVERMKNSPDInleKDWKLVTLFIGVNDLCHYCENPEahlatEYVQHIQQALDILSEELPRAFVNVVEVMel 1256
Cdd:pfam00657   56 DLPIQLEQLLRLISDVKDQ---AKPDLVTIFIGANDLCNFLSSPA-----RSKKRVPDLLDELRANLPQLGLGARKFW-- 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1257 aslyqgqggkcAMLAAQNNCTclrhsqssLEKQELKKVNWNLQHGISSFSYWHQY--TQREDFAVVVQPF--FQNTLTPL 1332
Cdd:pfam00657  126 -----------VHGLGPLGCT--------PPKGCYELYNALAEEYNERLNELVNSlaAAAEDANVVYVDIygFEDPTDPC 186

                          250       260       270
                   ....*....|....*....|....*....|
gi 283436112  1333 NERGDTDltffseDCFHFSDRGHAEMAIAL 1362
Cdd:pfam00657  187 CGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
741-1015 2.31e-22

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 96.87  E-value: 2.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   741 VAALGDSLTAGngigskpddlpdvttqyrglsysaGGDGSLENvTTLPNILREFNRNLTGYavgtgDANDTNAFLNQAVP 820
Cdd:pfam00657    1 IVAFGDSLTDG------------------------GGDGPGGR-FSWGDLLADFLARKLGV-----PGSGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   821 GAKAEDLMSQVQTLMQKMKDdhrVNFHEDWKVITVLIGGSDLCDYCtdsnlYSAANFVHHLRNALDVLHREVPRVLVNLV 900
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112   901 DFLNPTImrqVFLGNpdkCPvqqasvLCNCVLTLRENSQElarleafsraYRSSMRELVGSGRYDtQEDFSVVLQPF--F 978
Cdd:pfam00657  123 KFWVHGL---GPLGC---TP------PKGCYELYNALAEE----------YNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 283436112   979 QNIQLPVLADGLPdtsffaPDCIHPNQKFHSQLARAL 1015
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 741-1016 9.21e-08

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 53.96  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  741 VAALGDSLTAGNGigskPDDLPDVTTQYRGLSYSAGGDGSlenvttlpnilrefnrnltgyavgtgdandtnAFLNQAVP 820
Cdd:cd00229     1 ILVIGDSITAGYG----ASSGSTFYSLLLYLLLLAGGPGV--------------------------------EVINLGVS 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  821 GAKAEDLMSQVqtlmqkmkDDHRVNFHEDWKVITVLIGGSDLcdycTDSNLYSAANFVHHLRNALDVLHREVPRVLVNLV 900
Cdd:cd00229    45 GATTADALRRL--------GLRLALLKDKPDLVIIELGTNDL----GRGGDTSIDEFKANLEELLDALRERAPGAKVILI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  901 DFLNPTimrqvflgnpdkcpvqqasvlcncvltlrensQELARLEAFSRAYRSSMRELvgsgRYDTQEDFSVVLQPFFQn 980
Cdd:cd00229   113 TPPPPP--------------------------------PREGLLGRALPRYNEAIKAV----AAENPAPSGVDLVDLAA- 155

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 283436112  981 iqlpvlADGLPDTSFFAPDCIHPNQKFHSQLARALW 1016
Cdd:cd00229   156 ------LLGDEDKSLYSPDGIHPNPAGHKLIAEALA 185
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 394-670 8.61e-07

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 50.87  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  394 IGALGDSLTAGNGAgsTPGNVLDVLTQYRGLSWSVGGDENIgtvttlanilrefnpslkgfsvgtgketspnaflNQAVA 473
Cdd:cd00229     1 ILVIGDSITAGYGA--SSGSTFYSLLLYLLLLAGGPGVEVI----------------------------------NLGVS 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  474 GGRAEDLpvqARRLvdlmkNDTRIHFQEDWKIITLFIGGNDLCDFCNdlvhYSPQNFTDNIGKALDILHAEVPRAFVNLV 553
Cdd:cd00229    45 GATTADA---LRRL-----GLRLALLKDKPDLVIIELGTNDLGRGGD----TSIDEFKANLEELLDALRERAPGAKVILI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  554 TVLeIVNLRELYQEKKVYCPRMILRSLCpcvlkFDDNSTELATLIEFNKKFQEkthqliesgrydtredftvvvqpffen 633
Cdd:cd00229   113 TPP-PPPPREGLLGRALPRYNEAIKAVA-----AENPAPSGVDLVDLAALLGD--------------------------- 159

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 283436112  634 vdmpktseglPDNSFFAPDCFHFSSKSHSRAASALWN 670
Cdd:cd00229   160 ----------EDKSLYSPDGIHPNPAGHKLIAEALAS 186
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 385-556 9.84e-06

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 47.72  E-value: 9.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  385 RLKPADINVIGALGDSLTAGNGAGstpgnvldvltqyRGLSWsvggdenigtVTTLANILREFNPslkgfsvgtgketsp 464
Cdd:COG2755     2 KAAAGKPLRIVALGDSITAGYGAS-------------RERGW----------PALLARRLAAADV--------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  465 nAFLNQAVAGGRAEDLPVQARRLVDlmkndtrihfQEDWKIITLFIGGNDLcdfcNDLVHYSPQNFTDNIGKALDILHAE 544
Cdd:COG2755    44 -RVVNAGISGATTADLLARLDRDLL----------ALKPDLVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAA 108

                         170
                  ....*....|..
gi 283436112  545 VPRAFVNLVTVL 556
Cdd:COG2755   109 GPGARVVLVTPP 120
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 1097-1364 1.21e-05

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 47.41  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1097 VAALGDSLTTAVGArpnnsSDLPTSWRGLSWSIGGDGNLETHTTlpnilkkfnpyllgfststwegtaglNVAAEGARAR 1176
Cdd:cd00229     1 ILVIGDSITAGYGA-----SSGSTFYSLLLYLLLLAGGPGVEVI--------------------------NLGVSGATTA 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1177 DMPAQAWDLVERMKNSPDinlekdwkLVTLFIGVNDLCHYCENPEAhlatEYVQHIQQALDILSEELPRAFVNVVEVMEL 1256
Cdd:cd00229    50 DALRRLGLRLALLKDKPD--------LVIIELGTNDLGRGGDTSID----EFKANLEELLDALRERAPGAKVILITPPPP 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112 1257 AslyqGQGGKCAMLAAQNNctclrhsqSSLEKQelkkvnwnlqhgissfsywhQYTQREDFAVVVQPFFQntltplnERG 1336
Cdd:cd00229   118 P----PREGLLGRALPRYN--------EAIKAV--------------------AAENPAPSGVDLVDLAA-------LLG 158

                         250       260
                  ....*....|....*....|....*...
gi 283436112 1337 DTDLTFFSEDCFHFSDRGHAEMAIALWN 1364
Cdd:cd00229   159 DEDKSLYSPDGIHPNPAGHKLIAEALAS 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 1099-1356 3.71e-05

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 46.00  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1099 ALGDSLTTAVGArpnnsSDLPTSWRGLswsiggdgnlethttLPNILKKFNPYllgfstsTWEGTAGLNvaaeGARARDM 1178
Cdd:pfam13472    1 ALGDSITAGYGA-----TGGDRSYPGW---------------LARLLARRLGA-------DVVNNLGIS----GATTRLD 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1179 PAQAWDLVERMKnspdinlekdWKLVTLFIGVNDLCHycenpeAHLATEYVQHIQQALDILSEELPRAFVNVVEVMELAS 1258
Cdd:pfam13472   50 LLERLDDVLRLK----------PDLVVILLGTNDLGR------GVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGP 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436112  1259 LYQGQGGKCAMLAAQNNctclrhsqsslekQELKKVnwnlqhgissfsywhqyTQREDFAVVvqpffqNTLTPLNERGDT 1338
Cdd:pfam13472  114 PPPLDERRLNARIAEYN-------------AAIREV-----------------AAERGVPYV------DLWDALRDDGGW 157

                          250
                   ....*....|....*...
gi 283436112  1339 DLTFFSEDCFHFSDRGHA 1356
Cdd:pfam13472  158 LPDLLADDGLHPNAAGYR 175
 
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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