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Conserved domains on  [gi|20302091|ref|NP_620253|]
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phospholipase B1, membrane-associated precursor [Rattus norvegicus]

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 ...
 387-681 5.35e-132

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: 409.04  E-value: 5.35e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  387 VHRLRPADIKVIGAMGDSLTAGNGAGSSpgNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKEN 466
Cdd:cd01824    2 VHRLRPGDIKVIAALGDSLTAGNGAGSA--NNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  467 TPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILH 546
Cdd:cd01824   80 LPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  547 AEVPRAFVNMVSVIEITPLRELFNEPKvSCPRMiLRSLCPCVLNLGENSaeLAQLVERNRQYQEETGKLIESGRYDtRDD 626
Cdd:cd01824  160 DEVPRAFVNLVGLLNVASLRSLTKKPL-QCETL-LAPECPCLLGPTENS--YQDLKKFYKEYQNEVEEIVESGEFD-RED 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 20302091  627 FTVVLQPMFENVVMPRTLEGlPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVG 681
Cdd:cd01824  235 FAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 733-1028 4.81e-126

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: 392.86  E-value: 4.81e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  733 SVHTLRPADIQVVAALGDSVTAGNGISSqeGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDV 812
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  813 NSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDIL 892
Cdd:cd01824   79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  893 HKEVPRALVNLVDFMNPSIIRQVFLKnPDKCPvNQTSVLCNCVLTPGEDSHelARLEAFTKSYQSSMLQLVESGRYDtRE 972
Cdd:cd01824  159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20302091  973 DFSVVLQPFLFNIRLPILENGnPDTSFFAPDCILLSQKFHTQLARALWANMLEPLG 1028
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 ...
 1089-1376 8.23e-120

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: 375.91  E-value: 8.23e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1089 SVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENT- 1167
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1168 --AGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYE 1245
Cdd:cd01824   81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1246 ELPRVFINVVEVMELSGL--LHDQGGKCAMPLAvqKNCSCLkRSQNLMAMQELKKVNGNLQSALSELSYWHRYmQREDFA 1323
Cdd:cd01824  161 EVPRAFVNLVGLLNVASLrsLTKKPLQCETLLA--PECPCL-LGPTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 20302091 1324 VTVQPFFRNTFVPLDERgGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVG 1376
Cdd:cd01824  237 VVVQPFFEDTSLPPLPD-GPDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 63-321 2.00e-68

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: 232.23  E-value: 2.00e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091   63 SVHSLRPSDIKLVAAIGNLETPpAPGSGVVNmekpqSLESELQN----VCIGIM------TALSDIIRHFNPSVLMPTCS 132
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTA-GNGAGSAN-----NLDLLTEYrglsWSIGGDstlrglTTLPNILREFNPSLYGYSVG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  133 PGKGT--------AGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRhLMKHMEMLSG 204
Cdd:cd01824   75 TGDETlpdsgfnvAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  205 VLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGF--SPAPEICKCSEEITKLSKAVMQ---WSYQEAWEDLLASSKFNKh 279
Cdd:cd01824  154 ALDILRDEVPRAFVNLVGLLNVASLRSLTKKPLQceTLLAPECPCLLGPTENSYQDLKkfyKEYQNEVEEIVESGEFDR- 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20302091  280 ETFAVVFQSFFSEVELPLER--------------PSPQDSTTLALRIWNSMMEPVG 321
Cdd:cd01824  233 EDFAVVVQPFFEDTSLPPLPdgpdlsffspdcfhFSQRGHAIAANALWNNLLEPVG 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 ...
 387-681 5.35e-132

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: 409.04  E-value: 5.35e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  387 VHRLRPADIKVIGAMGDSLTAGNGAGSSpgNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKEN 466
Cdd:cd01824    2 VHRLRPGDIKVIAALGDSLTAGNGAGSA--NNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  467 TPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILH 546
Cdd:cd01824   80 LPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  547 AEVPRAFVNMVSVIEITPLRELFNEPKvSCPRMiLRSLCPCVLNLGENSaeLAQLVERNRQYQEETGKLIESGRYDtRDD 626
Cdd:cd01824  160 DEVPRAFVNLVGLLNVASLRSLTKKPL-QCETL-LAPECPCLLGPTENS--YQDLKKFYKEYQNEVEEIVESGEFD-RED 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 20302091  627 FTVVLQPMFENVVMPRTLEGlPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVG 681
Cdd:cd01824  235 FAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 733-1028 4.81e-126

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: 392.86  E-value: 4.81e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  733 SVHTLRPADIQVVAALGDSVTAGNGISSqeGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDV 812
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  813 NSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDIL 892
Cdd:cd01824   79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  893 HKEVPRALVNLVDFMNPSIIRQVFLKnPDKCPvNQTSVLCNCVLTPGEDSHelARLEAFTKSYQSSMLQLVESGRYDtRE 972
Cdd:cd01824  159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20302091  973 DFSVVLQPFLFNIRLPILENGnPDTSFFAPDCILLSQKFHTQLARALWANMLEPLG 1028
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 ...
 1089-1376 8.23e-120

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: 375.91  E-value: 8.23e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1089 SVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENT- 1167
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1168 --AGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYE 1245
Cdd:cd01824   81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1246 ELPRVFINVVEVMELSGL--LHDQGGKCAMPLAvqKNCSCLkRSQNLMAMQELKKVNGNLQSALSELSYWHRYmQREDFA 1323
Cdd:cd01824  161 EVPRAFVNLVGLLNVASLrsLTKKPLQCETLLA--PECPCL-LGPTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 20302091 1324 VTVQPFFRNTFVPLDERgGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVG 1376
Cdd:cd01824  237 VVVQPFFEDTSLPPLPD-GPDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 63-321 2.00e-68

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: 232.23  E-value: 2.00e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091   63 SVHSLRPSDIKLVAAIGNLETPpAPGSGVVNmekpqSLESELQN----VCIGIM------TALSDIIRHFNPSVLMPTCS 132
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTA-GNGAGSAN-----NLDLLTEYrglsWSIGGDstlrglTTLPNILREFNPSLYGYSVG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  133 PGKGT--------AGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRhLMKHMEMLSG 204
Cdd:cd01824   75 TGDETlpdsgfnvAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  205 VLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGF--SPAPEICKCSEEITKLSKAVMQ---WSYQEAWEDLLASSKFNKh 279
Cdd:cd01824  154 ALDILRDEVPRAFVNLVGLLNVASLRSLTKKPLQceTLLAPECPCLLGPTENSYQDLKkfyKEYQNEVEEIVESGEFDR- 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20302091  280 ETFAVVFQSFFSEVELPLER--------------PSPQDSTTLALRIWNSMMEPVG 321
Cdd:cd01824  233 EDFAVVVQPFFEDTSLPPLPdgpdlsffspdcfhFSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
398-672 4.88e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 104.58  E-value: 4.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    398 IGAMGDSLTAGNGAGSSpgnvldvltqyrglswsvggdetieTVTTLANILREFNPSLKGFSVgtgkeNTPRASFNQAVA 477
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-------------------------GRFSWGDLLADFLARKLGVPG-----SGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    478 GAKSDGLAAQAKKLVSLMKDDKtinFQEDWKIITVFIGGNDLCGSCnnlarFSPQTFTDNIKTALDILHAEVPRafvnmv 557
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISDVK---DQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQ------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    558 svieitpLRELFNEPKVSCPRMILRslCPCVLNLGENSAElaqlverNRQYQEETGKLIESGRYDtRDDFTVVLQPM--F 635
Cdd:pfam00657  117 -------LGLGARKFWVHGLGPLGC--TPPKGCYELYNAL-------AEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 20302091    636 ENVVMPRTLEGLPdssffaPDCFHFNVKTHARSAIAL 672
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1134-1367 1.94e-20

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 91.10  E-value: 1.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091   1134 GGDGTLeTHTTLPNILKKFNPSILGFSTGTleNTAGLNVAEEGARAQDMPAQAQALVKKMKStptINIQEDWKLITLLIG 1213
Cdd:pfam00657   12 GGDGPG-GRFSWGDLLADFLARKLGVPGSG--YNHGANFAIGGATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091   1214 NNDLCLYCEDPENystreYVKYIQHALDIFYEELPRvFINVVEVMELSGLLhdqggkcamPLAVQKNCSCLKRsqnlmam 1293
Cdd:pfam00657   86 ANDLCNFLSSPAR-----SKKRVPDLLDELRANLPQ-LGLGARKFWVHGLG---------PLGCTPPKGCYEL------- 143

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20302091   1294 qelkkVNGNLQSALSELSYWHRYMQRE--DFAVTVQPF--FRNTFVPLDERGGLDltffseDCFHFSVRGHAEMAIAL 1367
Cdd:pfam00657  144 -----YNALAEEYNERLNELVNSLAAAaeDANVVYVDIygFEDPTDPCCGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
745-1019 5.80e-18

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 84.16  E-value: 5.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    745 VAALGDSVTAGNGissqegdladvttqyrglsYSAGGDkflenvTTLPNILREFNGNLTGYSVGTGDVnsasaFLNQAVP 824
Cdd:pfam00657    1 IVAFGDSLTDGGG-------------------DGPGGR------FSWGDLLADFLARKLGVPGSGYNH-----GANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    825 GAKAENLASQVQTLIQKMKNdtrVNFHQDWKVITVMIGASDLCDFCKdsnrySAANFSDHLRNALDILHKEVPRaLVNLV 904
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFLS-----SPARSKKRVPDLLDELRANLPQ-LGLGA 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    905 DFMNPSIIRQVfLKNPDKcpvnqtsvlcncvltpgedsHELARLEAFTKSYQSSMLQLVESGRYDtREDFSVVLQPF--L 982
Cdd:pfam00657  122 RKFWVHGLGPL-GCTPPK--------------------GCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 20302091    983 FNIRLPILENGNPdtsffaPDCILLSQKFHTQLARAL 1019
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 389-674 5.71e-08

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: 54.26  E-value: 5.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  389 RLRPADIKVIGAMGDSLTAGNGAGSSPGnvldvltqYRGLswsvggdetietvttLANILREfnpslKGFSVgtgkentp 468
Cdd:COG2755    2 KAAAGKPLRIVALGDSITAGYGASRERG--------WPAL---------------LARRLAA-----ADVRV-------- 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  469 rasFNQAVAGAKSDGLAAQAKKLVSLMKDDktinfqedwkIITVFIGGNDLcgscNNLARFSPQTFTDNIKTALDILHAE 548
Cdd:COG2755   46 ---VNAGISGATTADLLARLDRDLLALKPD----------LVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAA 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  549 VPRAfvnMVSVIEITPlrelFNEPKvscprmilrslcpcvlNLGENSAELAQLVernRQYQEETG-KLIesgrydtrdDF 627
Cdd:COG2755  109 GPGA---RVVLVTPPP----RLRPN----------------YLNERIEAYNAAI---RELAAEYGvPLV---------DL 153

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 20302091  628 TVVLQPMFEnvvmprtleglpDSSFFAPDCFHFNVKTHARSAIALWK 674
Cdd:COG2755  154 YAALRDAGD------------LPDLLTADGLHPNAAGYRLIAEAVLP 188
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 745-901 4.02e-05

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: 46.18  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  745 VAALGDSVTAGNGISSQEGdladvttqYRGLsysaggdkflenvttLPNILREFNGNltgysvgtgdvnsasaFLNQAVP 824
Cdd:COG2755   11 IVALGDSITAGYGASRERG--------WPAL---------------LARRLAAADVR----------------VVNAGIS 51

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20302091  825 GAKAENLASQVQTLIQKMKndtrvnfhqdWKVITVMIGASDLcdfcKDSNRYSAANFSDHLRNALDILHKEVPRALV 901
Cdd:COG2755   52 GATTADLLARLDRDLLALK----------PDLVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAAGPGARV 114
 
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 ...
 387-681 5.35e-132

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: 409.04  E-value: 5.35e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  387 VHRLRPADIKVIGAMGDSLTAGNGAGSSpgNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKEN 466
Cdd:cd01824    2 VHRLRPGDIKVIAALGDSLTAGNGAGSA--NNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  467 TPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILH 546
Cdd:cd01824   80 LPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  547 AEVPRAFVNMVSVIEITPLRELFNEPKvSCPRMiLRSLCPCVLNLGENSaeLAQLVERNRQYQEETGKLIESGRYDtRDD 626
Cdd:cd01824  160 DEVPRAFVNLVGLLNVASLRSLTKKPL-QCETL-LAPECPCLLGPTENS--YQDLKKFYKEYQNEVEEIVESGEFD-RED 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 20302091  627 FTVVLQPMFENVVMPRTLEGlPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVG 681
Cdd:cd01824  235 FAVVVQPFFEDTSLPPLPDG-PDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 733-1028 4.81e-126

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: 392.86  E-value: 4.81e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  733 SVHTLRPADIQVVAALGDSVTAGNGISSqeGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDV 812
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  813 NSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDIL 892
Cdd:cd01824   79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  893 HKEVPRALVNLVDFMNPSIIRQVFLKnPDKCPvNQTSVLCNCVLTPGEDSHelARLEAFTKSYQSSMLQLVESGRYDtRE 972
Cdd:cd01824  159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20302091  973 DFSVVLQPFLFNIRLPILENGnPDTSFFAPDCILLSQKFHTQLARALWANMLEPLG 1028
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 ...
 1089-1376 8.23e-120

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: 375.91  E-value: 8.23e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1089 SVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENT- 1167
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1168 --AGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYE 1245
Cdd:cd01824   81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091 1246 ELPRVFINVVEVMELSGL--LHDQGGKCAMPLAvqKNCSCLkRSQNLMAMQELKKVNGNLQSALSELSYWHRYmQREDFA 1323
Cdd:cd01824  161 EVPRAFVNLVGLLNVASLrsLTKKPLQCETLLA--PECPCL-LGPTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 20302091 1324 VTVQPFFRNTFVPLDERgGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVG 1376
Cdd:cd01824  237 VVVQPFFEDTSLPPLPD-GPDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 63-321 2.00e-68

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: 232.23  E-value: 2.00e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091   63 SVHSLRPSDIKLVAAIGNLETPpAPGSGVVNmekpqSLESELQN----VCIGIM------TALSDIIRHFNPSVLMPTCS 132
Cdd:cd01824    1 SVHRLRPGDIKVIAALGDSLTA-GNGAGSAN-----NLDLLTEYrglsWSIGGDstlrglTTLPNILREFNPSLYGYSVG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  133 PGKGT--------AGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRhLMKHMEMLSG 204
Cdd:cd01824   75 TGDETlpdsgfnvAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  205 VLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGF--SPAPEICKCSEEITKLSKAVMQ---WSYQEAWEDLLASSKFNKh 279
Cdd:cd01824  154 ALDILRDEVPRAFVNLVGLLNVASLRSLTKKPLQceTLLAPECPCLLGPTENSYQDLKkfyKEYQNEVEEIVESGEFDR- 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20302091  280 ETFAVVFQSFFSEVELPLER--------------PSPQDSTTLALRIWNSMMEPVG 321
Cdd:cd01824  233 EDFAVVVQPFFEDTSLPPLPdgpdlsffspdcfhFSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
398-672 4.88e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 104.58  E-value: 4.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    398 IGAMGDSLTAGNGAGSSpgnvldvltqyrglswsvggdetieTVTTLANILREFNPSLKGFSVgtgkeNTPRASFNQAVA 477
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-------------------------GRFSWGDLLADFLARKLGVPG-----SGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    478 GAKSDGLAAQAKKLVSLMKDDKtinFQEDWKIITVFIGGNDLCGSCnnlarFSPQTFTDNIKTALDILHAEVPRafvnmv 557
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISDVK---DQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQ------ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    558 svieitpLRELFNEPKVSCPRMILRslCPCVLNLGENSAElaqlverNRQYQEETGKLIESGRYDtRDDFTVVLQPM--F 635
Cdd:pfam00657  117 -------LGLGARKFWVHGLGPLGC--TPPKGCYELYNAL-------AEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 20302091    636 ENVVMPRTLEGLPdssffaPDCFHFNVKTHARSAIAL 672
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1134-1367 1.94e-20

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 91.10  E-value: 1.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091   1134 GGDGTLeTHTTLPNILKKFNPSILGFSTGTleNTAGLNVAEEGARAQDMPAQAQALVKKMKStptINIQEDWKLITLLIG 1213
Cdd:pfam00657   12 GGDGPG-GRFSWGDLLADFLARKLGVPGSG--YNHGANFAIGGATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091   1214 NNDLCLYCEDPENystreYVKYIQHALDIFYEELPRvFINVVEVMELSGLLhdqggkcamPLAVQKNCSCLKRsqnlmam 1293
Cdd:pfam00657   86 ANDLCNFLSSPAR-----SKKRVPDLLDELRANLPQ-LGLGARKFWVHGLG---------PLGCTPPKGCYEL------- 143

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20302091   1294 qelkkVNGNLQSALSELSYWHRYMQRE--DFAVTVQPF--FRNTFVPLDERGGLDltffseDCFHFSVRGHAEMAIAL 1367
Cdd:pfam00657  144 -----YNALAEEYNERLNELVNSLAAAaeDANVVYVDIygFEDPTDPCCGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
745-1019 5.80e-18

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 84.16  E-value: 5.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    745 VAALGDSVTAGNGissqegdladvttqyrglsYSAGGDkflenvTTLPNILREFNGNLTGYSVGTGDVnsasaFLNQAVP 824
Cdd:pfam00657    1 IVAFGDSLTDGGG-------------------DGPGGR------FSWGDLLADFLARKLGVPGSGYNH-----GANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    825 GAKAENLASQVQTLIQKMKNdtrVNFHQDWKVITVMIGASDLCDFCKdsnrySAANFSDHLRNALDILHKEVPRaLVNLV 904
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFLS-----SPARSKKRVPDLLDELRANLPQ-LGLGA 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    905 DFMNPSIIRQVfLKNPDKcpvnqtsvlcncvltpgedsHELARLEAFTKSYQSSMLQLVESGRYDtREDFSVVLQPF--L 982
Cdd:pfam00657  122 RKFWVHGLGPL-GCTPPK--------------------GCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 20302091    983 FNIRLPILENGNPdtsffaPDCILLSQKFHTQLARAL 1019
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 389-674 5.71e-08

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: 54.26  E-value: 5.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  389 RLRPADIKVIGAMGDSLTAGNGAGSSPGnvldvltqYRGLswsvggdetietvttLANILREfnpslKGFSVgtgkentp 468
Cdd:COG2755    2 KAAAGKPLRIVALGDSITAGYGASRERG--------WPAL---------------LARRLAA-----ADVRV-------- 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  469 rasFNQAVAGAKSDGLAAQAKKLVSLMKDDktinfqedwkIITVFIGGNDLcgscNNLARFSPQTFTDNIKTALDILHAE 548
Cdd:COG2755   46 ---VNAGISGATTADLLARLDRDLLALKPD----------LVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAA 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  549 VPRAfvnMVSVIEITPlrelFNEPKvscprmilrslcpcvlNLGENSAELAQLVernRQYQEETG-KLIesgrydtrdDF 627
Cdd:COG2755  109 GPGA---RVVLVTPPP----RLRPN----------------YLNERIEAYNAAI---RELAAEYGvPLV---------DL 153

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 20302091  628 TVVLQPMFEnvvmprtleglpDSSFFAPDCFHFNVKTHARSAIALWK 674
Cdd:COG2755  154 YAALRDAGD------------LPDLLTADGLHPNAAGYRLIAEAVLP 188
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 398-674 1.31e-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: 53.18  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  398 IGAMGDSLTAGNGAGSspgnvldvltqyrglswsvggdetietvttlanilrEFNPSLKGFSVGTGKENTPRASFNQAVA 477
Cdd:cd00229    1 ILVIGDSITAGYGASS------------------------------------GSTFYSLLLYLLLLAGGPGVEVINLGVS 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  478 GAKSDGLAAQAKKLVSLMKDDktinfqedWKIITVFIGGNDLCGSCNnlarFSPQTFTDNIKTALDILHAEVPRAfvnmv 557
Cdd:cd00229   45 GATTADALRRLGLRLALLKDK--------PDLVIIELGTNDLGRGGD----TSIDEFKANLEELLDALRERAPGA----- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  558 SVIEITPLrelfnepkvscprmilrslcPCVLNLGENSAELAQLVERNRQYQEETGKliesgrydtrddftvvlqPMFEN 637
Cdd:cd00229  108 KVILITPP--------------------PPPPREGLLGRALPRYNEAIKAVAAENPA------------------PSGVD 149

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 20302091  638 VVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWK 674
Cdd:cd00229  150 LVDLAALLGDEDKSLYSPDGIHPNPAGHKLIAEALAS 186
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 745-901 4.02e-05

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: 46.18  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  745 VAALGDSVTAGNGISSQEGdladvttqYRGLsysaggdkflenvttLPNILREFNGNltgysvgtgdvnsasaFLNQAVP 824
Cdd:COG2755   11 IVALGDSITAGYGASRERG--------WPAL---------------LARRLAAADVR----------------VVNAGIS 51

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20302091  825 GAKAENLASQVQTLIQKMKndtrvnfhqdWKVITVMIGASDLcdfcKDSNRYSAANFSDHLRNALDILHKEVPRALV 901
Cdd:COG2755   52 GATTADLLARLDRDLLALK----------PDLVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAAGPGARV 114
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 400-667 4.32e-04

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: 42.92  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    400 AMGDSLTAGNGAGSSPGnvldvltqyRGLSWsvggdetietvttLANILREFNPSlkgfsvgtgkentpRASFNQAVAGA 479
Cdd:pfam13472    1 ALGDSITAGYGATGGDR---------SYPGW-------------LARLLARRLGA--------------DVVNNLGISGA 44

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    480 KSDGLAAQAKKLVSlmkddktinfQEDWKIITVFIGGNDLcgscnnLARFSPQTFTDNIKTALDILHAEVPRAfvnmvsv 559
Cdd:pfam13472   45 TTRLDLLERLDDVL----------RLKPDLVVILLGTNDL------GRGVSAARAAANLEALIDALRAAGPDA------- 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091    560 ieitplrelfnepkvscpRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKliesgrydtRDDFTVV-LQPMFENv 638
Cdd:pfam13472  102 ------------------RVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAA---------ERGVPYVdLWDALRD- 153

                          250       260
                   ....*....|....*....|....*....
gi 20302091    639 vmprtlEGLPDSSFFAPDCFHFNVKTHAR 667
Cdd:pfam13472  154 ------DGGWLPDLLADDGLHPNAAGYRL 176
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 398-519 4.89e-04

Members of the SGNH-hydrolase superfamily, 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 Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. This subfamily contains sequences similar to Bacillus YpmR.


Pssm-ID: 239947  Cd Length: 204  Bit Score: 43.01  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302091  398 IGAMGDSLTAGNGAGSSPGNVLDVLTQYRGlswsvggDETIETVTTLanilrefnpslkgfsvgtgkentprasfNQAVA 477
Cdd:cd04506    2 IVALGDSLTEGVGDETGKGGYVGRLDKLIE-------TKTVKKVTVQ----------------------------NFGVS 46

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 20302091  478 GAKSDGLAAQakklvslMKDDKTINFQEDWKIITVFIGGNDL 519
Cdd:cd04506   47 GDRSDQLLKR-------LKTKKVQKELKKADVITITIGGNDL 81
 
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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