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Conserved domains on  [gi|568934417|ref|XP_006504111|]
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phospholipase B1, membrane-associated isoform X2 [Mus musculus]

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 2.91e-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: 2.91e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  387 VHSLRPADIKIIGALGDSLTAGNGAGasPWNILDVLTEYRGLSWSVGGDETIKTVTTLPNILREFNPSLKGFSVGTGKES 466
Cdd:cd01824     2 VHRLRPGDIKVIAALGDSLTAGNGAG--SANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  467 TSRASFNQAVAGAKSDGLAGQARKLVDLMKADKTINFQEDWKIITVFIGGNDLCASCSNSTRFSPQNFIDNIKNALDILH 546
Cdd:cd01824    80 LPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  547 AEVPRAFVNMAMVMEITPLRELFNEPtVSCPrNILSRLCPCVLGLGDNSEElsSLVQRNRDYQKKTEELINSGRYDtRDN 626
Cdd:cd01824   160 DEVPRAFVNLVGLLNVASLRSLTKKP-LQCE-TLLAPECPCLLGPTENSYQ--DLKKFYKEYQNEVEEIVESGEFD-RED 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568934417  627 FTVVVQPLFENVSMPRTPEGvPDKSFFAPDCFHFNAKTHARSAIALWKNMLEPVG 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 ...
 1038-1325 3.19e-121

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: 379.76  E-value: 3.19e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1038 SVHELRPADIKVVAAMGDFLTTATGARPSGYKRLATPWRGLSWSIGGDGKLETHTTLPNILKKFNPSITGFSTGTLDNK- 1116
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1117 --AGLNVAEEGARAQDMPAQAKTLVKKMKSTPTINLQEDWKLITLLIGNNDLCLYCENPEDNSTKEYVKYIQQALDILYE 1194
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1195 ELPRVFINVVEVMELAGLHHVQGGK--CAMPLAvqKNCSCLRHsQNLTAMQELKKLNWNLQSGISELSYWHRYmEREDFA 1272
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLA--PECPCLLG-PTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568934417 1273 VTVQPFFRNTFIPLNeREGLDLTFFSEDCFYFSDRGHAEMAIALWNNMLEPVG 1325
Cdd:cd01824   237 VVVQPFFEDTSLPPL-PDGPDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 733-977 1.51e-91

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: 298.10  E-value: 1.51e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  733 SVHTLRPADIQVVAALGDSLTAGNGISSqeGNLTDVSTQYRGLSY----------------------------------- 777
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWsiggdstlrglttlpnilrefnpslygysvgtgde 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  778 ----------------RNLTSQVRTLVQKMKSDNRVNFNRDWKVITVMIGASDLCDFCTDSNHYSAANFFDHLQNALDIL 841
Cdd:cd01824    79 tlpdsgfnvaepgaksEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  842 HKEVPRALVNLVDFINPSIIREVFLKnPDKCPvNQSSVLCNCVLTPRKDSYelARLEAFTKSYQSSMLQLVESGRYDtRE 921
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568934417  922 DFSVVLQPFLLNTKLPVLENGkPDTSFFAPDCIHLNQKFHTQLARALWANMLEPLG 977
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 ...
 65-321 3.36e-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: 231.46  E-value: 3.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   65 SVHSLRPSDIKLVAAIGNPEIP--LAPGSGTINMEkpqsIKNQPQDVCMGIM------TVLSDIIRHFSPSVLMPTCSPG 136
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAgnGAGSANNLDLL----TEYRGLSWSIGGDstlrglTTLPNILREFNPSLYGYSVGTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  137 KGT--------AVH-TTAEDLWIQAKELVRRLKDNPQLDFEKDWKLITVFFSNTSQCHLCPSAQQKShLMRHMEMLWGVL 207
Cdd:cd01824    77 DETlpdsgfnvAEPgAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRKAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  208 DYLHHEVPRAFVNLVDLSEVLAMdlqHQETGFSPAPEV-----CKCTETTTLSK----AVMQWSYQEAWEDLLASSKFNK 278
Cdd:cd01824   156 DILRDEVPRAFVNLVGLLNVASL---RSLTKKPLQCETllapeCPCLLGPTENSyqdlKKFYKEYQNEVEEIVESGEFDR 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568934417  279 hETFAVVFQPFFDEIEPPLKRS--------------SPQDPTTLALRIWNSMMEPVG 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 2.91e-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: 2.91e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  387 VHSLRPADIKIIGALGDSLTAGNGAGasPWNILDVLTEYRGLSWSVGGDETIKTVTTLPNILREFNPSLKGFSVGTGKES 466
Cdd:cd01824     2 VHRLRPGDIKVIAALGDSLTAGNGAG--SANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  467 TSRASFNQAVAGAKSDGLAGQARKLVDLMKADKTINFQEDWKIITVFIGGNDLCASCSNSTRFSPQNFIDNIKNALDILH 546
Cdd:cd01824    80 LPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  547 AEVPRAFVNMAMVMEITPLRELFNEPtVSCPrNILSRLCPCVLGLGDNSEElsSLVQRNRDYQKKTEELINSGRYDtRDN 626
Cdd:cd01824   160 DEVPRAFVNLVGLLNVASLRSLTKKP-LQCE-TLLAPECPCLLGPTENSYQ--DLKKFYKEYQNEVEEIVESGEFD-RED 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568934417  627 FTVVVQPLFENVSMPRTPEGvPDKSFFAPDCFHFNAKTHARSAIALWKNMLEPVG 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 ...
 1038-1325 3.19e-121

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: 379.76  E-value: 3.19e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1038 SVHELRPADIKVVAAMGDFLTTATGARPSGYKRLATPWRGLSWSIGGDGKLETHTTLPNILKKFNPSITGFSTGTLDNK- 1116
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1117 --AGLNVAEEGARAQDMPAQAKTLVKKMKSTPTINLQEDWKLITLLIGNNDLCLYCENPEDNSTKEYVKYIQQALDILYE 1194
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1195 ELPRVFINVVEVMELAGLHHVQGGK--CAMPLAvqKNCSCLRHsQNLTAMQELKKLNWNLQSGISELSYWHRYmEREDFA 1272
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLA--PECPCLLG-PTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568934417 1273 VTVQPFFRNTFIPLNeREGLDLTFFSEDCFYFSDRGHAEMAIALWNNMLEPVG 1325
Cdd:cd01824   237 VVVQPFFEDTSLPPL-PDGPDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 733-977 1.51e-91

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: 298.10  E-value: 1.51e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  733 SVHTLRPADIQVVAALGDSLTAGNGISSqeGNLTDVSTQYRGLSY----------------------------------- 777
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWsiggdstlrglttlpnilrefnpslygysvgtgde 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  778 ----------------RNLTSQVRTLVQKMKSDNRVNFNRDWKVITVMIGASDLCDFCTDSNHYSAANFFDHLQNALDIL 841
Cdd:cd01824    79 tlpdsgfnvaepgaksEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  842 HKEVPRALVNLVDFINPSIIREVFLKnPDKCPvNQSSVLCNCVLTPRKDSYelARLEAFTKSYQSSMLQLVESGRYDtRE 921
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568934417  922 DFSVVLQPFLLNTKLPVLENGkPDTSFFAPDCIHLNQKFHTQLARALWANMLEPLG 977
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 ...
 65-321 3.36e-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: 231.46  E-value: 3.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   65 SVHSLRPSDIKLVAAIGNPEIP--LAPGSGTINMEkpqsIKNQPQDVCMGIM------TVLSDIIRHFSPSVLMPTCSPG 136
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAgnGAGSANNLDLL----TEYRGLSWSIGGDstlrglTTLPNILREFNPSLYGYSVGTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  137 KGT--------AVH-TTAEDLWIQAKELVRRLKDNPQLDFEKDWKLITVFFSNTSQCHLCPSAQQKShLMRHMEMLWGVL 207
Cdd:cd01824    77 DETlpdsgfnvAEPgAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRKAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  208 DYLHHEVPRAFVNLVDLSEVLAMdlqHQETGFSPAPEV-----CKCTETTTLSK----AVMQWSYQEAWEDLLASSKFNK 278
Cdd:cd01824   156 DILRDEVPRAFVNLVGLLNVASL---RSLTKKPLQCETllapeCPCLLGPTENSyqdlKKFYKEYQNEVEEIVESGEFDR 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568934417  279 hETFAVVFQPFFDEIEPPLKRS--------------SPQDPTTLALRIWNSMMEPVG 321
Cdd:cd01824   233 -EDFAVVVQPFFEDTSLPPLPDgpdlsffspdcfhfSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
398-672 8.97e-24

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 100.73  E-value: 8.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   398 IGALGDSLTAGNGAGASpwnildvlteyrglswsvggdetikTVTTLPNILREFNPSLKGFSVgtgkeSTSRASFNQAVA 477
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-------------------------GRFSWGDLLADFLARKLGVPG-----SGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   478 GAKSDGLAGQARKLVDLMKadkTINFQEDWKIITVFIGGNDLCASCsnstrFSPQNFIDNIKNALDILHAEVPRAFVNMA 557
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLIS---DVKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   558 MVMeitplreLFNEPTVSCprnilsrlCPCVLGLGDNSEElsslvqrNRDYQKKTEELINSGRYDtRDNFTVVVQPL--F 635
Cdd:pfam00657  123 KFW-------VHGLGPLGC--------TPPKGCYELYNAL-------AEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 568934417   636 ENVSMPRTPEGVPdksffaPDCFHFNAKTHARSAIAL 672
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1050-1316 9.78e-20

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 89.17  E-value: 9.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  1050 VAAMGDFLTTATGARPSGykrlatpwrglswsiggdgkletHTTLPNILKKFNPSITGFSTGTLDNkaGLNVAEEGARAQ 1129
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPGG-----------------------RFSWGDLLADFLARKLGVPGSGYNH--GANFAIGGATIE 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  1130 DMPAQAKTLVKKMKStptINLQEDWKLITLLIGNNDLCLYCENPEdnstkEYVKYIQQALDILYEELPRvFINVVEVMEL 1209
Cdd:pfam00657   56 DLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFLSSPA-----RSKKRVPDLLDELRANLPQ-LGLGARKFWV 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  1210 AGLHhvqggkcamPLAVQKNCSClrhsqnltamqeLKKLNWNLQSGISELSYWHRYM--EREDFAVTVQPF--FRNTFIP 1285
Cdd:pfam00657  127 HGLG---------PLGCTPPKGC------------YELYNALAEEYNERLNELVNSLaaAAEDANVVYVDIygFEDPTDP 185

                          250       260       270
                   ....*....|....*....|....*....|.
gi 568934417  1286 LNEREGLDltffseDCFYFSDRGHAEMAIAL 1316
Cdd:pfam00657  186 CCGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
745-968 4.60e-15

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 75.69  E-value: 4.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   745 VAALGDSLTAG--NGISSQEGN---LTDVSTQY----------------RGLSYRNLTSQVRTLVQKMKsdnRVNFNRDW 803
Cdd:pfam00657    1 IVAFGDSLTDGggDGPGGRFSWgdlLADFLARKlgvpgsgynhganfaiGGATIEDLPIQLEQLLRLIS---DVKDQAKP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   804 KVITVMIGASDLCDFCtdsnhYSAANFFDHLQNALDILHKEVPRALVNLVDFInpsiireVFLKNPdkcpvnqssVLCnc 883
Cdd:pfam00657   78 DLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGARKFW-------VHGLGP---------LGC-- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   884 vlTPRKDSYElaRLEAFTKSYQSSMLQLVESGRYDtREDFSVVLQPF--LLNTKLPVLENGkpdtsfFAPDCIHLNQKFH 961
Cdd:pfam00657  135 --TPPKGCYE--LYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygFEDPTDPCCGIG------LEPDGLHPSEKGY 203


                   ....*..
gi 568934417   962 TQLARAL 968
Cdd:pfam00657  204 KAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 398-567 9.77e-09

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: 56.58  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  398 IGALGDSLTAGNGAGaspwnildvlteyRGLSWsvggdetiktVTTLPNILREfnpslKGFSVgtgkestsrasFNQAVA 477
Cdd:COG2755    11 IVALGDSITAGYGAS-------------RERGW----------PALLARRLAA-----ADVRV-----------VNAGIS 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  478 GAKSDGLAGQARKLVDLMKADktinfqedwkIITVFIGGNDLcascSNSTRFSPQNFIDNIKNALDILHAEVPRAFVnma 557
Cdd:COG2755    52 GATTADLLARLDRDLLALKPD----------LVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAAGPGARV--- 114

                         170
                  ....*....|
gi 568934417  558 MVMEITPLRE 567
Cdd:COG2755   115 VLVTPPPRLR 124
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 745-970 3.43e-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: 49.26  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  745 VAALGDSLTAGNGISSQEG-------NLTDVSTQY-----RGLSYRNLTSQVRTLVQKMKSDnrvnfnrdwkVITVMIGA 812
Cdd:COG2755    11 IVALGDSITAGYGASRERGwpallarRLAAADVRVvnagiSGATTADLLARLDRDLLALKPD----------LVVIELGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  813 SDLcdfcTDSNHYSAANFFDHLQNALDILHKEVPRALVnlvdfinpsiirevflknpdkcpvnqssvlcnCVLTPRKDSY 892
Cdd:COG2755    81 NDL----LRGLGVSPEEFRANLEALIDRLRAAGPGARV--------------------------------VLVTPPPRLR 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  893 ElARLEAFTKSYQSSMLQLVEsgrydtREDFSVV--LQPFLLNTKLPvlengkpdtSFFAPDCIHLNQKFHTQLARALWA 970
Cdd:COG2755   125 P-NYLNERIEAYNAAIRELAA------EYGVPLVdlYAALRDAGDLP---------DLLTADGLHPNAAGYRLIAEAVLP 188
 
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 2.91e-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: 2.91e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  387 VHSLRPADIKIIGALGDSLTAGNGAGasPWNILDVLTEYRGLSWSVGGDETIKTVTTLPNILREFNPSLKGFSVGTGKES 466
Cdd:cd01824     2 VHRLRPGDIKVIAALGDSLTAGNGAG--SANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  467 TSRASFNQAVAGAKSDGLAGQARKLVDLMKADKTINFQEDWKIITVFIGGNDLCASCSNSTRFSPQNFIDNIKNALDILH 546
Cdd:cd01824    80 LPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  547 AEVPRAFVNMAMVMEITPLRELFNEPtVSCPrNILSRLCPCVLGLGDNSEElsSLVQRNRDYQKKTEELINSGRYDtRDN 626
Cdd:cd01824   160 DEVPRAFVNLVGLLNVASLRSLTKKP-LQCE-TLLAPECPCLLGPTENSYQ--DLKKFYKEYQNEVEEIVESGEFD-RED 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568934417  627 FTVVVQPLFENVSMPRTPEGvPDKSFFAPDCFHFNAKTHARSAIALWKNMLEPVG 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 ...
 1038-1325 3.19e-121

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: 379.76  E-value: 3.19e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1038 SVHELRPADIKVVAAMGDFLTTATGARPSGYKRLATPWRGLSWSIGGDGKLETHTTLPNILKKFNPSITGFSTGTLDNK- 1116
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1117 --AGLNVAEEGARAQDMPAQAKTLVKKMKSTPTINLQEDWKLITLLIGNNDLCLYCENPEDNSTKEYVKYIQQALDILYE 1194
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417 1195 ELPRVFINVVEVMELAGLHHVQGGK--CAMPLAvqKNCSCLRHsQNLTAMQELKKLNWNLQSGISELSYWHRYmEREDFA 1272
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLA--PECPCLLG-PTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568934417 1273 VTVQPFFRNTFIPLNeREGLDLTFFSEDCFYFSDRGHAEMAIALWNNMLEPVG 1325
Cdd:cd01824   237 VVVQPFFEDTSLPPL-PDGPDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 733-977 1.51e-91

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: 298.10  E-value: 1.51e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  733 SVHTLRPADIQVVAALGDSLTAGNGISSqeGNLTDVSTQYRGLSY----------------------------------- 777
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWsiggdstlrglttlpnilrefnpslygysvgtgde 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  778 ----------------RNLTSQVRTLVQKMKSDNRVNFNRDWKVITVMIGASDLCDFCTDSNHYSAANFFDHLQNALDIL 841
Cdd:cd01824    79 tlpdsgfnvaepgaksEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  842 HKEVPRALVNLVDFINPSIIREVFLKnPDKCPvNQSSVLCNCVLTPRKDSYelARLEAFTKSYQSSMLQLVESGRYDtRE 921
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568934417  922 DFSVVLQPFLLNTKLPVLENGkPDTSFFAPDCIHLNQKFHTQLARALWANMLEPLG 977
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 ...
 65-321 3.36e-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: 231.46  E-value: 3.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   65 SVHSLRPSDIKLVAAIGNPEIP--LAPGSGTINMEkpqsIKNQPQDVCMGIM------TVLSDIIRHFSPSVLMPTCSPG 136
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAgnGAGSANNLDLL----TEYRGLSWSIGGDstlrglTTLPNILREFNPSLYGYSVGTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  137 KGT--------AVH-TTAEDLWIQAKELVRRLKDNPQLDFEKDWKLITVFFSNTSQCHLCPSAQQKShLMRHMEMLWGVL 207
Cdd:cd01824    77 DETlpdsgfnvAEPgAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRKAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  208 DYLHHEVPRAFVNLVDLSEVLAMdlqHQETGFSPAPEV-----CKCTETTTLSK----AVMQWSYQEAWEDLLASSKFNK 278
Cdd:cd01824   156 DILRDEVPRAFVNLVGLLNVASL---RSLTKKPLQCETllapeCPCLLGPTENSyqdlKKFYKEYQNEVEEIVESGEFDR 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568934417  279 hETFAVVFQPFFDEIEPPLKRS--------------SPQDPTTLALRIWNSMMEPVG 321
Cdd:cd01824   233 -EDFAVVVQPFFEDTSLPPLPDgpdlsffspdcfhfSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
398-672 8.97e-24

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 100.73  E-value: 8.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   398 IGALGDSLTAGNGAGASpwnildvlteyrglswsvggdetikTVTTLPNILREFNPSLKGFSVgtgkeSTSRASFNQAVA 477
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-------------------------GRFSWGDLLADFLARKLGVPG-----SGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   478 GAKSDGLAGQARKLVDLMKadkTINFQEDWKIITVFIGGNDLCASCsnstrFSPQNFIDNIKNALDILHAEVPRAFVNMA 557
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLIS---DVKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   558 MVMeitplreLFNEPTVSCprnilsrlCPCVLGLGDNSEElsslvqrNRDYQKKTEELINSGRYDtRDNFTVVVQPL--F 635
Cdd:pfam00657  123 KFW-------VHGLGPLGC--------TPPKGCYELYNAL-------AEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 568934417   636 ENVSMPRTPEGVPdksffaPDCFHFNAKTHARSAIAL 672
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1050-1316 9.78e-20

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 89.17  E-value: 9.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  1050 VAAMGDFLTTATGARPSGykrlatpwrglswsiggdgkletHTTLPNILKKFNPSITGFSTGTLDNkaGLNVAEEGARAQ 1129
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPGG-----------------------RFSWGDLLADFLARKLGVPGSGYNH--GANFAIGGATIE 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  1130 DMPAQAKTLVKKMKStptINLQEDWKLITLLIGNNDLCLYCENPEdnstkEYVKYIQQALDILYEELPRvFINVVEVMEL 1209
Cdd:pfam00657   56 DLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFLSSPA-----RSKKRVPDLLDELRANLPQ-LGLGARKFWV 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  1210 AGLHhvqggkcamPLAVQKNCSClrhsqnltamqeLKKLNWNLQSGISELSYWHRYM--EREDFAVTVQPF--FRNTFIP 1285
Cdd:pfam00657  127 HGLG---------PLGCTPPKGC------------YELYNALAEEYNERLNELVNSLaaAAEDANVVYVDIygFEDPTDP 185

                          250       260       270
                   ....*....|....*....|....*....|.
gi 568934417  1286 LNEREGLDltffseDCFYFSDRGHAEMAIAL 1316
Cdd:pfam00657  186 CCGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
745-968 4.60e-15

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 75.69  E-value: 4.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   745 VAALGDSLTAG--NGISSQEGN---LTDVSTQY----------------RGLSYRNLTSQVRTLVQKMKsdnRVNFNRDW 803
Cdd:pfam00657    1 IVAFGDSLTDGggDGPGGRFSWgdlLADFLARKlgvpgsgynhganfaiGGATIEDLPIQLEQLLRLIS---DVKDQAKP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   804 KVITVMIGASDLCDFCtdsnhYSAANFFDHLQNALDILHKEVPRALVNLVDFInpsiireVFLKNPdkcpvnqssVLCnc 883
Cdd:pfam00657   78 DLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGARKFW-------VHGLGP---------LGC-- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   884 vlTPRKDSYElaRLEAFTKSYQSSMLQLVESGRYDtREDFSVVLQPF--LLNTKLPVLENGkpdtsfFAPDCIHLNQKFH 961
Cdd:pfam00657  135 --TPPKGCYE--LYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygFEDPTDPCCGIG------LEPDGLHPSEKGY 203


                   ....*..
gi 568934417   962 TQLARAL 968
Cdd:pfam00657  204 KAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 398-567 9.77e-09

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: 56.58  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  398 IGALGDSLTAGNGAGaspwnildvlteyRGLSWsvggdetiktVTTLPNILREfnpslKGFSVgtgkestsrasFNQAVA 477
Cdd:COG2755    11 IVALGDSITAGYGAS-------------RERGW----------PALLARRLAA-----ADVRV-----------VNAGIS 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  478 GAKSDGLAGQARKLVDLMKADktinfqedwkIITVFIGGNDLcascSNSTRFSPQNFIDNIKNALDILHAEVPRAFVnma 557
Cdd:COG2755    52 GATTADLLARLDRDLLALKPD----------LVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAAGPGARV--- 114

                         170
                  ....*....|
gi 568934417  558 MVMEITPLRE 567
Cdd:COG2755   115 VLVTPPPRLR 124
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 398-674 1.45e-06

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: 50.10  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  398 IGALGDSLTAGNGAGA---SPWNILDVLTEYRGLSWSVggdetiktvttlpnilrefnpslkgfsvgtgkestsrasFNQ 474
Cdd:cd00229     1 ILVIGDSITAGYGASSgstFYSLLLYLLLLAGGPGVEV---------------------------------------INL 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  475 AVAGAKSDGLAGQARKLVDLMKadktinfqEDWKIITVFIGGNDLCASCsnstRFSPQNFIDNIKNALDILHAEVPRAFV 554
Cdd:cd00229    42 GVSGATTADALRRLGLRLALLK--------DKPDLVIIELGTNDLGRGG----DTSIDEFKANLEELLDALRERAPGAKV 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  555 NmamVMEITPLRElfneptvscprnilsrlcpcvlglgdnseelssLVQRNRDYQKKTEELINSGRYDTRDNFTVVVQPL 634
Cdd:cd00229   110 I---LITPPPPPP---------------------------------REGLLGRALPRYNEAIKAVAAENPAPSGVDLVDL 153

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568934417  635 FenvsmprTPEGVPDKSFFAPDCFHFNAKTHARSAIALWK 674
Cdd:cd00229   154 A-------ALLGDEDKSLYSPDGIHPNPAGHKLIAEALAS 186
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 745-970 2.30e-06

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: 49.72  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  745 VAALGDSLTAGNGISSQEGNLTDVSTQYR-----GLSYRNLTSQVRTLVQKMKSDN--RVNFNRDWKVITVMIGASDLcd 817
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLLYLLLlaggpGVEVINLGVSGATTADALRRLGlrLALLKDKPDLVIIELGTNDL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  818 fcTDSNHYSAANFFDHLQNALDILHKEVPRALVNLVDFINPsiirevflknpdkcpvnqssvlcncvltprkdsyelARL 897
Cdd:cd00229    79 --GRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPP------------------------------------PPR 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568934417  898 EAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLLNTKlpvlengKPDTSFFAPDCIHLNQKFHTQLARALWA 970
Cdd:cd00229   121 EGLLGRALPRYNEAIKAVAAENPAPSGVDLVDLAALLG-------DEDKSLYSPDGIHPNPAGHKLIAEALAS 186
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 745-970 3.43e-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: 49.26  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  745 VAALGDSLTAGNGISSQEG-------NLTDVSTQY-----RGLSYRNLTSQVRTLVQKMKSDnrvnfnrdwkVITVMIGA 812
Cdd:COG2755    11 IVALGDSITAGYGASRERGwpallarRLAAADVRVvnagiSGATTADLLARLDRDLLALKPD----------LVVIELGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  813 SDLcdfcTDSNHYSAANFFDHLQNALDILHKEVPRALVnlvdfinpsiirevflknpdkcpvnqssvlcnCVLTPRKDSY 892
Cdd:COG2755    81 NDL----LRGLGVSPEEFRANLEALIDRLRAAGPGARV--------------------------------VLVTPPPRLR 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  893 ElARLEAFTKSYQSSMLQLVEsgrydtREDFSVV--LQPFLLNTKLPvlengkpdtSFFAPDCIHLNQKFHTQLARALWA 970
Cdd:COG2755   125 P-NYLNERIEAYNAAIRELAA------EYGVPLVdlYAALRDAGDLP---------DLLTADGLHPNAAGYRLIAEAVLP 188
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 398-519 2.59e-03

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: 40.69  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417  398 IGALGDSLTAGngagaspwnildvlteyrglswsVGgDETiktvttlpnilrefnpsLKGFSVGTGKESTSR------AS 471
Cdd:cd04506     2 IVALGDSLTEG-----------------------VG-DET-----------------GKGGYVGRLDKLIETktvkkvTV 40

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568934417  472 FNQAVAGAKSDGLAGQARK---LVDLMKADktinfqedwkIITVFIGGNDL 519
Cdd:cd04506    41 QNFGVSGDRSDQLLKRLKTkkvQKELKKAD----------VITITIGGNDL 81
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 747-850 4.31e-03

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: 39.84  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934417   747 ALGDSLTAGNGISSQEGNLTDVSTQYRGLSYRNLTSQVR-----TLVQKMKSDNRVNFNRDWKVITVMIGASDLCdfctd 821
Cdd:pfam13472    1 ALGDSITAGYGATGGDRSYPGWLARLLARRLGADVVNNLgisgaTTRLDLLERLDDVLRLKPDLVVILLGTNDLG----- 75

                           90       100
                   ....*....|....*....|....*....
gi 568934417   822 sNHYSAANFFDHLQNALDILHKEVPRALV 850
Cdd:pfam13472   76 -RGVSAARAAANLEALIDALRAAGPDARV 103
 
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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