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Conserved domains on  [gi|1958781846|ref|XP_038967688|]
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phospholipase B1, membrane-associated isoform X2 [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 ...
239-534 2.73e-129

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: 391.32  E-value: 2.73e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 239 SVHTLRPADIQVVAALGDSVTAGNGISSqeGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDV 318
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 319 NSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDIL 398
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 399 HKEVPRALVNLVDFMNPSIIRQVFLKnPDKCPvNQTSVLCNCVLTPGEDSHelARLEAFTKSYQSSMLQLVESGRYDtRE 478
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958781846 479 DFSVVLQPFLFNIRLPILENGnPDTSFFAPDCILLSQKFHTQLARALWANMLEPLG 534
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 ...
595-882 9.32e-123

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: 374.37  E-value: 9.32e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 595 SVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENT- 673
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 674 --AGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYE 751
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 752 ELPRVFINVVEVMELSGL--LHDQGGKCAMPLAvqKNCSCLkRSQNLMAMQELKKVNGNLQSALSELSYWHRYmQREDFA 829
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLrsLTKKPLQCETLLA--PECPCL-LGPTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958781846 830 VTVQPFFRNTFVPLDERgGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVG 882
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 ...
1-187 1.25e-70

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: 236.08  E-value: 1.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846   1 MKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKv 80
Cdd:cd01824   108 MKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRDEVPRAFVNLVGLLNVASLRSLTKKPL- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  81 SCPRMiLRSLCPCVLNLGENSaeLAQLVERNRQYQEETGKLIESGRYDtRDDFTVVLQPMFENVVMPRTLEGlPDSSFFA 160
Cdd:cd01824   187 QCETL-LAPECPCLLGPTENS--YQDLKKFYKEYQNEVEEIVESGEFD-REDFAVVVQPFFEDTSLPPLPDG-PDLSFFS 261
                         170       180
                  ....*....|....*....|....*..
gi 1958781846 161 PDCFHFNVKTHARSAIALWKNMLEPVG 187
Cdd:cd01824   262 PDCFHFSQRGHAIAANALWNNLLEPVG 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 ...
239-534 2.73e-129

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: 391.32  E-value: 2.73e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 239 SVHTLRPADIQVVAALGDSVTAGNGISSqeGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDV 318
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 319 NSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDIL 398
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 399 HKEVPRALVNLVDFMNPSIIRQVFLKnPDKCPvNQTSVLCNCVLTPGEDSHelARLEAFTKSYQSSMLQLVESGRYDtRE 478
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958781846 479 DFSVVLQPFLFNIRLPILENGnPDTSFFAPDCILLSQKFHTQLARALWANMLEPLG 534
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 ...
595-882 9.32e-123

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: 374.37  E-value: 9.32e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 595 SVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENT- 673
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 674 --AGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYE 751
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 752 ELPRVFINVVEVMELSGL--LHDQGGKCAMPLAvqKNCSCLkRSQNLMAMQELKKVNGNLQSALSELSYWHRYmQREDFA 829
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLrsLTKKPLQCETLLA--PECPCL-LGPTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958781846 830 VTVQPFFRNTFVPLDERgGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVG 882
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 ...
1-187 1.25e-70

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: 236.08  E-value: 1.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846   1 MKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKv 80
Cdd:cd01824   108 MKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRDEVPRAFVNLVGLLNVASLRSLTKKPL- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  81 SCPRMiLRSLCPCVLNLGENSaeLAQLVERNRQYQEETGKLIESGRYDtRDDFTVVLQPMFENVVMPRTLEGlPDSSFFA 160
Cdd:cd01824   187 QCETL-LAPECPCLLGPTENS--YQDLKKFYKEYQNEVEEIVESGEFD-REDFAVVVQPFFEDTSLPPLPDG-PDLSFFS 261
                         170       180
                  ....*....|....*....|....*..
gi 1958781846 161 PDCFHFNVKTHARSAIALWKNMLEPVG 187
Cdd:cd01824   262 PDCFHFSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
640-873 1.21e-20

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 91.10  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 640 GGDGTLeTHTTLPNILKKFNPSILGFSTGTleNTAGLNVAEEGARAQDMPAQAQALVKKMKStptINIQEDWKLITLLIG 719
Cdd:pfam00657  12 GGDGPG-GRFSWGDLLADFLARKLGVPGSG--YNHGANFAIGGATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 720 NNDLCLYCEDPENystreYVKYIQHALDIFYEELPRvFINVVEVMELSGLLhdqggkcamPLAVQKNCSCLKRsqnlmam 799
Cdd:pfam00657  86 ANDLCNFLSSPAR-----SKKRVPDLLDELRANLPQ-LGLGARKFWVHGLG---------PLGCTPPKGCYEL------- 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958781846 800 qelkkVNGNLQSALSELSYWHRYMQRE--DFAVTVQPF--FRNTFVPLDERGGLDltffseDCFHFSVRGHAEMAIAL 873
Cdd:pfam00657 144 -----YNALAEEYNERLNELVNSLAAAaeDANVVYVDIygFEDPTDPCCGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
251-525 3.61e-18

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 84.16  E-value: 3.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 251 VAALGDSVTAGNGissqegdladvttqyrglsYSAGGDkflenvTTLPNILREFNGNLTGYSVGTGDVnsasaFLNQAVP 330
Cdd:pfam00657   1 IVAFGDSLTDGGG-------------------DGPGGR------FSWGDLLADFLARKLGVPGSGYNH-----GANFAIG 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 331 GAKAENLASQVQTLIQKMKNdtrVNFHQDWKVITVMIGASDLCDFCKdsnrySAANFSDHLRNALDILHKEVPRaLVNLV 410
Cdd:pfam00657  51 GATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFLS-----SPARSKKRVPDLLDELRANLPQ-LGLGA 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 411 DFMNPSIIRQVfLKNPDKcpvnqtsvlcncvltpgedsHELARLEAFTKSYQSSMLQLVESGRYDtREDFSVVLQPF--L 488
Cdd:pfam00657 122 RKFWVHGLGPL-GCTPPK--------------------GCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958781846 489 FNIRLPILENGNPdtsffaPDCILLSQKFHTQLARAL 525
Cdd:pfam00657 180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
7-178 2.36e-13

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 69.91  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846   7 INFQEDWKIITVFIGGNDLCGSCnnlarFSPQTFTDNIKTALDILHAEVPRafvnmvsvieitpLRELFNEPKVSCPRMI 86
Cdd:pfam00657  71 VKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQ-------------LGLGARKFWVHGLGPL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  87 LRslCPCVLNLGENSAElaqlverNRQYQEETGKLIESGRYDtRDDFTVVLQPM--FENVVMPRTLEGLPdssffaPDCF 164
Cdd:pfam00657 133 GC--TPPKGCYELYNAL-------AEEYNERLNELVNSLAAA-AEDANVVYVDIygFEDPTDPCCGIGLE------PDGL 196
                         170
                  ....*....|....
gi 1958781846 165 HFNVKTHARSAIAL 178
Cdd:pfam00657 197 HPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
251-407 2.54e-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: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 251 VAALGDSVTAGNGISSQEGdladvttqYRGLsysaggdkflenvttLPNILREFNGNltgysvgtgdvnsasaFLNQAVP 330
Cdd:COG2755    11 IVALGDSITAGYGASRERG--------WPAL---------------LARRLAAADVR----------------VVNAGIS 51
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781846 331 GAKAENLASQVQTLIQKMKndtrvnfhqdWKVITVMIGASDLcdfcKDSNRYSAANFSDHLRNALDILHKEVPRALV 407
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 ...
239-534 2.73e-129

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: 391.32  E-value: 2.73e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 239 SVHTLRPADIQVVAALGDSVTAGNGISSqeGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDV 318
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGS--ANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 319 NSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDIL 398
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 399 HKEVPRALVNLVDFMNPSIIRQVFLKnPDKCPvNQTSVLCNCVLTPGEDSHelARLEAFTKSYQSSMLQLVESGRYDtRE 478
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKK-PLQCE-TLLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958781846 479 DFSVVLQPFLFNIRLPILENGnPDTSFFAPDCILLSQKFHTQLARALWANMLEPLG 534
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 ...
595-882 9.32e-123

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: 374.37  E-value: 9.32e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 595 SVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENT- 673
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDETl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 674 --AGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYE 751
Cdd:cd01824    81 pdSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 752 ELPRVFINVVEVMELSGL--LHDQGGKCAMPLAvqKNCSCLkRSQNLMAMQELKKVNGNLQSALSELSYWHRYmQREDFA 829
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLrsLTKKPLQCETLLA--PECPCL-LGPTENSYQDLKKFYKEYQNEVEEIVESGEF-DREDFA 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958781846 830 VTVQPFFRNTFVPLDERgGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVG 882
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 ...
1-187 1.25e-70

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: 236.08  E-value: 1.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846   1 MKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKv 80
Cdd:cd01824   108 MKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRDEVPRAFVNLVGLLNVASLRSLTKKPL- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  81 SCPRMiLRSLCPCVLNLGENSaeLAQLVERNRQYQEETGKLIESGRYDtRDDFTVVLQPMFENVVMPRTLEGlPDSSFFA 160
Cdd:cd01824   187 QCETL-LAPECPCLLGPTENS--YQDLKKFYKEYQNEVEEIVESGEFD-REDFAVVVQPFFEDTSLPPLPDG-PDLSFFS 261
                         170       180
                  ....*....|....*....|....*..
gi 1958781846 161 PDCFHFNVKTHARSAIALWKNMLEPVG 187
Cdd:cd01824   262 PDCFHFSQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
640-873 1.21e-20

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 91.10  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 640 GGDGTLeTHTTLPNILKKFNPSILGFSTGTleNTAGLNVAEEGARAQDMPAQAQALVKKMKStptINIQEDWKLITLLIG 719
Cdd:pfam00657  12 GGDGPG-GRFSWGDLLADFLARKLGVPGSG--YNHGANFAIGGATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 720 NNDLCLYCEDPENystreYVKYIQHALDIFYEELPRvFINVVEVMELSGLLhdqggkcamPLAVQKNCSCLKRsqnlmam 799
Cdd:pfam00657  86 ANDLCNFLSSPAR-----SKKRVPDLLDELRANLPQ-LGLGARKFWVHGLG---------PLGCTPPKGCYEL------- 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958781846 800 qelkkVNGNLQSALSELSYWHRYMQRE--DFAVTVQPF--FRNTFVPLDERGGLDltffseDCFHFSVRGHAEMAIAL 873
Cdd:pfam00657 144 -----YNALAEEYNERLNELVNSLAAAaeDANVVYVDIygFEDPTDPCCGIGLEP------DGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
251-525 3.61e-18

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 84.16  E-value: 3.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 251 VAALGDSVTAGNGissqegdladvttqyrglsYSAGGDkflenvTTLPNILREFNGNLTGYSVGTGDVnsasaFLNQAVP 330
Cdd:pfam00657   1 IVAFGDSLTDGGG-------------------DGPGGR------FSWGDLLADFLARKLGVPGSGYNH-----GANFAIG 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 331 GAKAENLASQVQTLIQKMKNdtrVNFHQDWKVITVMIGASDLCDFCKdsnrySAANFSDHLRNALDILHKEVPRaLVNLV 410
Cdd:pfam00657  51 GATIEDLPIQLEQLLRLISD---VKDQAKPDLVTIFIGANDLCNFLS-----SPARSKKRVPDLLDELRANLPQ-LGLGA 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 411 DFMNPSIIRQVfLKNPDKcpvnqtsvlcncvltpgedsHELARLEAFTKSYQSSMLQLVESGRYDtREDFSVVLQPF--L 488
Cdd:pfam00657 122 RKFWVHGLGPL-GCTPPK--------------------GCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958781846 489 FNIRLPILENGNPdtsffaPDCILLSQKFHTQLARAL 525
Cdd:pfam00657 180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
7-178 2.36e-13

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 69.91  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846   7 INFQEDWKIITVFIGGNDLCGSCnnlarFSPQTFTDNIKTALDILHAEVPRafvnmvsvieitpLRELFNEPKVSCPRMI 86
Cdd:pfam00657  71 VKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQ-------------LGLGARKFWVHGLGPL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  87 LRslCPCVLNLGENSAElaqlverNRQYQEETGKLIESGRYDtRDDFTVVLQPM--FENVVMPRTLEGLPdssffaPDCF 164
Cdd:pfam00657 133 GC--TPPKGCYELYNAL-------AEEYNERLNELVNSLAAA-AEDANVVYVDIygFEDPTDPCCGIGLE------PDGL 196
                         170
                  ....*....|....
gi 1958781846 165 HFNVKTHARSAIAL 178
Cdd:pfam00657 197 HPSEKGYKAVAEAI 210
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
10-180 7.88e-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: 47.41  E-value: 7.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  10 QEDWKIITVFIGGNDLCGSCNnlarFSPQTFTDNIKTALDILHAEVPRAfvnmvSVIEITPLrelfnepkvscprmilrs 89
Cdd:cd00229    63 KDKPDLVIIELGTNDLGRGGD----TSIDEFKANLEELLDALRERAPGA-----KVILITPP------------------ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  90 lcPCVLNLGENSAELAQLVERNRQYQEETGKliesgrydtrddftvvlqPMFENVVMPRTLEGLPDSSFFAPDCFHFNVK 169
Cdd:cd00229   116 --PPPPREGLLGRALPRYNEAIKAVAAENPA------------------PSGVDLVDLAALLGDEDKSLYSPDGIHPNPA 175
                         170
                  ....*....|.
gi 1958781846 170 THARSAIALWK 180
Cdd:cd00229   176 GHKLIAEALAS 186
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
251-407 2.54e-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: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846 251 VAALGDSVTAGNGISSQEGdladvttqYRGLsysaggdkflenvttLPNILREFNGNltgysvgtgdvnsasaFLNQAVP 330
Cdd:COG2755    11 IVALGDSITAGYGASRERG--------WPAL---------------LARRLAAADVR----------------VVNAGIS 51
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781846 331 GAKAENLASQVQTLIQKMKndtrvnfhqdWKVITVMIGASDLcdfcKDSNRYSAANFSDHLRNALDILHKEVPRALV 407
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 ...
10-173 2.15e-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: 40.22  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  10 QEDWKIITVFIGGNDLcgscnnLARFSPQTFTDNIKTALDILHAEVPRAfvnmvsvieitplrelfnepkvscpRMILRS 89
Cdd:pfam13472  59 RLKPDLVVILLGTNDL------GRGVSAARAAANLEALIDALRAAGPDA-------------------------RVLLIG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781846  90 LCPCVLNLGENSAELAQLVERNRQYQEETGKliesgrydtRDDFTVV-LQPMFENvvmprtlEGLPDSSFFAPDCFHFNV 168
Cdd:pfam13472 108 PLPVGPPPPLDERRLNARIAEYNAAIREVAA---------ERGVPYVdLWDALRD-------DGGWLPDLLADDGLHPNA 171

                  ....*
gi 1958781846 169 KTHAR 173
Cdd:pfam13472 172 AGYRL 176
 
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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