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Conserved domains on  [gi|742122978|ref|XP_010839003|]
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PREDICTED: phospholipase B1, membrane-associated [Bison bison bison]

Protein Classification

Phospholipase_B_like domain-containing protein( domain architecture ID 10232815)

Phospholipase_B_like domain-containing protein

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 ...
 321-616 2.75e-130

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: 403.65  E-value: 2.75e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  321 SVHRLKLADIKVIGALGDSLTAGNGAGskPGNVLDVLTQYRGLSWSVGGDKNLSSVITLPNMLREFNPSLKGFSVGKGSE 400
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAG--SANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  401 SSSGAYLNQAVPGAQAEDLPVQARRLVDLMKNDVNINFQEDWKIITLFIGGNDLCDVCDDPVRFSPQNFVDNIGQALDIL 480
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  481 HAEVPRAFVNLVKVLEIINLRKLYQDKnVSCPRLiLRNLCPCVLKYDDNATelASLIEVNKKYQEGTHQLVESGRYDtRE 560
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKKP-LQCETL-LAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 742122978  561 DFTVVVQPFLEKVDMPMTPEGlPDNSYFAPDCFHFSSKAHAHAASALWNNMLQPVG 616
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 ...
 668-963 2.61e-128

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: 398.25  E-value: 2.61e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  668 SVHTLRPADIQVVAALGDSLTAGNGIGSKPNdlSDVTTQYRGLSYSSGGDSSLENVTTLPNILRKFNGNLTGYAVGTGDA 747
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANN--LDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  748 NETNAFLNQAVPGAKAEELVSQVQTLIQKMKSDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSADNFFDHLRNALDIL 827
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  828 HREVPRALVNLVDFMSPSIMRQVFlGNPDKCPVhQASILCNCVLTPRESSQelAKLESITRAYQSSMRELVESGRYeTRE 907
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLT-KKPLQCET-LLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEF-DRE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 742122978  908 DFSVVLQPFFYNIRLPVLADGrPDVSFFAPDCLNPSQKFHSQLSRALWVNMLEPLG 963
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 ...
 1024-1310 7.57e-128

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: 397.10  E-value: 7.57e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1024 SVHELRPADIKVVAALGDSLTTAVGARPSNSSDLPTSWRGLSWSIGGDGDLGTHTTLPNILKKFNPNILGFSTGT---RE 1100
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTgdeTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1101 ETAGLNVATEGARARDMPAQARDLVERMKTSPEINLQKDWKLITLFIGSNDLCHYCDNEEARSAEEYVKYIRQALDILYE 1180
Cdd:cd01824    81 PDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1181 QLPRAFINVVEVMELADLHQGQDGK--CVMPLPAqsNCTCLQGSQENlpEMQELKTVNWNFQSALSTLSYQ-YLQREDFA 1257
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLAP--ECPCLLGPTEN--SYQDLKKFYKEYQNEVEEIVESgEFDREDFA 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 742122978 1258 VVVQPFFQNTLVPLNKRgGADLTFFSEDCFHFSERGHAEMAIALWNNMLEPLG 1310
Cdd:cd01824   237 VVVQPFFEDTSLPPLPD-GPDLSFFSPDCFHFSQRGHAIAANALWNNLLEPVG 288
SGNH_hydrolase super family cl01053
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 19-254 3.57e-59

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.


The actual alignment was detected with superfamily member cd01824:

Pssm-ID: 470049  Cd Length: 288  Bit Score: 205.65  E-value: 3.57e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   19 VHSLRPSDIKFVAAIGNVSIPPDSGTD----DLEEQEwtekQELQACMGV------VTVLSDVIRYFSPSVLKPICTLGT 88
Cdd:cd01824     2 VHRLRPGDIKVIAALGDSLTAGNGAGSannlDLLTEY----RGLSWSIGGdstlrgLTTLPNILREFNPSLYGYSVGTGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   89 EV---------VHHDAAEDLWVQAKDLVRNMKENQQLDFQNDWKLINVFFSNASQCRLCSSTQQQShVTSSMDQLTRTLD 159
Cdd:cd01824    78 ETlpdsgfnvaEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRKALD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  160 YLHQEVPKAFVNLVDLSE-----ALRGSHWHQKTLLSPtaqPCTCSGETSRLSSVVTQWT---YQETWERLLASSKYNeQ 231
Cdd:cd01824   157 ILRDEVPRAFVNLVGLLNvaslrSLTKKPLQCETLLAP---ECPCLLGPTENSYQDLKKFykeYQNEVEEIVESGEFD-R 232

                         250       260
                  ....*....|....*....|...
gi 742122978  232 ESFAVVFQPFFYERALPPTSMQP 254
Cdd:cd01824   233 EDFAVVVQPFFEDTSLPPLPDGP 255
 
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 ...
 321-616 2.75e-130

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: 403.65  E-value: 2.75e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  321 SVHRLKLADIKVIGALGDSLTAGNGAGskPGNVLDVLTQYRGLSWSVGGDKNLSSVITLPNMLREFNPSLKGFSVGKGSE 400
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAG--SANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  401 SSSGAYLNQAVPGAQAEDLPVQARRLVDLMKNDVNINFQEDWKIITLFIGGNDLCDVCDDPVRFSPQNFVDNIGQALDIL 480
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  481 HAEVPRAFVNLVKVLEIINLRKLYQDKnVSCPRLiLRNLCPCVLKYDDNATelASLIEVNKKYQEGTHQLVESGRYDtRE 560
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKKP-LQCETL-LAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 742122978  561 DFTVVVQPFLEKVDMPMTPEGlPDNSYFAPDCFHFSSKAHAHAASALWNNMLQPVG 616
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 ...
 668-963 2.61e-128

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: 398.25  E-value: 2.61e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  668 SVHTLRPADIQVVAALGDSLTAGNGIGSKPNdlSDVTTQYRGLSYSSGGDSSLENVTTLPNILRKFNGNLTGYAVGTGDA 747
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANN--LDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  748 NETNAFLNQAVPGAKAEELVSQVQTLIQKMKSDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSADNFFDHLRNALDIL 827
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  828 HREVPRALVNLVDFMSPSIMRQVFlGNPDKCPVhQASILCNCVLTPRESSQelAKLESITRAYQSSMRELVESGRYeTRE 907
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLT-KKPLQCET-LLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEF-DRE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 742122978  908 DFSVVLQPFFYNIRLPVLADGrPDVSFFAPDCLNPSQKFHSQLSRALWVNMLEPLG 963
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 ...
 1024-1310 7.57e-128

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: 397.10  E-value: 7.57e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1024 SVHELRPADIKVVAALGDSLTTAVGARPSNSSDLPTSWRGLSWSIGGDGDLGTHTTLPNILKKFNPNILGFSTGT---RE 1100
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTgdeTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1101 ETAGLNVATEGARARDMPAQARDLVERMKTSPEINLQKDWKLITLFIGSNDLCHYCDNEEARSAEEYVKYIRQALDILYE 1180
Cdd:cd01824    81 PDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1181 QLPRAFINVVEVMELADLHQGQDGK--CVMPLPAqsNCTCLQGSQENlpEMQELKTVNWNFQSALSTLSYQ-YLQREDFA 1257
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLAP--ECPCLLGPTEN--SYQDLKKFYKEYQNEVEEIVESgEFDREDFA 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 742122978 1258 VVVQPFFQNTLVPLNKRgGADLTFFSEDCFHFSERGHAEMAIALWNNMLEPLG 1310
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 ...
 19-254 3.57e-59

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: 205.65  E-value: 3.57e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   19 VHSLRPSDIKFVAAIGNVSIPPDSGTD----DLEEQEwtekQELQACMGV------VTVLSDVIRYFSPSVLKPICTLGT 88
Cdd:cd01824     2 VHRLRPGDIKVIAALGDSLTAGNGAGSannlDLLTEY----RGLSWSIGGdstlrgLTTLPNILREFNPSLYGYSVGTGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   89 EV---------VHHDAAEDLWVQAKDLVRNMKENQQLDFQNDWKLINVFFSNASQCRLCSSTQQQShVTSSMDQLTRTLD 159
Cdd:cd01824    78 ETlpdsgfnvaEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRKALD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  160 YLHQEVPKAFVNLVDLSE-----ALRGSHWHQKTLLSPtaqPCTCSGETSRLSSVVTQWT---YQETWERLLASSKYNeQ 231
Cdd:cd01824   157 ILRDEVPRAFVNLVGLLNvaslrSLTKKPLQCETLLAP---ECPCLLGPTENSYQDLKKFykeYQNEVEEIVESGEFD-R 232

                         250       260
                  ....*....|....*....|...
gi 742122978  232 ESFAVVFQPFFYERALPPTSMQP 254
Cdd:cd01824   233 EDFAVVVQPFFEDTSLPPLPDGP 255
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1036-1301 3.90e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 104.96  E-value: 3.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1036 VAALGDSLTTAVGARPsnssdlptswrglswsiggdgdlGTHTTLPNILKKFNPNILGFSTGTReeTAGLNVATEGARAR 1115
Cdd:pfam00657    1 IVAFGDSLTDGGGDGP-----------------------GGRFSWGDLLADFLARKLGVPGSGY--NHGANFAIGGATIE 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1116 DMPAQARDLVERMKtspEINLQKDWKLITLFIGSNDLCHYCdneeaRSAEEYVKYIRQALDILYEQLPRAFINVVEVMel 1195
Cdd:pfam00657   56 DLPIQLEQLLRLIS---DVKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGARKFW-- 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1196 adlhqgqdgkcVMPLPaQSNCTCLQGSQENLPEMQELktvnwnFQSALSTL--SYQYlQREDFAVVVQPF--FQNTLVPL 1271
Cdd:pfam00657  126 -----------VHGLG-PLGCTPPKGCYELYNALAEE------YNERLNELvnSLAA-AAEDANVVYVDIygFEDPTDPC 186

                          250       260       270
                   ....*....|....*....|....*....|
gi 742122978  1272 NKRGGadltffSEDCFHFSERGHAEMAIAL 1301
Cdd:pfam00657  187 CGIGL------EPDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
333-595 6.89e-22

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 95.33  E-value: 6.89e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   333 IGALGDSLTAGNGAGSKpGNVldvltqyrglSWsvggdknlssvitlPNMLREFNPSLKGFSVgkgseSSSGAYLNQAVP 412
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-GRF----------SW--------------GDLLADFLARKLGVPG-----SGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   413 GAQAEDLPVQARRLVDLMKNDVNinfQEDWKIITLFIGGNDLCDVCddpvrFSPQNFVDNIGQALDILHAEVPRAFVNLV 492
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISDVKD---QAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   493 KVleiinlrklyqdkNVSCPRLILRNLCPCVLKYddnatelasLIEVNKKYQEGTHQLVESGRYDtREDFTVVVQPFLEk 572
Cdd:pfam00657  123 KF-------------WVHGLGPLGCTPPKGCYEL---------YNALAEEYNERLNELVNSLAAA-AEDANVVYVDIYG- 178

                          250       260
                   ....*....|....*....|...
gi 742122978   573 vdmPMTPEGLPDNSYFAPDCFHF 595
Cdd:pfam00657  179 ---FEDPTDPCCGIGLEPDGLHP 198
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
680-954 8.79e-19

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 86.47  E-value: 8.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   680 VAALGDSLTAGNGIGSKPNdlsdvttqyrglsyssggdsslenvTTLPNILRKFNGNLTGYavgtgDANETNAFLNQAVP 759
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPGGR-------------------------FSWGDLLADFLARKLGV-----PGSGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   760 GAKAEELVSQVQTLIQKMksdHRVNFHEDWKVITVLIGGSDLCDYCtdsnlYSADNFFDHLRNALDILHREVPRaLVNLV 839
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLI---SDVKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQ-LGLGA 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   840 DFMSPSIMRQvflgnpdkcpvhqasILCncvlTPResSQELAKLESITRAYQSSMRELVESGRYEtREDFSVVLQPF--F 917
Cdd:pfam00657  122 RKFWVHGLGP---------------LGC----TPP--KGCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 742122978   918 YNIRLPVLADGRPdvsffaPDCLNPSQKFHSQLSRAL 954
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 331-487 3.79e-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: 48.87  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  331 KVIGALGDSLTAGNGAGskpgnvldvltqyRGLSWsvggdknlssvitlPNMLREFnpsLKGFSVgkgsesssgAYLNQA 410
Cdd:COG2755     9 LRIVALGDSITAGYGAS-------------RERGW--------------PALLARR---LAAADV---------RVVNAG 49

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742122978  411 VPGAQAEDLPVQARRLVDLMKNDVninfqedwkiITLFIGGNDLCdvcdDPVRFSPQNFVDNIGQALDILHAEVPRA 487
Cdd:COG2755    50 ISGATTADLLARLDRDLLALKPDL----------VVIELGTNDLL----RGLGVSPEEFRANLEALIDRLRAAGPGA 112
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 680-955 1.85e-04

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: 43.86  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  680 VAALGDSLTAGNGIGskpndlsdvttqyRGLSYssggdsslenvttlPNILRKFngnLTGYAVgtgdanetnAFLNQAVP 759
Cdd:COG2755    11 IVALGDSITAGYGAS-------------RERGW--------------PALLARR---LAAADV---------RVVNAGIS 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  760 GAKAEELVSQVQTLIQKMKSDhrvnfhedwkVITVLIGGSDLcdycTDSNLYSADNFFDHLRNALDILHREVPRAlvnlv 839
Cdd:COG2755    52 GATTADLLARLDRDLLALKPD----------LVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAAGPGA----- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  840 dfmspsimrQVFLGNPdkcpvhqasilcncvlTPRESSQelaKLESITRAYQSSMRELVesgryetrEDFSVVLQPFFyn 919
Cdd:COG2755   113 ---------RVVLVTP----------------PPRLRPN---YLNERIEAYNAAIRELA--------AEYGVPLVDLY-- 154

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 742122978  920 irlPVLADGRPDVSFFAPDCLNPSQKFHSQLSRALW 955
Cdd:COG2755   155 ---AALRDAGDLPDLLTADGLHPNAAGYRLIAEAVL 187
 
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 ...
 321-616 2.75e-130

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: 403.65  E-value: 2.75e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  321 SVHRLKLADIKVIGALGDSLTAGNGAGskPGNVLDVLTQYRGLSWSVGGDKNLSSVITLPNMLREFNPSLKGFSVGKGSE 400
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAG--SANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  401 SSSGAYLNQAVPGAQAEDLPVQARRLVDLMKNDVNINFQEDWKIITLFIGGNDLCDVCDDPVRFSPQNFVDNIGQALDIL 480
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  481 HAEVPRAFVNLVKVLEIINLRKLYQDKnVSCPRLiLRNLCPCVLKYDDNATelASLIEVNKKYQEGTHQLVESGRYDtRE 560
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLTKKP-LQCETL-LAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEFD-RE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 742122978  561 DFTVVVQPFLEKVDMPMTPEGlPDNSYFAPDCFHFSSKAHAHAASALWNNMLQPVG 616
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 ...
 668-963 2.61e-128

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: 398.25  E-value: 2.61e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  668 SVHTLRPADIQVVAALGDSLTAGNGIGSKPNdlSDVTTQYRGLSYSSGGDSSLENVTTLPNILRKFNGNLTGYAVGTGDA 747
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANN--LDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTGDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  748 NETNAFLNQAVPGAKAEELVSQVQTLIQKMKSDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSADNFFDHLRNALDIL 827
Cdd:cd01824    79 TLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  828 HREVPRALVNLVDFMSPSIMRQVFlGNPDKCPVhQASILCNCVLTPRESSQelAKLESITRAYQSSMRELVESGRYeTRE 907
Cdd:cd01824   159 RDEVPRAFVNLVGLLNVASLRSLT-KKPLQCET-LLAPECPCLLGPTENSY--QDLKKFYKEYQNEVEEIVESGEF-DRE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 742122978  908 DFSVVLQPFFYNIRLPVLADGrPDVSFFAPDCLNPSQKFHSQLSRALWVNMLEPLG 963
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 ...
 1024-1310 7.57e-128

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: 397.10  E-value: 7.57e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1024 SVHELRPADIKVVAALGDSLTTAVGARPSNSSDLPTSWRGLSWSIGGDGDLGTHTTLPNILKKFNPNILGFSTGT---RE 1100
Cdd:cd01824     1 SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYGYSVGTgdeTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1101 ETAGLNVATEGARARDMPAQARDLVERMKTSPEINLQKDWKLITLFIGSNDLCHYCDNEEARSAEEYVKYIRQALDILYE 1180
Cdd:cd01824    81 PDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGSPQTFVKNLRKALDILRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978 1181 QLPRAFINVVEVMELADLHQGQDGK--CVMPLPAqsNCTCLQGSQENlpEMQELKTVNWNFQSALSTLSYQ-YLQREDFA 1257
Cdd:cd01824   161 EVPRAFVNLVGLLNVASLRSLTKKPlqCETLLAP--ECPCLLGPTEN--SYQDLKKFYKEYQNEVEEIVESgEFDREDFA 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 742122978 1258 VVVQPFFQNTLVPLNKRgGADLTFFSEDCFHFSERGHAEMAIALWNNMLEPLG 1310
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 ...
 19-254 3.57e-59

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: 205.65  E-value: 3.57e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   19 VHSLRPSDIKFVAAIGNVSIPPDSGTD----DLEEQEwtekQELQACMGV------VTVLSDVIRYFSPSVLKPICTLGT 88
Cdd:cd01824     2 VHRLRPGDIKVIAALGDSLTAGNGAGSannlDLLTEY----RGLSWSIGGdstlrgLTTLPNILREFNPSLYGYSVGTGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   89 EV---------VHHDAAEDLWVQAKDLVRNMKENQQLDFQNDWKLINVFFSNASQCRLCSSTQQQShVTSSMDQLTRTLD 159
Cdd:cd01824    78 ETlpdsgfnvaEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDANPGS-PQTFVKNLRKALD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  160 YLHQEVPKAFVNLVDLSE-----ALRGSHWHQKTLLSPtaqPCTCSGETSRLSSVVTQWT---YQETWERLLASSKYNeQ 231
Cdd:cd01824   157 ILRDEVPRAFVNLVGLLNvaslrSLTKKPLQCETLLAP---ECPCLLGPTENSYQDLKKFykeYQNEVEEIVESGEFD-R 232

                         250       260
                  ....*....|....*....|...
gi 742122978  232 ESFAVVFQPFFYERALPPTSMQP 254
Cdd:cd01824   233 EDFAVVVQPFFEDTSLPPLPDGP 255
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
1036-1301 3.90e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 104.96  E-value: 3.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1036 VAALGDSLTTAVGARPsnssdlptswrglswsiggdgdlGTHTTLPNILKKFNPNILGFSTGTReeTAGLNVATEGARAR 1115
Cdd:pfam00657    1 IVAFGDSLTDGGGDGP-----------------------GGRFSWGDLLADFLARKLGVPGSGY--NHGANFAIGGATIE 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1116 DMPAQARDLVERMKtspEINLQKDWKLITLFIGSNDLCHYCdneeaRSAEEYVKYIRQALDILYEQLPRAFINVVEVMel 1195
Cdd:pfam00657   56 DLPIQLEQLLRLIS---DVKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGARKFW-- 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1196 adlhqgqdgkcVMPLPaQSNCTCLQGSQENLPEMQELktvnwnFQSALSTL--SYQYlQREDFAVVVQPF--FQNTLVPL 1271
Cdd:pfam00657  126 -----------VHGLG-PLGCTPPKGCYELYNALAEE------YNERLNELvnSLAA-AAEDANVVYVDIygFEDPTDPC 186

                          250       260       270
                   ....*....|....*....|....*....|
gi 742122978  1272 NKRGGadltffSEDCFHFSERGHAEMAIAL 1301
Cdd:pfam00657  187 CGIGL------EPDGLHPSEKGYKAVAEAI 210
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
333-595 6.89e-22

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 95.33  E-value: 6.89e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   333 IGALGDSLTAGNGAGSKpGNVldvltqyrglSWsvggdknlssvitlPNMLREFNPSLKGFSVgkgseSSSGAYLNQAVP 412
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPG-GRF----------SW--------------GDLLADFLARKLGVPG-----SGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   413 GAQAEDLPVQARRLVDLMKNDVNinfQEDWKIITLFIGGNDLCDVCddpvrFSPQNFVDNIGQALDILHAEVPRAFVNLV 492
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLISDVKD---QAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQLGLGAR 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   493 KVleiinlrklyqdkNVSCPRLILRNLCPCVLKYddnatelasLIEVNKKYQEGTHQLVESGRYDtREDFTVVVQPFLEk 572
Cdd:pfam00657  123 KF-------------WVHGLGPLGCTPPKGCYEL---------YNALAEEYNERLNELVNSLAAA-AEDANVVYVDIYG- 178

                          250       260
                   ....*....|....*....|...
gi 742122978   573 vdmPMTPEGLPDNSYFAPDCFHF 595
Cdd:pfam00657  179 ---FEDPTDPCCGIGLEPDGLHP 198
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
680-954 8.79e-19

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 86.47  E-value: 8.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   680 VAALGDSLTAGNGIGSKPNdlsdvttqyrglsyssggdsslenvTTLPNILRKFNGNLTGYavgtgDANETNAFLNQAVP 759
Cdd:pfam00657    1 IVAFGDSLTDGGGDGPGGR-------------------------FSWGDLLADFLARKLGV-----PGSGYNHGANFAIG 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   760 GAKAEELVSQVQTLIQKMksdHRVNFHEDWKVITVLIGGSDLCDYCtdsnlYSADNFFDHLRNALDILHREVPRaLVNLV 839
Cdd:pfam00657   51 GATIEDLPIQLEQLLRLI---SDVKDQAKPDLVTIFIGANDLCNFL-----SSPARSKKRVPDLLDELRANLPQ-LGLGA 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978   840 DFMSPSIMRQvflgnpdkcpvhqasILCncvlTPResSQELAKLESITRAYQSSMRELVESGRYEtREDFSVVLQPF--F 917
Cdd:pfam00657  122 RKFWVHGLGP---------------LGC----TPP--KGCYELYNALAEEYNERLNELVNSLAAA-AEDANVVYVDIygF 179

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 742122978   918 YNIRLPVLADGRPdvsffaPDCLNPSQKFHSQLSRAL 954
Cdd:pfam00657  180 EDPTDPCCGIGLE------PDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 331-487 3.79e-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: 48.87  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  331 KVIGALGDSLTAGNGAGskpgnvldvltqyRGLSWsvggdknlssvitlPNMLREFnpsLKGFSVgkgsesssgAYLNQA 410
Cdd:COG2755     9 LRIVALGDSITAGYGAS-------------RERGW--------------PALLARR---LAAADV---------RVVNAG 49

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742122978  411 VPGAQAEDLPVQARRLVDLMKNDVninfqedwkiITLFIGGNDLCdvcdDPVRFSPQNFVDNIGQALDILHAEVPRA 487
Cdd:COG2755    50 ISGATTADLLARLDRDLLALKPDL----------VVIELGTNDLL----RGLGVSPEEFRANLEALIDRLRAAGPGA 112
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 333-492 1.81e-05

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


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 47.02  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  333 IGALGDSLTAGNGAGSKPGNVLDVLTQYRglswsvggdknlssviTLPNMLREFNpslkgfsvgkgsesssgaylNQAVP 412
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLLYLLL----------------LAGGPGVEVI--------------------NLGVS 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  413 GAQAEDLPVQARRLVDLMKndvninfqEDWKIITLFIGGNDLCDVCDDPvrfsPQNFVDNIGQALDILHAEVPRAFVNLV 492
Cdd:cd00229    45 GATTADALRRLGLRLALLK--------DKPDLVIIELGTNDLGRGGDTS----IDEFKANLEELLDALRERAPGAKVILI 112
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 680-955 1.85e-04

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: 43.86  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  680 VAALGDSLTAGNGIGskpndlsdvttqyRGLSYssggdsslenvttlPNILRKFngnLTGYAVgtgdanetnAFLNQAVP 759
Cdd:COG2755    11 IVALGDSITAGYGAS-------------RERGW--------------PALLARR---LAAADV---------RVVNAGIS 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  760 GAKAEELVSQVQTLIQKMKSDhrvnfhedwkVITVLIGGSDLcdycTDSNLYSADNFFDHLRNALDILHREVPRAlvnlv 839
Cdd:COG2755    52 GATTADLLARLDRDLLALKPD----------LVVIELGTNDL----LRGLGVSPEEFRANLEALIDRLRAAGPGA----- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  840 dfmspsimrQVFLGNPdkcpvhqasilcncvlTPRESSQelaKLESITRAYQSSMRELVesgryetrEDFSVVLQPFFyn 919
Cdd:COG2755   113 ---------RVVLVTP----------------PPRLRPN---YLNERIEAYNAAIRELA--------AEYGVPLVDLY-- 154

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 742122978  920 irlPVLADGRPDVSFFAPDCLNPSQKFHSQLSRALW 955
Cdd:COG2755   155 ---AALRDAGDLPDLLTADGLHPNAAGYRLIAEAVL 187
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 1038-1295 4.60e-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: 42.53  E-value: 4.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1038 ALGDSLTtaVGARPSNSSDLPTSWrglswsiggdgdlgthttLPNILKKFNP----NILGFStgtreetaglnvateGAR 1113
Cdd:pfam13472    1 ALGDSIT--AGYGATGGDRSYPGW------------------LARLLARRLGadvvNNLGIS---------------GAT 45

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1114 -ARDMPAQARDLvermktspeinLQKDWKLITLFIGSNDLCHycdneeARSAEEYVKYIRQALDILYEQLPRAFINVVev 1192
Cdd:pfam13472   46 tRLDLLERLDDV-----------LRLKPDLVVILLGTNDLGR------GVSAARAAANLEALIDALRAAGPDARVLLI-- 106

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  1193 meladlhqgqdgkcvmplpaqsncTCLQGSQENLPEMQELKTVNWNFQSALSTLSyqylQREDFAVVvqpffqNTLVPLN 1272
Cdd:pfam13472  107 ------------------------GPLPVGPPPPLDERRLNARIAEYNAAIREVA----AERGVPYV------DLWDALR 152

                          250       260
                   ....*....|....*....|...
gi 742122978  1273 KRGGADLTFFSEDCFHFSERGHA 1295
Cdd:pfam13472  153 DDGGWLPDLLADDGLHPNAAGYR 175
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 716-844 1.25e-03

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: 41.63  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742122978  716 GDSSLENVTTLPNILRKFNGNLTGYAVGTGDANETNAflnqAVPGAKAEELVSQVQtliqkmksDHRVNFHEDWKVITVL 795
Cdd:cd00229     5 GDSITAGYGASSGSTFYSLLLYLLLLAGGPGVEVINL----GVSGATTADALRRLG--------LRLALLKDKPDLVIIE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 742122978  796 IGGSDLcdycTDSNLYSADNFFDHLRNALDILHREVPRALVNLVDFMSP 844
Cdd:cd00229    73 LGTNDL----GRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPP 117
 
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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