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Conserved domains on  [gi|1262154580|gb|PFN85272|]
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lipase [Bacillus thuringiensis]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110766)

SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity

CATH:  3.40.50.1110
EC:  3.1.-.-
Gene Ontology:  GO:0016788
PubMed:  35871440|15522763
SCOP:  3001315

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 18-203 5.37e-72

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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


:

Pssm-ID: 238870  Cd Length: 185  Bit Score: 216.37  E-value: 5.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  18 RFVAIGDSFTEGIGDEVEGIALKSWVDHFVQLCE---NDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDV 94
Cdd:cd01832     1 RYVALGDSITEGVGDPVPDGGYRGWADRLAAALAaadPGIEYANLAVRGRRTAQILAEQLPAALALRPDLVTLLAGGNDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  95 LKGRWNHDAYKNDMEFMVDTLSKAGADIIIANFPDFTVRLPFAfekkQVIKEQLLEANEVIRSLSREYKLHHVDFWNHHL 174
Cdd:cd01832    81 LRPGTDPDTYRADLEEAVRRLRAAGARVVVFTIPDPAVLEPFR----RRVRARLAAYNAVIRAVAARYGAVHVDLWEHPE 156

                         170       180
                  ....*....|....*....|....*....
gi 1262154580 175 VNDNTLWSKDLIHPNSKGYVKVAELIFSS 203
Cdd:cd01832   157 FADPRLWASDRLHPSAAGHARLAALVLAA 185
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 18-203 5.37e-72

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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


Pssm-ID: 238870  Cd Length: 185  Bit Score: 216.37  E-value: 5.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  18 RFVAIGDSFTEGIGDEVEGIALKSWVDHFVQLCE---NDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDV 94
Cdd:cd01832     1 RYVALGDSITEGVGDPVPDGGYRGWADRLAAALAaadPGIEYANLAVRGRRTAQILAEQLPAALALRPDLVTLLAGGNDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  95 LKGRWNHDAYKNDMEFMVDTLSKAGADIIIANFPDFTVRLPFAfekkQVIKEQLLEANEVIRSLSREYKLHHVDFWNHHL 174
Cdd:cd01832    81 LRPGTDPDTYRADLEEAVRRLRAAGARVVVFTIPDPAVLEPFR----RRVRARLAAYNAVIRAVAARYGAVHVDLWEHPE 156

                         170       180
                  ....*....|....*....|....*....
gi 1262154580 175 VNDNTLWSKDLIHPNSKGYVKVAELIFSS 203
Cdd:cd01832   157 FADPRLWASDRLHPSAAGHARLAALVLAA 185
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 17-204 4.98e-38

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: 130.15  E-value: 4.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  17 KRFVAIGDSFTEGIGDEVEGialkSWVDHFVQ-LCENDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDVL 95
Cdd:COG2755     9 LRIVALGDSITAGYGASRER----GWPALLARrLAAADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  96 KG-RWNHDAYKNDMEFMVDTLSKAG--ADIIIANfpdftvrlPFAFEKKQVIKEQLLEANEVIRSLSREYKLHHVDFWNH 172
Cdd:COG2755    85 RGlGVSPEEFRANLEALIDRLRAAGpgARVVLVT--------PPPRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYAA 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1262154580 173 --HLVNDNTLWSKDLIHPNSKGYVKVAELIFSSL 204
Cdd:COG2755   157 lrDAGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 21-193 1.51e-29

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: 108.02  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  21 AIGDSFTEGIGDEVEGIALKSWVDHFVQLCENDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDVLKGRWN 100
Cdd:pfam13472   1 ALGDSITAGYGATGGDRSYPGWLARLLARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580 101 hDAYKNDMEFMVDTLSKAGADIIIANFPDFTVrLPFAFEKKQVIKEQLLEANEVIRSLSREYKLHHVDFWNHHLVNDNTL 180
Cdd:pfam13472  81 -ARAAANLEALIDALRAAGPDARVLLIGPLPV-GPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 1262154580 181 ---WSKDLIHPNSKGY 193
Cdd:pfam13472 159 pdlLADDGLHPNAAGY 174
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 18-203 5.37e-72

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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


Pssm-ID: 238870  Cd Length: 185  Bit Score: 216.37  E-value: 5.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  18 RFVAIGDSFTEGIGDEVEGIALKSWVDHFVQLCE---NDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDV 94
Cdd:cd01832     1 RYVALGDSITEGVGDPVPDGGYRGWADRLAAALAaadPGIEYANLAVRGRRTAQILAEQLPAALALRPDLVTLLAGGNDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  95 LKGRWNHDAYKNDMEFMVDTLSKAGADIIIANFPDFTVRLPFAfekkQVIKEQLLEANEVIRSLSREYKLHHVDFWNHHL 174
Cdd:cd01832    81 LRPGTDPDTYRADLEEAVRRLRAAGARVVVFTIPDPAVLEPFR----RRVRARLAAYNAVIRAVAARYGAVHVDLWEHPE 156

                         170       180
                  ....*....|....*....|....*....
gi 1262154580 175 VNDNTLWSKDLIHPNSKGYVKVAELIFSS 203
Cdd:cd01832   157 FADPRLWASDRLHPSAAGHARLAALVLAA 185
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 17-204 4.98e-38

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: 130.15  E-value: 4.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  17 KRFVAIGDSFTEGIGDEVEGialkSWVDHFVQ-LCENDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDVL 95
Cdd:COG2755     9 LRIVALGDSITAGYGASRER----GWPALLARrLAAADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  96 KG-RWNHDAYKNDMEFMVDTLSKAG--ADIIIANfpdftvrlPFAFEKKQVIKEQLLEANEVIRSLSREYKLHHVDFWNH 172
Cdd:COG2755    85 RGlGVSPEEFRANLEALIDRLRAAGpgARVVLVT--------PPPRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYAA 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1262154580 173 --HLVNDNTLWSKDLIHPNSKGYVKVAELIFSSL 204
Cdd:COG2755   157 lrDAGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 21-193 1.51e-29

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: 108.02  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  21 AIGDSFTEGIGDEVEGIALKSWVDHFVQLCENDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDVLKGRWN 100
Cdd:pfam13472   1 ALGDSITAGYGATGGDRSYPGWLARLLARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580 101 hDAYKNDMEFMVDTLSKAGADIIIANFPDFTVrLPFAFEKKQVIKEQLLEANEVIRSLSREYKLHHVDFWNHHLVNDNTL 180
Cdd:pfam13472  81 -ARAAANLEALIDALRAAGPDARVLLIGPLPV-GPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 1262154580 181 ---WSKDLIHPNSKGY 193
Cdd:pfam13472 159 pdlLADDGLHPNAAGY 174
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 20-202 5.51e-22

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: 88.62  E-value: 5.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  20 VAIGDSFTEGIGDEVEGIALKSWVDHFVQLCENDIEYANFAKRGLVTEEI--RSQQLEKALTFNPDLVSLIAGANDVLKG 97
Cdd:cd00229     2 LVIGDSITAGYGASSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADAlrRLGLRLALLKDKPDLVIIELGTNDLGRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  98 RWNH-DAYKNDMEFMVDTL--SKAGADIIIANFPDFTVRLPFAFEKKQVIKEQLLEANEVIRSLSreyKLHHVDFWNHHL 174
Cdd:cd00229    82 GDTSiDEFKANLEELLDALreRAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENPAPS---GVDLVDLAALLG 158

                         170       180
                  ....*....|....*....|....*...
gi 1262154580 175 VNDNTLWSKDLIHPNSKGYVKVAELIFS 202
Cdd:cd00229   159 DEDKSLYSPDGIHPNPAGHKLIAEALAS 186
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
20-200 2.32e-18

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 79.54  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  20 VAIGDSFTEGIGDEveGIALKSW----VDHFVQLC----ENDIEYANFAKRGLVTEEIrSQQLEKALTF--------NPD 83
Cdd:pfam00657   2 VAFGDSLTDGGGDG--PGGRFSWgdllADFLARKLgvpgSGYNHGANFAIGGATIEDL-PIQLEQLLRLisdvkdqaKPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  84 LVSLIAGANDVLKGRWNHDAYKNDMEFMVDTLSKAGADI-------------IIANFPDFTVRLPFAFEKKQvIKEQLLE 150
Cdd:pfam00657  79 LVTIFIGANDLCNFLSSPARSKKRVPDLLDELRANLPQLglgarkfwvhglgPLGCTPPKGCYELYNALAEE-YNERLNE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1262154580 151 ANEVIRSLSREYKLHHVDFWNHHLVNDNTLW---SKDLIHPNSKGYVKVAELI 200
Cdd:pfam00657 158 LVNSLAAAAEDANVVYVDIYGFEDPTDPCCGiglEPDGLHPSEKGYKAVAEAI 210
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 18-204 1.50e-17

sialate O-acetylesterase_like family of the SGNH hydrolases, 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 found in other serine hydrolases.


Pssm-ID: 238865  Cd Length: 188  Bit Score: 76.71  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  18 RFVAIGDSFTEGIGDEVEGialkSWVDHFVQLCENDIEYANFAK--RGLVTE----EIRSQQLEKALTFNPDLVSLIAGA 91
Cdd:cd01827     2 KVACVGNSITEGAGLRAYD----SYPSPLAQMLGDGYEVGNFGKsaRTVLNKgdhpYMNEERYKNALAFNPNIVIIKLGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  92 NDVLKGRWNH-DAYKNDMEFMVDTLSKAGA--DIIIANFPDFTVRLPFAFEkKQVIKEqllEANEVIRSLSREYKLHHVD 168
Cdd:cd01827    78 NDAKPQNWKYkDDFKKDYETMIDSFQALPSkpKIYICYPIPAYYGDGGFIN-DNIIKK---EIQPMIDKIAKKLNLKLID 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1262154580 169 FWN---HH--LVNDNtlwskdlIHPNSKGYVKVAELIFSSL 204
Cdd:cd01827   154 LHTplkGKpeLVPDW-------VHPNEKGAYILAKVVYKAI 187
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 17-204 1.11e-12

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.


Pssm-ID: 239945  Cd Length: 183  Bit Score: 63.50  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  17 KRFVAIGDSFTEGIGDEVEgialKSWVDHFVQlcENDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDVLK 96
Cdd:cd04501     1 MRVVCLGDSITYGYPVGPE----ASWVNLLAE--FLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  97 GRWNhDAYKNDMEFMVDTLSKAGADIIIANFPdfTVRLPFAFEKKQVIKEQLLEANEVIRSLSREYKLHHVDFwNHHLVN 176
Cdd:cd04501    75 NTSL-EMIKDNIRSMVELAEANGIKVILASPL--PVDDYPWKPQWLRPANKLKSLNRWLKDYARENGLLFLDF-YSPLLD 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1262154580 177 DNTLWSKDL-----IHPNSKGYVKVAELIFSSL 204
Cdd:cd04501   151 ERNVGLKPGlltdgLHPSREGYRVMAPLAEKAL 183
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 17-200 3.20e-11

SGNH_hydrolase subfamily. SGNH hydrolases are 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 found in other serine hydrolases.


Pssm-ID: 238872  Cd Length: 191  Bit Score: 60.00  E-value: 3.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  17 KRFVAIGDSFTEGIGdevegiaLKSWVDHFVQLC--ENDIEYANFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDV 94
Cdd:cd01834     2 DRIVFIGNSITDRGG-------YVGYVETYLAARypELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  95 LKGRWNH---DAYKNDMEFMVDTLSKAGADIIIA-----NFPDFTVRLPFAFEKKQVIKEQlleaNEVIRSLSREYKLHH 166
Cdd:cd01834    75 FRGFDDPvglEKFKTNLRRLIDRLKNKESAPRIVlvspiAYEANEDPLPDGAEYNANLAAY----ADAVRELAAENGVAF 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1262154580 167 VDFwnHHLVND------NTLWSKDLIHPNSKGYVKVAELI 200
Cdd:cd01834   151 VDL--FTPMKEafqkagEAVLTVDGVHPNEAGHRALARLW 188
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 20-200 7.21e-11

sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, 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 found in other serine hydrolases.


Pssm-ID: 238866  Cd Length: 169  Bit Score: 58.44  E-value: 7.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  20 VAIGDSFTEGIGDEvegialkswvdhfvqLCENDIEYANFAKRGLVTEEIRsQQLEKALTFNPDLVSLIAGANDVLKGRW 99
Cdd:cd01828     3 VFLGDSLTEGGPWA---------------LLFPDVKVANRGISGDTTRGLL-ARLDEDVALQPKAIFIMIGINDLAQGTS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580 100 NHDAYKNdMEFMVDTLSK--AGADIIIANfpdftvrLPFAFEKKQVIKEQLLEANEVIRSLSREYKLHHVDFWNHHLVND 177
Cdd:cd01828    67 DEDIVAN-YRTILEKLRKhfPNIKIVVQS-------ILPVGELKSIPNEQIEELNRQLAQLAQQEGVTFLDLWAVFTNAD 138

                         170       180
                  ....*....|....*....|....*.
gi 1262154580 178 NTL---WSKDLIHPNSKGYVKVAELI 200
Cdd:cd01828   139 GDLkneFTTDGLHLNAKGYAVWAAAL 164
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 20-204 7.33e-10

Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.


Pssm-ID: 238860 [Multi-domain]  Cd Length: 177  Bit Score: 55.98  E-value: 7.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  20 VAIGDSFTEGIGDEVEgialKSWVDhfvQLCEN------DIEYANFAKRGLVTEEIRSqQLEKALT-FNPDLVSLIAGAN 92
Cdd:cd01822     4 LALGDSLTAGYGLPPE----EGWPA---LLQKRldargiDVTVINAGVSGDTTAGGLA-RLPALLAqHKPDLVILELGGN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  93 DVLKGRwNHDAYKNDMEFMVDTLSKAGADIIIANfpdftVRLPFAFEkkqviKEQLLEANEVIRSLSREYKLHHVDFWNH 172
Cdd:cd01822    76 DGLRGI-PPDQTRANLRQMIETAQARGAPVLLVG-----MQAPPNYG-----PRYTRRFAAIYPELAEEYGVPLVPFFLE 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1262154580 173 HLVNDNTLWSKDLIHPNSKGYVKVAELIFSSL 204
Cdd:cd01822   145 GVAGDPELMQSDGIHPNAEGQPIIAENVWPAL 176
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 18-204 3.10e-09

SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, 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 found in other serine hydrolases.


Pssm-ID: 238863  Cd Length: 189  Bit Score: 54.20  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  18 RFVAIGDSFTEG--IGDEVEGiALKSWVDhfvQLCENDIEYANFAKRGLVTEEIRSQQLekaltfNPDLVSLIAGANDVL 95
Cdd:cd01825     1 RIAQLGDSHIAGdfFTDVLRG-LLGVIYD---NLGVNGASASLLLKWDAEFLQAQLAAL------PPDLVILSYGTNEAF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  96 KGRWNHDAYKNDMEFMVDTLSKA--GADIIIANFPDftvrlpFAFEKKQVIKEQLLEANEVIRSLSREYKLHHVDFWNHH 173
Cdd:cd01825    71 NKQLNASEYRQQLREFIKRLRQIlpNASILLVGPPD------SLQKTGAGRWRTPPGLDAVIAAQRRVAKEEGIAFWDLY 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1262154580 174 LV--NDNTLW--------SKDLIHPNSKGYVKVAELIFSSL 204
Cdd:cd01825   145 AAmgGEGGIWqwaepglaRKDYVHLTPRGYERLANLLYEAL 185
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 17-203 1.34e-07

SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme 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, but may lack the carboxylic acid.


Pssm-ID: 238861  Cd Length: 259  Bit Score: 50.53  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  17 KRFVAIGDSFT--EGIGDEVEGIA------LKSWVDHFVQ-LCENDIEYANFAKRGLVTEEIRSQQLE------KALTFN 81
Cdd:cd01823     1 VRYVALGDSYAagPGAGPLDDGPDdgcrrsSNSYPTLLARaLGDETLSFTDVACSGATTTDGIEPQQGgiapqaGALDPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  82 PDLVSLIAGANDV-----------LKGRWNHDAYKNDMEFMVD-TLSKAGADI------IIANFPDFTV----------- 132
Cdd:cd01823    81 TDLVTITIGGNDLgfadvvkacilTGGGSSLAQEKGAADGARDaALDEVGARLkavldrIRERAPNARVvvvgyprlfpp 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580 133 -----------RLPFAFEKKQVIKEQLLEANEVIRS---LSREYKLHHVD----FWNHHLVNDNTLWSKDL--------- 185
Cdd:cd01823   161 dggdcdkscspGTPLTPADRPELNQLVDKLNALIRRaaaDAGDYKVRFVDtdapFAGHRACSPDPWSRSVLdllptrqgk 240

                         250
                  ....*....|....*....
gi 1262154580 186 -IHPNSKGYVKVAELIFSS 203
Cdd:cd01823   241 pFHPNAAGHRAIADLIVDA 259
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 20-201 8.18e-07

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: 47.63  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  20 VAIGDSFTEGIGDEVEgialKSWVDHFV-QLCEND----IEYANFAKRGLVTEEI----RSQQLEKALTfNPDLVSLIAG 90
Cdd:cd04506     3 VALGDSLTEGVGDETG----KGGYVGRLdKLIETKtvkkVTVQNFGVSGDRSDQLlkrlKTKKVQKELK-KADVITITIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  91 ANDVLKGrwnhdAYKNDMEFMVDTLSKAGA-------DIIIA---NFPDFTVRL-----PF--AFEKKQVIKEQLLEANE 153
Cdd:cd04506    78 GNDLMQV-----LEKNFLSLDVEDFKKAEEtyqnnlkKIFKEirkLNPDAPIFLvglynPFyvYFPNITEINDIVNDWNE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1262154580 154 VIRSLSREYKlhHVDFWN-HHLVNDNT---LWSKDLIHPNSKGYVKVAELIF 201
Cdd:cd04506   153 ASQKLASQYK--NAYFVPiFDLFSDGQnkyLLTSDHFHPNDKGYQLIADRVF 202
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 18-204 1.11e-06

SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are 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 found in other serine hydrolases.


Pssm-ID: 238871  Cd Length: 157  Bit Score: 46.46  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  18 RFVAIGDSFTEGIGDevegialkswvdhfvqlcendieyaNFAKRGLVTEEIRSQQLEKALTFNPDLVSLIAGANDVLKG 97
Cdd:cd01833     2 RIMPLGDSITWGDKD-------------------------HEGHSGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLN 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  98 RwNHDAYKNDMEFMVDTLSKAGAD--IIIANFPDFTvrlpFAFEKKQVikeqlLEANEVIRSLSREY-----KLHHVDFW 170
Cdd:cd01833    57 R-DPDTAPDRLRALIDQMRAANPDvkIIVATLIPTT----DASGNARI-----AEYNAAIPGVVADLrtagsPVVLVDMS 126

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1262154580 171 NhhlVNDNTLWSKDLIHPNSKGYVKVAELIFSSL 204
Cdd:cd01833   127 T---GYTTADDLYDGLHPNDQGYKKMADAWYEAL 157
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 18-200 2.61e-06

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases 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 Ser-His-Asp(Glu) triad found in other serine hydrolases


Pssm-ID: 238876  Cd Length: 199  Bit Score: 46.09  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  18 RFVAIGDSFTEGIGDEVE---GIALKswvDHFVQLCenDIEYANFAkrGLVTE---EIRSQQLEKALTFNPDLVSLIAGA 91
Cdd:cd01838     1 KIVLFGDSITQFSFDQGEfgfGAALA---DVYSRKL--DVINRGFS--GYNTRwalKVLPKIFLEEKLAQPDLVTIFFGA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  92 ND-VLKGRWNH---DAYKNDMEFMVDTLSKAGAD---IIIA----NFPDFTVRLPFAFEKKQVIKEQLLEANEVIRSLSR 160
Cdd:cd01838    74 NDaALPGQPQHvplDEYKENLRKIVSHLKSLSPKtkvILITpppvDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAE 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1262154580 161 EYKLHHVDFWNHHLVNDNTLWS--KDLIHPNSKGYVKVAELI 200
Cdd:cd01838   154 ELGVPVIDLWTAMQEEAGWLESllTDGLHFSSKGYELLFEEI 195
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 22-204 2.97e-05

NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, 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 two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.


Pssm-ID: 238879  Cd Length: 174  Bit Score: 42.70  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  22 IGDSFTEGIGdevegialkswvdhFVQLCENDIEYANFAKRGLVT----EEIRSQQLEKaltfNPDLVSLIAGANDVLKG 97
Cdd:cd01841     6 IGDSLFEGWP--------------LYEAEGKGKTVNNLGIAGISSrqylEHIEPQLIQK----NPSKVFLFLGTNDIGKE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  98 rwnhdaykNDMEFMVDTLSkagaDII---IANFPDFTVRLP------FAFEKKQVIKEQLLEANEVIRSLSREYKLHHVD 168
Cdd:cd01841    68 --------VSSNQFIKWYR----DIIeqiREEFPNTKIYLLsvlpvlEEDEIKTRSNTRIQRLNDAIKELAPELGVTFID 135

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1262154580 169 FW---NHHLVNDNTLWSKDLIHPNSKGYVKVAELIFSSL 204
Cdd:cd01841   136 LNdvlVDEFGNLKKEYTTDGLHFNPKGYQKLLEILEEYL 174
fatty_acyltransferase_like cd01846
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ...
 42-196 6.11e-05

Fatty acyltransferase-like subfamily of the SGNH hydrolases, 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 found in other serine hydrolases. Might catalyze fatty acid transfer between phosphatidylcholine and sterols.


Pssm-ID: 238882 [Multi-domain]  Cd Length: 270  Bit Score: 42.75  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  42 WVDHFVQL--CENDIEYANFAKRGLVT----------------EEIRSQQLEKALTFNPD-LVSLIAGANDVLKGRWNHD 102
Cdd:cd01846    41 WVEYLAATlgLSGLKQGYNYAVGGATAgaynvppypptlpglsDQVAAFLAAHKLRLPPDtLVAIWIGANDLLNALDLPQ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580 103 AYKNDMEFMVD-------TLSKAGA-DIIIANFPDFTvRLPFAFEKKQVIKEQL----LEANEVIRSLSREYK--LHHVD 168
Cdd:cd01846   121 NPDTLVTRAVDnlfqalqRLYAAGArNFLVLNLPDLG-LTPAFQAQGDAVAARAtaltAAYNAKLAEKLAELKaqHPGVN 199

                         170       180
                  ....*....|....*....|....*...
gi 1262154580 169 FwnhHLVNDNTLWSKDLIHPNSKGYVKV 196
Cdd:cd01846   200 I---LLFDTNALFNDILDNPAAYGFTNV 224
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 80-200 3.65e-04

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


Pssm-ID: 239946  Cd Length: 171  Bit Score: 39.58  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  80 FNPDLVSLIAGANDVLKGRWNHDAYKNDMEFMvdtlskagaDIIIANFPD---FTVRLPFAFEKKQVIkEQLLEANEVIR 156
Cdd:cd04502    49 YQPRRVVLYAGDNDLASGRTPEEVLRDFRELV---------NRIRAKLPDtpiAIISIKPSPARWALR-PKIRRFNALLK 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1262154580 157 SLSR-EYKLHHVDFWNHHLVNDN----TLWSKDLIHPNSKGYVKVAELI 200
Cdd:cd04502   119 ELAEtRPNLTYIDVASPMLDADGkpraELFQEDGLHLNDAGYALWRKVI 167
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 22-204 2.20e-03

SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are 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 found in other serine hydrolases.


Pssm-ID: 238874  Cd Length: 191  Bit Score: 37.63  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  22 IGDSFTEGIGDEVEGIALKSWV-DHFVQLCENDIEYANFAKRGLVTEEIRsQQLEKALTFNPDLVSLIAGANDVLKG--- 97
Cdd:cd01836     8 LGDSTAAGVGVETQDQALAGQLaRGLAAITGRGVRWRLFAKTGATSADLL-RQLAPLPETRFDVAVISIGVNDVTHLtsi 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262154580  98 -RWnhdayKNDMEFMVDTLSK--AGADIIIANFPDFTV--RLPFAFEKKQVIKEQLLeaNEVIRSLSREYklHHVDFWNH 172
Cdd:cd01836    87 aRW-----RKQLAELVDALRAkfPGARVVVTAVPPLGRfpALPQPLRWLLGRRARLL--NRALERLASEA--PRVTLLPA 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1262154580 173 HLVNDNTLWSKDLIHPNSKGYVKVAELIFSSL 204
Cdd:cd01836   158 TGPLFPALFASDGFHPSAAGYAVWAEALAPAI 189
COG3240 COG3240
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function ...
 79-137 3.08e-03

Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 442472 [Multi-domain]  Cd Length: 305  Bit Score: 37.71  E-value: 3.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1262154580  79 TFNP-DLVSLIAGANDVLKGRWNHDAYK-----------NDMEFMVDTLSKAGA-DIIIANFPDFTvRLPFA 137
Cdd:COG3240   127 TADPnALYIVWAGANDLLAALAAVGATPaqaqaaataaaANLAAAVGALAAAGArHILVPNLPDLG-LTPAA 197
 
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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