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Conserved domains on  [gi|917632135|ref|WP_052201191|]
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MULTISPECIES: GDSL-type esterase/lipase family protein [Pseudoalteromonas]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 85)

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; similar to plant GDSL esterase/lipase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase super family cl01053
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 64-234 3.06e-47

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 cd01828:

Pssm-ID: 470049  Cd Length: 169  Bit Score: 153.97  E-value: 3.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  64 DIVFVGDSITeQGLNWAIRFNDLRVRNRGISGDMTYGVLARLNELKAAPPKAIFLKIGVNDifnfhyIKQVKNLSSISEN 143
Cdd:cd01828    1 ALVFLGDSLT-EGGPWALLFPDVKVANRGISGDTTRGLLARLDEDVALQPKAIFIMIGIND------LAQGTSDEDIVAN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 144 IEKIVTQLNEALPNTQIYVQSILPdhrdfITQMAQTVNKQIKAI--------KHARFTYIDLHPAFLGAQGTLNEALTTD 215
Cdd:cd01828   74 YRTILEKLRKHFPNIKIVVQSILP-----VGELKSIPNEQIEELnrqlaqlaQQEGVTFLDLWAVFTNADGDLKNEFTTD 148

                        170
                 ....*....|....*....
gi 917632135 216 GTHLNEAGYALWAKQLAPI 234
Cdd:cd01828  149 GLHLNAKGYAVWAAALQPY 167
 
Name Accession Description Interval E-value
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 64-234 3.06e-47

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: 153.97  E-value: 3.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  64 DIVFVGDSITeQGLNWAIRFNDLRVRNRGISGDMTYGVLARLNELKAAPPKAIFLKIGVNDifnfhyIKQVKNLSSISEN 143
Cdd:cd01828    1 ALVFLGDSLT-EGGPWALLFPDVKVANRGISGDTTRGLLARLDEDVALQPKAIFIMIGIND------LAQGTSDEDIVAN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 144 IEKIVTQLNEALPNTQIYVQSILPdhrdfITQMAQTVNKQIKAI--------KHARFTYIDLHPAFLGAQGTLNEALTTD 215
Cdd:cd01828   74 YRTILEKLRKHFPNIKIVVQSILP-----VGELKSIPNEQIEELnrqlaqlaQQEGVTFLDLWAVFTNADGDLKNEFTTD 148

                        170
                 ....*....|....*....
gi 917632135 216 GTHLNEAGYALWAKQLAPI 234
Cdd:cd01828  149 GLHLNAKGYAVWAAALQPY 167
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 56-236 1.62e-41

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: 140.16  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  56 KLQPLRKGDIVFVGDSITE-----QGLNWAIRF------NDLRVRNRGISGDMTYGVLARL-NELKAAPPKAIFLKIGVN 123
Cdd:COG2755    2 KAAAGKPLRIVALGDSITAgygasRERGWPALLarrlaaADVRVVNAGISGATTADLLARLdRDLLALKPDLVVIELGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 124 DIFNFHYIkqvkNLSSISENIEKIVTQLNEALPNTQIYVQSILPDHR-DFITQMAQTVNKQIKAI-KHARFTYIDLHPAF 201
Cdd:COG2755   82 DLLRGLGV----SPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRpNYLNERIEAYNAAIRELaAEYGVPLVDLYAAL 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 917632135 202 LGAqGTLNEALTTDGTHLNEAGYALWAKQLAPIMK 236
Cdd:COG2755  158 RDA-GDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 67-226 1.35e-26

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: 101.08  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135   67 FVGDSITEqGLNW---------------AIRFNDLRVRNRGISGDMT-YGVLARLNELKAAPPKAIFLKIGVNDIFnfhy 130
Cdd:pfam13472   1 ALGDSITA-GYGAtggdrsypgwlarllARRLGADVVNNLGISGATTrLDLLERLDDVLRLKPDLVVILLGTNDLG---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  131 ikQVKNLSSISENIEKIVTQLNEALPNTQIYVQSILP------DHRDFITQMAQTVNKQIKAI-KHARFTYIDLHPAFLG 203
Cdd:pfam13472  76 --RGVSAARAAANLEALIDALRAAGPDARVLLIGPLPvgppppLDERRLNARIAEYNAAIREVaAERGVPYVDLWDALRD 153

                         170       180
                  ....*....|....*....|...
gi 917632135  204 AQGTLNEALTTDGTHLNEAGYAL 226
Cdd:pfam13472 154 DGGWLPDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 64-234 3.06e-47

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: 153.97  E-value: 3.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  64 DIVFVGDSITeQGLNWAIRFNDLRVRNRGISGDMTYGVLARLNELKAAPPKAIFLKIGVNDifnfhyIKQVKNLSSISEN 143
Cdd:cd01828    1 ALVFLGDSLT-EGGPWALLFPDVKVANRGISGDTTRGLLARLDEDVALQPKAIFIMIGIND------LAQGTSDEDIVAN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 144 IEKIVTQLNEALPNTQIYVQSILPdhrdfITQMAQTVNKQIKAI--------KHARFTYIDLHPAFLGAQGTLNEALTTD 215
Cdd:cd01828   74 YRTILEKLRKHFPNIKIVVQSILP-----VGELKSIPNEQIEELnrqlaqlaQQEGVTFLDLWAVFTNADGDLKNEFTTD 148

                        170
                 ....*....|....*....
gi 917632135 216 GTHLNEAGYALWAKQLAPI 234
Cdd:cd01828  149 GLHLNAKGYAVWAAALQPY 167
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 56-236 1.62e-41

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: 140.16  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  56 KLQPLRKGDIVFVGDSITE-----QGLNWAIRF------NDLRVRNRGISGDMTYGVLARL-NELKAAPPKAIFLKIGVN 123
Cdd:COG2755    2 KAAAGKPLRIVALGDSITAgygasRERGWPALLarrlaaADVRVVNAGISGATTADLLARLdRDLLALKPDLVVIELGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 124 DIFNFHYIkqvkNLSSISENIEKIVTQLNEALPNTQIYVQSILPDHR-DFITQMAQTVNKQIKAI-KHARFTYIDLHPAF 201
Cdd:COG2755   82 DLLRGLGV----SPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRpNYLNERIEAYNAAIRELaAEYGVPLVDLYAAL 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 917632135 202 LGAqGTLNEALTTDGTHLNEAGYALWAKQLAPIMK 236
Cdd:COG2755  158 RDA-GDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 63-231 2.56e-30

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: 110.88  E-value: 2.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  63 GDIVFVGDSITEQGLNWAIRFNDLRVRNRGISGDMTYGVLarlNELKAA----PPKAIFLKIGVNDIFNFHYIKQvknls 138
Cdd:cd01841    1 KNIVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYL---EHIEPQliqkNPSKVFLFLGTNDIGKEVSSNQ----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 139 sISENIEKIVTQLNEALPNTQIYVQSILP-DHRDFITQMAQTV----NKQIKAI-KHARFTYIDLHPAFLGAQGTLNEAL 212
Cdd:cd01841   73 -FIKWYRDIIEQIREEFPNTKIYLLSVLPvLEEDEIKTRSNTRiqrlNDAIKELaPELGVTFIDLNDVLVDEFGNLKKEY 151

                        170
                 ....*....|....*....
gi 917632135 213 TTDGTHLNEAGYALWAKQL 231
Cdd:cd01841  152 TTDGLHFNPKGYQKLLEIL 170
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 67-226 1.35e-26

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: 101.08  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135   67 FVGDSITEqGLNW---------------AIRFNDLRVRNRGISGDMT-YGVLARLNELKAAPPKAIFLKIGVNDIFnfhy 130
Cdd:pfam13472   1 ALGDSITA-GYGAtggdrsypgwlarllARRLGADVVNNLGISGATTrLDLLERLDDVLRLKPDLVVILLGTNDLG---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  131 ikQVKNLSSISENIEKIVTQLNEALPNTQIYVQSILP------DHRDFITQMAQTVNKQIKAI-KHARFTYIDLHPAFLG 203
Cdd:pfam13472  76 --RGVSAARAAANLEALIDALRAAGPDARVLLIGPLPvgppppLDERRLNARIAEYNAAIREVaAERGVPYVDLWDALRD 153

                         170       180
                  ....*....|....*....|...
gi 917632135  204 AQGTLNEALTTDGTHLNEAGYAL 226
Cdd:pfam13472 154 DGGWLPDLLADDGLHPNAAGYRL 176
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 43-238 1.86e-26

PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction.


Pssm-ID: 238858  Cd Length: 214  Bit Score: 101.60  E-value: 1.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  43 WLKNHygertAHFKLQPLRKG-DIVFVGDSITEQ----GL-NWAIRFNDLRVRNRGISGDMTYGVLARLN--ELKAAPPK 114
Cdd:cd01820   17 WMSRH-----ERFVAEAKQKEpDVVFIGDSITQNweftGLeVWRELYAPLHALNFGIGGDRTQNVLWRLEngELDGVNPK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 115 AIFLKIGVNDIFNFHYIKQvknlssISENIEKIVTQLNEALPNTQIYVQSILP--DHRDFITQMAQTVNK--QIKAIKHA 190
Cdd:cd01820   92 VVVLLIGTNNIGHTTTAEE------IAEGILAIVEEIREKLPNAKILLLGLLPrgQNPNPLRERNAQVNRllAVRYDGLP 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 917632135 191 RFTYIDLHPAFLGAQGTLNEALTTDGTHLNEAGYALWAKQLAPIMKTL 238
Cdd:cd01820  166 NVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTLARL 213
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 65-232 7.25e-26

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: 99.67  E-value: 7.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  65 IVFVGDSITEQG-------LNWAIRF--NDLRVRNRGISGDMTYGVLARLN-ELKAAPPKAIFLKIGVNDIFNFHYIKQv 134
Cdd:cd01834    4 IVFIGNSITDRGgyvgyveTYLAARYpeLKLTFRNLGWSGDTVSDLAARRDrDVLPAKPDVVSIMFGINDSFRGFDDPV- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 135 kNLSSISENIEKIVTQLNEALPNTQIYVQS--ILPDHRDFITQMAQtVNKQIKAI--------KHARFTYIDLHPAFLGA 204
Cdd:cd01834   83 -GLEKFKTNLRRLIDRLKNKESAPRIVLVSpiAYEANEDPLPDGAE-YNANLAAYadavrelaAENGVAFVDLFTPMKEA 160

                        170       180
                 ....*....|....*....|....*....
gi 917632135 205 QGTLNEA-LTTDGTHLNEAGYALWAKQLA 232
Cdd:cd01834  161 FQKAGEAvLTVDGVHPNEAGHRALARLWL 189
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 65-233 1.08e-19

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: 83.23  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  65 IVFVGDSITE------QGLNWAIRFNDLR--------VRNRGISGDMTYGVLARLNELKAA---PPKAIFLKIGVNDIFN 127
Cdd:cd00229    1 ILVIGDSITAgygassGSTFYSLLLYLLLlaggpgveVINLGVSGATTADALRRLGLRLALlkdKPDLVIIELGTNDLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 128 FhyikQVKNLSSISENIEKIVTQLNEALPNTQIYVQSILP-DHRDFITQMAQTVNKQIK---AIKHARFTYIDLHPAFLG 203
Cdd:cd00229   81 G----GDTSIDEFKANLEELLDALRERAPGAKVILITPPPpPPREGLLGRALPRYNEAIkavAAENPAPSGVDLVDLAAL 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 917632135 204 AQGTLNEALTTDGTHLNEAGYALWAKQLAP 233
Cdd:cd00229  157 LGDEDKSLYSPDGIHPNPAGHKLIAEALAS 186
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 65-234 6.93e-18

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: 78.83  E-value: 6.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  65 IVFVGDSITEQ-------GLNWAIR---FNDLRVRNRGISGDMTYGVLARLNEL----KAAPPKAIFLKIGVNDIFNFHY 130
Cdd:cd01838    2 IVLFGDSITQFsfdqgefGFGAALAdvySRKLDVINRGFSGYNTRWALKVLPKIfleeKLAQPDLVTIFFGANDAALPGQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 131 IKQVKnLSSISENIEKIVTQLNEALPNTQI-------------YVQSILPDHRDFIT--------QMAQTVNKQIKAIkh 189
Cdd:cd01838   82 PQHVP-LDEYKENLRKIVSHLKSLSPKTKVilitpppvdeeawEKSLEDGGSQPGRTnellkqyaEACVEVAEELGVP-- 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 917632135 190 arftYIDLHPAFLGAQGTLNEALtTDGTHLNEAGYALWAKQLAPI 234
Cdd:cd01838  159 ----VIDLWTAMQEEAGWLESLL-TDGLHFSSKGYELLFEEIVKV 198
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 64-233 2.41e-17

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: 76.56  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  64 DIVFVGDSITEQGLNWAIRFNDLRVRNRGISGDMTYGVLARLNELKAAP-PKAIFLKIGVNDIFNFHYIKQVKnlssisE 142
Cdd:cd04502    1 GILFYGSSSIRLWDTLADDLAPLPVVNRGFGGSTLADCLHYFDRLVLPYqPRRVVLYAGDNDLASGRTPEEVL------R 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 143 NIEKIVTQLNEALPNTQIYVQSILP-----DHRDFITQmaqtVNKQIK--AIKHARFTYIDLHPAFLGAQGTLNEAL-TT 214
Cdd:cd04502   75 DFRELVNRIRAKLPDTPIAIISIKPsparwALRPKIRR----FNALLKelAETRPNLTYIDVASPMLDADGKPRAELfQE 150

                        170
                 ....*....|....*....
gi 917632135 215 DGTHLNEAGYALWAKQLAP 233
Cdd:cd04502  151 DGLHLNDAGYALWRKVIKP 169
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 64-228 2.97e-16

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: 73.90  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  64 DIVFVGDSITE--------QGLNWAIRFNDLRVRNRGISGDMTYGVLARLNE-LKAAPPKAIFLKIGVNDIFnfhyikQV 134
Cdd:cd04501    2 RVVCLGDSITYgypvgpeaSWVNLLAEFLGKEVINRGINGDTTSQMLVRFYEdVIALKPAVVIIMGGTNDII------VN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 135 KNLSSISENIEKIVTQLNEAlpNTQIYVQSILPDHRDFITQMAQTVNKQIKA----IKH-AR---FTYIDLHPAFL-GAQ 205
Cdd:cd04501   76 TSLEMIKDNIRSMVELAEAN--GIKVILASPLPVDDYPWKPQWLRPANKLKSlnrwLKDyARengLLFLDFYSPLLdERN 153

                        170       180
                 ....*....|....*....|...
gi 917632135 206 GTLNEALTTDGTHLNEAGYALWA 228
Cdd:cd04501  154 VGLKPGLLTDGLHPSREGYRVMA 176
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 68-231 4.85e-14

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: 67.26  E-value: 4.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  68 VGDSITEQGLNwairfndlrvrNRGISGD-MTYGVLARLNELKAAPPKAIFLKIGVNDIFNFHYIKQvknlssISENIEK 146
Cdd:cd01833    6 LGDSITWGDKD-----------HEGHSGYlIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNRDPDT------APDRLRA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 147 IVTQLNEALPNTQIYVQSILPDHRDFITQMAQTVNKQIKAIKHAR------FTYIDLHPAFLGAqgtlneALTTDGTHLN 220
Cdd:cd01833   69 LIDQMRAANPDVKIIVATLIPTTDASGNARIAEYNAAIPGVVADLrtagspVVLVDMSTGYTTA------DDLYDGLHPN 142

                        170
                 ....*....|....*
gi 917632135 221 EAGY----ALWAKQL 231
Cdd:cd01833  143 DQGYkkmaDAWYEAL 157
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
65-231 4.25e-13

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 66.06  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135   65 IVFVGDSITEQGLN-------WA------------IRFNDLRVR-NRGISGDMTYGVLARLNELKA--------APPKAI 116
Cdd:pfam00657   1 IVAFGDSLTDGGGDgpggrfsWGdlladflarklgVPGSGYNHGaNFAIGGATIEDLPIQLEQLLRlisdvkdqAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  117 FLKIGVNDIFNFHYIKQVK------NLSSISENIEKIVTQLNEALPNTqIYVQSILPDH----------RDFITQMAQTV 180
Cdd:pfam00657  81 TIFIGANDLCNFLSSPARSkkrvpdLLDELRANLPQLGLGARKFWVHG-LGPLGCTPPKgcyelynalaEEYNERLNELV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 917632135  181 NKQIKAIKHARFTYIDLHPAFLGAQGTLNEALTTDGTHLNEAGYALWAKQL 231
Cdd:pfam00657 160 NSLAAAAEDANVVYVDIYGFEDPTDPCCGIGLEPDGLHPSEKGYKAVAEAI 210
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 87-233 9.23e-13

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: 64.59  E-value: 9.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  87 RVRNRGISGDMTYGVLARLNELKAAPPKAIFLKIGVNDIFNFHYIKQVKnlssisENIEKIVTQLNEALPNTQIYVQSIL 166
Cdd:cd01836   42 RWRLFAKTGATSADLLRQLAPLPETRFDVAVISIGVNDVTHLTSIARWR------KQLAELVDALRAKFPGARVVVTAVP 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917632135 167 PDH---------RDFITQMAQTVNKQIK--AIKHARFTYIDLHpaFLGAQGTLNEalttDGTHLNEAGYALWAKQLAP 233
Cdd:cd01836  116 PLGrfpalpqplRWLLGRRARLLNRALErlASEAPRVTLLPAT--GPLFPALFAS----DGFHPSAAGYAVWAEALAP 187
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 65-231 2.56e-10

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: 238873  Cd Length: 193  Bit Score: 57.73  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  65 IVFVGDSI-----TEQGLNWAIRF--------NDLRVRNRGISGDMTYGVLARLNE-----LKAAPPKAIFLKIGVNDIf 126
Cdd:cd01835    4 LIVVGDSLvygwgDPEGGGWVGRLrarwmnlgDDPVLYNLGVRGDGSEDVAARWRAewsrrGELNVPNRLVLSVGLNDT- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 127 nfHYIKQVKNLSSISENIEKIVTQLNEALPNTQIYVQSILP----DHRDFITQMAQTVNKQIKAIKHARFTYIDLHPAFL 202
Cdd:cd01835   83 --ARGGRKRPQLSARAFLFGLNQLLEEAKRLVPVLVVGPTPvdeaKMPYSNRRIARLETAFAEVCLRRDVPFLDTFTPLL 160

                        170       180
                 ....*....|....*....|....*....
gi 917632135 203 GAQGTLNEALTTDGTHLNEAGYALWAKQL 231
Cdd:cd01835  161 NHPQWRRELAATDGIHPNAAGYGWLAWLV 189
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 65-233 5.66e-10

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: 56.89  E-value: 5.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  65 IVFVGDSITEqGLN----------WAIRF--------NDLRVRNRGISGDMTYGVLAR-LNELKAAPPKAIFLKIGVNDI 125
Cdd:cd01832    2 YVALGDSITE-GVGdpvpdggyrgWADRLaaalaaadPGIEYANLAVRGRRTAQILAEqLPAALALRPDLVTLLAGGNDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 126 FNFHyikqvKNLSSISENIEKIVTQLneALPNTQIYVQSIlPDH-------RDFITQMAqTVNKQIKAI--KH-ARFTYI 195
Cdd:cd01832   81 LRPG-----TDPDTYRADLEEAVRRL--RAAGARVVVFTI-PDPavlepfrRRVRARLA-AYNAVIRAVaaRYgAVHVDL 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 917632135 196 DLHPAFLGAQgtlneALTTDGTHLNEAGYALWAKQLAP 233
Cdd:cd01832  152 WEHPEFADPR-----LWASDRLHPSAAGHARLAALVLA 184
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 65-233 8.90e-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: 8.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  65 IVFVGDSIT-------EQGL------NWAIRFNDLRVRNRGISGDMTYGVLARLNE-LKAAPPKAIFLKIGVNDIFNFHY 130
Cdd:cd01822    3 ILALGDSLTagyglppEEGWpallqkRLDARGIDVTVINAGVSGDTTAGGLARLPAlLAQHKPDLVILELGGNDGLRGIP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 131 IKQVKNlssiseNIEKIVTQLNEAlpNTQIYVQSI-LPDHrdfitqMAQTVNKQIKAI--KHARFTYIDLHPAFLGAQGT 207
Cdd:cd01822   83 PDQTRA------NLRQMIETAQAR--GAPVLLVGMqAPPN------YGPRYTRRFAAIypELAEEYGVPLVPFFLEGVAG 148

                        170       180
                 ....*....|....*....|....*.
gi 917632135 208 LNEALTTDGTHLNEAGYALWAKQLAP 233
Cdd:cd01822  149 DPELMQSDGIHPNAEGQPIIAENVWP 174
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 64-232 6.75e-08

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: 51.09  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  64 DIVFVGDSITE-------QGlNWAIRFNDL---------RVRNRGISGDMTYGVLARLN------ELKAAppKAIFLKIG 121
Cdd:cd04506    1 KIVALGDSLTEgvgdetgKG-GYVGRLDKLietktvkkvTVQNFGVSGDRSDQLLKRLKtkkvqkELKKA--DVITITIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 122 VNDIFNfhyIKQvKNLSSISE------------NIEKIVTQLNEALPNTQIYVQSI---LPDHRDFITQMAQTV---NKQ 183
Cdd:cd04506   78 GNDLMQ---VLE-KNFLSLDVedfkkaeetyqnNLKKIFKEIRKLNPDAPIFLVGLynpFYVYFPNITEINDIVndwNEA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 917632135 184 IKAI----KHARFTYIDlhpaFLGAQGTLNEALTTDGTHLNEAGYALWAKQLA 232
Cdd:cd04506  154 SQKLasqyKNAYFVPIF----DLFSDGQNKYLLTSDHFHPNDKGYQLIADRVF 202
SGNH_hydrolase_like_6 cd01844
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 65-234 1.25e-07

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: 238881  Cd Length: 177  Bit Score: 50.01  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  65 IVFVGDSITE------QGLNW-AI--RFNDLRVRNRGISGDmtygvlARLNELKA-----APPKAIFLKIGVNdifnfhy 130
Cdd:cd01844    2 WVFYGTSISQgacasrPGMAWtAIlaRRLGLEVINLGFSGN------ARLEPEVAellrdVPADLYIIDCGPN------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 131 ikQVKNLSSISENIEKIVTQLNEALPNTQIYVQS--------ILPDHRDFITQMAQTVNKQIKAIK---HARFTYIDlHP 199
Cdd:cd01844   69 --IVGAEAMVRERLGPLVKGLRETHPDTPILLVSprycpdaeLTPGRGKLTLAVRRALREAFEKLRadgVPNLYYLD-GE 145

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 917632135 200 AFLGAqgtlNEALTTDGTHLNEAGYALWAKQLAPI 234
Cdd:cd01844  146 ELLGP----DGEALVDGIHPTDLGHMRYADRFEPV 176
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 107-232 2.59e-04

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: 40.72  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 107 ELKAAPPKAIFLKIGVNDIFNFHYikqvkNLSSISENIEKIVTQLNEALPNTQIYVQSILP------DHRDFITQMAQTV 180
Cdd:cd01825   51 QLAALPPDLVILSYGTNEAFNKQL-----NASEYRQQLREFIKRLRQILPNASILLVGPPDslqktgAGRWRTPPGLDAV 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 917632135 181 -NKQIKAIKHARFTYIDLHpAFLGAQGTL----NEALT-TDGTHLNEAGYALWAKQLA 232
Cdd:cd01825  126 iAAQRRVAKEEGIAFWDLY-AAMGGEGGIwqwaEPGLArKDYVHLTPRGYERLANLLY 182
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 84-231 3.30e-04

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: 40.90  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135  84 NDLRVRNRGISGDMTYGVLARLNELKAAPPKAI-------FLKIGVNDIFNFHYIKQV---------------------K 135
Cdd:cd01823   45 ETLSFTDVACSGATTTDGIEPQQGGIAPQAGALdpdtdlvTITIGGNDLGFADVVKACiltgggsslaqekgaadgardA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632135 136 NLSSISENIEKIVTQLNEALPNTQIYV---------------------QSILPDHRDFITQMAQTVNKQIKAIKHA---- 190
Cdd:cd01823  125 ALDEVGARLKAVLDRIRERAPNARVVVvgyprlfppdggdcdkscspgTPLTPADRPELNQLVDKLNALIRRAAADagdy 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 917632135 191 RFTYIDLHPAFLG-----AQGTLNEALTTDGT------HLNEAGYALWAKQL 231
Cdd:cd01823  205 KVRFVDTDAPFAGhracsPDPWSRSVLDLLPTrqgkpfHPNAAGHRAIADLI 256
 
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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