NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1777675043|ref|WP_154330871|]
View 

MULTISPECIES: SGNH/GDSL hydrolase family protein [Stenotrophomonas]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10139723)

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|7610479
SCOP:  3001315

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 79-255 1.04e-73

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: 222.97  E-value: 1.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGSA------AFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGNTgpaTQ 152
Cdd:cd04501     2 RVVCLGDSITYGYPVGPEAswvnllAEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT---SL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 153 AMIEDNLHAMVDLARAHGIRVVLASVLPVSEYPWMPGI-TPAPKVRALNSALKRYADAQHLVYLDYYAPMAN-VAGGLDP 230
Cdd:cd04501    79 EMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWlRPANKLKSLNRWLKDYARENGLLFLDFYSPLLDeRNVGLKP 158

                         170       180
                  ....*....|....*....|....*
gi 1777675043 231 PLAADGVHPTAKGYAMMAPLAEAAI 255
Cdd:cd04501   159 GLLTDGLHPSREGYRVMAPLAEKAL 183
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 79-255 1.04e-73

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: 222.97  E-value: 1.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGSA------AFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGNTgpaTQ 152
Cdd:cd04501     2 RVVCLGDSITYGYPVGPEAswvnllAEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT---SL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 153 AMIEDNLHAMVDLARAHGIRVVLASVLPVSEYPWMPGI-TPAPKVRALNSALKRYADAQHLVYLDYYAPMAN-VAGGLDP 230
Cdd:cd04501    79 EMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWlRPANKLKSLNRWLKDYARENGLLFLDFYSPLLDeRNVGLKP 158

                         170       180
                  ....*....|....*....|....*
gi 1777675043 231 PLAADGVHPTAKGYAMMAPLAEAAI 255
Cdd:cd04501   159 GLLTDGLHPSREGYRVMAPLAEKAL 183
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 72-256 7.35e-47

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: 154.42  E-value: 7.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  72 PAVPGQPRVVFFGDSITEGWGREGS-------AAFFPGKGW--LNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTND 142
Cdd:COG2755     3 AAAGKPLRIVALGDSITAGYGASRErgwpallARRLAAADVrvVNAGISGATTADLLARLDRDLLALKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 143 IAGNTGpATQAMIEDNLHAMVDLARAHG--IRVVLASVLPVSEYPWMpgitpAPKVRALNSALKRYADAQHLVYLDYYAP 220
Cdd:COG2755    83 LLRGLG-VSPEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRPNYL-----NERIEAYNAAIRELAAEYGVPLVDLYAA 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1777675043 221 MAnVAGGLDPPLAADGVHPTAKGYAMMAPLAEAAIR 256
Cdd:COG2755   157 LR-DAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 82-245 1.26e-36

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: 127.66  E-value: 1.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  82 FFGDSITEGWGREGS------------AAFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGNTGP 149
Cdd:pfam13472   1 ALGDSITAGYGATGGdrsypgwlarllARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 150 ATqamIEDNLHAMVDLARAHG--IRVVLASVLPVSEYPWMPGITPAPKVRALNSALKRYADAQHLVYLDYYAPMANVAGG 227
Cdd:pfam13472  81 AR---AAANLEALIDALRAAGpdARVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGW 157

                         170
                  ....*....|....*...
gi 1777675043 228 LDPPLAADGVHPTAKGYA 245
Cdd:pfam13472 158 LPDLLADDGLHPNAAGYR 175
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 79-255 1.04e-73

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: 222.97  E-value: 1.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGSA------AFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGNTgpaTQ 152
Cdd:cd04501     2 RVVCLGDSITYGYPVGPEAswvnllAEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT---SL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 153 AMIEDNLHAMVDLARAHGIRVVLASVLPVSEYPWMPGI-TPAPKVRALNSALKRYADAQHLVYLDYYAPMAN-VAGGLDP 230
Cdd:cd04501    79 EMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWlRPANKLKSLNRWLKDYARENGLLFLDFYSPLLDeRNVGLKP 158

                         170       180
                  ....*....|....*....|....*
gi 1777675043 231 PLAADGVHPTAKGYAMMAPLAEAAI 255
Cdd:cd04501   159 GLLTDGLHPSREGYRVMAPLAEKAL 183
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 79-246 8.92e-48

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: 156.29  E-value: 8.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGSaafFPGKGWLNRGISGQTTAQMLVRFPQDVlALKPQVVVILAGTNDIAGNTGPATqamIEDN 158
Cdd:cd01828     1 ALVFLGDSLTEGGPWALL---FPDVKVANRGISGDTTRGLLARLDEDV-ALQPKAIFIMIGINDLAQGTSDED---IVAN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 159 LHAMVDLARAH--GIRVVLASVLPVSEYPWmpgiTPAPKVRALNSALKRYADAQHLVYLDYYAPMANVAGGLDPPLAADG 236
Cdd:cd01828    74 YRTILEKLRKHfpNIKIVVQSILPVGELKS----IPNEQIEELNRQLAQLAQQEGVTFLDLWAVFTNADGDLKNEFTTDG 149

                         170
                  ....*....|
gi 1777675043 237 VHPTAKGYAM 246
Cdd:cd01828   150 LHLNAKGYAV 159
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 72-256 7.35e-47

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: 154.42  E-value: 7.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  72 PAVPGQPRVVFFGDSITEGWGREGS-------AAFFPGKGW--LNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTND 142
Cdd:COG2755     3 AAAGKPLRIVALGDSITAGYGASRErgwpallARRLAAADVrvVNAGISGATTADLLARLDRDLLALKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 143 IAGNTGpATQAMIEDNLHAMVDLARAHG--IRVVLASVLPVSEYPWMpgitpAPKVRALNSALKRYADAQHLVYLDYYAP 220
Cdd:COG2755    83 LLRGLG-VSPEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRPNYL-----NERIEAYNAAIRELAAEYGVPLVDLYAA 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1777675043 221 MAnVAGGLDPPLAADGVHPTAKGYAMMAPLAEAAIR 256
Cdd:COG2755   157 LR-DAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 82-245 1.26e-36

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: 127.66  E-value: 1.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  82 FFGDSITEGWGREGS------------AAFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGNTGP 149
Cdd:pfam13472   1 ALGDSITAGYGATGGdrsypgwlarllARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 150 ATqamIEDNLHAMVDLARAHG--IRVVLASVLPVSEYPWMPGITPAPKVRALNSALKRYADAQHLVYLDYYAPMANVAGG 227
Cdd:pfam13472  81 AR---AAANLEALIDALRAAGpdARVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGW 157

                         170
                  ....*....|....*...
gi 1777675043 228 LDPPLAADGVHPTAKGYA 245
Cdd:pfam13472 158 LPDLLADDGLHPNAAGYR 175
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 79-250 8.32e-27

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: 102.76  E-value: 8.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGS-----AAFFPGKGW--LNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTND-IAGNTGPA 150
Cdd:cd01834     3 RIVFIGNSITDRGGYVGYvetylAARYPELKLtfRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDsFRGFDDPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 151 TQAMIEDNLHAMVD--LARAHGIRVVLasvlpVSEYPWMPGITPAPKVRALNSALKRYADAQHLV-------YLDYYAPM 221
Cdd:cd01834    83 GLEKFKTNLRRLIDrlKNKESAPRIVL-----VSPIAYEANEDPLPDGAEYNANLAAYADAVRELaaengvaFVDLFTPM 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1777675043 222 ANVAGGLDP-PLAADGVHPTAKGYAMMAPL 250
Cdd:cd01834   158 KEAFQKAGEaVLTVDGVHPNEAGHRALARL 187
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 80-248 1.39e-25

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: 99.41  E-value: 1.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  80 VVFFGDSITEGWGREGSAAFFPGKGWL------------NRGISGQTTAQMLVRF--PQDVLALKPQVVVILAGTNDIAG 145
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLLYLlllaggpgveviNLGVSGATTADALRRLglRLALLKDKPDLVIIELGTNDLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 146 NTGPATQAmIEDNLHAMVDLAR--AHGIRVVLASVLPVSEYPWMPGITPAPKVRALNSALKRYADAQHLVYLDYYAPMAN 223
Cdd:cd00229    81 GGDTSIDE-FKANLEELLDALRerAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENPAPSGVDLVDLAALLGD 159

                         170       180
                  ....*....|....*....|....*
gi 1777675043 224 VAGGLdppLAADGVHPTAKGYAMMA 248
Cdd:cd00229   160 EDKSL---YSPDGIHPNPAGHKLIA 181
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 78-259 2.37e-22

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: 91.58  E-value: 2.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  78 PRVVFFGDSITEGWGREGSAA---FFPGKGWLNRGISGQTTAQMLVRFPQDVLA-LKPQVVVILAGTNDIaGNTGPATQa 153
Cdd:cd01820    33 PDVVFIGDSITQNWEFTGLEVwreLYAPLHALNFGIGGDRTQNVLWRLENGELDgVNPKVVVLLIGTNNI-GHTTTAEE- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 154 mIEDNLHAMVDLARAH--GIRVVLASVLPVSEYPwmpgitpaPKVRALNSAL-----KRYADAQHLVYLDYYAPMANVAG 226
Cdd:cd01820   111 -IAEGILAIVEEIREKlpNAKILLLGLLPRGQNP--------NPLRERNAQVnrllaVRYDGLPNVTFLDIDKGFVQSDG 181

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1777675043 227 GLDPPLAADGVHPTAKGYAMMAPLAEAAIRRAM 259
Cdd:cd01820   182 TISHHDMPDYLHLTAAGYRKWADALHPTLARLL 214
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 78-248 2.60e-22

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: 90.26  E-value: 2.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  78 PRVVFFGDSITEGWGREGSAAFFP---------GKGW--LNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGN 146
Cdd:cd01822     1 VTILALGDSLTAGYGLPPEEGWPAllqkrldarGIDVtvINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 147 TGPatqAMIEDNLHAMVDLARAHGIRVVLASV-LPvseyPWMpGITPAPKVRALNSALkryADAQHLVYLDYYapMANVA 225
Cdd:cd01822    81 IPP---DQTRANLRQMIETAQARGAPVLLVGMqAP----PNY-GPRYTRRFAAIYPEL---AEEYGVPLVPFF--LEGVA 147

                         170       180
                  ....*....|....*....|...
gi 1777675043 226 gGLDPPLAADGVHPTAKGYAMMA 248
Cdd:cd01822   148 -GDPELMQSDGIHPNAEGQPIIA 169
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
80-248 5.06e-22

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 90.71  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  80 VVFFGDSITEGWGREGSAAF---------------FPGKGWL---NRGISGQTTAQM------LVRFPQDVL-ALKPQVV 134
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGGRFswgdlladflarklgVPGSGYNhgaNFAIGGATIEDLpiqleqLLRLISDVKdQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 135 VILAGTNDIAGNTGPATQ---------AMIEDNLHAMVDLAR---AHGIRVVLAS--VLPVSEYPWMpGITPAPKVRALN 200
Cdd:pfam00657  81 TIFIGANDLCNFLSSPARskkrvpdllDELRANLPQLGLGARkfwVHGLGPLGCTppKGCYELYNAL-AEEYNERLNELV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1777675043 201 SALKRYADAQHLVYLDYYAPMANVAGGLDPPLAADGVHPTAKGYAMMA 248
Cdd:pfam00657 160 NSLAAAAEDANVVYVDIYGFEDPTDPCCGIGLEPDGLHPSEKGYKAVA 207
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 79-248 5.49e-21

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: 87.69  E-value: 5.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGSAAFfpgkGW------------LNRGISGQTTAQMLVRFPQDVL---ALKPQVVVILAGTNDI 143
Cdd:cd01838     1 KIVLFGDSITQFSFDQGEFGF----GAaladvysrkldvINRGFSGYNTRWALKVLPKIFLeekLAQPDLVTIFFGANDA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 144 AgntGPATQAMIE-----DNLHAMVDL--ARAHGIRVVLASVLPVSEYPW--MPGITPAPKVRaLNSALKRYADA----- 209
Cdd:cd01838    77 A---LPGQPQHVPldeykENLRKIVSHlkSLSPKTKVILITPPPVDEEAWekSLEDGGSQPGR-TNELLKQYAEAcveva 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1777675043 210 --QHLVYLDYYAPMANvAGGLDPPLAADGVHPTAKGYAMMA 248
Cdd:cd01838   153 eeLGVPVIDLWTAMQE-EAGWLESLLTDGLHFSSKGYELLF 192
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 79-248 9.36e-21

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: 85.75  E-value: 9.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGRegsaaffpgkgwlNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGNTGPATqamIEDN 158
Cdd:cd01833     2 RIMPLGDSITWGDKD-------------HEGHSGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNRDPDT---APDR 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 159 LHAMVDLARAHGIRVVLAsvlpVSEYPWMPGITPAPKVRALNSALK-----RYADAQHLVYLDYYAPManvaggLDPPLA 233
Cdd:cd01833    66 LRALIDQMRAANPDVKII----VATLIPTTDASGNARIAEYNAAIPgvvadLRTAGSPVVLVDMSTGY------TTADDL 135

                         170
                  ....*....|....*
gi 1777675043 234 ADGVHPTAKGYAMMA 248
Cdd:cd01833   136 YDGLHPNDQGYKKMA 150
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 81-245 2.76e-19

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: 82.38  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  81 VFFGDSITEGWGRegSAAFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIaGNTGPATQAMieDNLH 160
Cdd:cd01841     4 VFIGDSLFEGWPL--YEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDI-GKEVSSNQFI--KWYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 161 AMVDLARAH--GIRVVLASVLPVSEYPWMPGITPAPKVRaLNSALKRYADAQHLVYLDYYAPMANVAGGLDPPLAADGVH 238
Cdd:cd01841    79 DIIEQIREEfpNTKIYLLSVLPVLEEDEIKTRSNTRIQR-LNDAIKELAPELGVTFIDLNDVLVDEFGNLKKEYTTDGLH 157


                  ....*..
gi 1777675043 239 PTAKGYA 245
Cdd:cd01841   158 FNPKGYQ 164
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 80-255 2.79e-18

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: 79.64  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  80 VVFFGDSITEGWgrEGSAAFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDIAGNTGPATqamIEDNL 159
Cdd:cd04502     2 ILFYGSSSIRLW--DTLADDLAPLPVVNRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTPEE---VLRDF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 160 HAMVDLARAH--GIRVVLASVLPvseypwmpgiTPA-----PKVRALNSALKRYADAQHLV-YLDYYAPMANVAGGLDPP 231
Cdd:cd04502    77 RELVNRIRAKlpDTPIAIISIKP----------SPArwalrPKIRRFNALLKELAETRPNLtYIDVASPMLDADGKPRAE 146

                         170       180
                  ....*....|....*....|....*
gi 1777675043 232 L-AADGVHPTAKGYAMMAPLAEAAI 255
Cdd:cd04502   147 LfQEDGLHLNDAGYALWRKVIKPAL 171
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 79-254 5.64e-15

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: 71.15  E-value: 5.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWG---------------REGSAAFFPGKGWLNRGISGQTTAQMLVRFPQDVLALKPQVVVILAGTNDI 143
Cdd:cd01832     1 RYVALGDSITEGVGdpvpdggyrgwadrlAAALAAADPGIEYANLAVRGRRTAQILAEQLPAALALRPDLVTLLAGGNDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 144 AGNTGPATQamIEDNLHAMVDLARAHGIRVVLASVlpvseyPWMPGITP-----APKVRALNSALKRYADAQHLVYLDYY 218
Cdd:cd01832    81 LRPGTDPDT--YRADLEEAVRRLRAAGARVVVFTI------PDPAVLEPfrrrvRARLAAYNAVIRAVAARYGAVHVDLW 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1777675043 219 ApMANVAGGLDppLAADGVHPTAKGYAMMAPLAEAA 254
Cdd:cd01832   153 E-HPEFADPRL--WASDRLHPSAAGHARLAALVLAA 185
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 80-248 1.56e-12

SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. 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: 238868  Cd Length: 204  Bit Score: 64.57  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  80 VVFFGDSITEGWG---------------REGSAAFFPGKGWLNRGISGQTTAQ------MLVRFPQDVLALkPQV--VVI 136
Cdd:cd01830     2 VVALGDSITDGRGstpdannrwpdllaaRLAARAGTRGIAVLNAGIGGNRLLAdglgpsALARFDRDVLSQ-PGVrtVII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 137 LAGTNDI-AGNTGPATQAMIEDNLHA----MVDLARAHGIRVVLASVLPVSEYPWMpgiTPA-PKVR-ALNSALKRYADA 209
Cdd:cd01830    81 LEGVNDIgASGTDFAAAPVTAEELIAgyrqLIRRAHARGIKVIGATITPFEGSGYY---TPArEATRqAVNEWIRTSGAF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1777675043 210 QHLVYLDyyapmANVAGGLDP--PLAA----DGVHPTAKGYAMMA 248
Cdd:cd01830   158 DAVVDFD-----AALRDPADPsrLRPAydsgDHLHPNDAGYQAMA 197
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 79-257 2.41e-11

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: 61.13  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWG-------------REGSAAFFPGKGWLNRGISGQTTAQMLVRFpQDVLALKPQVVVILAGTNDIAG 145
Cdd:cd01836     4 RLLVLGDSTAAGVGvetqdqalagqlaRGLAAITGRGVRWRLFAKTGATSADLLRQL-APLPETRFDVAVISIGVNDVTH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 146 NTGPATQAMiedNLHAMVDLARAH--GIRVVLASVLPVSEYPWMPGitpaP-------KVRALNSALKRYADAQHLV-YL 215
Cdd:cd01836    83 LTSIARWRK---QLAELVDALRAKfpGARVVVTAVPPLGRFPALPQ----PlrwllgrRARLLNRALERLASEAPRVtLL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1777675043 216 DYYAPMANVaggldpPLAADGVHPTAKGYAMMAPLAEAAIRR 257
Cdd:cd01836   156 PATGPLFPA------LFASDGFHPSAAGYAVWAEALAPAIAA 191
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 79-259 1.65e-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: 55.74  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGwgregsaAFFPGK--GWL-----NRGISGqTTAQMLVRFPQDVL-----ALKPQVVVILAGTNDiAGN 146
Cdd:cd01825     1 RIAQLGDSHIAG-------DFFTDVlrGLLgviydNLGVNG-ASASLLLKWDAEFLqaqlaALPPDLVILSYGTNE-AFN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 147 TGPATQAMIEdNLHAMVDLARAHGIRVV--LASVLPVSEYPWMPGITPAPKVRALNSALKRYADAQHLVYLDYYAPMANV 224
Cdd:cd01825    72 KQLNASEYRQ-QLREFIKRLRQILPNASilLVGPPDSLQKTGAGRWRTPPGLDAVIAAQRRVAKEEGIAFWDLYAAMGGE 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1777675043 225 AGG---LDPPLAA-DGVHPTAKGYAMMAPLAEAAIRRAM 259
Cdd:cd01825   151 GGIwqwAEPGLARkDYVHLTPRGYERLANLLYEALLKAY 189
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 79-250 1.67e-09

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: 55.81  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGsaaffpGKGWLNR-----------------GISGQTTAQMLVR----FPQDVLALKPQVVVIL 137
Cdd:cd01835     3 RLIVVGDSLVYGWGDPE------GGGWVGRlrarwmnlgddpvlynlGVRGDGSEDVAARwraeWSRRGELNVPNRLVLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 138 AGTNDIAGNTGPATQAMIED--NLHAMVDLARAHGIRVVLASVLPVSEyPWMPGitpapkvraLNSALKRYADAQHLV-- 213
Cdd:cd01835    77 VGLNDTARGGRKRPQLSARAflFGLNQLLEEAKRLVPVLVVGPTPVDE-AKMPY---------SNRRIARLETAFAEVcl 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1777675043 214 -----YLDYYAPMANVAGGLDPPLAADGVHPTAKGYAMMAPL 250
Cdd:cd01835   147 rrdvpFLDTFTPLLNHPQWRRELAATDGIHPNAAGYGWLAWL 188
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 79-248 3.84e-07

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: 48.98  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGrEGSAAFFP-------GKGWL--NRGISGQTtaqMLVRFPQD---------VLALKPQVVVILAGT 140
Cdd:cd01827     2 KVACVGNSITEGAG-LRAYDSYPsplaqmlGDGYEvgNFGKSART---VLNKGDHPymneeryknALAFNPNIVIIKLGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 141 NDiAGNTGPATQAMIEDNLHAMVDLARAHGIR--VVLASVLPVSEYPWMPgITPAPKVRALNSALKRYADAQHLVYLDYY 218
Cdd:cd01827    78 ND-AKPQNWKYKDDFKKDYETMIDSFQALPSKpkIYICYPIPAYYGDGGF-INDNIIKKEIQPMIDKIAKKLNLKLIDLH 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1777675043 219 APMANVaggldPPLAADGVHPTAKGYAMMA 248
Cdd:cd01827   156 TPLKGK-----PELVPDWVHPNEKGAYILA 180
SGNH_hydrolase_like_6 cd01844
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 79-248 9.56e-06

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: 45.01  E-value: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGregsaAFFPGKGWLNR------------GISG-----QTTAQMLVRFPqdvlalkPQVVVILAGTN 141
Cdd:cd01844     1 PWVFYGTSISQGAC-----ASRPGMAWTAIlarrlglevinlGFSGnarlePEVAELLRDVP-------ADLYIIDCGPN 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 142 DIAgntgpaTQAMIEDNLHAMVDLARAHGIRVVLASVLPVSeYPWMPgITPAP------KVRALNSALK--RYADAQHLV 213
Cdd:cd01844    69 IVG------AEAMVRERLGPLVKGLRETHPDTPILLVSPRY-CPDAE-LTPGRgkltlaVRRALREAFEklRADGVPNLY 140

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1777675043 214 YLDYYapmaNVAGGLDPPLAaDGVHPTAKGYAMMA 248
Cdd:cd01844   141 YLDGE----ELLGPDGEALV-DGIHPTDLGHMRYA 170
SGNH_hydrolase_peri2 cd01829
SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 79-257 3.49e-05

SGNH_peri2; 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: 238867  Cd Length: 200  Bit Score: 43.42  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGWGREGSAAFF--PGKGWLNRGI--SGqttaqmLVR---------FPQDVLALKPQVVVILAGTND--- 142
Cdd:cd01829     1 RVLVIGDSLAQGLAPGLLRALAdnPGIRVINRSKgsSG------LVRpdffdwpekLKELIAEEKPDVVVVFLGANDrqd 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 143 ---IAGNTGPATQ---AMIEDNLHAMVDLARAHGIRVVLASvLPVSEYPWMPGitpapKVRALNSALKRYADAQHLVYLD 216
Cdd:cd01829    75 irdGDGYLKFGSPeweEEYRQRIDELLNVARAKGVPVIWVG-LPAMRSPKLSA-----DMVYLNSLYREEVAKAGGEFVD 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1777675043 217 ----------YYAPMANVAGGLDPPL-AADGVHPTAKGYAMMAPLAEAAIRR 257
Cdd:cd01829   149 vwdgfvdengRFTYSGTDVNGKKVRLrTNDGIHFTAAGGRKLAFYVEKLIRR 200
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
 79-257 1.10e-04

SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating enzyme) of A. tumefaciens. 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: 238877  Cd Length: 208  Bit Score: 42.26  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043  79 RVVFFGDSITEGW-----GREGSAAFFPGK----------GW--LNRGISGQTT-------AQM--LVRFPQDVLALKPQ 132
Cdd:cd01839     1 TILCFGDSNTWGIipdtgGRYPFEDRWPGVlekalgangeNVrvIEDGLPGRTTvlddpffPGRngLTYLPQALESHSPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 133 VVVILA-GTNDIAG--NTGPATQAMIednLHAMVDLARAHGI-------RVVLASVLPVS-EYPWMPGIT--PAPKVRAL 199
Cdd:cd01839    81 DLVIIMlGTNDLKSyfNLSAAEIAQG---LGALVDIIRTAPIepgmpapKILIVAPPPIRtPKGSLAGKFagAEEKSKGL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1777675043 200 NSALKRYADAQHLVYLDyyapmanvAGGLDPPLAADGVHPTAKGYAMMAPLAEAAIRR 257
Cdd:cd01839   158 ADAYRALAEELGCHFFD--------AGSVGSTSPVDGVHLDADQHAALGQALASVIRA 207
SGNH_hydrolase_yrhL_like cd01840
yrhL-like subfamily of SGNH-hydrolases, a diverse family of lipases and esterases. The ...
 131-259 5.64e-03

yrhL-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 the Ser-His-Asp(Glu) triad found in other serine hydrolases. Most members of this sub-family appear to co-occur with N-terminal acyltransferase domains. Might be involved in lipid metabolism.


Pssm-ID: 238878  Cd Length: 150  Bit Score: 36.45  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777675043 131 PQVVVILAGTNdiagntGPATQAMIEDNLHAmvdLARAHgiRVVLasVLPVSEYPWMPgitpapKVRA-LNSALKRYada 209
Cdd:cd01840    51 RKTVVIGLGTN------GPFTKDQLDELLDA---LGPDR--QVYL--VNPHVPRPWEP------DVNAyLLDAAKKY--- 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1777675043 210 QHLVYLDYYAPMANVAGGLDPplaaDGVHPTAKGyammAPLAEAAIRRAM 259
Cdd:cd01840   109 KNVTIIDWYKAAKGHPDWFYG----DGVHPNPAG----AKLYAALIAKAI 150
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH