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Conserved domains on  [gi|490454036|ref|WP_004324866|]
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MULTISPECIES: SGNH/GDSL hydrolase family protein [Bacteroides]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110814)

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

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 29-233 1.77e-64

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: 205.99  E-value: 1.77e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  29 GERAVFLGNSITDGGHYHSYIWLYYMTRFPDMPIRVFNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDSGYFEYN 108
Cdd:cd01834    1 GDRIVFIGNSITDRGGYVGYVETYLAARYPELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDSFRGFDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 109 GDKPKEFgeqkyqesIKNYQQMEKRFKDlPDTRIVMVGTSPYDETVQLKENTPFKTKNETIKRLVEYQKESAAKNNWEFT 188
Cdd:cd01834   81 PVGLEKF--------KTNLRRLIDRLKN-KESAPRIVLVSPIAYEANEDPLPDGAEYNANLAAYADAVRELAAENGVAFV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490454036 189 DLNAPMTAINQQYQqkdptFTLCGSDRIHPDNDGHMVMAYLFLKA 233
Cdd:cd01834  152 DLFTPMKEAFQKAG-----EAVLTVDGVHPNEAGHRALARLWLEA 191
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 29-233 1.77e-64

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: 205.99  E-value: 1.77e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  29 GERAVFLGNSITDGGHYHSYIWLYYMTRFPDMPIRVFNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDSGYFEYN 108
Cdd:cd01834    1 GDRIVFIGNSITDRGGYVGYVETYLAARYPELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDSFRGFDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 109 GDKPKEFgeqkyqesIKNYQQMEKRFKDlPDTRIVMVGTSPYDETVQLKENTPFKTKNETIKRLVEYQKESAAKNNWEFT 188
Cdd:cd01834   81 PVGLEKF--------KTNLRRLIDRLKN-KESAPRIVLVSPIAYEANEDPLPDGAEYNANLAAYADAVRELAAENGVAFV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490454036 189 DLNAPMTAINQQYQqkdptFTLCGSDRIHPDNDGHMVMAYLFLKA 233
Cdd:cd01834  152 DLFTPMKEAFQKAG-----EAVLTVDGVHPNEAGHRALARLWLEA 191
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 31-233 2.13e-29

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: 113.59  E-value: 2.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  31 RAVFLGNSITDG------GHYHSYIWlyymTRFPDMPIRVFNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDSGY 104
Cdd:COG2755   10 RIVALGDSITAGygasreRGWPALLA----RRLAAADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLLR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 105 feYNGDKPKEFgeqkyqesIKNYQQMEKRFKDL-PDTRIVMVGTSPYDETVQLkentpfktkNETIKRLVEYQKESAAKN 183
Cdd:COG2755   86 --GLGVSPEEF--------RANLEALIDRLRAAgPGARVVLVTPPPRLRPNYL---------NERIEAYNAAIRELAAEY 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490454036 184 NWEFTDLNAPMTAinqqyQQKDPtfTLCGSDRIHPDNDGHMVMAYLFLKA 233
Cdd:COG2755  147 GVPLVDLYAALRD-----AGDLP--DLLTADGLHPNAAGYRLIAEAVLPA 189
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 34-223 6.55e-16

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: 75.27  E-value: 6.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036   34 FLGNSITDG--GHYHSYIWLYYMTRF--PDMPIRVFNG-GIGGDT-AYDMNKRLDgDIFAMKPSVLMVTFGMNDSGYfey 107
Cdd:pfam13472   1 ALGDSITAGygATGGDRSYPGWLARLlaRRLGADVVNNlGISGATtRLDLLERLD-DVLRLKPDLVVILLGTNDLGR--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  108 ngDKPKEFGEQKYQESIKNYQQMekrfkdLPDTRIVMVGTSPydetVQLKENTPFKTKNETIKRLVEYQKESAAKNNWEF 187
Cdd:pfam13472  77 --GVSAARAAANLEALIDALRAA------GPDARVLLIGPLP----VGPPPPLDERRLNARIAEYNAAIREVAAERGVPY 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 490454036  188 TDLNAPMTAinqqyqQKDPTFTLCGSDRIHPDNDGH 223
Cdd:pfam13472 145 VDLWDALRD------DGGWLPDLLADDGLHPNAAGY 174
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 29-233 1.77e-64

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: 205.99  E-value: 1.77e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  29 GERAVFLGNSITDGGHYHSYIWLYYMTRFPDMPIRVFNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDSGYFEYN 108
Cdd:cd01834    1 GDRIVFIGNSITDRGGYVGYVETYLAARYPELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDSFRGFDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 109 GDKPKEFgeqkyqesIKNYQQMEKRFKDlPDTRIVMVGTSPYDETVQLKENTPFKTKNETIKRLVEYQKESAAKNNWEFT 188
Cdd:cd01834   81 PVGLEKF--------KTNLRRLIDRLKN-KESAPRIVLVSPIAYEANEDPLPDGAEYNANLAAYADAVRELAAENGVAFV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490454036 189 DLNAPMTAINQQYQqkdptFTLCGSDRIHPDNDGHMVMAYLFLKA 233
Cdd:cd01834  152 DLFTPMKEAFQKAG-----EAVLTVDGVHPNEAGHRALARLWLEA 191
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 31-233 2.13e-29

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: 113.59  E-value: 2.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  31 RAVFLGNSITDG------GHYHSYIWlyymTRFPDMPIRVFNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDSGY 104
Cdd:COG2755   10 RIVALGDSITAGygasreRGWPALLA----RRLAAADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLLR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 105 feYNGDKPKEFgeqkyqesIKNYQQMEKRFKDL-PDTRIVMVGTSPYDETVQLkentpfktkNETIKRLVEYQKESAAKN 183
Cdd:COG2755   86 --GLGVSPEEF--------RANLEALIDRLRAAgPGARVVLVTPPPRLRPNYL---------NERIEAYNAAIRELAAEY 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490454036 184 NWEFTDLNAPMTAinqqyQQKDPtfTLCGSDRIHPDNDGHMVMAYLFLKA 233
Cdd:COG2755  147 GVPLVDLYAALRD-----AGDLP--DLLTADGLHPNAAGYRLIAEAVLPA 189
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 31-233 1.54e-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: 239945  Cd Length: 183  Bit Score: 83.15  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  31 RAVFLGNSITDG-GHYHSYIWLYYMTRFPDMPirVFNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDsgyfeyng 109
Cdd:cd04501    2 RVVCLGDSITYGyPVGPEASWVNLLAEFLGKE--VINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTND-------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 110 dkpkeFGEQKYQESIK-NYQQMEKRFKDLpDTRIVMVGTSPYDETvqlKENTPFKTKNETIKRLVEYQKESAAKNNWEFT 188
Cdd:cd04501   72 -----IIVNTSLEMIKdNIRSMVELAEAN-GIKVILASPLPVDDY---PWKPQWLRPANKLKSLNRWLKDYARENGLLFL 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490454036 189 DLNAPMtaINQQYQQKDPTFTLcgsDRIHPDNDGHMVMAYLFLKA 233
Cdd:cd04501  143 DFYSPL--LDERNVGLKPGLLT---DGLHPSREGYRVMAPLAEKA 182
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 33-233 1.77e-18

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: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  33 VFLGNSITDGGHYHSYIWLYY-----MTRFPDMPIRVFNGGIGGDTAYDMNKRLDGDIFAM--KPSVLMVTFGMNDSGyf 105
Cdd:cd00229    2 LVIGDSITAGYGASSGSTFYSlllylLLLAGGPGVEVINLGVSGATTADALRRLGLRLALLkdKPDLVIIELGTNDLG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 106 eYNGDKPKEfgeqkyqESIKNYQQM-EKRFKDLPDTRIVMVGTSPYDETVQLkentpfktKNETIKRLVEYQKESAAKNN 184
Cdd:cd00229   80 -RGGDTSID-------EFKANLEELlDALRERAPGAKVILITPPPPPPREGL--------LGRALPRYNEAIKAVAAENP 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490454036 185 WEFTDLNAPMTAINQQYQQKdptftLCGSDRIHPDNDGHMVMAYLFLKA 233
Cdd:cd00229  144 APSGVDLVDLAALLGDEDKS-----LYSPDGIHPNPAGHKLIAEALASA 187
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 34-223 6.55e-16

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: 75.27  E-value: 6.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036   34 FLGNSITDG--GHYHSYIWLYYMTRF--PDMPIRVFNG-GIGGDT-AYDMNKRLDgDIFAMKPSVLMVTFGMNDSGYfey 107
Cdd:pfam13472   1 ALGDSITAGygATGGDRSYPGWLARLlaRRLGADVVNNlGISGATtRLDLLERLD-DVLRLKPDLVVILLGTNDLGR--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  108 ngDKPKEFGEQKYQESIKNYQQMekrfkdLPDTRIVMVGTSPydetVQLKENTPFKTKNETIKRLVEYQKESAAKNNWEF 187
Cdd:pfam13472  77 --GVSAARAAANLEALIDALRAA------GPDARVLLIGPLP----VGPPPPLDERRLNARIAEYNAAIREVAAERGVPY 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 490454036  188 TDLNAPMTAinqqyqQKDPTFTLCGSDRIHPDNDGH 223
Cdd:pfam13472 145 VDLWDALRD------DGGWLPDLLADDGLHPNAAGY 174
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 33-222 1.63e-13

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: 68.46  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  33 VFLGNSITDGGHYHSyiwlyymtRFPDmpIRVFNGGIGGDTAYDMNKRLDGDIfAMKPSVLMVTFGMNDsgyfeyngdkp 112
Cdd:cd01828    3 VFLGDSLTEGGPWAL--------LFPD--VKVANRGISGDTTRGLLARLDEDV-ALQPKAIFIMIGIND----------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 113 keFGEQKYQESI-KNYQQM-EKRFKDLPDTRIVMVGTSPYDETVQlkentpfkTKNETIKRLVEYQKESAAKNNWEFTDL 190
Cdd:cd01828   61 --LAQGTSDEDIvANYRTIlEKLRKHFPNIKIVVQSILPVGELKS--------IPNEQIEELNRQLAQLAQQEGVTFLDL 130

                        170       180       190
                 ....*....|....*....|....*....|..
gi 490454036 191 NAPMTAiNQQYQQKDPTftlcgSDRIHPDNDG 222
Cdd:cd01828  131 WAVFTN-ADGDLKNEFT-----TDGLHLNAKG 156
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
33-230 6.42e-13

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 67.60  E-value: 6.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036   33 VFLGNSITDGGHYHSY-------IWLYYMTRFPDMP----IRVFNGGIGGDTAYDMN------KRLDGDI-FAMKPSVLM 94
Cdd:pfam00657   2 VAFGDSLTDGGGDGPGgrfswgdLLADFLARKLGVPgsgyNHGANFAIGGATIEDLPiqleqlLRLISDVkDQAKPDLVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036   95 VTFGMNDSGYFEYNGDKPKEFGEQKYQESIKNYQQMEKRFKDLPDTRIVMVGTSPydetvqlkENTPFKTKNETIKRLVE 174
Cdd:pfam00657  82 IFIGANDLCNFLSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTP--------PKGCYELYNALAEEYNE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  175 YQKESAAKNNWEFTDLNAPMTAINQQYQQKDPtftLCG----SDRIHPDNDGHMVMAYLF 230
Cdd:pfam00657 154 RLNELVNSLAAAAEDANVVYVDIYGFEDPTDP---CCGiglePDGLHPSEKGYKAVAEAI 210
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 35-227 1.56e-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: 51.29  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  35 LGNSITDGGHYHSYIwlYYMTRFPDM---PIRVFNGGIGGDTAYD------MNKRLDGDIFAMKPSVLMVTFGMNDSgyf 105
Cdd:cd01827    6 VGNSITEGAGLRAYD--SYPSPLAQMlgdGYEVGNFGKSARTVLNkgdhpyMNEERYKNALAFNPNIVIIKLGTNDA--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 106 eyngdKPKEFgeqKYQESI-KNYQQMEKRFKDLPDT-RIVMVGTSP-YDetvqlkeNTPFKTKNETIKR-LVEYQKESAA 181
Cdd:cd01827   81 -----KPQNW---KYKDDFkKDYETMIDSFQALPSKpKIYICYPIPaYY-------GDGGFINDNIIKKeIQPMIDKIAK 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490454036 182 KNNWEFTDLNAPMTAinqqyqqKDPtftlCGSDRIHPDNDGHMVMA 227
Cdd:cd01827  146 KLNLKLIDLHTPLKG-------KPE----LVPDWVHPNEKGAYILA 180
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 58-231 1.08e-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: 238873  Cd Length: 193  Bit Score: 48.87  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  58 PDMPIRVFNGGIGGDTAYDMNKRL--------DGDifamKPSVLMVTFGMNDSGyfEYNGDKPKefgeQKYQESIKNYQQ 129
Cdd:cd01835   34 LGDDPVLYNLGVRGDGSEDVAARWraewsrrgELN----VPNRLVLSVGLNDTA--RGGRKRPQ----LSARAFLFGLNQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 130 MEKRFKDLpdTRIVMVGTSPYDETVQlkentPFKtkNETIKRLVEYQKESAAKNNWEFTDLNAPMTAiNQQYQQKdptft 209
Cdd:cd01835  104 LLEEAKRL--VPVLVVGPTPVDEAKM-----PYS--NRRIARLETAFAEVCLRRDVPFLDTFTPLLN-HPQWRRE----- 168

                        170       180
                 ....*....|....*....|..
gi 490454036 210 LCGSDRIHPDNDGHMVMAYLFL 231
Cdd:cd01835  169 LAATDGIHPNAAGYGWLAWLVL 190
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 33-217 6.21e-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: 46.86  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  33 VFLGNSIT------DGGHYHSYIWLYYMTRFpdmpiRVFNGGIGGDTAYDMNKRLDGDIF---AMKPSVLMVTFGMNDSG 103
Cdd:cd01838    3 VLFGDSITqfsfdqGEFGFGAALADVYSRKL-----DVINRGFSGYNTRWALKVLPKIFLeekLAQPDLVTIFFGANDAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 104 YFEYNGDKPkefgEQKYQESIKNYQQMEKRFkdLPDTRIVMVGTSPYDETVQLKEN-----TPFKTkNETIKRLVEYQKE 178
Cdd:cd01838   78 LPGQPQHVP----LDEYKENLRKIVSHLKSL--SPKTKVILITPPPVDEEAWEKSLedggsQPGRT-NELLKQYAEACVE 150

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490454036 179 SAAKNNWEFTDLNAPMtainqqyQQKDPTFTLCGSDRIH 217
Cdd:cd01838  151 VAEELGVPVIDLWTAM-------QEEAGWLESLLTDGLH 182
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 31-233 6.28e-06

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: 46.50  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  31 RAVFLGNSITDGGhyhsyiwlyymtRFPD-----MPIRVFNGGIGGDTAYDMNK----RLDGDIFAMKPSVLMVTFGMND 101
Cdd:cd01825    1 RIAQLGDSHIAGD------------FFTDvlrglLGVIYDNLGVNGASASLLLKwdaeFLQAQLAALPPDLVILSYGTNE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 102 SGYFEYNgdkpkefgEQKYQesiKNYQQMEKRFKD-LPDTRIVMVGTSPydeTVQLKENTPFKTkNETIKRLVEYQKESA 180
Cdd:cd01825   69 AFNKQLN--------ASEYR---QQLREFIKRLRQiLPNASILLVGPPD---SLQKTGAGRWRT-PPGLDAVIAAQRRVA 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490454036 181 AKNNWEFTDLNAPM--TAINQQYQQKDptftLCGSDRIHPDNDGHMVMAYLFLKA 233
Cdd:cd01825  134 KEEGIAFWDLYAAMggEGGIWQWAEPG----LARKDYVHLTPRGYERLANLLYEA 184
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 33-191 8.44e-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: 43.09  E-value: 8.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  33 VFLGNSITDGghyhsyiWLYYmtRFPDMPIRVFNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDSGyfeyNGDKP 112
Cdd:cd01841    4 VFIGDSLFEG-------WPLY--EAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIG----KEVSS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 113 KEFgeqkyqesIKNYQQMEKRFK-DLPDTRIVMVGTSPydetvqLKENTPFKTKNET-IKRLVEYQKESAAKNNWEFTDL 190
Cdd:cd01841   71 NQF--------IKWYRDIIEQIReEFPNTKIYLLSVLP------VLEEDEIKTRSNTrIQRLNDAIKELAPELGVTFIDL 136


                 .
gi 490454036 191 N 191
Cdd:cd01841  137 N 137
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 57-217 8.13e-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: 39.96  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036  57 FPDMPIRvfNGGIGGDTAYDMNKRLDGDIFAMKPSVLMVTFGMNDSGyfeyNGDKPKEFgEQKYQESIKNYQQmekrfkD 136
Cdd:cd04502   20 LAPLPVV--NRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLA----SGRTPEEV-LRDFRELVNRIRA------K 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490454036 137 LPDTRIVMVGTSPYDETVQLKENtpFKTKNETIKRLVEyqkesaAKNNWEFTDLNAPMTAinqqyQQKDPTFTLCGSDRI 216
Cdd:cd04502   87 LPDTPIAIISIKPSPARWALRPK--IRRFNALLKELAE------TRPNLTYIDVASPMLD-----ADGKPRAELFQEDGL 153


                 .
gi 490454036 217 H 217
Cdd:cd04502  154 H 154
 
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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