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Conserved domains on  [gi|2292857777|gb|UVT91488|]
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SGNH/GDSL hydrolase family protein [Streptococcus mutans]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110892)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 41-213 2.02e-68

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: 207.18  E-value: 2.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFFPLKKYLGHDLPLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRGYPLSDIVARISNIIA 120
Cdd:cd01841     3 IVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSSNQFIKWYRDIIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 121 QIRANHILTKIYVLSVLPVNESDQ---YAGKVKIRNNALIQVLNHHLqvlsGVNYIDLYPLLLDEKGELAEDYTTDGLHL 197
Cdd:cd01841    83 QIREEFPNTKIYLLSVLPVLEEDEiktRSNTRIQRLNDAIKELAPEL----GVTFIDLNDVLVDEFGNLKKEYTTDGLHF 158

                         170
                  ....*....|....*.
gi 2292857777 198 TQTAYDKIAQTIKTDL 213
Cdd:cd01841   159 NPKGYQKLLEILEEYL 174
 
Name Accession Description Interval E-value
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 41-213 2.02e-68

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: 207.18  E-value: 2.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFFPLKKYLGHDLPLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRGYPLSDIVARISNIIA 120
Cdd:cd01841     3 IVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSSNQFIKWYRDIIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 121 QIRANHILTKIYVLSVLPVNESDQ---YAGKVKIRNNALIQVLNHHLqvlsGVNYIDLYPLLLDEKGELAEDYTTDGLHL 197
Cdd:cd01841    83 QIREEFPNTKIYLLSVLPVLEEDEiktRSNTRIQRLNDAIKELAPEL----GVTFIDLNDVLVDEFGNLKKEYTTDGLHF 158

                         170
                  ....*....|....*.
gi 2292857777 198 TQTAYDKIAQTIKTDL 213
Cdd:cd01841   159 NPKGYQKLLEILEEYL 174
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 37-209 2.75e-40

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: 135.93  E-value: 2.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  37 KADSIVFAGDSITEFFP----------LKKYLG-HDLPLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRG 105
Cdd:COG2755     7 KPLRIVALGDSITAGYGasrergwpalLARRLAaADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLLRG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 106 Y--PLSDIVARISNIIAQIRANHILTKIYVLSVLPVNESDQYAGKVKIRNNALIQVLNHHlqvlsGVNYIDLYPLLLDEk 183
Cdd:COG2755    87 LgvSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAIRELAAEY-----GVPLVDLYAALRDA- 160

                         170       180
                  ....*....|....*....|....*.
gi 2292857777 184 GELAEDYTTDGLHLTQTAYDKIAQTI 209
Cdd:COG2755   161 GDLPDLLTADGLHPNAAGYRLIAEAV 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 43-204 1.40e-27

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: 103.01  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  43 FAGDSITE-------------FFP--LKKYLGHDLpLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRGYP 107
Cdd:pfam13472   1 ALGDSITAgygatggdrsypgWLArlLARRLGADV-VNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 108 LSDIVARISNIIAQIRANHILTKIYVLSVLPVNESDQYAGKvkiRNNALIQVLNHHLQVLS---GVNYIDLYPLLLDEKG 184
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLDER---RLNARIAEYNAAIREVAaerGVPYVDLWDALRDDGG 156

                         170       180
                  ....*....|....*....|
gi 2292857777 185 ELAEDYTTDGLHLTQTAYDK 204
Cdd:pfam13472 157 WLPDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 41-213 2.02e-68

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: 207.18  E-value: 2.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFFPLKKYLGHDLPLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRGYPLSDIVARISNIIA 120
Cdd:cd01841     3 IVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSSNQFIKWYRDIIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 121 QIRANHILTKIYVLSVLPVNESDQ---YAGKVKIRNNALIQVLNHHLqvlsGVNYIDLYPLLLDEKGELAEDYTTDGLHL 197
Cdd:cd01841    83 QIREEFPNTKIYLLSVLPVLEEDEiktRSNTRIQRLNDAIKELAPEL----GVTFIDLNDVLVDEFGNLKKEYTTDGLHF 158

                         170
                  ....*....|....*.
gi 2292857777 198 TQTAYDKIAQTIKTDL 213
Cdd:cd01841   159 NPKGYQKLLEILEEYL 174
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 41-210 4.59e-46

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: 150.12  E-value: 4.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFFPLKKYLGhDLPLVNRGIAGTDSVWLLEHIeDQVLTLSPAKVFLMIGINDIGRGYPLSDIVARISNIIA 120
Cdd:cd01828     2 LVFLGDSLTEGGPWALLFP-DVKVANRGISGDTTRGLLARL-DEDVALQPKAIFIMIGINDLAQGTSDEDIVANYRTILE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 121 QIRANHILTKIYVLSVLPVnesdqyaGKVKIRNNALIQVLNHHLQVL---SGVNYIDLYPLLLDEKGELAEDYTTDGLHL 197
Cdd:cd01828    80 KLRKHFPNIKIVVQSILPV-------GELKSIPNEQIEELNRQLAQLaqqEGVTFLDLWAVFTNADGDLKNEFTTDGLHL 152

                         170
                  ....*....|...
gi 2292857777 198 TQTAYDKIAQTIK 210
Cdd:cd01828   153 NAKGYAVWAAALQ 165
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 37-209 2.75e-40

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: 135.93  E-value: 2.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  37 KADSIVFAGDSITEFFP----------LKKYLG-HDLPLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRG 105
Cdd:COG2755     7 KPLRIVALGDSITAGYGasrergwpalLARRLAaADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLLRG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 106 Y--PLSDIVARISNIIAQIRANHILTKIYVLSVLPVNESDQYAGKVKIRNNALIQVLNHHlqvlsGVNYIDLYPLLLDEk 183
Cdd:COG2755    87 LgvSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAIRELAAEY-----GVPLVDLYAALRDA- 160

                         170       180
                  ....*....|....*....|....*.
gi 2292857777 184 GELAEDYTTDGLHLTQTAYDKIAQTI 209
Cdd:COG2755   161 GDLPDLLTADGLHPNAAGYRLIAEAV 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 43-204 1.40e-27

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: 103.01  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  43 FAGDSITE-------------FFP--LKKYLGHDLpLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRGYP 107
Cdd:pfam13472   1 ALGDSITAgygatggdrsypgWLArlLARRLGADV-VNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 108 LSDIVARISNIIAQIRANHILTKIYVLSVLPVNESDQYAGKvkiRNNALIQVLNHHLQVLS---GVNYIDLYPLLLDEKG 184
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLDER---RLNARIAEYNAAIREVAaerGVPYVDLWDALRDDGG 156

                         170       180
                  ....*....|....*....|
gi 2292857777 185 ELAEDYTTDGLHLTQTAYDK 204
Cdd:pfam13472 157 WLPDLLADDGLHPNAAGYRL 176
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 41-209 2.28e-23

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: 92.48  E-value: 2.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITE--------------FFPLKKYLGHDLPLVNRGIAGTDSVWLLE--HIEDQVLTLSPAKVFLMIGINDIGR 104
Cdd:cd00229     1 ILVIGDSITAgygassgstfysllLYLLLLAGGPGVEVINLGVSGATTADALRrlGLRLALLKDKPDLVIIELGTNDLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 105 G--YPLSDIVARISNIIAQIRANHILTKIYVLSVLPVNESDQYAGKVKIRNNALIQVLNHHLQVLSGVNYIDLYPLLlde 182
Cdd:cd00229    81 GgdTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENPAPSGVDLVDLAALL--- 157

                         170       180
                  ....*....|....*....|....*..
gi 2292857777 183 KGELAEDYTTDGLHLTQTAYDKIAQTI 209
Cdd:cd00229   158 GDEDKSLYSPDGIHPNPAGHKLIAEAL 184
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 41-207 5.55e-23

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: 91.23  E-value: 5.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFFP----------LKKYLGhdLPLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRGYPLSD 110
Cdd:cd04501     3 VVCLGDSITYGYPvgpeaswvnlLAEFLG--KEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNTSLEM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 111 IVARISNIIAQIRANHIltKIYVLSVLPVNE--SDQYAGKVKIRNNALIQVLNHHLQVLsGVNYIDLYPLLLDEK-GELA 187
Cdd:cd04501    81 IKDNIRSMVELAEANGI--KVILASPLPVDDypWKPQWLRPANKLKSLNRWLKDYAREN-GLLFLDFYSPLLDERnVGLK 157

                         170       180
                  ....*....|....*....|
gi 2292857777 188 EDYTTDGLHLTQTAYDKIAQ 207
Cdd:cd04501   158 PGLLTDGLHPSREGYRVMAP 177
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 41-210 2.76e-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: 78.48  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFFPLKKYLGHDLPLVNRGIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGINDIGRGYPLSDIVARISNIIA 120
Cdd:cd04502     2 ILFYGSSSIRLWDTLADDLAPLPVVNRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTPEEVLRDFRELVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 121 QIRANHILTKIYVLSVLPVNESDQYAGKVKiRNNALIQVLNHHlqvLSGVNYIDLYPLLLDEKGEL-AEDYTTDGLHLTQ 199
Cdd:cd04502    82 RIRAKLPDTPIAIISIKPSPARWALRPKIR-RFNALLKELAET---RPNLTYIDVASPMLDADGKPrAELFQEDGLHLND 157

                         170
                  ....*....|.
gi 2292857777 200 TAYDKIAQTIK 210
Cdd:cd04502   158 AGYALWRKVIK 168
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 31-209 6.28e-18

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: 78.49  E-value: 6.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  31 KANSKVKADSIVFAGDSIT---EFFPL---KKYLGHdLPLVNRGIAG--TDSV-WLLEHIE-DQVltlSPAKVFLMIGIN 100
Cdd:cd01820    25 VAEAKQKEPDVVFIGDSITqnwEFTGLevwRELYAP-LHALNFGIGGdrTQNVlWRLENGElDGV---NPKVVVLLIGTN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 101 DIGRGYPLSDIVARISNIIAQIRANHILTKIYVLSVLPvneSDQYAGKVKIRNNALIQVLNHHLQVLSGVNYIDLYPLLL 180
Cdd:cd01820   101 NIGHTTTAEEIAEGILAIVEEIREKLPNAKILLLGLLP---RGQNPNPLRERNAQVNRLLAVRYDGLPNVTFLDIDKGFV 177

                         170       180
                  ....*....|....*....|....*....
gi 2292857777 181 DEKGELAEDYTTDGLHLTQTAYDKIAQTI 209
Cdd:cd01820   178 QSDGTISHHDMPDYLHLTAAGYRKWADAL 206
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 45-207 3.10e-17

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: 75.35  E-value: 3.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  45 GDSITEffplkkylGHDlplVNRGIAGtdsvWLLEHIEDQVLTLS----PAKVFLMIGINDIGRGYPLSDIVARISNIIA 120
Cdd:cd01833     7 GDSITW--------GDK---DHEGHSG----YLIDQIAAAAADWVlaakPDVVLLHLGTNDLVLNRDPDTAPDRLRALID 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 121 QIRANHILTKIYVLSVLPVNESDQYAgKVKIRNNALIQVLNHHLQVLSGVNYIDLYPLLLDekgelAEDYtTDGLHLTQT 200
Cdd:cd01833    72 QMRAANPDVKIIVATLIPTTDASGNA-RIAEYNAAIPGVVADLRTAGSPVVLVDMSTGYTT-----ADDL-YDGLHPNDQ 144


                  ....*..
gi 2292857777 201 AYDKIAQ 207
Cdd:cd01833   145 GYKKMAD 151
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 39-209 8.94e-17

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: 75.02  E-value: 8.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  39 DSIVFAGDSITE------FFPL---KKYLGHDLPLVNRGIAGtDSVW-LLEHIEDQVLTLSPAKVFLMIGINDIGRGYPL 108
Cdd:cd01834     2 DRIVFIGNSITDrggyvgYVETylaARYPELKLTFRNLGWSG-DTVSdLAARRDRDVLPAKPDVVSIMFGINDSFRGFDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 109 SDIVARISN----IIAQIRANHILTKIYVLS-------VLPVNESDQYAGKVKIRNNALIQVLNHHlqvlsGVNYIDLYP 177
Cdd:cd01834    81 PVGLEKFKTnlrrLIDRLKNKESAPRIVLVSpiayeanEDPLPDGAEYNANLAAYADAVRELAAEN-----GVAFVDLFT 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2292857777 178 LLLDE-KGELAEDYTTDGLHLTQTAYDKIAQTI 209
Cdd:cd01834   156 PMKEAfQKAGEAVLTVDGVHPNEAGHRALARLW 188
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 41-209 3.91e-16

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: 73.44  E-value: 3.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFF----------PLKKYLGHDLPLVNRGIAGTDSVWLLE---HIEDQVLTLSPAKVFLMIGINDI---GR 104
Cdd:cd01838     2 IVLFGDSITQFSfdqgefgfgaALADVYSRKLDVINRGFSGYNTRWALKvlpKIFLEEKLAQPDLVTIFFGANDAalpGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 105 GY--PLSDIVARISNIIAQIRANHILTKIYVLSVLPVNE-----SDQYAGKVKIRNNALIQVLNHHLQVL---SGVNYID 174
Cdd:cd01838    82 PQhvPLDEYKENLRKIVSHLKSLSPKTKVILITPPPVDEeawekSLEDGGSQPGRTNELLKQYAEACVEVaeeLGVPVID 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2292857777 175 LYPLLLDEKGELaEDYTTDGLHLTQTAYDKIAQTI 209
Cdd:cd01838   162 LWTAMQEEAGWL-ESLLTDGLHFSSKGYELLFEEI 195
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
41-206 2.58e-11

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 60.66  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITEFF----------------PLKKYLGHDLP----LVNRGIAGTDSVW-------LLEHIEDQVLTLSPAKV 93
Cdd:pfam00657   1 IVAFGDSLTDGGgdgpggrfswgdlladFLARKLGVPGSgynhGANFAIGGATIEDlpiqleqLLRLISDVKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  94 FLMIGINDIGRGY-PLSDIVARISNIIAQIRAN----------HILTKIYVLSVLPVNESDQ-YAGKVKIRNNALIQVLN 161
Cdd:pfam00657  81 TIFIGANDLCNFLsSPARSKKRVPDLLDELRANlpqlglgarkFWVHGLGPLGCTPPKGCYElYNALAEEYNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2292857777 162 HHLQVLSGVN--YIDLYPLLLDEKGELAEDYTTDGLHLTQTAYDKIA 206
Cdd:pfam00657 161 SLAAAAEDANvvYVDIYGFEDPTDPCCGIGLEPDGLHPSEKGYKAVA 207
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 39-213 3.25e-09

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: 54.06  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  39 DSIVFAGDSIT--------EFFP--LKKYL---GHDLPLVNRGIAGTDSV-------WLLEHIEdqvltlsPAKVFLMIG 98
Cdd:cd01822     1 VTILALGDSLTagyglppeEGWPalLQKRLdarGIDVTVINAGVSGDTTAgglarlpALLAQHK-------PDLVILELG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  99 INDIGRGYPLSDIVARISNIIAQIRANhiltKIYVLSV---LPVNESDQYAGKVkirnNALIQVLNHHLQVLsgvnyidL 175
Cdd:cd01822    74 GNDGLRGIPPDQTRANLRQMIETAQAR----GAPVLLVgmqAPPNYGPRYTRRF----AAIYPELAEEYGVP-------L 138

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2292857777 176 YPLLLDEKGELAEDYTTDGLHLTQTAYDKIAQTIKTDL 213
Cdd:cd01822   139 VPFFLEGVAGDPELMQSDGIHPNAEGQPIIAENVWPAL 176
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 90-210 5.09e-08

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: 51.18  E-value: 5.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  90 PAKVFLMIGIND---IGRGYPLSDIVARISNIIAQIRANHILTKIYVLSVLPVNESDQYAgkvkirNNALIQVLNhhlQV 166
Cdd:cd01835    70 PNRLVLSVGLNDtarGGRKRPQLSARAFLFGLNQLLEEAKRLVPVLVVGPTPVDEAKMPY------SNRRIARLE---TA 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2292857777 167 LS------GVNYIDLYPLLLDEKGELAEDYTTDGLHLTQTAYDKIAQTIK 210
Cdd:cd01835   141 FAevclrrDVPFLDTFTPLLNHPQWRRELAATDGIHPNAAGYGWLAWLVL 190
SGNH_hydrolase_peri2 cd01829
SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 41-209 2.19e-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: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  41 IVFAGDSITE--FFPLKKYLG--HDLPLVNR-----GIAGTDSVWLLEHIEDQVLTLSPAKVFLMIGIND-----IGRGY 106
Cdd:cd01829     2 VLVIGDSLAQglAPGLLRALAdnPGIRVINRskgssGLVRPDFFDWPEKLKELIAEEKPDVVVVFLGANDrqdirDGDGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 107 --PLSDivaRISNIIAQiRANHILT-----KIYVLSV-LPVNESDQYAGKVKIRNNALIQvlnhHLQVLSGVnYIDLYPL 178
Cdd:cd01829    82 lkFGSP---EWEEEYRQ-RIDELLNvarakGVPVIWVgLPAMRSPKLSADMVYLNSLYRE----EVAKAGGE-FVDVWDG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2292857777 179 LLDEKGELAeDYTT------------DGLHLTQTAYDKIAQTI 209
Cdd:cd01829   153 FVDENGRFT-YSGTdvngkkvrlrtnDGIHFTAAGGRKLAFYV 194
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 66-207 5.96e-05

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: 42.26  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  66 NRGIAGtdsvWLLEHI-EDQV---LTLSPAKVFLMIGINDIGR-GYPLSDIVARISNIIAQIRANHIltKIYVLSVLPVN 140
Cdd:cd01832    44 NLAVRG----RRTAQIlAEQLpaaLALRPDLVTLLAGGNDILRpGTDPDTYRADLEEAVRRLRAAGA--RVVVFTIPDPA 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777 141 ESDQYAGKVKIRnnalIQVLNHHLQVLS---GVNYIDLYpllLDEKGELAEDYTTDGLHLTQTAYDKIAQ 207
Cdd:cd01832   118 VLEPFRRRVRAR----LAAYNAVIRAVAaryGAVHVDLW---EHPEFADPRLWASDRLHPSAAGHARLAA 180
SGNH_hydrolase_like_6 cd01844
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 61-207 2.24e-04

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: 40.38  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292857777  61 DLPLVNRGIAGTDsvwLLEHIEDQVLTLSPAKVF-LMIGINDIGrgyPLSDIVARISNIIAQIRANHILTKIYVLS--VL 137
Cdd:cd01844    31 GLEVINLGFSGNA---RLEPEVAELLRDVPADLYiIDCGPNIVG---AEAMVRERLGPLVKGLRETHPDTPILLVSprYC 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2292857777 138 PVNESDQYAGKvkiRNNALIQVLNHHLQVL-----SGVNYIDLYPLLLDEkgelaEDYTTDGLHLTQTAYDKIAQ 207
Cdd:cd01844   105 PDAELTPGRGK---LTLAVRRALREAFEKLradgvPNLYYLDGEELLGPD-----GEALVDGIHPTDLGHMRYAD 171
 
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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