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Conserved domains on  [gi|499327256|ref|WP_011017748|]
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SGNH/GDSL hydrolase family protein [Streptococcus pyogenes]

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 ...
 30-204 1.65e-64

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: 196.78  E-value: 1.65e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  30 GGIVFAGDSLIEFFPLKKAFGSCLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDIGLGYDKCHIVKTIVEL 109
Cdd:cd01841    1 KNIVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSSNQFIKWYRDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256 110 ISQIRSHCVYSQIYLLSLLPVSN---NPRYQKTVKIRTNAMIDAINKDLAmiptIEFINLNTCLKDEKGGLSDENTLDGL 186
Cdd:cd01841   81 IEQIREEFPNTKIYLLSVLPVLEedeIKTRSNTRIQRLNDAIKELAPELG----VTFIDLNDVLVDEFGNLKKEYTTDGL 156

                        170
                 ....*....|....*...
gi 499327256 187 HLNFPAYAKLAEIIQSYI 204
Cdd:cd01841  157 HFNPKGYQKLLEILEEYL 174
 
Name Accession Description Interval E-value
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 30-204 1.65e-64

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: 196.78  E-value: 1.65e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  30 GGIVFAGDSLIEFFPLKKAFGSCLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDIGLGYDKCHIVKTIVEL 109
Cdd:cd01841    1 KNIVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSSNQFIKWYRDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256 110 ISQIRSHCVYSQIYLLSLLPVSN---NPRYQKTVKIRTNAMIDAINKDLAmiptIEFINLNTCLKDEKGGLSDENTLDGL 186
Cdd:cd01841   81 IEQIREEFPNTKIYLLSVLPVLEedeIKTRSNTRIQRLNDAIKELAPELG----VTFIDLNDVLVDEFGNLKKEYTTDGL 156

                        170
                 ....*....|....*...
gi 499327256 187 HLNFPAYAKLAEIIQSYI 204
Cdd:cd01841  157 HFNPKGYQKLLEILEEYL 174
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 32-204 1.54e-21

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: 87.39  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  32 IVFAGDSLIEFFPLKKAFG-----------SCLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDI--GLGYD 98
Cdd:COG2755   11 IVALGDSITAGYGASRERGwpallarrlaaADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLlrGLGVS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  99 KCHIVKTIVELISQIRSHCVYSQIYLLSLLPVSNNPRYQKTVKiRTNAMIDAINKDLAmiptIEFINLNTCLKDEkGGLS 178
Cdd:COG2755   91 PEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIE-AYNAAIRELAAEYG----VPLVDLYAALRDA-GDLP 164

                        170       180
                 ....*....|....*....|....*.
gi 499327256 179 DENTLDGLHLNFPAYAKLAEIIQSYI 204
Cdd:COG2755  165 DLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 55-189 5.37e-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: 72.19  E-value: 5.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256   55 IINRGIAG--IDSQWLLRHFSVQitDLEPKHIFLLIGCNDIGLGYDKCHIVKTIVELISQIRSHCVYSQIYLLSLLPVSN 132
Cdd:pfam13472  36 VNNLGISGatTRLDLLERLDDVL--RLKPDLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGP 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499327256  133 NPRYQKTVKIRTNAMIDAINKDLAMIPTIEFINLNTCLKDEKGGLSDENTLDGLHLN 189
Cdd:pfam13472 114 PPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGWLPDLLADDGLHPN 170
 
Name Accession Description Interval E-value
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 30-204 1.65e-64

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: 196.78  E-value: 1.65e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  30 GGIVFAGDSLIEFFPLKKAFGSCLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDIGLGYDKCHIVKTIVEL 109
Cdd:cd01841    1 KNIVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSSNQFIKWYRDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256 110 ISQIRSHCVYSQIYLLSLLPVSN---NPRYQKTVKIRTNAMIDAINKDLAmiptIEFINLNTCLKDEKGGLSDENTLDGL 186
Cdd:cd01841   81 IEQIREEFPNTKIYLLSVLPVLEedeIKTRSNTRIQRLNDAIKELAPELG----VTFIDLNDVLVDEFGNLKKEYTTDGL 156

                        170
                 ....*....|....*...
gi 499327256 187 HLNFPAYAKLAEIIQSYI 204
Cdd:cd01841  157 HFNPKGYQKLLEILEEYL 174
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 32-204 1.39e-34

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: 120.46  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  32 IVFAGDSLIEFFPLKKAFGScLPIINRGIAGIDSQWLLRHFSvQITDLEPKHIFLLIGCNDIGLGYDKCHIVKTIVELIS 111
Cdd:cd01828    2 LVFLGDSLTEGGPWALLFPD-VKVANRGISGDTTRGLLARLD-EDVALQPKAIFIMIGINDLAQGTSDEDIVANYRTILE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256 112 QIRSHCVYSQIYLLSLLPVSNNPRyqktvkiRTNAMIDAINKDLAMI---PTIEFINLNTCLKDEKGGLSDENTLDGLHL 188
Cdd:cd01828   80 KLRKHFPNIKIVVQSILPVGELKS-------IPNEQIEELNRQLAQLaqqEGVTFLDLWAVFTNADGDLKNEFTTDGLHL 152

                        170
                 ....*....|....*.
gi 499327256 189 NFPAYAKLAEIIQSYI 204
Cdd:cd01828  153 NAKGYAVWAAALQPYL 168
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 32-204 1.54e-21

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: 87.39  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  32 IVFAGDSLIEFFPLKKAFG-----------SCLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDI--GLGYD 98
Cdd:COG2755   11 IVALGDSITAGYGASRERGwpallarrlaaADVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLlrGLGVS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  99 KCHIVKTIVELISQIRSHCVYSQIYLLSLLPVSNNPRYQKTVKiRTNAMIDAINKDLAmiptIEFINLNTCLKDEkGGLS 178
Cdd:COG2755   91 PEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIE-AYNAAIRELAAEYG----VPLVDLYAALRDA-GDLP 164

                        170       180
                 ....*....|....*....|....*.
gi 499327256 179 DENTLDGLHLNFPAYAKLAEIIQSYI 204
Cdd:COG2755  165 DLLTADGLHPNAAGYRLIAEAVLPAL 190
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 31-204 5.97e-19

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: 80.02  E-value: 5.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  31 GIVFAGDSLIEFFPLKKAFGSCLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDIGLGYDKCHIVKTIVELI 110
Cdd:cd04502    1 GILFYGSSSIRLWDTLADDLAPLPVVNRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTPEEVLRDFRELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256 111 SQIRSHCVYSQIYLLSLLPvsNNPRYQKTVKI-RTNAMIdainKDLAM-IPTIEFINLNTCLKDEKGGLSDENTL-DGLH 187
Cdd:cd04502   81 NRIRAKLPDTPIAIISIKP--SPARWALRPKIrRFNALL----KELAEtRPNLTYIDVASPMLDADGKPRAELFQeDGLH 154

                        170
                 ....*....|....*..
gi 499327256 188 LNFPAYAKLAEIIQSYI 204
Cdd:cd04502  155 LNDAGYALWRKVIKPAL 171
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 55-189 5.37e-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: 72.19  E-value: 5.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256   55 IINRGIAG--IDSQWLLRHFSVQitDLEPKHIFLLIGCNDIGLGYDKCHIVKTIVELISQIRSHCVYSQIYLLSLLPVSN 132
Cdd:pfam13472  36 VNNLGISGatTRLDLLERLDDVL--RLKPDLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGP 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499327256  133 NPRYQKTVKIRTNAMIDAINKDLAMIPTIEFINLNTCLKDEKGGLSDENTLDGLHLN 189
Cdd:pfam13472 114 PPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGWLPDLLADDGLHPN 170
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 32-204 2.77e-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.


Pssm-ID: 239945  Cd Length: 183  Bit Score: 70.43  E-value: 2.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  32 IVFAGDSLIEFFP---------LKKAFGScLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDIGLGYDKCHI 102
Cdd:cd04501    3 VVCLGDSITYGYPvgpeaswvnLLAEFLG-KEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNTSLEMI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256 103 VKTIVELISQIRSHcvYSQIYLLSLLPVSN---NPRYQKTVK--IRTNAMIdainKDLAMIPTIEFINLNTCLKDEK-GG 176
Cdd:cd04501   82 KDNIRSMVELAEAN--GIKVILASPLPVDDypwKPQWLRPANklKSLNRWL----KDYARENGLLFLDFYSPLLDERnVG 155

                        170       180
                 ....*....|....*....|....*...
gi 499327256 177 LSDENTLDGLHLNFPAYAKLAEIIQSYI 204
Cdd:cd04501  156 LKPGLLTDGLHPSREGYRVMAPLAEKAL 183
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 10-204 1.33e-14

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: 69.24  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  10 RHyqEQKLIEYRNKNqlaPKggIVFAGDSLI---EFFPL---KKAFGScLPIINRGIAGIDSQ---WLLRHFsvQITDLE 80
Cdd:cd01820   20 RH--ERFVAEAKQKE---PD--VVFIGDSITqnwEFTGLevwRELYAP-LHALNFGIGGDRTQnvlWRLENG--ELDGVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  81 PKHIFLLIGCNDIGLGYDKCHIVKTIVELISQIRSHCVYSQIYLLSLLPvsnnpRYQKTVKIRtnAMIDAINKDLAM--- 157
Cdd:cd01820   90 PKVVVLLIGTNNIGHTTTAEEIAEGILAIVEEIREKLPNAKILLLGLLP-----RGQNPNPLR--ERNAQVNRLLAVryd 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499327256 158 -IPTIEFINLNTCLKDEKGGLSDENTLDGLHLNFPAYAKLAEIIQSYI 204
Cdd:cd01820  163 gLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTL 210
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 32-203 6.81e-14

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: 67.05  E-value: 6.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  32 IVFAGDSLIE--------------FFPLKKAFGSCLPIINRGIAGIDSQWLLRHFSV--QITDLEPKHIFLLIGCNDIGL 95
Cdd:cd00229    1 ILVIGDSITAgygassgstfysllLYLLLLAGGPGVEVINLGVSGATTADALRRLGLrlALLKDKPDLVIIELGTNDLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  96 GYDK--CHIVKTIVELISQIRSHCVYSQIYLLSLLPVSNNPRYQKTVKIRTNAMIDAINKDLAMIPTIEFINLNTCLKDE 173
Cdd:cd00229   81 GGDTsiDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENPAPSGVDLVDLAALLGDE 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 499327256 174 KGGLsdeNTLDGLHLNFPAYAKLAEIIQSY 203
Cdd:cd00229  161 DKSL---YSPDGIHPNPAGHKLIAEALASA 187
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 32-200 4.11e-09

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: 54.18  E-value: 4.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  32 IVFAGDSLIEFF----------PLKKAFGSCLPIINRGIAGIDSQWLLR---HFSVQITDLEPKHIFLLIGCNDIGLGYD 98
Cdd:cd01838    2 IVLFGDSITQFSfdqgefgfgaALADVYSRKLDVINRGFSGYNTRWALKvlpKIFLEEKLAQPDLVTIFFGANDAALPGQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  99 KCHI-----VKTIVELISQIRSHCVYSQIYLLSLLPVsNNPRYQKTV------KIRTNAMI----DAInKDLAMIPTIEF 163
Cdd:cd01838   82 PQHVpldeyKENLRKIVSHLKSLSPKTKVILITPPPV-DEEAWEKSLedggsqPGRTNELLkqyaEAC-VEVAEELGVPV 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 499327256 164 INLNTCLKDEKGGLSDENTlDGLHLNFPAYAKLAEII 200
Cdd:cd01838  160 IDLWTAMQEEAGWLESLLT-DGLHFSSKGYELLFEEI 195
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 32-200 1.54e-07

SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238872  Cd Length: 191  Bit Score: 49.60  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  32 IVFAGDSLIE------FFP--LKKAF-GSCLPIINRGIAGIDSQWLLRHFSVQITDLEPKHIFLLIGCNDIGLGYDKCHI 102
Cdd:cd01834    4 IVFIGNSITDrggyvgYVEtyLAARYpELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDSFRGFDDPVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256 103 V----KTIVELISQIRSHCVYSQIYLLSLLPVSNNPR-------YQKTVKIRTNAMidainKDLAMIPTIEFINLNTCLK 171
Cdd:cd01834   84 LekfkTNLRRLIDRLKNKESAPRIVLVSPIAYEANEDplpdgaeYNANLAAYADAV-----RELAAENGVAFVDLFTPMK 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 499327256 172 DEKGGLSDEN-TLDGLHLNFPAYAKLAEII 200
Cdd:cd01834  159 EAFQKAGEAVlTVDGVHPNEAGHRALARLW 188
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
36-200 2.65e-06

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 46.41  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256   36 GDSLIEFFPLKKAF--GSCLPIINRGIAGIDSQWL---LRHFSVQITD----LEPKHIFLLIGCNDIGLGY-----DKCH 101
Cdd:pfam00657  23 GDLLADFLARKLGVpgSGYNHGANFAIGGATIEDLpiqLEQLLRLISDvkdqAKPDLVTIFIGANDLCNFLssparSKKR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  102 IVKTIVELISQIRSHCVYSQIYLLSLL-PVSNNP------RYQKTVKI---RTNAMIDAINKDLAMiPTIEFINLNTCLK 171
Cdd:pfam00657 103 VPDLLDELRANLPQLGLGARKFWVHGLgPLGCTPpkgcyeLYNALAEEyneRLNELVNSLAAAAED-ANVVYVDIYGFED 181

                         170       180
                  ....*....|....*....|....*....
gi 499327256  172 DEKGGLSDENTLDGLHLNFPAYAKLAEII 200
Cdd:pfam00657 182 PTDPCCGIGLEPDGLHPSEKGYKAVAEAI 210
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 84-199 1.01e-05

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: 43.76  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499327256  84 IFLLIGCNDIGLGYDkchiVKTIVE----LISQIRSHCVYSQIYLLSLLPVSNNPRYQKTVKIrtNAMIDAINKDLAmip 159
Cdd:cd01833   44 VLLHLGTNDLVLNRD----PDTAPDrlraLIDQMRAANPDVKIIVATLIPTTDASGNARIAEY--NAAIPGVVADLR--- 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499327256 160 T----IEFINLNTCLkdekggLSDENTLDGLHLNFPAYAKLAEI 199
Cdd:cd01833  115 TagspVVLVDMSTGY------TTADDLYDGLHPNDQGYKKMADA 152
 
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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