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Conserved domains on  [gi|2770876657|ref|WP_366934449|]
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SGNH/GDSL hydrolase family protein [Methylobacterium sp.]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10006586)

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.-.-
PubMed:  35871440|15522763
SCOP:  3001315

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 39-235 1.93e-33

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: 119.75  E-value: 1.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  39 TQGQAIRIVAFGSSSTEGSGASsPSTTYPAQLQRDLAARlgamgsvhsSVTVLNRGKGGDDSEAMARRLERDVLADKPDL 118
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYGAS-RERGWPALLARRLAAA---------DVRVVNAGISGATTADLLARLDRDLLALKPDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 119 VIWQTGSNDPMSG--VSVERFAELTRAGILAMRATG--ADVVLMD-QQWCKKLSTTDGAEAYGAALHAIATELNVPVIRR 193
Cdd:COG2755    74 VVIELGTNDLLRGlgVSPEEFRANLEALIDRLRAAGpgARVVLVTpPPRLRPNYLNERIEAYNAAIRELAAEYGVPLVDL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2770876657 194 NAMMRAWAAqgllsPTQMIGPDGLHMTDAGYDRLARAATAQL 235
Cdd:COG2755   154 YAALRDAGD-----LPDLLTADGLHPNAAGYRLIAEAVLPAL 190
 
Name Accession Description Interval E-value
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 39-235 1.93e-33

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: 119.75  E-value: 1.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  39 TQGQAIRIVAFGSSSTEGSGASsPSTTYPAQLQRDLAARlgamgsvhsSVTVLNRGKGGDDSEAMARRLERDVLADKPDL 118
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYGAS-RERGWPALLARRLAAA---------DVRVVNAGISGATTADLLARLDRDLLALKPDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 119 VIWQTGSNDPMSG--VSVERFAELTRAGILAMRATG--ADVVLMD-QQWCKKLSTTDGAEAYGAALHAIATELNVPVIRR 193
Cdd:COG2755    74 VVIELGTNDLLRGlgVSPEEFRANLEALIDRLRAAGpgARVVLVTpPPRLRPNYLNERIEAYNAAIRELAAEYGVPLVDL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2770876657 194 NAMMRAWAAqgllsPTQMIGPDGLHMTDAGYDRLARAATAQL 235
Cdd:COG2755   154 YAALRDAGD-----LPDLLTADGLHPNAAGYRLIAEAVLPAL 190
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 46-230 1.00e-22

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: 91.70  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  46 IVAFGSSSTEGSGASSPSTTYPAQLQRDLAARLGamgsvhsSVTVLNRGKGGDDSEAMARRLE--RDVLADKPDLVIWQT 123
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLLYLLLLAGGP-------GVEVINLGVSGATTADALRRLGlrLALLKDKPDLVIIEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 124 GSNDPMSG--VSVERFAELTRAGILAMR--ATGADVVLMDQQWCKKLSTTDGA--EAYGAALHAIATELNVPVirrNAMM 197
Cdd:cd00229    74 GTNDLGRGgdTSIDEFKANLEELLDALRerAPGAKVILITPPPPPPREGLLGRalPRYNEAIKAVAAENPAPS---GVDL 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2770876657 198 RAWAAQGLLSPTQMIGPDGLHMTDAGYDRLARA 230
Cdd:cd00229   151 VDLAALLGDEDKSLYSPDGIHPNPAGHKLIAEA 183
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 48-226 2.04e-22

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: 90.30  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  48 AFGSSSTEGSGASSPSTTYPAQLQRDLAARLGAmgsvhssVTVLNRGKGGDDSEAMARRLERDVLADKPDLVIWQTGSND 127
Cdd:pfam13472   1 ALGDSITAGYGATGGDRSYPGWLARLLARRLGA-------DVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTND 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 128 PMSGVSVERFAELTRAGILAMRATGADVVLMDQ--------QWCKKLSTTDGAEAYGAALHAIATELNVPVIRrnamMRA 199
Cdd:pfam13472  74 LGRGVSAARAAANLEALIDALRAAGPDARVLLIgplpvgppPPLDERRLNARIAEYNAAIREVAAERGVPYVD----LWD 149

                         170       180
                  ....*....|....*....|....*..
gi 2770876657 200 WAAQGLLSPTQMIGPDGLHMTDAGYDR 226
Cdd:pfam13472 150 ALRDDGGWLPDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 39-235 1.93e-33

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: 119.75  E-value: 1.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  39 TQGQAIRIVAFGSSSTEGSGASsPSTTYPAQLQRDLAARlgamgsvhsSVTVLNRGKGGDDSEAMARRLERDVLADKPDL 118
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYGAS-RERGWPALLARRLAAA---------DVRVVNAGISGATTADLLARLDRDLLALKPDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 119 VIWQTGSNDPMSG--VSVERFAELTRAGILAMRATG--ADVVLMD-QQWCKKLSTTDGAEAYGAALHAIATELNVPVIRR 193
Cdd:COG2755    74 VVIELGTNDLLRGlgVSPEEFRANLEALIDRLRAAGpgARVVLVTpPPRLRPNYLNERIEAYNAAIRELAAEYGVPLVDL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2770876657 194 NAMMRAWAAqgllsPTQMIGPDGLHMTDAGYDRLARAATAQL 235
Cdd:COG2755   154 YAALRDAGD-----LPDLLTADGLHPNAAGYRLIAEAVLPAL 190
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 46-230 1.00e-22

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: 91.70  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  46 IVAFGSSSTEGSGASSPSTTYPAQLQRDLAARLGamgsvhsSVTVLNRGKGGDDSEAMARRLE--RDVLADKPDLVIWQT 123
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLLYLLLLAGGP-------GVEVINLGVSGATTADALRRLGlrLALLKDKPDLVIIEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 124 GSNDPMSG--VSVERFAELTRAGILAMR--ATGADVVLMDQQWCKKLSTTDGA--EAYGAALHAIATELNVPVirrNAMM 197
Cdd:cd00229    74 GTNDLGRGgdTSIDEFKANLEELLDALRerAPGAKVILITPPPPPPREGLLGRalPRYNEAIKAVAAENPAPS---GVDL 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2770876657 198 RAWAAQGLLSPTQMIGPDGLHMTDAGYDRLARA 230
Cdd:cd00229   151 VDLAALLGDEDKSLYSPDGIHPNPAGHKLIAEA 183
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 48-226 2.04e-22

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: 90.30  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  48 AFGSSSTEGSGASSPSTTYPAQLQRDLAARLGAmgsvhssVTVLNRGKGGDDSEAMARRLERDVLADKPDLVIWQTGSND 127
Cdd:pfam13472   1 ALGDSITAGYGATGGDRSYPGWLARLLARRLGA-------DVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTND 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 128 PMSGVSVERFAELTRAGILAMRATGADVVLMDQ--------QWCKKLSTTDGAEAYGAALHAIATELNVPVIRrnamMRA 199
Cdd:pfam13472  74 LGRGVSAARAAANLEALIDALRAAGPDARVLLIgplpvgppPPLDERRLNARIAEYNAAIREVAAERGVPYVD----LWD 149

                         170       180
                  ....*....|....*....|....*..
gi 2770876657 200 WAAQGLLSPTQMIGPDGLHMTDAGYDR 226
Cdd:pfam13472 150 ALRDDGGWLPDLLADDGLHPNAAGYRL 176
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 45-230 4.12e-17

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: 76.40  E-value: 4.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  45 RIVAFGSSSTEGSGASsPSTTYPAQLQRDLAARLgamgsvhSSVTVLNRGKGGDDSEAMARRLERDVLADKPDLVIWQTG 124
Cdd:cd01822     2 TILALGDSLTAGYGLP-PEEGWPALLQKRLDARG-------IDVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 125 SNDPMSGVSVERfaelTRAGILAM----RATGADVVLMDQQwckkLSTTDGAEaYGAALHAI----ATELNVP------- 189
Cdd:cd01822    74 GNDGLRGIPPDQ----TRANLRQMietaQARGAPVLLVGMQ----APPNYGPR-YTRRFAAIypelAEEYGVPlvpffle 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2770876657 190 -VIRRNAMMRAwaaqgllsptqmigpDGLHMTDAGYDRLARA 230
Cdd:cd01822   145 gVAGDPELMQS---------------DGIHPNAEGQPIIAEN 171
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 85-230 8.26e-16

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: 73.10  E-value: 8.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  85 HSSVTVLNRGKGGDDSEAMARRLERDVLADKPDLVIWQTGSND----PMSGVSVERFAELTRAGI--LAMRATGADVVLM 158
Cdd:cd01834    31 ELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDsfrgFDDPVGLEKFKTNLRRLIdrLKNKESAPRIVLV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 159 DQQW--CKKLSTTDGAE------AYGAALHAIATELNVPVIRRNAMMRAWAAQgllSPTQMIGPDGLHMTDAGYDRLARA 230
Cdd:cd01834   111 SPIAyeANEDPLPDGAEynanlaAYADAVRELAAENGVAFVDLFTPMKEAFQK---AGEAVLTVDGVHPNEAGHRALARL 187
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 45-230 5.93e-14

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: 68.43  E-value: 5.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  45 RIVAFGSSSTEGSGASSPSTtYPAQLQRDLAARLgamgsvhssvTVLNRGKGGDDSEAMARRLERDVL---ADKPDLVIW 121
Cdd:cd01838     1 KIVLFGDSITQFSFDQGEFG-FGAALADVYSRKL----------DVINRGFSGYNTRWALKVLPKIFLeekLAQPDLVTI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 122 QTGSND-----PMSGVSVERFAELTRAGI--LAMRATGADVVLM------DQQWCKKLSTTDG--------AEAYGAALH 180
Cdd:cd01838    70 FFGANDaalpgQPQHVPLDEYKENLRKIVshLKSLSPKTKVILItpppvdEEAWEKSLEDGGSqpgrtnelLKQYAEACV 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2770876657 181 AIATELNVPVIR-RNAMMR-AWAAQGLLSptqmigpDGLHMTDAGYDRLARA 230
Cdd:cd01838   150 EVAEELGVPVIDlWTAMQEeAGWLESLLT-------DGLHFSSKGYELLFEE 194
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 44-235 4.13e-13

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: 65.81  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  44 IRIVAFGSSSTEGSGASsPSTTYPAQLqrdlaarlgamgSVHSSVTVLNRGKGGDDSEAMARRLERDVLADKPDLVIWQT 123
Cdd:cd04501     1 MRVVCLGDSITYGYPVG-PEASWVNLL------------AEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 124 GSNDPMSGVSVERFAEltraGILAM----RATGADVVL------MDQQWCKKLSTTDGA-EAYGAALHAIATELNVPVIR 192
Cdd:cd04501    68 GTNDIIVNTSLEMIKD----NIRSMvelaEANGIKVILasplpvDDYPWKPQWLRPANKlKSLNRWLKDYARENGLLFLD 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2770876657 193 RNAMM---RAWAAQGLLSptqmigPDGLHMTDAGYDRLARAATAQL 235
Cdd:cd04501   144 FYSPLldeRNVGLKPGLL------TDGLHPSREGYRVMAPLAEKAL 183
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 86-230 8.01e-12

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: 61.91  E-value: 8.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  86 SSVTVLNRGKGGDDSEAMARRLERDVlADKPDLVIWQTGSNDPMSGVSVERFAELTRAGILAMRAT--GADVVLMDQQWC 163
Cdd:cd01828    20 PDVKVANRGISGDTTRGLLARLDEDV-ALQPKAIFIMIGINDLAQGTSDEDIVANYRTILEKLRKHfpNIKIVVQSILPV 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2770876657 164 KKLSTTDGA--EAYGAALHAIATELNVPVIRRNAMMRawAAQGLLSPTqmIGPDGLHMTDAGYDRLARA 230
Cdd:cd01828    99 GELKSIPNEqiEELNRQLAQLAQQEGVTFLDLWAVFT--NADGDLKNE--FTTDGLHLNAKGYAVWAAA 163
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
46-230 2.18e-11

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 61.43  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  46 IVAFGSSSTEGSGASS-PSTTYPAQLQRDLAARLGAMGSvhSSVTVLNRGKGGDDSEAMARRLER-------DVLADKPD 117
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPgGRFSWGDLLADFLARKLGVPGS--GYNHGANFAIGGATIEDLPIQLEQllrlisdVKDQAKPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 118 LVIWQTGSNDPMSG-VSVERFAELTR--------------AGILAMRATGADVVLM-DQQWCKKLSTTDGAEAYGAALHA 181
Cdd:pfam00657  79 LVTIFIGANDLCNFlSSPARSKKRVPdlldelranlpqlgLGARKFWVHGLGPLGCtPPKGCYELYNALAEEYNERLNEL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2770876657 182 I------ATELNVPVIRRNAMM---RAWAAQGLlsptqmiGPDGLHMTDAGYDRLARA 230
Cdd:pfam00657 159 VnslaaaAEDANVVYVDIYGFEdptDPCCGIGL-------EPDGLHPSEKGYKAVAEA 209
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 45-231 1.50e-09

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: 55.74  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  45 RIVAFGSSSTEGSGASSPSTTYPAQLQRdLAARLGAmgsVHSSVTVLNRGKGGddseamaRRLERDV-------LADKPD 117
Cdd:cd01832     1 RYVALGDSITEGVGDPVPDGGYRGWADR-LAAALAA---ADPGIEYANLAVRG-------RRTAQILaeqlpaaLALRPD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 118 LVIWQTGSNDPMS-GVSVERFAELTRAGILAMRATGADVVLM---DQQWCKKLSTTDGA--EAYGAALHAIATELNVPVI 191
Cdd:cd01832    70 LVTLLAGGNDILRpGTDPDTYRADLEEAVRRLRAAGARVVVFtipDPAVLEPFRRRVRArlAAYNAVIRAVAARYGAVHV 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2770876657 192 RrnammrAWAAQGLLSPtQMIGPDGLHMTDAGYDRLARAA 231
Cdd:cd01832   150 D------LWEHPEFADP-RLWASDRLHPSAAGHARLAALV 182
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 44-127 2.07e-05

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: 43.97  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  44 IRIVAFGSSSTEGSGASSpSTTYPAQLQRDLAA--RLGAMGSvhSSVTVLNRGkggdDSEAMARRLERDVLADKPDLVIW 121
Cdd:cd01827     1 IKVACVGNSITEGAGLRA-YDSYPSPLAQMLGDgyEVGNFGK--SARTVLNKG----DHPYMNEERYKNALAFNPNIVII 73


                  ....*.
gi 2770876657 122 QTGSND 127
Cdd:cd01827    74 KLGTND 79
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 88-236 3.07e-05

Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.


Pssm-ID: 238859  Cd Length: 198  Bit Score: 43.36  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  88 VTVLNRGKGGDDS---------EAMARRLERDvladkpDLVIWQTGSND-----PMSGVSVERFAE-LTRAgILAMRATG 152
Cdd:cd01821    35 ITVVNHAKGGRSSrsfrdegrwDAILKLIKPG------DYVLIQFGHNDqkpkdPEYTEPYTTYKEyLRRY-IAEARAKG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 153 ADVVLMDQQ----W--CKKLSTTDGAeaYGAALHAIATELNVPVIRRNAMMRAWAaqgllsptQMIGP------------ 214
Cdd:cd01821   108 ATPILVTPVtrrtFdeGGKVEDTLGD--YPAAMRELAAEEGVPLIDLNAASRALY--------EAIGPekskkyfpegpg 177

                         170       180
                  ....*....|....*....|..
gi 2770876657 215 DGLHMTDAGYDRLARAAtAQLL 236
Cdd:cd01821   178 DNTHFSEKGADVVARLV-AEEL 198
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 46-230 6.84e-05

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: 42.61  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  46 IVAFGSSSTEGSGaSSPST--TYPAQLQRDLAARLGAmgsvhSSVTVLNRGKGGD------DSEAMARRLERDVLAdKPD 117
Cdd:cd01830     2 VVALGDSITDGRG-STPDAnnRWPDLLAARLAARAGT-----RGIAVLNAGIGGNrlladgLGPSALARFDRDVLS-QPG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 118 LV----------IWQTGSNDPMSGVSVERFAELTRAGILAMRATGADVVLMdqqwckKLSTTDGAEAYGAALHAIATELN 187
Cdd:cd01830    75 VRtviilegvndIGASGTDFAAAPVTAEELIAGYRQLIRRAHARGIKVIGA------TITPFEGSGYYTPAREATRQAVN 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2770876657 188 V---------PVIRRNAMMRAWAAQGLLSPtQMIGPDGLHMTDAGYDRLARA 230
Cdd:cd01830   149 EwirtsgafdAVVDFDAALRDPADPSRLRP-AYDSGDHLHPNDAGYQAMADA 199
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 43-237 5.72e-04

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: 39.56  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  43 AIRIVAFGSSSTEGSGASSPSTTYPAQLQRDLAARLGamgsvhSSVTVLNRGKGGDDSEAMARRLERdVLADKPDLVIWQ 122
Cdd:cd01836     2 PLRLLVLGDSTAAGVGVETQDQALAGQLARGLAAITG------RGVRWRLFAKTGATSADLLRQLAP-LPETRFDVAVIS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 123 TGSNDPMSGVSVERF-AELTRA-GILAMRATGADVVlmdqqwckkLSTTDGAEAYGAALHAIATELNVPVIRRNAMMRAW 200
Cdd:cd01836    75 IGVNDVTHLTSIARWrKQLAELvDALRAKFPGARVV---------VTAVPPLGRFPALPQPLRWLLGRRARLLNRALERL 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2770876657 201 AAQ---------GLLSPTQMIGPDGLHMTDAGYDRLARAATAQLLA 237
Cdd:cd01836   146 ASEaprvtllpaTGPLFPALFASDGFHPSAAGYAVWAEALAPAIAA 191
SGNH_hydrolase_like_6 cd01844
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 45-235 5.94e-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: 39.61  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657  45 RIVAFGSSSTEGSGASSPSTTYPAQlqrdLAARLGamgsvhssVTVLNRGKGGDDS-EAMARRLERDVladKPDLVIWQT 123
Cdd:cd01844     1 PWVFYGTSISQGACASRPGMAWTAI----LARRLG--------LEVINLGFSGNARlEPEVAELLRDV---PADLYIIDC 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770876657 124 GSNdpMSGVSVERFAELTrAGILAMRATGADV--VLMDQQWCKKLSTTDGAEAYGAALHAIATElnvpvirRNAMMRAWA 201
Cdd:cd01844    66 GPN--IVGAEAMVRERLG-PLVKGLRETHPDTpiLLVSPRYCPDAELTPGRGKLTLAVRRALRE-------AFEKLRADG 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2770876657 202 AQGL--LSPTQMIGP------DGLHMTDAGYDRLARAATAQL 235
Cdd:cd01844   136 VPNLyyLDGEELLGPdgealvDGIHPTDLGHMRYADRFEPVL 177
 
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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