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Conserved domains on  [gi|2196777896|ref|WP_238869439|]
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MULTISPECIES: SGNH/GDSL hydrolase family protein [Proteiniphilum]

Protein Classification

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

SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 33-209 2.26e-76

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: 227.98  E-value: 2.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  33 DRVVFMGNSITEG--------WINLVpEFFADRSYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTgps 104
Cdd:cd04501     1 MRVVCLGDSITYGypvgpeasWVNLL-AEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 105 TLEMIEDNIHSMAELAKAHGIQVVLCSVLPAYDYPWRTG-LEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNG-L 182
Cdd:cd04501    77 SLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQwLRPANKLKSLNRWLKDYARENGLLFLDFYSPLLDERNVgL 156

                         170       180
                  ....*....|....*....|....*..
gi 2196777896 183 PEELSGDGVHPNKAGYTIMAPIVENAI 209
Cdd:cd04501   157 KPGLLTDGLHPSREGYRVMAPLAEKAL 183
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 33-209 2.26e-76

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: 227.98  E-value: 2.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  33 DRVVFMGNSITEG--------WINLVpEFFADRSYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTgps 104
Cdd:cd04501     1 MRVVCLGDSITYGypvgpeasWVNLL-AEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 105 TLEMIEDNIHSMAELAKAHGIQVVLCSVLPAYDYPWRTG-LEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNG-L 182
Cdd:cd04501    77 SLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQwLRPANKLKSLNRWLKDYARENGLLFLDFYSPLLDERNVgL 156

                         170       180
                  ....*....|....*....|....*..
gi 2196777896 183 PEELSGDGVHPNKAGYTIMAPIVENAI 209
Cdd:cd04501   157 KPGLLTDGLHPSREGYRVMAPLAEKAL 183
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 34-210 2.15e-47

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 154.42  E-value: 2.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEG--------WINLVPEFFADRS--YINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTGP 103
Cdd:COG2755    10 RIVALGDSITAGygasrergWPALLARRLAAADvrVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLLRGLGV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 104 StLEMIEDNIHSMAELAKAHG--IQVVLCSVlpaydYPWRTGLEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNg 181
Cdd:COG2755    90 S-PEEFRANLEALIDRLRAAGpgARVVLVTP-----PPRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYAALRDAGD- 162

                         170       180
                  ....*....|....*....|....*....
gi 2196777896 182 LPEELSGDGVHPNKAGYTIMAPIVENAIA 210
Cdd:COG2755   163 LPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 37-200 1.39e-34

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: 121.11  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  37 FMGNSITEG---------WINLVPEFFADR----SYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTGP 103
Cdd:pfam13472   1 ALGDSITAGygatggdrsYPGWLARLLARRlgadVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 104 STlemIEDNIHSMAELAKAHG--IQVVLCSVLPAYDYPWRTGLEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNG 181
Cdd:pfam13472  81 AR---AAANLEALIDALRAAGpdARVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGW 157

                         170
                  ....*....|....*....
gi 2196777896 182 LPEELSGDGVHPNKAGYTI 200
Cdd:pfam13472 158 LPDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 33-209 2.26e-76

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: 227.98  E-value: 2.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  33 DRVVFMGNSITEG--------WINLVpEFFADRSYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTgps 104
Cdd:cd04501     1 MRVVCLGDSITYGypvgpeasWVNLL-AEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 105 TLEMIEDNIHSMAELAKAHGIQVVLCSVLPAYDYPWRTG-LEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNG-L 182
Cdd:cd04501    77 SLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQwLRPANKLKSLNRWLKDYARENGLLFLDFYSPLLDERNVgL 156

                         170       180
                  ....*....|....*....|....*..
gi 2196777896 183 PEELSGDGVHPNKAGYTIMAPIVENAI 209
Cdd:cd04501   157 KPGLLTDGLHPSREGYRVMAPLAEKAL 183
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 34-210 2.15e-47

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 154.42  E-value: 2.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEG--------WINLVPEFFADRS--YINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTGP 103
Cdd:COG2755    10 RIVALGDSITAGygasrergWPALLARRLAAADvrVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDLLRGLGV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 104 StLEMIEDNIHSMAELAKAHG--IQVVLCSVlpaydYPWRTGLEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNg 181
Cdd:COG2755    90 S-PEEFRANLEALIDRLRAAGpgARVVLVTP-----PPRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYAALRDAGD- 162

                         170       180
                  ....*....|....*....|....*....
gi 2196777896 182 LPEELSGDGVHPNKAGYTIMAPIVENAIA 210
Cdd:COG2755   163 LPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 37-200 1.39e-34

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: 121.11  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  37 FMGNSITEG---------WINLVPEFFADR----SYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTGP 103
Cdd:pfam13472   1 ALGDSITAGygatggdrsYPGWLARLLARRlgadVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 104 STlemIEDNIHSMAELAKAHG--IQVVLCSVLPAYDYPWRTGLEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNG 181
Cdd:pfam13472  81 AR---AAANLEALIDALRAAGpdARVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGW 157

                         170
                  ....*....|....*....
gi 2196777896 182 LPEELSGDGVHPNKAGYTI 200
Cdd:pfam13472 158 LPDLLADDGLHPNAAGYRL 176
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 34-210 4.80e-33

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: 117.00  E-value: 4.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEGWinlvP--EFFADRSYINRGISGQTTPQMLIRFRQDVlNLWPKVVVILAGTNDIAGNTGPstlEMIED 111
Cdd:cd01828     1 ALVFLGDSLTEGG----PwaLLFPDVKVANRGISGDTTRGLLARLDEDV-ALQPKAIFIMIGINDLAQGTSD---EDIVA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 112 NIHSMAELAKAH--GIQVVLCSVLPAYDYPWRtglePAPRIVELNKRLNKYAGTHGVVYCDFFQAMADERNGLPEELSGD 189
Cdd:cd01828    73 NYRTILEKLRKHfpNIKIVVQSILPVGELKSI----PNEQIEELNRQLAQLAQQEGVTFLDLWAVFTNADGDLKNEFTTD 148

                         170       180
                  ....*....|....*....|.
gi 2196777896 190 GVHPNKAGYTIMAPIVENAIA 210
Cdd:cd01828   149 GLHLNAKGYAVWAAALQPYLA 169
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 32-204 2.24e-30

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: 110.85  E-value: 2.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  32 DDRVVFMGNSITE--GWINLVPEFFADR------SYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTND-IAGNTG 102
Cdd:cd01834     1 GDRIVFIGNSITDrgGYVGYVETYLAARypelklTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDsFRGFDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 103 PSTLEMIEDNIHSM-AELA-KAHGIQVVLCSVlPAYDYPwrtgLEPAPRIVELNKRLNKYAG-------THGVVYCDFFQ 173
Cdd:cd01834    81 PVGLEKFKTNLRRLiDRLKnKESAPRIVLVSP-IAYEAN----EDPLPDGAEYNANLAAYADavrelaaENGVAFVDLFT 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2196777896 174 AMADERNGLPEE-LSGDGVHPNKAGYTIMAPI 204
Cdd:cd01834   156 PMKEAFQKAGEAvLTVDGVHPNEAGHRALARL 187
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 36-209 2.07e-24

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: 94.70  E-value: 2.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  36 VFMGNSITEGWInLVPEFFADRSYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIaGNTGPS--TLEMIEDNI 113
Cdd:cd01841     4 VFIGDSLFEGWP-LYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDI-GKEVSSnqFIKWYRDII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 114 HSMAELAKAHgiQVVLCSVLPAYDYPWRTGLEPApRIVELNKRLNKYAGTHGVVYCDFFQAMADERNGLPEELSGDGVHP 193
Cdd:cd01841    82 EQIREEFPNT--KIYLLSVLPVLEEDEIKTRSNT-RIQRLNDAIKELAPELGVTFIDLNDVLVDEFGNLKKEYTTDGLHF 158

                         170
                  ....*....|....*.
gi 2196777896 194 NKAGYTIMAPIVENAI 209
Cdd:cd01841   159 NPKGYQKLLEILEEYL 174
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 22-213 1.76e-23

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: 93.51  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  22 NAKLGPARTCDDRVVFMGNSITEGWINLVPE----FFADRSYINRGISGQTTPQMLIRFRQDVL-NLWPKVVVILAGTND 96
Cdd:cd01820    22 ERFVAEAKQKEPDVVFIGDSITQNWEFTGLEvwreLYAPLHALNFGIGGDRTQNVLWRLENGELdGVNPKVVVLLIGTNN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  97 IaGNTGPS--TLEMIEDNIHSMAElaKAHGIQVVLCSVLPAYDYP-WRTglepaPRIVELNKRLN-KYAGTHGVVYCD-- 170
Cdd:cd01820   102 I-GHTTTAeeIAEGILAIVEEIRE--KLPNAKILLLGLLPRGQNPnPLR-----ERNAQVNRLLAvRYDGLPNVTFLDid 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2196777896 171 --FFQAMADerngLPEELSGDGVHPNKAGYTIMAPIVENAIARAL 213
Cdd:cd01820   174 kgFVQSDGT----ISHHDMPDYLHLTAAGYRKWADALHPTLARLL 214
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
35-202 1.97e-22

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 90.71  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  35 VVFMGNSITEG----------WINLVPEFFAD---------RSYINRGISGQTTPQM------LIRFRQDVLNLW-PKVV 88
Cdd:pfam00657   1 IVAFGDSLTDGggdgpggrfsWGDLLADFLARklgvpgsgyNHGANFAIGGATIEDLpiqleqLLRLISDVKDQAkPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  89 VILAGTNDIAGNTG---------PSTLEMIEDNIHSM---AELAKAHGIQVVLCSVLPAYDYPWRT-GLEPAPRIVELNK 155
Cdd:pfam00657  81 TIFIGANDLCNFLSsparskkrvPDLLDELRANLPQLglgARKFWVHGLGPLGCTPPKGCYELYNAlAEEYNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2196777896 156 RLNKYAGTHGVVYCDFFQAMaDERNGLPE-ELSGDGVHPNKAGYTIMA 202
Cdd:pfam00657 161 SLAAAAEDANVVYVDIYGFE-DPTDPCCGiGLEPDGLHPSEKGYKAVA 207
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 35-208 9.37e-21

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: 85.54  E-value: 9.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  35 VVFMGNSITEGWINLVPEFFA-------------DRSYINRGISGQTTPQMLIRF--RQDVLNLWPKVVVILAGTNDIAG 99
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYslllyllllaggpGVEVINLGVSGATTADALRRLglRLALLKDKPDLVIIELGTNDLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 100 NTGPSTLEmIEDNIHSM--AELAKAHGIQVVLCSVLPAYDYPWRTGlEPAPRIVELNKRLNKYAGTHGVVycDFFQAMAD 177
Cdd:cd00229    81 GGDTSIDE-FKANLEELldALRERAPGAKVILITPPPPPPREGLLG-RALPRYNEAIKAVAAENPAPSGV--DLVDLAAL 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2196777896 178 ERNGLPEELSGDGVHPNKAGYTIMAPIVENA 208
Cdd:cd00229   157 LGDEDKSLYSPDGIHPNPAGHKLIAEALASA 187
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 35-205 3.38e-18

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: 79.21  E-value: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  35 VVFMGNSITEG----------WINLVPEFFADRS------YINRGISGQTT------PQMLIRFRQDVLNLwPKV--VVI 90
Cdd:cd01830     2 VVALGDSITDGrgstpdannrWPDLLAARLAARAgtrgiaVLNAGIGGNRLladglgPSALARFDRDVLSQ-PGVrtVII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  91 LAGTNDIAG-----NTGPSTLEMIEDNIHSMAELAKAHGIQVVLCSVLPAYDYPWRTGLEPAPRiVELNKRLNKYAGTHG 165
Cdd:cd01830    81 LEGVNDIGAsgtdfAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATR-QAVNEWIRTSGAFDA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2196777896 166 VVycDFFQAMADERNG---LPEELSGDGVHPNKAGYTIMAPIV 205
Cdd:cd01830   160 VV--DFDAALRDPADPsrlRPAYDSGDHLHPNDAGYQAMADAV 200
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 33-209 5.09e-18

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: 77.94  E-value: 5.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  33 DRVVFMGNSIT--------EGWINLVPEFFADRSY----INRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDiaGN 100
Cdd:cd01822     1 VTILALGDSLTagyglppeEGWPALLQKRLDARGIdvtvINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGND--GL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 101 TGPStLEMIEDNIHSMAELAKAHGIQVVLCSVLPAYDYPWRTGLEPAPRIVELnkrlnkyAGTHGVVYCDFFqaMADERn 180
Cdd:cd01822    79 RGIP-PDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPEL-------AEEYGVPLVPFF--LEGVA- 147

                         170       180
                  ....*....|....*....|....*....
gi 2196777896 181 GLPEELSGDGVHPNKAGYTIMAPIVENAI 209
Cdd:cd01822   148 GDPELMQSDGIHPNAEGQPIIAENVWPAL 176
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 34-213 6.04e-18

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: 78.45  E-value: 6.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITE--------GWINLVPEFFADR-SYINRGISGQTTPQMLIRFRQDVLNLW---PKVVVILAGTNDIA--G 99
Cdd:cd01838     1 KIVLFGDSITQfsfdqgefGFGAALADVYSRKlDVINRGFSGYNTRWALKVLPKIFLEEKlaqPDLVTIFFGANDAAlpG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 100 NTGPSTLEMIEDNIHSMAELAK--AHGIQVVLCSVLPAYDYPW-RTGLEPAPRIVELNKRLNKY-------AGTHGVVYC 169
Cdd:cd01838    81 QPQHVPLDEYKENLRKIVSHLKslSPKTKVILITPPPVDEEAWeKSLEDGGSQPGRTNELLKQYaeacvevAEELGVPVI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2196777896 170 DFFQAMADERNGLPEELSgDGVHPNKAGYTIMApiveNAIARAL 213
Cdd:cd01838   161 DLWTAMQEEAGWLESLLT-DGLHFSSKGYELLF----EEIVKVI 199
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 35-209 9.72e-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: 77.33  E-value: 9.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  35 VVFMGNSITEGWINLvPEFFADRSYINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTGPstlEMIEDNIH 114
Cdd:cd04502     2 ILFYGSSSIRLWDTL-ADDLAPLPVVNRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTP---EEVLRDFR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 115 SMAELAKAH--GIQVVLCSVLPAydyPWRTGLEpaPRIVELNKRLNKYAGTH-GVVYCDFFQAMADERNGLPEELSG-DG 190
Cdd:cd04502    78 ELVNRIRAKlpDTPIAIISIKPS---PARWALR--PKIRRFNALLKELAETRpNLTYIDVASPMLDADGKPRAELFQeDG 152

                         170
                  ....*....|....*....
gi 2196777896 191 VHPNKAGYTIMAPIVENAI 209
Cdd:cd04502   153 LHLNDAGYALWRKVIKPAL 171
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 34-209 3.88e-14

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: 67.26  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEGWINlvpeffadrsyiNRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDIAGNTGPSTlemIEDNI 113
Cdd:cd01833     2 RIMPLGDSITWGDKD------------HEGHSGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNRDPDT---APDRL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 114 HSMAE--LAKAHGIQVVLCSVLPAYDYPWrtglepAPRIVELNKRLNKYAGTH-----GVVYCDFFQAMaderngLPEEL 186
Cdd:cd01833    67 RALIDqmRAANPDVKIIVATLIPTTDASG------NARIAEYNAAIPGVVADLrtagsPVVLVDMSTGY------TTADD 134

                         170       180
                  ....*....|....*....|...
gi 2196777896 187 SGDGVHPNKAGYTIMAPIVENAI 209
Cdd:cd01833   135 LYDGLHPNDQGYKKMADAWYEAL 157
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 34-202 1.96e-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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


Pssm-ID: 238870  Cd Length: 185  Bit Score: 66.14  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEG------------WINLVPEFFADRS----YINRGISGQTTPQMLIRFRQDVLNLWPKVVVILAGTNDI 97
Cdd:cd01832     1 RYVALGDSITEGvgdpvpdggyrgWADRLAAALAAADpgieYANLAVRGRRTAQILAEQLPAALALRPDLVTLLAGGNDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  98 -AGNTGPSTLEmieDNIHSMAELAKAHGIQVVLCSvLPAYDYPWRTGLEPAPRIVELNKRLNKYAGTHGVVYCDFFqamA 176
Cdd:cd01832    81 lRPGTDPDTYR---ADLEEAVRRLRAAGARVVVFT-IPDPAVLEPFRRRVRARLAAYNAVIRAVAARYGAVHVDLW---E 153

                         170       180
                  ....*....|....*....|....*.
gi 2196777896 177 DERNGLPEELSGDGVHPNKAGYTIMA 202
Cdd:cd01832   154 HPEFADPRLWASDRLHPSAAGHARLA 179
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 34-207 4.63e-10

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: 56.96  E-value: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEG----------------WINLVPEFfadrSYINRGISGQTTPQMLIRFRQDVLNLW----PKVVVILAG 93
Cdd:cd01835     3 RLIVVGDSLVYGwgdpegggwvgrlrarWMNLGDDP----VLYNLGVRGDGSEDVAARWRAEWSRRGelnvPNRLVLSVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  94 TNDIAGNTGP---STLEMIEDNIHSMAELAKaHGIQVVLCSvLPAYDYPWRTGLEPapRIVELNKRLNKYAGTHGVVYCD 170
Cdd:cd01835    79 LNDTARGGRKrpqLSARAFLFGLNQLLEEAK-RLVPVLVVG-PTPVDEAKMPYSNR--RIARLETAFAEVCLRRDVPFLD 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2196777896 171 FFQAMADERNGLPEELSGDGVHPNKAGYTIMAPIVEN 207
Cdd:cd01835   155 TFTPLLNHPQWRRELAATDGIHPNAAGYGWLAWLVLH 191
SGNH_hydrolase_yrhL_like cd01840
yrhL-like subfamily of SGNH-hydrolases, a diverse family of lipases and esterases. The ...
 85-209 4.46e-07

yrhL-like subfamily of SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Most members of this sub-family appear to co-occur with N-terminal acyltransferase domains. Might be involved in lipid metabolism.


Pssm-ID: 238878  Cd Length: 150  Bit Score: 47.62  E-value: 4.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  85 PKVVVILAGTNdiagntGPSTLEMIEdniHSMAELAKAHgiQVVLCSVLPaydypwrtglePAPRIVELNKRLNKYAGTH 164
Cdd:cd01840    51 RKTVVIGLGTN------GPFTKDQLD---ELLDALGPDR--QVYLVNPHV-----------PRPWEPDVNAYLLDAAKKY 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2196777896 165 -GVVYCDFFQAMaderNGLPEELSGDGVHPNKAGYTIMAPIVENAI 209
Cdd:cd01840   109 kNVTIIDWYKAA----KGHPDWFYGDGVHPNPAGAKLYAALIAKAI 150
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 34-214 1.27e-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: 47.27  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEGwinlvpEFFADR-------SYINRGISGQTTPQMLiRFRQDVLN-----LWPKVVVILAGTNDiAGNT 101
Cdd:cd01825     1 RIAQLGDSHIAG------DFFTDVlrgllgvIYDNLGVNGASASLLL-KWDAEFLQaqlaaLPPDLVILSYGTNE-AFNK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 102 GPStLEMIEDNIHSMAELAKAHGIQVVlCSVLPAYDYPWRTG---LEPAPRIVELNKRLNKYAGTHGVVYCDFFQAMADE 178
Cdd:cd01825    73 QLN-ASEYRQQLREFIKRLRQILPNAS-ILLVGPPDSLQKTGagrWRTPPGLDAVIAAQRRVAKEEGIAFWDLYAAMGGE 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2196777896 179 RNGLPEELSG----DGVHPNKAGYTIMApiveNAIARALL 214
Cdd:cd01825   151 GGIWQWAEPGlarkDYVHLTPRGYERLA----NLLYEALL 186
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 34-209 1.48e-06

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: 47.05  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  34 RVVFMGNSITEGwINLV-----PEFFAD---RSYI--NRGISGQTtpqMLIRFRQD---------VLNLWPKVVVILAGT 94
Cdd:cd01827     2 KVACVGNSITEG-AGLRaydsyPSPLAQmlgDGYEvgNFGKSART---VLNKGDHPymneeryknALAFNPNIVIIKLGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  95 NDiAGNTGPSTLEMIEDNIHSMAELAKAHGIQ--VVLCSVLPAYDYPWRT------GLEPAPRIVELNKRLNkyagthgV 166
Cdd:cd01827    78 ND-AKPQNWKYKDDFKKDYETMIDSFQALPSKpkIYICYPIPAYYGDGGFindniiKKEIQPMIDKIAKKLN-------L 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2196777896 167 VYCDFFQAMADERNGLPeelsgDGVHPNKAGYTIMAPIVENAI 209
Cdd:cd01827   150 KLIDLHTPLKGKPELVP-----DWVHPNEKGAYILAKVVYKAI 187
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 63-214 1.74e-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: 41.10  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896  63 GISGQTTPQmLIRFRQDVLNLWPKVVVILAGTNDIAGNTGPStlEMIEDNIHSMAELAKAHGIQVVLCSVLPaydypwrt 142
Cdd:cd01836    47 AKTGATSAD-LLRQLAPLPETRFDVAVISIGVNDVTHLTSIA--RWRKQLAELVDALRAKFPGARVVVTAVP-------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777896 143 glePAPRIVELNKRLNKYAGTHGV-------------VYCDFFQAMADERnglPEELSGDGVHPNKAGYTIMApiveNAI 209
Cdd:cd01836   116 ---PLGRFPALPQPLRWLLGRRARllnralerlaseaPRVTLLPATGPLF---PALFASDGFHPSAAGYAVWA----EAL 185


                  ....*
gi 2196777896 210 ARALL 214
Cdd:cd01836   186 APAIA 190
 
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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