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Conserved domains on  [gi|1034608081|ref|XP_016882337|]
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platelet-activating factor acetylhydrolase IB subunit alpha1 isoform X1 [Homo sapiens]

Protein Classification

platelet-activating factor acetylhydrolase IB subunit( domain architecture ID 10110665)

platelet-activating factor (PAF) acetylhydrolase (PAF-AH) IB subunit is the catalytic subunit of a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position

PubMed:  11983068

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 7-192 5.32e-110

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: 314.23  E-value: 5.32e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081   7 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDGTQHVLWRL 84
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  85 ENGELEHIRPKIVVVWVGTNNHGHT--AEQVTGGIKAIVQ-------------LGLLPRGQHPNPLREKNRQVNELVRAA 149
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEeireklpnakillLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034608081 150 LAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 192
Cdd:cd01820   161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWA 203
 
Name Accession Description Interval E-value
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 7-192 5.32e-110

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: 314.23  E-value: 5.32e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081   7 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDGTQHVLWRL 84
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  85 ENGELEHIRPKIVVVWVGTNNHGHT--AEQVTGGIKAIVQ-------------LGLLPRGQHPNPLREKNRQVNELVRAA 149
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEeireklpnakillLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034608081 150 LAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 192
Cdd:cd01820   161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWA 203
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 34-188 1.27e-22

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: 90.47  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  34 SKDKEPEVVFIGDSLVQLM--HQCEIWRELF------SPLHALNFGIGGDGTQHVLWRLEnGELEHIRPKIVVVWVGTNN 105
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYgaSRERGWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 106 ----HGHTAEQVTGGIKAIVQ-------------LGLLPRGqHPNPLREKNRQVNELVRaALAGHPRAHFLDADPGFvHS 168
Cdd:COG2755    83 llrgLGVSPEEFRANLEALIDrlraagpgarvvlVTPPPRL-RPNYLNERIEAYNAAIR-ELAAEYGVPLVDLYAAL-RD 159

                         170       180
                  ....*....|....*....|
gi 1034608081 169 DGTISHHDMYDYLHLSRLGY 188
Cdd:COG2755   160 AGDLPDLLTADGLHPNAAGY 179
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 43-188 8.48e-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: 8.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  43 FIGDSLVQ---LMHQCEIWRELFSPLHA--------LNFGIGGDGTQHvLWRLENGELEHIRPKIVVVWVGTNN--HGHT 109
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 110 AEQVTGGIKAIVQ-------------LGLLPRGQHPNP----LREKNRQVNELVRAaLAGHPRAHFLDADPGFVHSDGTI 172
Cdd:pfam13472  80 AARAAANLEALIDalraagpdarvllIGPLPVGPPPPLderrLNARIAEYNAAIRE-VAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 1034608081 173 SHHDMYDYLHLSRLGY 188
Cdd:pfam13472 159 PDLLADDGLHPNAAGY 174
 
Name Accession Description Interval E-value
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 7-192 5.32e-110

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: 314.23  E-value: 5.32e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081   7 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDGTQHVLWRL 84
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  85 ENGELEHIRPKIVVVWVGTNNHGHT--AEQVTGGIKAIVQ-------------LGLLPRGQHPNPLREKNRQVNELVRAA 149
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEeireklpnakillLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034608081 150 LAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 192
Cdd:cd01820   161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWA 203
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 34-188 1.27e-22

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: 90.47  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  34 SKDKEPEVVFIGDSLVQLM--HQCEIWRELF------SPLHALNFGIGGDGTQHVLWRLEnGELEHIRPKIVVVWVGTNN 105
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYgaSRERGWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 106 ----HGHTAEQVTGGIKAIVQ-------------LGLLPRGqHPNPLREKNRQVNELVRaALAGHPRAHFLDADPGFvHS 168
Cdd:COG2755    83 llrgLGVSPEEFRANLEALIDrlraagpgarvvlVTPPPRL-RPNYLNERIEAYNAAIR-ELAAEYGVPLVDLYAAL-RD 159

                         170       180
                  ....*....|....*....|
gi 1034608081 169 DGTISHHDMYDYLHLSRLGY 188
Cdd:COG2755   160 AGDLPDLLTADGLHPNAAGY 179
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 40-188 2.39e-18

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: 78.86  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  40 EVVFIGDSLVQLMHqceiWRELFSPLHALNFGIGGDGTQHVLWRLEngELEHIRPKIVVVWVGTNN--HGHTAEQVTG-- 115
Cdd:cd01828     1 ALVFLGDSLTEGGP----WALLFPDVKVANRGISGDTTRGLLARLD--EDVALQPKAIFIMIGINDlaQGTSDEDIVAny 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 116 ------------GIKAIVQlGLLPRGQHPNPLREKNRQVNELVRaALAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHL 183
Cdd:cd01828    75 rtileklrkhfpNIKIVVQ-SILPVGELKSIPNEQIEELNRQLA-QLAQQEGVTFLDLWAVFTNADGDLKNEFTTDGLHL 152


                  ....*
gi 1034608081 184 SRLGY 188
Cdd:cd01828   153 NAKGY 157
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 43-188 8.48e-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: 8.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  43 FIGDSLVQ---LMHQCEIWRELFSPLHA--------LNFGIGGDGTQHvLWRLENGELEHIRPKIVVVWVGTNN--HGHT 109
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 110 AEQVTGGIKAIVQ-------------LGLLPRGQHPNP----LREKNRQVNELVRAaLAGHPRAHFLDADPGFVHSDGTI 172
Cdd:pfam13472  80 AARAAANLEALIDalraagpdarvllIGPLPVGPPPPLderrLNARIAEYNAAIRE-VAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 1034608081 173 SHHDMYDYLHLSRLGY 188
Cdd:pfam13472 159 PDLLADDGLHPNAAGY 174
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 41-188 1.05e-12

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: 63.97  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  41 VVFIGDSLVQLMH--QCEIWRELFSPLHAL---------NFGIGGDGTQHVLWRLENG-ELEHIRPKIVVVWVGTNNHGH 108
Cdd:cd00229     1 ILVIGDSITAGYGasSGSTFYSLLLYLLLLaggpgveviNLGVSGATTADALRRLGLRlALLKDKPDLVIIELGTNDLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 109 ----TAEQVTGGIKAIVQ-------------LGLLPRGQHPNPLREKNRQVNELVRAALAGHPR---AHFLDADPGFVHS 168
Cdd:cd00229    81 ggdtSIDEFKANLEELLDalrerapgakvilITPPPPPPREGLLGRALPRYNEAIKAVAAENPApsgVDLVDLAALLGDE 160

                         170       180
                  ....*....|....*....|
gi 1034608081 169 DgtiSHHDMYDYLHLSRLGY 188
Cdd:cd00229   161 D---KSLYSPDGIHPNPAGH 177
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
41-188 1.32e-06

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 47.18  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  41 VVFIGDSLVQLMHQC--------EIWRELFS---------PLHALNFGIGGDGTQ------HVLWRLENGELEHIRPKIV 97
Cdd:pfam00657   1 IVAFGDSLTDGGGDGpggrfswgDLLADFLArklgvpgsgYNHGANFAIGGATIEdlpiqlEQLLRLISDVKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  98 VVWVGTN---NHGHTAEQVT------------------GGIKAIVQLGLLPRGQHPNPLREK---------NRQVNELVR 147
Cdd:pfam00657  81 TIFIGANdlcNFLSSPARSKkrvpdlldelranlpqlgLGARKFWVHGLGPLGCTPPKGCYElynalaeeyNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034608081 148 AALAGHPRAHFLDAD-PGFVHSDGTISHHDM-YDYLHLSRLGY 188
Cdd:pfam00657 161 SLAAAAEDANVVYVDiYGFEDPTDPCCGIGLePDGLHPSEKGY 203
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 41-188 4.50e-05

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 239946  Cd Length: 171  Bit Score: 42.28  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  41 VVFIGDSLVQLmhqceiW---RELFSPLHALNFGIGGdgtQHVLWRLENGE--LEHIRPKIVVVWVGTN--NHGHTAEQV 113
Cdd:cd04502     2 ILFYGSSSIRL------WdtlADDLAPLPVVNRGFGG---STLADCLHYFDrlVLPYQPRRVVLYAGDNdlASGRTPEEV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 114 TGGIKAIV----------QLGLLprGQHPNPLR----EKNRQVNELVRAALAGHPRAHFLDADPGFVHSDGtISHHDMY- 178
Cdd:cd04502    73 LRDFRELVnriraklpdtPIAII--SIKPSPARwalrPKIRRFNALLKELAETRPNLTYIDVASPMLDADG-KPRAELFq 149

                         170
                  ....*....|.
gi 1034608081 179 -DYLHLSRLGY 188
Cdd:cd04502   150 eDGLHLNDAGY 160
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 39-189 9.91e-05

NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.


Pssm-ID: 238879  Cd Length: 174  Bit Score: 41.55  E-value: 9.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  39 PEVVFIGDSLVqlmhqcEIW--RELFSPLHAL-NFGIGGDGTQhvlWRLENGELEHIR--PKIVVVWVGTNN--HGHTAE 111
Cdd:cd01841     1 KNIVFIGDSLF------EGWplYEAEGKGKTVnNLGIAGISSR---QYLEHIEPQLIQknPSKVFLFLGTNDigKEVSSN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081 112 QVTGGIKAIVQ-------------LGLLPRGQHPNPLREKNRQVNELVRA--ALAGHPRAHFLDADPGFVHSDGTISHHD 176
Cdd:cd01841    72 QFIKWYRDIIEqireefpntkiylLSVLPVLEEDEIKTRSNTRIQRLNDAikELAPELGVTFIDLNDVLVDEFGNLKKEY 151

                         170
                  ....*....|...
gi 1034608081 177 MYDYLHLSRLGYT 189
Cdd:cd01841   152 TTDGLHFNPKGYQ 164
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 41-104 1.05e-04

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: 41.47  E-value: 1.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034608081  41 VVFIGDSLVQLMHQCEIW------RELFSP-LHALNFGIGGDGTQHVLWRLENGELEH--IRPKIVVVWVGTN 104
Cdd:cd01838     2 IVLFGDSITQFSFDQGEFgfgaalADVYSRkLDVINRGFSGYNTRWALKVLPKIFLEEklAQPDLVTIFFGAN 74
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 40-123 1.09e-04

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 239945  Cd Length: 183  Bit Score: 41.54  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608081  40 EVVFIGDSLVQ--LMHQCEIWREL---FSPLHALNFGIGGDGTQHVLWRLENgELEHIRPKIVVVWVGTNN--HGHTAEQ 112
Cdd:cd04501     2 RVVCLGDSITYgyPVGPEASWVNLlaeFLGKEVINRGINGDTTSQMLVRFYE-DVIALKPAVVIIMGGTNDiiVNTSLEM 80

                          90
                  ....*....|.
gi 1034608081 113 VTGGIKAIVQL 123
Cdd:cd04501    81 IKDNIRSMVEL 91
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 41-104 3.07e-03

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: 37.27  E-value: 3.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034608081  41 VVFIGDSLVQLMHqceiWRELFSP-LHAL---------NFGIGGDGTQHVLWRLENGELEHiRPKIVVVWVGTN 104
Cdd:cd01834     4 IVFIGNSITDRGG----YVGYVETyLAARypelkltfrNLGWSGDTVSDLAARRDRDVLPA-KPDVVSIMFGIN 72
 
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.
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