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Conserved domains on  [gi|12653259|gb|AAH00398|]
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Platelet-activating factor acetylhydrolase, isoform Ib, beta subunit 30kDa [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 ...
 8-217 9.44e-122

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: 344.27  E-value: 9.44e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259   8 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 85
Cdd:cd01820   1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  86 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVS 163
Cdd:cd01820  81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 12653259 164 LPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLL 217
Cdd:cd01820 161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTLARLL 214
 
Name Accession Description Interval E-value
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 8-217 9.44e-122

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: 344.27  E-value: 9.44e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259   8 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 85
Cdd:cd01820   1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  86 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVS 163
Cdd:cd01820  81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 12653259 164 LPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLL 217
Cdd:cd01820 161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTLARLL 214
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 36-205 3.33e-26

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: 100.10  E-value: 3.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  36 KDKEPDVLFVGDSMVQLMQQYEI--WRELF------SPLHALNFGIGGDTTRHVLWRLKnGELENIKPKVIVVWVGTNN- 106
Cdd:COG2755   5 AGKPLRIVALGDSITAGYGASRErgWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTNDl 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 107 ---HENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEkPNPLRQKNAKVNQLLKvslpKLA---NVQLLDTDGGFv 180
Cdd:COG2755  84 lrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLR-PNYLNERIEAYNAAIR----ELAaeyGVPLVDLYAAL- 157

                       170       180
                ....*....|....*....|....*
gi 12653259 181 HSDGAISCHDMFDFLHLTGGGYAKI 205
Cdd:COG2755 158 RDAGDLPDLLTADGLHPNAAGYRLI 182
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 44-204 1.58e-21

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: 87.60  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259    44 FVGDSMVQ---LMQQYEIWRELFSPLHA--------LNFGIGGDTTRHvLWRLKNGELENIKPKVIVVWVGTNN--HENT 110
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259   111 AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRG----EKPNPLRQKNAKVNQLLKvSLPKLANVQLLDTDGGFVHSDGAI 186
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGppppLDERRLNARIAEYNAAIR-EVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*...
gi 12653259   187 SCHDMFDFLHLTGGGYAK 204
Cdd:pfam13472 159 PDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 8-217 9.44e-122

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: 344.27  E-value: 9.44e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259   8 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 85
Cdd:cd01820   1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  86 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVS 163
Cdd:cd01820  81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 12653259 164 LPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLL 217
Cdd:cd01820 161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTLARLL 214
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 36-205 3.33e-26

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: 100.10  E-value: 3.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  36 KDKEPDVLFVGDSMVQLMQQYEI--WRELF------SPLHALNFGIGGDTTRHVLWRLKnGELENIKPKVIVVWVGTNN- 106
Cdd:COG2755   5 AGKPLRIVALGDSITAGYGASRErgWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTNDl 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 107 ---HENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEkPNPLRQKNAKVNQLLKvslpKLA---NVQLLDTDGGFv 180
Cdd:COG2755  84 lrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLR-PNYLNERIEAYNAAIR----ELAaeyGVPLVDLYAAL- 157

                       170       180
                ....*....|....*....|....*
gi 12653259 181 HSDGAISCHDMFDFLHLTGGGYAKI 205
Cdd:COG2755 158 RDAGDLPDLLTADGLHPNAAGYRLI 182
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 41-204 3.64e-25

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: 96.96  E-value: 3.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  41 DVLFVGDSMVQLMQqyeiWRELFSPLHALNFGIGGDTTRHVLWRLKngELENIKPKVIVVWVGTNN--HENTAEEVAGGI 118
Cdd:cd01828   1 ALVFLGDSLTEGGP----WALLFPDVKVANRGISGDTTRGLLARLD--EDVALQPKAIFIMIGINDlaQGTSDEDIVANY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 119 EAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLkVSLPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLT 198
Cdd:cd01828  75 RTILEKLRKHFPNIKIVVQSILPVGELKSIPNEQIEELNRQL-AQLAQQEGVTFLDLWAVFTNADGDLKNEFTTDGLHLN 153


                ....*.
gi 12653259 199 GGGYAK 204
Cdd:cd01828 154 AKGYAV 159
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 44-204 1.58e-21

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: 87.60  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259    44 FVGDSMVQ---LMQQYEIWRELFSPLHA--------LNFGIGGDTTRHvLWRLKNGELENIKPKVIVVWVGTNN--HENT 110
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259   111 AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRG----EKPNPLRQKNAKVNQLLKvSLPKLANVQLLDTDGGFVHSDGAI 186
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGppppLDERRLNARIAEYNAAIR-EVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*...
gi 12653259   187 SCHDMFDFLHLTGGGYAK 204
Cdd:pfam13472 159 PDLLADDGLHPNAAGYRL 176
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 42-205 2.70e-17

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: 76.68  E-value: 2.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  42 VLFVGDSMVQLMQ-------QYEIWRELFSPLHAL----NFGIGGDTTRHVLWRLKNGELENI-KPKVIVVWVGTN---- 105
Cdd:cd00229   1 ILVIGDSITAGYGassgstfYSLLLYLLLLAGGPGveviNLGVSGATTADALRRLGLRLALLKdKPDLVIIELGTNdlgr 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 106 NHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLK---VSLPKLANVQLLDTDGGFVHS 182
Cdd:cd00229  81 GGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKavaAENPAPSGVDLVDLAALLGDE 160

                       170       180
                ....*....|....*....|...
gi 12653259 183 DGAiscHDMFDFLHLTGGGYAKI 205
Cdd:cd00229 161 DKS---LYSPDGIHPNPAGHKLI 180
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 41-213 7.62e-12

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: 61.54  E-value: 7.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  41 DVLFVGDSMVQLmqqYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNgELENIKPKVIVVWVGTN--NHENTAEEVAGGI 118
Cdd:cd04502   1 GILFYGSSSIRL---WDTLADDLAPLPVVNRGFGGSTLADCLHYFDR-LVLPYQPRRVVLYAGDNdlASGRTPEEVLRDF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 119 EAIVQLINTRQPQAKIIVLGLlprgeKPNPLR----QKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGaISCHDMF-- 192
Cdd:cd04502  77 RELVNRIRAKLPDTPIAIISI-----KPSPARwalrPKIRRFNALLKELAETRPNLTYIDVASPMLDADG-KPRAELFqe 150

                       170       180
                ....*....|....*....|.
gi 12653259 193 DFLHLTGGGYAKICKPLHELI 213
Cdd:cd04502 151 DGLHLNDAGYALWRKVIKPAL 171
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 40-213 1.36e-11

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: 60.81  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  40 PDVLFVGDSMVQLMQQYEIwreLFSPLHALNFGIGGDTTRhvlWRLKNGELENI--KPKVIVVWVGTNN--HENTAEEVA 115
Cdd:cd01841   1 KNIVFIGDSLFEGWPLYEA---EGKGKTVNNLGIAGISSR---QYLEHIEPQLIqkNPSKVFLFLGTNDigKEVSSNQFI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 116 GGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKV---NQLLKVSLPKLaNVQLLDTDGGFVHSDGAISCHDMF 192
Cdd:cd01841  75 KWYRDIIEQIREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIqrlNDAIKELAPEL-GVTFIDLNDVLVDEFGNLKKEYTT 153

                       170       180
                ....*....|....*....|.
gi 12653259 193 DFLHLTGGGYAKIckpLHELI 213
Cdd:cd01841 154 DGLHFNPKGYQKL---LEILE 171
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 42-217 4.66e-10

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: 57.26  E-value: 4.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  42 VLFvGDSMVQLM--QQYEIW----RELFSP-LHALNFGIGGDTTRHVLWRLKNGELE--NIKPKVIVVWVGTNN---HEN 109
Cdd:cd01838   3 VLF-GDSITQFSfdQGEFGFgaalADVYSRkLDVINRGFSGYNTRWALKVLPKIFLEekLAQPDLVTIFFGANDaalPGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 110 TA----EEVAGGIEAIVQLINTRQPQAKIIVLG--------LLPRGEKPNPLRQKNakvNQLLK------VSLPKLANVQ 171
Cdd:cd01838  82 PQhvplDEYKENLRKIVSHLKSLSPKTKVILITpppvdeeaWEKSLEDGGSQPGRT---NELLKqyaeacVEVAEELGVP 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 12653259 172 LLDTDGGFVHSDGAISChDMFDFLHLTGGGYakicKPLHELIMQLL 217
Cdd:cd01838 159 VIDLWTAMQEEAGWLES-LLTDGLHFSSKGY----ELLFEEIVKVI 199
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 42-205 1.30e-08

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: 52.24  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  42 VLFVGDSMVqlmqqyEIWRElfsplhalNFGIGGDTTRHVLwRLKNGELENIKPKVIVVWVGTN--NHENTAEEVAGGIE 119
Cdd:cd01833   3 IMPLGDSIT------WGDKD--------HEGHSGYLIDQIA-AAAADWVLAAKPDVVLLHLGTNdlVLNRDPDTAPDRLR 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 120 AIVQLINTRQPQAKIIVLGLLPRGEKPNPlrQKNAKVNQLLKVSLPKLAN----VQLLDTDGGFVHSDgaischDMFDFL 195
Cdd:cd01833  68 ALIDQMRAANPDVKIIVATLIPTTDASGN--ARIAEYNAAIPGVVADLRTagspVVLVDMSTGYTTAD------DLYDGL 139

                       170
                ....*....|
gi 12653259 196 HLTGGGYAKI 205
Cdd:cd01833 140 HPNDQGYKKM 149
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
42-205 2.01e-07

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 49.88  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259    42 VLFVGDSMVQLMQQY--------EIWRELFS---------PLHALNFGIGGDTTR------HVLWRLKNGELENIKPKVI 98
Cdd:pfam00657   1 IVAFGDSLTDGGGDGpggrfswgDLLADFLArklgvpgsgYNHGANFAIGGATIEdlpiqlEQLLRLISDVKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259    99 VVWVGTN---NHENTAEEVAGGIEAIVQLINTRQPQ-----AKIIVLGLLPRGEKPNP-----LRQKNAKVNQLLKVSLP 165
Cdd:pfam00657  81 TIFIGANdlcNFLSSPARSKKRVPDLLDELRANLPQlglgaRKFWVHGLGPLGCTPPKgcyelYNALAEEYNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 12653259   166 KLA------NVQLLDTdGGFVHSDGAiSCHDMF--DFLHLTGGGYAKI 205
Cdd:pfam00657 161 SLAaaaedaNVVYVDI-YGFEDPTDP-CCGIGLepDGLHPSEKGYKAV 206
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 42-205 1.42e-06

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: 47.29  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  42 VLFVGDSMVQLMQqYEIWRELF-------SPLHALNFGIGGDTTRHVLWRLKNGELEnIKPKVIVVWVGTN------NHE 108
Cdd:cd01834   4 IVFIGNSITDRGG-YVGYVETYlaarypeLKLTFRNLGWSGDTVSDLAARRDRDVLP-AKPDVVSIMFGINdsfrgfDDP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 109 NTAEEVAGGIEAIVQLINTRQPQAKIIVL--GLLPRGEKPNPLRQKNAKVNQLLKVSLPKLA---NVQLLDTDGGFVHS- 182
Cdd:cd01834  82 VGLEKFKTNLRRLIDRLKNKESAPRIVLVspIAYEANEDPLPDGAEYNANLAAYADAVRELAaenGVAFVDLFTPMKEAf 161

                       170       180
                ....*....|....*....|...
gi 12653259 183 DGAISCHDMFDFLHLTGGGYAKI 205
Cdd:cd01834 162 QKAGEAVLTVDGVHPNEAGHRAL 184
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 41-124 4.56e-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: 239945  Cd Length: 183  Bit Score: 42.70  E-value: 4.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  41 DVLFVGDSmvqLMQQY-----EIWREL---FSPLHALNFGIGGDTTRHVLWRLKNgELENIKPKVIVVWVGTNN--HENT 110
Cdd:cd04501   2 RVVCLGDS---ITYGYpvgpeASWVNLlaeFLGKEVINRGINGDTTSQMLVRFYE-DVIALKPAVVIIMGGTNDiiVNTS 77

                        90
                ....*....|....
gi 12653259 111 AEEVAGGIEAIVQL 124
Cdd:cd04501  78 LEMIKDNIRSMVEL 91
SGNH_hydrolase_peri2 cd01829
SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 42-215 7.77e-04

SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238867  Cd Length: 200  Bit Score: 39.18  E-value: 7.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  42 VLFVGDSMVQlmqqyEIWRELFSPLHAlNFGIG------GDT----TRHVLW--RLKNgELENIKPKVIVVWVGTNN--- 106
Cdd:cd01829   2 VLVIGDSLAQ-----GLAPGLLRALAD-NPGIRvinrskGSSglvrPDFFDWpeKLKE-LIAEEKPDVVVVFLGANDrqd 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259 107 -----------HENTAEEVAGGIEAIVQLIntRQPQAKIIVLGLLP-RGEKpnpLRQKNAKVNQLLKVSLPKlANVQLLD 174
Cdd:cd01829  75 irdgdgylkfgSPEWEEEYRQRIDELLNVA--RAKGVPVIWVGLPAmRSPK---LSADMVYLNSLYREEVAK-AGGEFVD 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 12653259 175 TDGGFVHSDG--AISCHDMF---------DFLHLTGGGYAKICKPLHELIMQ 215
Cdd:cd01829 149 VWDGFVDENGrfTYSGTDVNgkkvrlrtnDGIHFTAAGGRKLAFYVEKLIRR 200
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 89-217 4.13e-03

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: 36.87  E-value: 4.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  89 ELENIKPKVIVVWVGTN---NHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLR-QKNAKVNQLLKVsL 164
Cdd:cd01825  51 QLAALPPDLVILSYGTNeafNKQLNASEYRQQLREFIKRLRQILPNASILLVGPPDSLQKTGAGRwRTPPGLDAVIAA-Q 129

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12653259 165 PKLANvqlldtdggfvhsDGAISCHDMFDFL--------------------HLTGGGYAKICKPLHELIMQLL 217
Cdd:cd01825 130 RRVAK-------------EEGIAFWDLYAAMggeggiwqwaepglarkdyvHLTPRGYERLANLLYEALLKAY 189
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 42-151 7.30e-03

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: 36.09  E-value: 7.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12653259  42 VLFVGDSM-----VQLMQQ-------YEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELEniKPKVIVVWVGTNN--H 107
Cdd:cd01836   5 LLVLGDSTaagvgVETQDQalagqlaRGLAAITGRGVRWRLFAKTGATSADLLRQLAPLPET--RFDVAVISIGVNDvtH 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 12653259 108 ENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGE---KPNPLRQ 151
Cdd:cd01836  83 LTSIARWRKQLAELVDALRAKFPGARVVVTAVPPLGRfpaLPQPLRW 129
 
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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