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Conserved domains on  [gi|1720430520|ref|XP_030099984|]
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platelet-activating factor acetylhydrolase IB subunit alpha2 isoform X2 [Mus musculus]

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 ...
 11-220 8.45e-123

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: 346.97  E-value: 8.45e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  11 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 88
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  89 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVS 166
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720430520 167 LPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLL 220
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 ...
 11-220 8.45e-123

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: 346.97  E-value: 8.45e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  11 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 88
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  89 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVS 166
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720430520 167 LPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLL 220
Cdd:cd01820   161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTLARLL 214
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 39-208 9.06e-27

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: 101.64  E-value: 9.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  39 KDKEPDVLFVGDSMVQLMQQYEI--WRELF------SPLHALNFGIGGDTTRHVLWRLKnGELENIKPKVIVVWVGTNN- 109
Cdd:COG2755     5 AGKPLRIVALGDSITAGYGASRErgWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTNDl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 110 ---HENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEkPNPLRQKNAKVNQLLKvslpKLA---NVQLLDIDGGFv 183
Cdd:COG2755    84 lrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLR-PNYLNERIEAYNAAIR----ELAaeyGVPLVDLYAAL- 157

                         170       180
                  ....*....|....*....|....*
gi 1720430520 184 HSDGAISCHDMFDFLHLTGGGYAKI 208
Cdd:COG2755   158 RDAGDLPDLLTADGLHPNAAGYRLI 182
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 47-207 1.04e-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: 87.99  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  47 FVGDSMVQ---LMQQYEIWRELFSPLHA--------LNFGIGGDTTRHvLWRLKNGELENIKPKVIVVWVGTNN--HENT 113
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 114 AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRG----EKPNPLRQKNAKVNQLLKvSLPKLANVQLLDIDGGFVHSDGAI 189
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGppppLDERRLNARIAEYNAAIR-EVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*...
gi 1720430520 190 SCHDMFDFLHLTGGGYAK 207
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 ...
 11-220 8.45e-123

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: 346.97  E-value: 8.45e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  11 PAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQY--EIWRELFSPLHALNFGIGGDTTRHVLWRL 88
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  89 KNGELENIKPKVIVVWVGTNNHENT--AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVS 166
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720430520 167 LPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLL 220
Cdd:cd01820   161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTLARLL 214
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 39-208 9.06e-27

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: 101.64  E-value: 9.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  39 KDKEPDVLFVGDSMVQLMQQYEI--WRELF------SPLHALNFGIGGDTTRHVLWRLKnGELENIKPKVIVVWVGTNN- 109
Cdd:COG2755     5 AGKPLRIVALGDSITAGYGASRErgWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTNDl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 110 ---HENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEkPNPLRQKNAKVNQLLKvslpKLA---NVQLLDIDGGFv 183
Cdd:COG2755    84 lrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLR-PNYLNERIEAYNAAIR----ELAaeyGVPLVDLYAAL- 157

                         170       180
                  ....*....|....*....|....*
gi 1720430520 184 HSDGAISCHDMFDFLHLTGGGYAKI 208
Cdd:COG2755   158 RDAGDLPDLLTADGLHPNAAGYRLI 182
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 44-207 3.65e-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: 3.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  44 DVLFVGDSMVQLMQqyeiWRELFSPLHALNFGIGGDTTRHVLWRLKngELENIKPKVIVVWVGTNN--HENTAEEVAGGI 121
Cdd:cd01828     1 ALVFLGDSLTEGGP----WALLFPDVKVANRGISGDTTRGLLARLD--EDVALQPKAIFIMIGINDlaQGTSDEDIVANY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 122 EAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLkVSLPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLT 201
Cdd:cd01828    75 RTILEKLRKHFPNIKIVVQSILPVGELKSIPNEQIEELNRQL-AQLAQQEGVTFLDLWAVFTNADGDLKNEFTTDGLHLN 153


                  ....*.
gi 1720430520 202 GGGYAK 207
Cdd:cd01828   154 AKGYAV 159
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 47-207 1.04e-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: 87.99  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  47 FVGDSMVQ---LMQQYEIWRELFSPLHA--------LNFGIGGDTTRHvLWRLKNGELENIKPKVIVVWVGTNN--HENT 113
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 114 AEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRG----EKPNPLRQKNAKVNQLLKvSLPKLANVQLLDIDGGFVHSDGAI 189
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGppppLDERRLNARIAEYNAAIR-EVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*...
gi 1720430520 190 SCHDMFDFLHLTGGGYAK 207
Cdd:pfam13472 159 PDLLADDGLHPNAAGYRL 176
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 45-208 6.65e-18

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: 78.22  E-value: 6.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  45 VLFVGDSMVQLMQ-------QYEIWRELFSPLHAL----NFGIGGDTTRHVLWRLKNGELENI-KPKVIVVWVGTN---- 108
Cdd:cd00229     1 ILVIGDSITAGYGassgstfYSLLLYLLLLAGGPGveviNLGVSGATTADALRRLGLRLALLKdKPDLVIIELGTNdlgr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 109 NHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLK---VSLPKLANVQLLDIDGGFVHS 185
Cdd:cd00229    81 GGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKavaAENPAPSGVDLVDLAALLGDE 160

                         170       180
                  ....*....|....*....|...
gi 1720430520 186 DGAiscHDMFDFLHLTGGGYAKI 208
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 ...
 44-216 5.32e-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: 61.92  E-value: 5.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  44 DVLFVGDSMVQLmqqYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNgELENIKPKVIVVWVGTN--NHENTAEEVAGGI 121
Cdd:cd04502     1 GILFYGSSSIRL---WDTLADDLAPLPVVNRGFGGSTLADCLHYFDR-LVLPYQPRRVVLYAGDNdlASGRTPEEVLRDF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 122 EAIVQLINTRQPQAKIIVLGLlprgeKPNPLR----QKNAKVNQLLKVSLPKLANVQLLDIDGGFVHSDGaISCHDMF-- 195
Cdd:cd04502    77 RELVNRIRAKLPDTPIAIISI-----KPSPARwalrPKIRRFNALLKELAETRPNLTYIDVASPMLDADG-KPRAELFqe 150

                         170       180
                  ....*....|....*....|.
gi 1720430520 196 DFLHLTGGGYAKICKPLHELI 216
Cdd:cd04502   151 DGLHLNDAGYALWRKVIKPAL 171
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 43-216 9.91e-12

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: 61.19  E-value: 9.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  43 PDVLFVGDSMVQLMQQYEIwreLFSPLHALNFGIGGDTTRhvlWRLKNGELENI--KPKVIVVWVGTNN--HENTAEEVA 118
Cdd:cd01841     1 KNIVFIGDSLFEGWPLYEA---EGKGKTVNNLGIAGISSR---QYLEHIEPQLIqkNPSKVFLFLGTNDigKEVSSNQFI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 119 GGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKV---NQLLKVSLPKLaNVQLLDIDGGFVHSDGAISCHDMF 195
Cdd:cd01841    75 KWYRDIIEQIREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIqrlNDAIKELAPEL-GVTFIDLNDVLVDEFGNLKKEYTT 153

                         170       180
                  ....*....|....*....|.
gi 1720430520 196 DFLHLTGGGYAKIckpLHELI 216
Cdd:cd01841   154 DGLHFNPKGYQKL---LEILE 171
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 45-220 1.80e-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: 58.42  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  45 VLFvGDSMVQLM--QQYEIW----RELFSP-LHALNFGIGGDTTRHVLWRLKNGELE--NIKPKVIVVWVGTNN---HEN 112
Cdd:cd01838     3 VLF-GDSITQFSfdQGEFGFgaalADVYSRkLDVINRGFSGYNTRWALKVLPKIFLEekLAQPDLVTIFFGANDaalPGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 113 TA----EEVAGGIEAIVQLINTRQPQAKIIVLG--------LLPRGEKPNPLRQKNakvNQLLK------VSLPKLANVQ 174
Cdd:cd01838    82 PQhvplDEYKENLRKIVSHLKSLSPKTKVILITpppvdeeaWEKSLEDGGSQPGRT---NELLKqyaeacVEVAEELGVP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720430520 175 LLDIDGGFVHSDGAISChDMFDFLHLTGGGYakicKPLHELIMQLL 220
Cdd:cd01838   159 VIDLWTAMQEEAGWLES-LLTDGLHFSSKGY----ELLFEEIVKVI 199
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 45-208 2.16e-09

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: 54.55  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  45 VLFVGDSMVqlmqqyEIWRElfsplhalNFGIGGDTTRHVLwRLKNGELENIKPKVIVVWVGTN--NHENTAEEVAGGIE 122
Cdd:cd01833     3 IMPLGDSIT------WGDKD--------HEGHSGYLIDQIA-AAAADWVLAAKPDVVLLHLGTNdlVLNRDPDTAPDRLR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 123 AIVQLINTRQPQAKIIVLGLLPRGEKPNPlrQKNAKVNQLLKVSLPKLAN----VQLLDIDGGFVHSDgaischDMFDFL 198
Cdd:cd01833    68 ALIDQMRAANPDVKIIVATLIPTTDASGN--ARIAEYNAAIPGVVADLRTagspVVLVDMSTGYTTAD------DLYDGL 139

                         170
                  ....*....|
gi 1720430520 199 HLTGGGYAKI 208
Cdd:cd01833   140 HPNDQGYKKM 149
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
45-208 2.77e-08

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 52.19  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  45 VLFVGDSMVQLMQQY--------EIWRELFS---------PLHALNFGIGGDTTR------HVLWRLKNGELENIKPKVI 101
Cdd:pfam00657   1 IVAFGDSLTDGGGDGpggrfswgDLLADFLArklgvpgsgYNHGANFAIGGATIEdlpiqlEQLLRLISDVKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 102 VVWVGTN---NHENTAEEVAGGIEAIVQLINTRQPQ-----AKIIVLGLLPRGEKPNP-----LRQKNAKVNQLLKVSLP 168
Cdd:pfam00657  81 TIFIGANdlcNFLSSPARSKKRVPDLLDELRANLPQlglgaRKFWVHGLGPLGCTPPKgcyelYNALAEEYNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720430520 169 KLA------NVQLLDIdGGFVHSDGAiSCHDMF--DFLHLTGGGYAKI 208
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 ...
 45-208 8.27e-07

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


Pssm-ID: 238872  Cd Length: 191  Bit Score: 47.67  E-value: 8.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  45 VLFVGDSMVQLMQqYEIWRELF-------SPLHALNFGIGGDTTRHVLWRLKNGELEnIKPKVIVVWVGTN------NHE 111
Cdd:cd01834     4 IVFIGNSITDRGG-YVGYVETYlaarypeLKLTFRNLGWSGDTVSDLAARRDRDVLP-AKPDVVSIMFGINdsfrgfDDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 112 NTAEEVAGGIEAIVQLINTRQPQAKIIVL--GLLPRGEKPNPLRQKNAKVNQLLKVSLPKLA---NVQLLDIDGGFVHS- 185
Cdd:cd01834    82 VGLEKFKTNLRRLIDRLKNKESAPRIVLVspIAYEANEDPLPDGAEYNANLAAYADAVRELAaenGVAFVDLFTPMKEAf 161

                         170       180
                  ....*....|....*....|...
gi 1720430520 186 DGAISCHDMFDFLHLTGGGYAKI 208
Cdd:cd01834   162 QKAGEAVLTVDGVHPNEAGHRAL 184
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 44-127 5.15e-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: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  44 DVLFVGDSmvqLMQQY-----EIWREL---FSPLHALNFGIGGDTTRHVLWRLKNgELENIKPKVIVVWVGTNN--HENT 113
Cdd:cd04501     2 RVVCLGDS---ITYGYpvgpeASWVNLlaeFLGKEVINRGINGDTTSQMLVRFYE-DVIALKPAVVIIMGGTNDiiVNTS 77

                          90
                  ....*....|....
gi 1720430520 114 AEEVAGGIEAIVQL 127
Cdd:cd04501    78 LEMIKDNIRSMVEL 91
SGNH_hydrolase_peri2 cd01829
SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 45-218 1.15e-03

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: 38.80  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  45 VLFVGDSMVQlmqqyEIWRELFSPLHAlNFGIG------GDT----TRHVLW--RLKNgELENIKPKVIVVWVGTNN--- 109
Cdd:cd01829     2 VLVIGDSLAQ-----GLAPGLLRALAD-NPGIRvinrskGSSglvrPDFFDWpeKLKE-LIAEEKPDVVVVFLGANDrqd 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520 110 -----------HENTAEEVAGGIEAIVQLIntRQPQAKIIVLGLLP-RGEKpnpLRQKNAKVNQLLKVSLPKlANVQLLD 177
Cdd:cd01829    75 irdgdgylkfgSPEWEEEYRQRIDELLNVA--RAKGVPVIWVGLPAmRSPK---LSADMVYLNSLYREEVAK-AGGEFVD 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720430520 178 IDGGFVHSDG--AISCHDMF---------DFLHLTGGGYAKICKPLHELIMQ 218
Cdd:cd01829   149 VWDGFVDENGrfTYSGTDVNgkkvrlrtnDGIHFTAAGGRKLAFYVEKLIRR 200
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 92-220 4.03e-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: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  92 ELENIKPKVIVVWVGTN---NHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLR-QKNAKVNQLLKVsL 167
Cdd:cd01825    51 QLAALPPDLVILSYGTNeafNKQLNASEYRQQLREFIKRLRQILPNASILLVGPPDSLQKTGAGRwRTPPGLDAVIAA-Q 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720430520 168 PKLANvqlldidggfvhsDGAISCHDMFDFL--------------------HLTGGGYAKICKPLHELIMQLL 220
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 ...
 45-154 7.47e-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: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  45 VLFVGDSM-----VQLMQQ-------YEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELEniKPKVIVVWVGTNN--H 110
Cdd:cd01836     5 LLVLGDSTaagvgVETQDQalagqlaRGLAAITGRGVRWRLFAKTGATSADLLRQLAPLPET--RFDVAVISIGVNDvtH 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720430520 111 ENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGE---KPNPLRQ 154
Cdd:cd01836    83 LTSIARWRKQLAELVDALRAKFPGARVVVTAVPPLGRfpaLPQPLRW 129
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 73-142 8.78e-03

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. This subfamily contains sequences similar to Bacillus YpmR.


Pssm-ID: 239947  Cd Length: 204  Bit Score: 36.07  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430520  73 NFGIGGDTTRHVLWRLKNGE-LENIK-PKVIVVWVGTNN---------HENTAEEVAGGIEA-------IVQLINTRQPQ 134
Cdd:cd04506    42 NFGVSGDRSDQLLKRLKTKKvQKELKkADVITITIGGNDlmqvleknfLSLDVEDFKKAEETyqnnlkkIFKEIRKLNPD 121


                  ....*...
gi 1720430520 135 AKIIVLGL 142
Cdd:cd04506   122 APIFLVGL 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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