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Conserved domains on  [gi|225543099|ref|NP_001139412|]
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platelet-activating factor acetylhydrolase IB subunit alpha1 [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 ...
 7-205 1.12e-119

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: 339.27  E-value: 1.12e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099   7 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDGTQHVLWRL 84
Cdd:cd01820    1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  85 ENGELEHIRPKIVVVWVGTNNHGHT--AEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAA 162
Cdd:cd01820   81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225543099 163 LAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 205
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 ...
 7-205 1.12e-119

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: 339.27  E-value: 1.12e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099   7 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDGTQHVLWRL 84
Cdd:cd01820    1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  85 ENGELEHIRPKIVVVWVGTNNHGHT--AEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAA 162
Cdd:cd01820   81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225543099 163 LAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 205
Cdd:cd01820  161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWA 203
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 34-201 2.25e-30

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: 111.27  E-value: 2.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  34 SKDKEPEVVFIGDSLVQLM--HQCEIWRELF------SPLHALNFGIGGDGTQHVLWRLEnGELEHIRPKIVVVWVGTNN 105
Cdd:COG2755    4 AAGKPLRIVALGDSITAGYgaSRERGWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTND 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 106 ----HGHTAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGqHPNPLREKNRQVNELVRaALAGHPRAHFLDADPGFvHS 181
Cdd:COG2755   83 llrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRL-RPNYLNERIEAYNAAIR-ELAAEYGVPLVDLYAAL-RD 159

                        170       180
                 ....*....|....*....|
gi 225543099 182 DGTISHHDMYDYLHLSRLGY 201
Cdd:COG2755  160 AGDLPDLLTADGLHPNAAGY 179
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 43-201 7.69e-23

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: 91.07  E-value: 7.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099   43 FIGDSLVQ---LMHQCEIWRELFSPLHA--------LNFGIGGDGTQHvLWRLENGELEHIRPKIVVVWVGTNN--HGHT 109
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  110 AEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNP----LREKNRQVNELVRaALAGHPRAHFLDADPGFVHSDGTI 185
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLderrLNARIAEYNAAIR-EVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 225543099  186 SHHDMYDYLHLSRLGY 201
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 ...
 7-205 1.12e-119

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: 339.27  E-value: 1.12e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099   7 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDGTQHVLWRL 84
Cdd:cd01820    1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  85 ENGELEHIRPKIVVVWVGTNNHGHT--AEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAA 162
Cdd:cd01820   81 ENGELDGVNPKVVVLLIGTNNIGHTttAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225543099 163 LAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 205
Cdd:cd01820  161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWA 203
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 34-201 2.25e-30

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: 111.27  E-value: 2.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  34 SKDKEPEVVFIGDSLVQLM--HQCEIWRELF------SPLHALNFGIGGDGTQHVLWRLEnGELEHIRPKIVVVWVGTNN 105
Cdd:COG2755    4 AAGKPLRIVALGDSITAGYgaSRERGWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTND 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 106 ----HGHTAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGqHPNPLREKNRQVNELVRaALAGHPRAHFLDADPGFvHS 181
Cdd:COG2755   83 llrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRL-RPNYLNERIEAYNAAIR-ELAAEYGVPLVDLYAAL-RD 159

                        170       180
                 ....*....|....*....|
gi 225543099 182 DGTISHHDMYDYLHLSRLGY 201
Cdd:COG2755  160 AGDLPDLLTADGLHPNAAGY 179
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 43-201 7.69e-23

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: 91.07  E-value: 7.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099   43 FIGDSLVQ---LMHQCEIWRELFSPLHA--------LNFGIGGDGTQHvLWRLENGELEHIRPKIVVVWVGTNN--HGHT 109
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  110 AEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNP----LREKNRQVNELVRaALAGHPRAHFLDADPGFVHSDGTI 185
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLderrLNARIAEYNAAIR-EVAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 225543099  186 SHHDMYDYLHLSRLGY 201
Cdd:pfam13472 159 PDLLADDGLHPNAAGY 174
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 40-201 1.21e-22

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: 90.42  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  40 EVVFIGDSLVQLMHqceiWRELFSPLHALNFGIGGDGTQHVLWRLEngELEHIRPKIVVVWVGTNN--HGHTAEQVTGGI 117
Cdd:cd01828    1 ALVFLGDSLTEGGP----WALLFPDVKVANRGISGDTTRGLLARLD--EDVALQPKAIFIMIGINDlaQGTSDEDIVANY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 118 KAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRaALAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLS 197
Cdd:cd01828   75 RTILEKLRKHFPNIKIVVQSILPVGELKSIPNEQIEELNRQLA-QLAQQEGVTFLDLWAVFTNADGDLKNEFTTDGLHLN 153


                 ....
gi 225543099 198 RLGY 201
Cdd:cd01828  154 AKGY 157
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 41-201 8.97e-20

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: 83.23  E-value: 8.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  41 VVFIGDSLVQLMH--QCEIWRELFSPLHAL---------NFGIGGDGTQHVLWRLENG-ELEHIRPKIVVVWVGTNNHGH 108
Cdd:cd00229    1 ILVIGDSITAGYGasSGSTFYSLLLYLLLLaggpgveviNLGVSGATTADALRRLGLRlALLKDKPDLVIIELGTNDLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 109 ----TAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGHPR---AHFLDADPGFVHS 181
Cdd:cd00229   81 ggdtSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENPApsgVDLVDLAALLGDE 160

                        170       180
                 ....*....|....*....|
gi 225543099 182 DgtiSHHDMYDYLHLSRLGY 201
Cdd:cd00229  161 D---KSLYSPDGIHPNPAGH 177
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 41-201 1.83e-10

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: 57.68  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  41 VVFIGDSLVQLmhqceiW---RELFSPLHALNFGIGGdgtQHVLWRLENGE--LEHIRPKIVVVWVGTN--NHGHTAEQV 113
Cdd:cd04502    2 ILFYGSSSIRL------WdtlADDLAPLPVVNRGFGG---STLADCLHYFDrlVLPYQPRRVVLYAGDNdlASGRTPEEV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 114 TGGIKAIVQLVNERQPQARVVVLGLLP---RGQhpnpLREKNRQVNELVRAALAGHPRAHFLDADPGFVHSDGtISHHDM 190
Cdd:cd04502   73 LRDFRELVNRIRAKLPDTPIAIISIKPspaRWA----LRPKIRRFNALLKELAETRPNLTYIDVASPMLDADG-KPRAEL 147

                        170
                 ....*....|...
gi 225543099 191 Y--DYLHLSRLGY 201
Cdd:cd04502  148 FqeDGLHLNDAGY 160
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
41-201 1.03e-09

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 56.43  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099   41 VVFIGDSLVQLMHQC--------EIWRELFS---------PLHALNFGIGGDGTQ------HVLWRLENGELEHIRPKIV 97
Cdd:pfam00657   1 IVAFGDSLTDGGGDGpggrfswgDLLADFLArklgvpgsgYNHGANFAIGGATIEdlpiqlEQLLRLISDVKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099   98 VVWVGTN---NHGHTAEQVTGGIKAIVQLVNERQPQ-----ARVVVLGLLPRGQHPNPLREK---------NRQVNELVR 160
Cdd:pfam00657  81 TIFIGANdlcNFLSSPARSKKRVPDLLDELRANLPQlglgaRKFWVHGLGPLGCTPPKGCYElynalaeeyNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 225543099  161 AALAGHPRAHFLDAD-PGFVHSDGTISHHDM-YDYLHLSRLGY 201
Cdd:pfam00657 161 SLAAAAEDANVVYVDiYGFEDPTDPCCGIGLePDGLHPSEKGY 203
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 39-202 2.68e-09

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: 54.64  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  39 PEVVFIGDSLVqlmhqcEIW--RELFSPLHAL-NFGIGGDGTQhvlWRLENGELEHIR--PKIVVVWVGTNN--HGHTAE 111
Cdd:cd01841    1 KNIVFIGDSLF------EGWplYEAEGKGKTVnNLGIAGISSR---QYLEHIEPQLIQknPSKVFLFLGTNDigKEVSSN 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 112 QVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRA--ALAGHPRAHFLDADPGFVHSDGTISHHD 189
Cdd:cd01841   72 QFIKWYRDIIEQIREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIQRLNDAikELAPELGVTFIDLNDVLVDEFGNLKKEY 151

                        170
                 ....*....|...
gi 225543099 190 MYDYLHLSRLGYT 202
Cdd:cd01841  152 TTDGLHFNPKGYQ 164
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 41-201 3.80e-07

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: 48.79  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  41 VVFIGDSLVQLMHQCEIW------RELFSP-LHALNFGIGGDGTQHVLWRLENGELEH--IRPKIVVVWVGTN------- 104
Cdd:cd01838    2 IVLFGDSITQFSFDQGEFgfgaalADVYSRkLDVINRGFSGYNTRWALKVLPKIFLEEklAQPDLVTIFFGANdaalpgq 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 105 -NHGHTAEQVTgGIKAIVQLVNERQPQARVVVLG------LLPRGQHPNPLREKNRqVNELVRA------ALAGHPRAHF 171
Cdd:cd01838   82 pQHVPLDEYKE-NLRKIVSHLKSLSPKTKVILITpppvdeEAWEKSLEDGGSQPGR-TNELLKQyaeacvEVAEELGVPV 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 225543099 172 LDADPGFVHSDGTIShHDMYDYLHLSRLGY 201
Cdd:cd01838  160 IDLWTAMQEEAGWLE-SLLTDGLHFSSKGY 188
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 93-201 1.10e-06

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: 46.84  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  93 RPKIVVVWVGTN--NHGHTAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRgqHPNPLREKNRQVNELVRAALAGHPRA- 169
Cdd:cd01833   40 KPDVVLLHLGTNdlVLNRDPDTAPDRLRALIDQMRAANPDVKIIVATLIPT--TDASGNARIAEYNAAIPGVVADLRTAg 117

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 225543099 170 ---HFLDADPGFVHSDgtishhDMYDYLHLSRLGY 201
Cdd:cd01833  118 spvVLVDMSTGYTTAD------DLYDGLHPNDQGY 146
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 40-201 6.47e-06

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: 45.01  E-value: 6.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  40 EVVFIGDSLVQ--LMHQCEIWREL---FSPLHALNFGIGGDGTQHVLWRLENgELEHIRPKIVVVWVGTNN--HGHTAEQ 112
Cdd:cd04501    2 RVVCLGDSITYgyPVGPEASWVNLlaeFLGKEVINRGINGDTTSQMLVRFYE-DVIALKPAVVIIMGGTNDiiVNTSLEM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 113 VTGGIKAIVQLVNErqpqARV-VVLGLLPRGQHPNPLREKNRQVNELVR-----AALAGHPRAHFLD-----ADPGFVHS 181
Cdd:cd04501   81 IKDNIRSMVELAEA----NGIkVILASPLPVDDYPWKPQWLRPANKLKSlnrwlKDYARENGLLFLDfysplLDERNVGL 156

                        170       180
                 ....*....|....*....|
gi 225543099 182 DGTIShhdmYDYLHLSRLGY 201
Cdd:cd04501  157 KPGLL----TDGLHPSREGY 172
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 41-201 1.23e-05

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: 44.59  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  41 VVFIGDSLVQLMHqceiWRELFSP-LHAL---------NFGIGGDGTQHVLWRLENGELEHiRPKIVVVWVGTNNHGHTA 110
Cdd:cd01834    4 IVFIGNSITDRGG----YVGYVETyLAARypelkltfrNLGWSGDTVSDLAARRDRDVLPA-KPDVVSIMFGINDSFRGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 111 EQVTG------GIKAIVQLVNERQPQARVVVL--GLLPRGQHPNPLR-EKNRQVNELVRA--ALAGHPRAHFLDADPGFV 179
Cdd:cd01834   79 DDPVGlekfktNLRRLIDRLKNKESAPRIVLVspIAYEANEDPLPDGaEYNANLAAYADAvrELAAENGVAFVDLFTPMK 158

                        170       180
                 ....*....|....*....|....*..
gi 225543099 180 -----HSDGTISHhdmyDYLHLSRLGY 201
Cdd:cd01834  159 eafqkAGEAVLTV----DGVHPNEAGH 181
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 109-178 4.35e-04

SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this 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, but may lack the carboxylic acid.


Pssm-ID: 238861  Cd Length: 259  Bit Score: 40.51  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 109 TAEQVTGGIKAIVQLVNERQPQARVVVLG----LLPRGQHPNP---------------LREKNRQVNELVR--AALAGHP 167
Cdd:cd01823  125 ALDEVGARLKAVLDRIRERAPNARVVVVGyprlFPPDGGDCDKscspgtpltpadrpeLNQLVDKLNALIRraAADAGDY 204

                         90
                 ....*....|.
gi 225543099 168 RAHFLDADPGF 178
Cdd:cd01823  205 KVRFVDTDAPF 215
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 41-161 7.92e-04

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


Pssm-ID: 238873  Cd Length: 193  Bit Score: 39.24  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  41 VVFIGDSLV-------------QLMHQceiWRELFSPLHALNFGIGGDGTQHVLWRLEN-----GELEHirPKIVVVWVG 102
Cdd:cd01835    4 LIVVGDSLVygwgdpegggwvgRLRAR---WMNLGDDPVLYNLGVRGDGSEDVAARWRAewsrrGELNV--PNRLVLSVG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225543099 103 TNNH---GHTAEQVT--GGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLRekNRQVNELVRA 161
Cdd:cd01835   79 LNDTargGRKRPQLSarAFLFGLNQLLEEAKRLVPVLVVGPTPVDEAKMPYS--NRRIARLETA 140
SGNH_hydrolase_peri2 cd01829
SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 41-183 3.79e-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: 37.26  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099  41 VVFIGDSLVQlmhqcEIWRELFSPLHA------LNFGIGGDG---TQHVLW--RLENgELEHIRPKIVVVWVGTN----- 104
Cdd:cd01829    2 VLVIGDSLAQ-----GLAPGLLRALADnpgirvINRSKGSSGlvrPDFFDWpeKLKE-LIAEEKPDVVVVFLGANdrqdi 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543099 105 --NHGH----TAEQVTGGIKAIVQLVNE-RQPQARVVVLGLLPRGQhpNPLREKNRQVNELVRAALAGHPrAHFLDADPG 177
Cdd:cd01829   76 rdGDGYlkfgSPEWEEEYRQRIDELLNVaRAKGVPVIWVGLPAMRS--PKLSADMVYLNSLYREEVAKAG-GEFVDVWDG 152


                 ....*.
gi 225543099 178 FVHSDG 183
Cdd:cd01829  153 FVDENG 158
 
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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