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Conserved domains on  [gi|1270111405|ref|NP_001344279|]
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platelet-activating factor acetylhydrolase IB subunit alpha1 isoform a [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 ...
 8-206 3.80e-117

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: 332.72  E-value: 3.80e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405   8 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDSTQHVLWRL 85
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  86 ENGELEHIRPKIVVVWVGTNN--HSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAA 163
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNigHTTTAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270111405 164 LAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 206
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 ...
 8-206 3.80e-117

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: 332.72  E-value: 3.80e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405   8 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDSTQHVLWRL 85
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  86 ENGELEHIRPKIVVVWVGTNN--HSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAA 163
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNigHTTTAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270111405 164 LAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 206
Cdd:cd01820   161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWA 203
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 35-202 6.26e-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: 110.12  E-value: 6.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  35 SKDKEPEVVFIGDSLVQLM--HQCEIWRELF------SPLHALNFGIGGDSTQHVLWRLEnGELEHIRPKIVVVWVGTNN 106
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYgaSRERGWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 107 ----HSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGqHPNPLREKNRQVNELVRaALAGYPRAHFLDADPGFvHS 182
Cdd:COG2755    83 llrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRL-RPNYLNERIEAYNAAIR-ELAAEYGVPLVDLYAAL-RD 159

                         170       180
                  ....*....|....*....|
gi 1270111405 183 DGTISHHDMYDYLHLSRLGY 202
Cdd:COG2755   160 AGDLPDLLTADGLHPNAAGY 179
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 44-202 8.11e-22

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: 88.37  E-value: 8.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  44 FIGDSLVQ---LMHQCEIWRELFSPLHA--------LNFGIGGDSTQHvLWRLENGELEHIRPKIVVVWVGTNN--HSHT 110
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 111 AEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNP----LREKNRQVNELVRAaLAGYPRAHFLDADPGFVHSDGTI 186
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLderrLNARIAEYNAAIRE-VAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 1270111405 187 SHHDMYDYLHLSRLGY 202
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 ...
 8-206 3.80e-117

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: 332.72  E-value: 3.80e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405   8 PASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQC--EIWRELFSPLHALNFGIGGDSTQHVLWRL 85
Cdd:cd01820     1 PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTglEVWRELYAPLHALNFGIGGDRTQNVLWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  86 ENGELEHIRPKIVVVWVGTNN--HSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAA 163
Cdd:cd01820    81 ENGELDGVNPKVVVLLIGTNNigHTTTAEEIAEGILAIVEEIREKLPNAKILLLGLLPRGQNPNPLRERNAQVNRLLAVR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270111405 164 LAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVC 206
Cdd:cd01820   161 YDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWA 203
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 35-202 6.26e-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: 110.12  E-value: 6.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  35 SKDKEPEVVFIGDSLVQLM--HQCEIWRELF------SPLHALNFGIGGDSTQHVLWRLEnGELEHIRPKIVVVWVGTNN 106
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYgaSRERGWPALLarrlaaADVRVVNAGISGATTADLLARLD-RDLLALKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 107 ----HSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGqHPNPLREKNRQVNELVRaALAGYPRAHFLDADPGFvHS 182
Cdd:COG2755    83 llrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRL-RPNYLNERIEAYNAAIR-ELAAEYGVPLVDLYAAL-RD 159

                         170       180
                  ....*....|....*....|
gi 1270111405 183 DGTISHHDMYDYLHLSRLGY 202
Cdd:COG2755   160 AGDLPDLLTADGLHPNAAGY 179
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 41-202 2.68e-23

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: 91.96  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  41 EVVFIGDSLVQLMHqceiWRELFSPLHALNFGIGGDSTQHVLWRLEngELEHIRPKIVVVWVGTNNHSH--TAEQVTGGI 118
Cdd:cd01828     1 ALVFLGDSLTEGGP----WALLFPDVKVANRGISGDTTRGLLARLD--EDVALQPKAIFIMIGINDLAQgtSDEDIVANY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 119 KAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRaALAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLS 198
Cdd:cd01828    75 RTILEKLRKHFPNIKIVVQSILPVGELKSIPNEQIEELNRQLA-QLAQQEGVTFLDLWAVFTNADGDLKNEFTTDGLHLN 153


                  ....
gi 1270111405 199 RLGY 202
Cdd:cd01828   154 AKGY 157
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 44-202 8.11e-22

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: 88.37  E-value: 8.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  44 FIGDSLVQ---LMHQCEIWRELFSPLHA--------LNFGIGGDSTQHvLWRLENGELEHIRPKIVVVWVGTNN--HSHT 110
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLArrlgadvvNNLGISGATTRL-DLLERLDDVLRLKPDLVVILLGTNDlgRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 111 AEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNP----LREKNRQVNELVRAaLAGYPRAHFLDADPGFVHSDGTI 186
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLderrLNARIAEYNAAIRE-VAAERGVPYVDLWDALRDDGGWL 158

                         170
                  ....*....|....*.
gi 1270111405 187 SHHDMYDYLHLSRLGY 202
Cdd:pfam13472 159 PDLLADDGLHPNAAGY 174
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 42-202 2.07e-19

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: 82.46  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  42 VVFIGDSLVQLMH--QCEIWRELFSPLHAL---------NFGIGGDSTQHVLWRLENG-ELEHIRPKIVVVWVGTN---- 105
Cdd:cd00229     1 ILVIGDSITAGYGasSGSTFYSLLLYLLLLaggpgveviNLGVSGATTADALRRLGLRlALLKDKPDLVIIELGTNdlgr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 106 NHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGYPR---AHFLDADPGFVHS 182
Cdd:cd00229    81 GGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENPApsgVDLVDLAALLGDE 160

                         170       180
                  ....*....|....*....|
gi 1270111405 183 DgtiSHHDMYDYLHLSRLGY 202
Cdd:cd00229   161 D---KSLYSPDGIHPNPAGH 177
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 40-203 1.09e-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: 55.80  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  40 PEVVFIGDSLVqlmhqcEIW--RELFSPLHAL-NFGIGGDSTQhvlWRLENGELEHIR--PKIVVVWVGTNN--HSHTAE 112
Cdd:cd01841     1 KNIVFIGDSLF------EGWplYEAEGKGKTVnNLGIAGISSR---QYLEHIEPQLIQknPSKVFLFLGTNDigKEVSSN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 113 QVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRA--ALAGYPRAHFLDADPGFVHSDGTISHHD 190
Cdd:cd01841    72 QFIKWYRDIIEQIREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIQRLNDAikELAPELGVTFIDLNDVLVDEFGNLKKEY 151

                         170
                  ....*....|...
gi 1270111405 191 MYDYLHLSRLGYT 203
Cdd:cd01841   152 TTDGLHFNPKGYQ 164
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
42-202 4.23e-09

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 54.50  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  42 VVFIGDSLVQLMHQC--------EIWRELFS---------PLHALNFGIGGDSTQ------HVLWRLENGELEHIRPKIV 98
Cdd:pfam00657   1 IVAFGDSLTDGGGDGpggrfswgDLLADFLArklgvpgsgYNHGANFAIGGATIEdlpiqlEQLLRLISDVKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  99 VVWVGTN---NHSHTAEQVTGGIK-AIVQLVNKLQ----PQARVVVLGLLPRGQHPNPLREK---------NRQVNELVR 161
Cdd:pfam00657  81 TIFIGANdlcNFLSSPARSKKRVPdLLDELRANLPqlglGARKFWVHGLGPLGCTPPKGCYElynalaeeyNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270111405 162 AALAGYPRAHFLDAD-PGFVHSDGTISHHDM-YDYLHLSRLGY 202
Cdd:pfam00657 161 SLAAAAEDANVVYVDiYGFEDPTDPCCGIGLePDGLHPSEKGY 203
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 42-202 9.50e-09

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: 53.06  E-value: 9.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  42 VVFIGDSLVQLmhqceiW---RELFSPLHALNFGIGGdST----QHVLWRLengeLEHIRPKIVVVWVGTNNHSH--TAE 112
Cdd:cd04502     2 ILFYGSSSIRL------WdtlADDLAPLPVVNRGFGG-STladcLHYFDRL----VLPYQPRRVVLYAGDNDLASgrTPE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 113 QVTGGIKAIVQLVNKLQPQARVVVLGLLP---RGQhpnpLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGtISHH 189
Cdd:cd04502    71 EVLRDFRELVNRIRAKLPDTPIAIISIKPspaRWA----LRPKIRRFNALLKELAETRPNLTYIDVASPMLDADG-KPRA 145

                         170
                  ....*....|....*
gi 1270111405 190 DMY--DYLHLSRLGY 202
Cdd:cd04502   146 ELFqeDGLHLNDAGY 160
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 42-202 7.35e-08

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: 51.10  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  42 VVFIGDSLVQLMHQCEIW------RELFSP-LHALNFGIGGDSTQHVLWRLENGELEH--IRPKIVVVWVGTNNHSHTAE 112
Cdd:cd01838     2 IVLFGDSITQFSFDQGEFgfgaalADVYSRkLDVINRGFSGYNTRWALKVLPKIFLEEklAQPDLVTIFFGANDAALPGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 113 QVTG-------GIKAIVQLVNKLQPQARVVVLG------LLPRGQHPNPLREKNRqVNELVRA------ALAGYPRAHFL 173
Cdd:cd01838    82 PQHVpldeykeNLRKIVSHLKSLSPKTKVILITpppvdeEAWEKSLEDGGSQPGR-TNELLKQyaeacvEVAEELGVPVI 160

                         170       180
                  ....*....|....*....|....*....
gi 1270111405 174 DADPGFVHSDGTIShHDMYDYLHLSRLGY 202
Cdd:cd01838   161 DLWTAMQEEAGWLE-SLLTDGLHFSSKGY 188
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 94-202 9.03e-07

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: 47.23  E-value: 9.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  94 RPKIVVVWVGTN--NHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRgqHPNPLREKNRQVNELVRAALAGYPRA- 170
Cdd:cd01833    40 KPDVVLLHLGTNdlVLNRDPDTAPDRLRALIDQMRAANPDVKIIVATLIPT--TDASGNARIAEYNAAIPGVVADLRTAg 117

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1270111405 171 ---HFLDADPGFVHSDgtishhDMYDYLHLSRLGY 202
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 ...
 41-202 6.11e-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: 42.31  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  41 EVVFIGDSLVQ--LMHQCEIWREL---FSPLHALNFGIGGDSTQHVLWRLENgELEHIRPKIVVVWVGTNN--HSHTAEQ 113
Cdd:cd04501     2 RVVCLGDSITYgyPVGPEASWVNLlaeFLGKEVINRGINGDTTSQMLVRFYE-DVIALKPAVVIIMGGTNDiiVNTSLEM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 114 VTGGIKAIVQLVNKlqpqARV-VVLGLLPRGQHPNPLREKNRQVNELV--RAALAGYPRAH---FLD-----ADPGFVHS 182
Cdd:cd04501    81 IKDNIRSMVELAEA----NGIkVILASPLPVDDYPWKPQWLRPANKLKslNRWLKDYARENgllFLDfysplLDERNVGL 156

                         170       180
                  ....*....|....*....|
gi 1270111405 183 DGTIShhdmYDYLHLSRLGY 202
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 ...
 42-202 2.53e-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: 238872  Cd Length: 191  Bit Score: 40.74  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  42 VVFIGDSLVQLMHqceiWRELFSP-LHAL---------NFGIGGDSTQHVLWRLENGELEHiRPKIVVVWVGTNN---HS 108
Cdd:cd01834     4 IVFIGNSITDRGG----YVGYVETyLAARypelkltfrNLGWSGDTVSDLAARRDRDVLPA-KPDVVSIMFGINDsfrGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 109 HTAEQVTGGIKAIVQLVNKLQPQARVVVLGLL-----PRGQHPNPLR-EKNRQVNELVRA--ALAGYPRAHFLDADPGFV 180
Cdd:cd01834    79 DDPVGLEKFKTNLRRLIDRLKNKESAPRIVLVspiayEANEDPLPDGaEYNANLAAYADAvrELAAENGVAFVDLFTPMK 158

                         170       180
                  ....*....|....*....|....*..
gi 1270111405 181 -----HSDGTISHhdmyDYLHLSRLGY 202
Cdd:cd01834   159 eafqkAGEAVLTV----DGVHPNEAGH 181
SGNH pfam19040
SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to ...
 32-201 6.75e-04

SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to membrane domains from the AT3 families pfam01757.


Pssm-ID: 436916  Cd Length: 245  Bit Score: 39.59  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  32 VADSKDKEPEVVFIGDSlvqlmHQCEIWRELFSPLHALNFGI----------------GGDSTQHVLWRLENGELEHIRP 95
Cdd:pfam19040  17 RLGDGAGPPSVLLWGDS-----HAAALAPGLDEAAKERGVSVlqitrsgcpplllrlpDAACAAFNAAILEALALLPSKP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  96 KIVVV---W---------VGTNNHSHTAEQVTGGIKAIVQLVNKLQPQ-ARVVVLGLLPR-------------------- 142
Cdd:pfam19040  92 DTVVLaarWslylegpafNDEGIGRDLSNTIAAFAAALRATVAALAAAgKKVVLLGPVPEyvprnarclaraggllrdpl 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270111405 143 -GQHPNPLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGT--ISHHDM--YDYLHLSRLG 201
Cdd:pfam19040 172 cSIPRAEYRARNARVNAALDELAAKPGKVRVIDPSPLFCDDGGRcsALDGTPlyFDDNHLSPAG 235
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 110-179 1.68e-03

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: 38.59  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405 110 TAEQVTGGIKAIVQLVNKLQPQARVVVLG----LLPRGQHPNP---------------LREKNRQVNELVR--AALAGYP 168
Cdd:cd01823   125 ALDEVGARLKAVLDRIRERAPNARVVVVGyprlFPPDGGDCDKscspgtpltpadrpeLNQLVDKLNALIRraAADAGDY 204

                          90
                  ....*....|.
gi 1270111405 169 RAHFLDADPGF 179
Cdd:cd01823   205 KVRFVDTDAPF 215
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 42-162 2.12e-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: 238873  Cd Length: 193  Bit Score: 38.09  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  42 VVFIGDSLV-------------QLMHQceiWRELFSPLHALNFGIGGDSTQHVLWRLEN-----GELEHirPKIVVVWVG 103
Cdd:cd01835     4 LIVVGDSLVygwgdpegggwvgRLRAR---WMNLGDDPVLYNLGVRGDGSEDVAARWRAewsrrGELNV--PNRLVLSVG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111405 104 TNNhshTAE--------QVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLRekNRQVNELVRA 162
Cdd:cd01835    79 LND---TARggrkrpqlSARAFLFGLNQLLEEAKRLVPVLVVGPTPVDEAKMPYS--NRRIARLETA 140
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 70-202 4.42e-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: 37.23  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111405  70 NFGIGGDSTQHVLWRLENGE-LEHI-RPKIVVVWVGTNNHSH---------TAEQVTGGIKA-------IVQLVNKLQPQ 131
Cdd:cd04506    42 NFGVSGDRSDQLLKRLKTKKvQKELkKADVITITIGGNDLMQvleknflslDVEDFKKAEETyqnnlkkIFKEIRKLNPD 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111405 132 ARVVVLGLL-PRGQHPNPLREKNRQV---NELVRAALAGYPRAHFLDADPGFVHSDGT-ISHhdmYDYLHLSRLGY 202
Cdd:cd04506   122 APIFLVGLYnPFYVYFPNITEINDIVndwNEASQKLASQYKNAYFVPIFDLFSDGQNKyLLT---SDHFHPNDKGY 194
 
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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