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Conserved domains on  [gi|1559988691|sp|A0A1E3P8S6|]
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RecName: Full=Ethanol acetyltransferase 1; AltName: Full=Acetyl-CoA hydrolase; AltName: Full=Acetyl-CoA thioesterase; AltName: Full=Alcohol acetyltransferase; Short=AAT; AltName: Full=Ethyl acetate esterase; Flags: Precursor

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 1001822)

alpha/beta fold hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
Gene Ontology:  GO:0016787
PubMed:  12369917|15381402|1409539
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 super family cl30399
esterase;
41-313 1.37e-23

esterase;


The actual alignment was detected with superfamily member PRK10673:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 98.65  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  41 LNIR--------SHEPIVFVHGIFGSKKNY---RHDCQKianvtHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCED 109
Cdd:PRK10673    3 LNIRaqtaqnphNNSPIVLVHGLFGSLDNLgvlARDLVN-----DHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 110 HGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQP---HIEIFltqfiksmlHVLNstKIRADDKDWKSKAN 186
Cdd:PRK10673   78 LQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHvrrHDEIF---------AAIN--AVSEAGATTRQQAA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 187 QAMRRYIPNGGIRDYLLanlinkvpkgyKSpvinYDDGYIHFQNPV---RHMTEVAVKNVSAWPtehvkglkfeGQVRFL 263
Cdd:PRK10673  147 AIMRQHLNEEGVIQFLL-----------KS----FVDGEWRFNVPVlwdQYPHIVGWEKIPAWP----------HPALFI 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1559988691 264 KGTKSAFIDEKGLEAIKEYFPNYSLSELN-ATHFILNERPQEYVKLICDFI 313
Cdd:PRK10673  202 RGGNSPYVTEAYRDDLLAQFPQARAHVIAgAGHWVHAEKPDAVLRAIRRYL 252
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
41-313 1.37e-23

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 98.65  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  41 LNIR--------SHEPIVFVHGIFGSKKNY---RHDCQKianvtHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCED 109
Cdd:PRK10673    3 LNIRaqtaqnphNNSPIVLVHGLFGSLDNLgvlARDLVN-----DHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 110 HGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQP---HIEIFltqfiksmlHVLNstKIRADDKDWKSKAN 186
Cdd:PRK10673   78 LQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHvrrHDEIF---------AAIN--AVSEAGATTRQQAA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 187 QAMRRYIPNGGIRDYLLanlinkvpkgyKSpvinYDDGYIHFQNPV---RHMTEVAVKNVSAWPtehvkglkfeGQVRFL 263
Cdd:PRK10673  147 AIMRQHLNEEGVIQFLL-----------KS----FVDGEWRFNVPVlwdQYPHIVGWEKIPAWP----------HPALFI 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1559988691 264 KGTKSAFIDEKGLEAIKEYFPNYSLSELN-ATHFILNERPQEYVKLICDFI 313
Cdd:PRK10673  202 RGGNSPYVTEAYRDDLLAQFPQARAHVIAgAGHWVHAEKPDAVLRAIRRYL 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 47-314 1.58e-21

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 91.99  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  47 EPIVFVHGIFGSKKNYRHDCQKIANvtHTPVYTIDLRNHGQSMH-ALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAK 125
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 126 ICMLTMLQNPDLVRSGVIIDnspieqphieifltqfiksmlhvlnstkiraddkdwksKANQAMRRYIPNGGIRDYLLAN 205
Cdd:COG0596   102 VALELAARHPERVAGLVLVD--------------------------------------EVLAALAEPLRRPGLAPEALAA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 206 LINKVPKGykspvinyddgyihfqNPVRHMTEVAVknvsawPTehvkglkfegqvRFLKGTKSAFIDEKGLEAIKEYFPN 285
Cdd:COG0596   144 LLRALART----------------DLRERLARITV------PT------------LVIWGEKDPIVPPALARRLAELLPN 189

                         250       260       270
                  ....*....|....*....|....*....|
gi 1559988691 286 YSLSEL-NATHFILNERPQEYVKLICDFIK 314
Cdd:COG0596   190 AELVVLpGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 48-302 5.34e-21

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 91.03  E-value: 5.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  48 PIVFVHGIFGSKKNYRHDCQKIANVTHTpVYTIDLRNHGQSMHAL-PFDYET--LAQDVTDFCEDHGLKKVNLIGYSLGA 124
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFR-VIALDLRGFGKSSRPKaQDDYRTddLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 125 KICMLTMLQNPDLVRSGVIIDNSPIEQPHIEIFLTQFiKSMLHVLNstKIRADDKdwksKANQAMRRYIPNGGIRDYLla 204
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFIL-ALFPGFFD--GFVADFA----PNPLGRLVAKLLALLLLRL-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 205 NLINKVPKGYKSPvinYDDGYIHFQNPVRhmteVAVKNVSAWPTEHV--KGLKFEGQVRFLKGTKSAFIDEKGLEAIKEY 282
Cdd:pfam00561 152 RLLKALPLLNKRF---PSGDYALAKSLVT----GALLFIETWSTELRakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQL 224

                         250       260
                  ....*....|....*....|.
gi 1559988691 283 FPN-YSLSELNATHFILNERP 302
Cdd:pfam00561 225 FPNaRLVVIPDAGHFAFLEGP 245
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
41-313 1.37e-23

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 98.65  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  41 LNIR--------SHEPIVFVHGIFGSKKNY---RHDCQKianvtHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCED 109
Cdd:PRK10673    3 LNIRaqtaqnphNNSPIVLVHGLFGSLDNLgvlARDLVN-----DHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 110 HGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQP---HIEIFltqfiksmlHVLNstKIRADDKDWKSKAN 186
Cdd:PRK10673   78 LQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHvrrHDEIF---------AAIN--AVSEAGATTRQQAA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 187 QAMRRYIPNGGIRDYLLanlinkvpkgyKSpvinYDDGYIHFQNPV---RHMTEVAVKNVSAWPtehvkglkfeGQVRFL 263
Cdd:PRK10673  147 AIMRQHLNEEGVIQFLL-----------KS----FVDGEWRFNVPVlwdQYPHIVGWEKIPAWP----------HPALFI 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1559988691 264 KGTKSAFIDEKGLEAIKEYFPNYSLSELN-ATHFILNERPQEYVKLICDFI 313
Cdd:PRK10673  202 RGGNSPYVTEAYRDDLLAQFPQARAHVIAgAGHWVHAEKPDAVLRAIRRYL 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 47-314 1.58e-21

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 91.99  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  47 EPIVFVHGIFGSKKNYRHDCQKIANvtHTPVYTIDLRNHGQSMH-ALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAK 125
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 126 ICMLTMLQNPDLVRSGVIIDnspieqphieifltqfiksmlhvlnstkiraddkdwksKANQAMRRYIPNGGIRDYLLAN 205
Cdd:COG0596   102 VALELAARHPERVAGLVLVD--------------------------------------EVLAALAEPLRRPGLAPEALAA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 206 LINKVPKGykspvinyddgyihfqNPVRHMTEVAVknvsawPTehvkglkfegqvRFLKGTKSAFIDEKGLEAIKEYFPN 285
Cdd:COG0596   144 LLRALART----------------DLRERLARITV------PT------------LVIWGEKDPIVPPALARRLAELLPN 189

                         250       260       270
                  ....*....|....*....|....*....|
gi 1559988691 286 YSLSEL-NATHFILNERPQEYVKLICDFIK 314
Cdd:COG0596   190 AELVVLpGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 48-302 5.34e-21

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 91.03  E-value: 5.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  48 PIVFVHGIFGSKKNYRHDCQKIANVTHTpVYTIDLRNHGQSMHAL-PFDYET--LAQDVTDFCEDHGLKKVNLIGYSLGA 124
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFR-VIALDLRGFGKSSRPKaQDDYRTddLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 125 KICMLTMLQNPDLVRSGVIIDNSPIEQPHIEIFLTQFiKSMLHVLNstKIRADDKdwksKANQAMRRYIPNGGIRDYLla 204
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFIL-ALFPGFFD--GFVADFA----PNPLGRLVAKLLALLLLRL-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 205 NLINKVPKGYKSPvinYDDGYIHFQNPVRhmteVAVKNVSAWPTEHV--KGLKFEGQVRFLKGTKSAFIDEKGLEAIKEY 282
Cdd:pfam00561 152 RLLKALPLLNKRF---PSGDYALAKSLVT----GALLFIETWSTELRakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQL 224

                         250       260
                  ....*....|....*....|.
gi 1559988691 283 FPN-YSLSELNATHFILNERP 302
Cdd:pfam00561 225 FPNaRLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 47-140 6.67e-11

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 63.04  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  47 EPIVFVHGIFGSKKNYRHDCQKIAnvTHTPVYTIDLRNHGQSMHAL-PFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAK 125
Cdd:PRK14875  132 TPVVLIHGFGGDLNNWLFNHAALA--AGRPVIALDLPGHGASSKAVgAGSLDELAAAVLAFLDALGIERAHLVGHSMGGA 209

                          90
                  ....*....|....*
gi 1559988691 126 ICMLTMLQNPDLVRS 140
Cdd:PRK14875  210 VALRLAARAPQRVAS 224
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 49-144 5.03e-10

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 59.47  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  49 IVFVHGIFGSKknyrHDCQKIA-NVTHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAKIC 127
Cdd:PRK11126    5 LVFLHGLLGSG----QDWQPVGeALPDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIA 80

                          90
                  ....*....|....*....
gi 1559988691 128 MLTMLQ--NPDLVrsGVII 144
Cdd:PRK11126   81 MYYACQglAGGLC--GLIV 97
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 46-140 1.57e-09

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 54.84  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  46 HEPIVFVHGIFGSKKNYRHDCQKIANvTHTPVYTIDLRNHGQSMHALpfdYETLAQDVTDFCEDHGLKKVNLIGYSLGAK 125
Cdd:COG1075     5 RYPVVLVHGLGGSAASWAPLAPRLRA-AGYPVYALNYPSTNGSIEDS---AEQLAAFVDAVLAATGAEKVDLVGHSMGGL 80

                          90
                  ....*....|....*..
gi 1559988691 126 IC--MLTMLQNPDLVRS 140
Cdd:COG1075    81 VAryYLKRLGGAAKVAR 97
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
48-156 9.54e-09

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 55.39  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  48 PIVFVHGIFGSKKNYRH---DCQK--IAnvthtpVYTIDLRNHGQS--MHALPFDYETLAQDVT---DFCEDHGLKKVNL 117
Cdd:COG2267    30 TVVLVHGLGEHSGRYAElaeALAAagYA------VLAFDLRGHGRSdgPRGHVDSFDDYVDDLRaalDALRARPGLPVVL 103

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1559988691 118 IGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQPHIEI 156
Cdd:COG2267   104 LGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGP 142
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 49-145 1.60e-08

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 54.40  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  49 IVFVHGIFGSKKNYRHdcqkiANVTHTPVYTIDLRNHGQSmHALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAkicM 128
Cdd:pfam12697   1 VVLVHGAGLSAAPLAA-----LLAAGVAVLAPDLPGHGSS-SPPPLDLADLADLAALLDELGAARPVVLVGHSLGG---A 71

                          90
                  ....*....|....*..
gi 1559988691 129 LTMLQNPDLVRSGVIID 145
Cdd:pfam12697  72 VALAAAAAALVVGVLVA 88
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
49-144 2.59e-06

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 48.09  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  49 IVFVHGIFGSK-KNYRHDCQKIAN---VthtpVYTIDLRNHGQSMHALPFDYETLAQDVTDFCEDHGL---KKVNLIGYS 121
Cdd:COG1506    26 VVYVHGGPGSRdDSFLPLAQALASrgyA----VLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYvdpDRIGIYGHS 101

                          90       100
                  ....*....|....*....|...
gi 1559988691 122 LGAKICMLTMLQNPDLVRSGVII 144
Cdd:COG1506   102 YGGYMALLAAARHPDRFKAAVAL 124
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 49-143 8.46e-06

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 46.44  E-value: 8.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  49 IVFVHGiFGSkknyrHdCQKIANVTHT------PVYTIDLRNHGQS----MHALPFDyeTLAQDVTDF----CEDHGLKK 114
Cdd:pfam12146   7 VVLVHG-LGE-----H-SGRYAHLADAlaaqgfAVYAYDHRGHGRSdgkrGHVPSFD--DYVDDLDTFvdkiREEHPGLP 77

                          90       100
                  ....*....|....*....|....*....
gi 1559988691 115 VNLIGYSLGAKICMLTMLQNPDLVRsGVI 143
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVD-GLI 105
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 47-203 1.02e-05

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 46.20  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  47 EPIVFVHGIFGSKKNYRhdcqKIANVTHTPVYTI--DLRNHGQSM---HALPFDYETLAQDV------TDFCED------ 109
Cdd:pfam07819   5 IPVLFIPGNAGSYKQVR----SIASVAANLYQVLrkLLQNDNGFHldfFSVDFNEELSAFHGrtlldqAEYLNDairyil 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 110 -------HGLKKVNLIGYSLGAKICMLTM-LQN--PDLVRSGVIIDnSPIEQPHI--EIFLTQFIKSMlhvlnstkirad 177
Cdd:pfam07819  81 slyasgrPGPTSVILIGHSMGGIVARAALtLPNyiPQSVNTIITLS-SPHAKPPLtfDGDILKFYERL------------ 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1559988691 178 DKDWKSKANQAMRRYIPN-------GGIRDYLL 203
Cdd:pfam07819 148 NAFWRKLYNDGDSNNLSNvllvsitGGIRDYMV 180
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 48-145 1.40e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 46.76  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  48 PIVFVHGIFGSKKNYRHDCQKIANvTHTpVYTIDLRNHGQSMHALPFDY--ETLAQDVTDFCEDHGLKKVNLIGYSLGAK 125
Cdd:PLN02679   90 PVLLVHGFGASIPHWRRNIGVLAK-NYT-VYAIDLLGFGASDKPPGFSYtmETWAELILDFLEEVVQKPTVLIGNSVGSL 167

                          90       100
                  ....*....|....*....|.
gi 1559988691 126 ICMLTMLQ-NPDLVRSGVIID 145
Cdd:PLN02679  168 ACVIAASEsTRDLVRGLVLLN 188
PLN02578 PLN02578
hydrolase
 48-147 3.14e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.60  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  48 PIVFVHGIFGSKKNYRHDCQKIANvTHTpVYTIDLRNHGQSMHAL-PFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAKI 126
Cdd:PLN02578   88 PIVLIHGFGASAFHWRYNIPELAK-KYK-VYALDLLGFGWSDKALiEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFT 165

                          90       100
                  ....*....|....*....|.
gi 1559988691 127 CMLTMLQNPDLVRsGVIIDNS 147
Cdd:PLN02578  166 ALSTAVGYPELVA-GVALLNS 185
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 42-174 2.96e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 42.42  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  42 NIR------SHEPIVFVHGIFGSKKNYRHDCQKIAnVTHTpVYTIDLRNHGQSMHALP--------FDYETLAQDVTDFC 107
Cdd:PLN02824   19 NIRyqragtSGPALVLVHGFGGNADHWRKNTPVLA-KSHR-VYAIDLLGYGYSDKPNPrsappnsfYTFETWGEQLNDFC 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691 108 EDHGLKKVNLIGYSLGAKICMLTMLQNPDLVRsGVIIDNSPIEQPHIE---IFLTQFIKSMLHVLNSTKI 174
Cdd:PLN02824   97 SDVVGDPAFVICNSVGGVVGLQAAVDAPELVR-GVMLINISLRGLHIKkqpWLGRPFIKAFQNLLRETAV 165
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
49-137 1.74e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.56  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  49 IVFVHGIFGSKKNYRHDCQKIAN---VTHTP-VYT--IDLRNHGQSM-HALPFDYETLAQDVT---DFCEDHGL---KKV 115
Cdd:COG0412    32 VVVLHEIFGLNPHIRDVARRLAAagyVVLAPdLYGrgGPGDDPDEARaLMGALDPELLAADLRaalDWLKAQPEvdaGRV 111

                          90       100
                  ....*....|....*....|..
gi 1559988691 116 NLIGYSLGAKICMLTMLQNPDL 137
Cdd:COG0412   112 GVVGFCFGGGLALLAAARGPDL 133
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 49-148 2.20e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 40.23  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691   49 IVFVHGIFGSKKNYRHDCQKIANVTHtpVYTIDLRNHGQSM---HA------LPFDYETLAQDVTDFCEDHGLKKVNLIG 119
Cdd:PLN02980  1374 VLFLHGFLGTGEDWIPIMKAISGSAR--CISIDLPGHGGSKiqnHAketqtePTLSVELVADLLYKLIEHITPGKVTLVG 1451

                           90       100
                   ....*....|....*....|....*....
gi 1559988691  120 YSLGAKICMLTMLQNPDLVRSGVIIDNSP 148
Cdd:PLN02980  1452 YSMGARIALYMALRFSDKIEGAVIISGSP 1480
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
48-127 2.45e-03

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 39.14  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559988691  48 PIVFVHGIFGSKKNY--RHDCQKIANV-THTPVYTIDLRNHGQSMHALPFdYETLAQDVTDFCEDHGLKK----VNLIGY 120
Cdd:pfam02089   1 PVVIWHGLGDSCASPgmQSLAELIKEAhPGTYVHSIDIGDGPSEDRKASF-FGNMNEQVEAVCEQLKPELpangFNAIGF 79


                  ....*..
gi 1559988691 121 SLGAKIC 127
Cdd:pfam02089  80 SQGGLFL 86
 
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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