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Conserved domains on  [gi|488309613|ref|WP_002378998|]
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MULTISPECIES: alpha/beta hydrolase [Enterococcus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

alpha/beta 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
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
79-336 6.13e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 129.22  E-value: 6.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  79 DLYYPQTSKQAVPVVLWVHGGGYVGGDKSGMKEFATRLVADSSVAFISMNYELAPDAPYPSQLQQVDELVQFLLEKKQAY 158
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 159 PmLDLSKLFIGGDSAGAQIALQYATvqtnanYAKELGmtaalpASHLKGTLSYCGPVDLKqmanqqsdnrfmkffvktva 238
Cdd:COG0657   82 G-IDPDRIAVAGDSAGGHLAAALAL------RARDRG------GPRPAAQVLIYPVLDLT-------------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 239 wsllgtkdwqTSAELQEVSlvdkvtkEFPPTYLTDGNSFSFQEQGLALVQRLKTLNVPVSALFFKDKkatiTHEYQFDYQ 318
Cdd:COG0657  129 ----------ASPLRADLA-------GLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGG----GHGFGLLAG 187

                        250
                 ....*....|....*...
gi 488309613 319 TKEAKQCYQETVQFVNTY 336
Cdd:COG0657  188 LPEARAALAEIAAFLRRA 205
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
79-336 6.13e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 129.22  E-value: 6.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  79 DLYYPQTSKQAVPVVLWVHGGGYVGGDKSGMKEFATRLVADSSVAFISMNYELAPDAPYPSQLQQVDELVQFLLEKKQAY 158
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 159 PmLDLSKLFIGGDSAGAQIALQYATvqtnanYAKELGmtaalpASHLKGTLSYCGPVDLKqmanqqsdnrfmkffvktva 238
Cdd:COG0657   82 G-IDPDRIAVAGDSAGGHLAAALAL------RARDRG------GPRPAAQVLIYPVLDLT-------------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 239 wsllgtkdwqTSAELQEVSlvdkvtkEFPPTYLTDGNSFSFQEQGLALVQRLKTLNVPVSALFFKDKkatiTHEYQFDYQ 318
Cdd:COG0657  129 ----------ASPLRADLA-------GLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGG----GHGFGLLAG 187

                        250
                 ....*....|....*...
gi 488309613 319 TKEAKQCYQETVQFVNTY 336
Cdd:COG0657  188 LPEARAALAEIAAFLRRA 205
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 79-275 2.10e-25

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 101.49  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613   79 DLYYPQTSKQAVPVVLWVHGGGYVGGDKSGMKEFATRLVA---DSSVAFISMNYELAPDAPYPSQLQQVDELVQFLLEKK 155
Cdd:pfam20434   2 DIYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKallKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  156 QAYPmLDLSKLFIGGDSAGAQIALQYATVQTNANYAKELG---MTAALPASHLKGTLSYCGPVDLKQMANQQSDNrfmkf 232
Cdd:pfam20434  82 AKYG-IDTNKIALMGFSAGGHLALLAGLSNNNKEFEGNVGdytPESSKESFKVNAVVDFYGPTDLLDMDSCGTHN----- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488309613  233 FVKTVAWSLLGtKDWQTSAEL-QEVSLVDKVTKEFPPTYLTDGN 275
Cdd:pfam20434 156 DAKSPETLLLG-APPLENPDLaKSASPITYVDKNDPPFLIIHGD 198
PRK10162 PRK10162
acetyl esterase;
80-179 3.14e-12

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 66.28  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  80 LYYPQTSKQAVpvVLWVHGGGYVGGDKSGMKEFAtRLVADSS-VAFISMNYELAPDAPYPSQLQQVDELVQFLLEKKQAY 158
Cdd:PRK10162  73 LYYPQPDSQAT--LFYLHGGGFILGNLDTHDRIM-RLLASYSgCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDY 149

                         90       100
                 ....*....|....*....|.
gi 488309613 159 PmLDLSKLFIGGDSAGAQIAL 179
Cdd:PRK10162 150 G-INMSRIGFAGDSAGAMLAL 169
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 47-133 2.01e-05

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 46.17  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  47 EIKDSASYdkalPNVQLQENQTYPSSRKKN--------TFDLYYPQTSK--QAVPVVLWVHGGGYVGGDKS--GMKEFAT 114
Cdd:cd00312   46 DVLDATSY----PPSCMQWDQLGGGLWNAKlpgsedclYLNVYTPKNTKpgNSLPVMVWIHGGGFMFGSGSlyPGDGLAR 121

                         90
                 ....*....|....*....
gi 488309613 115 RlvaDSSVAFISMNYELAP 133
Cdd:cd00312  122 E---GDNVIVVSINYRLGV 137
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
79-336 6.13e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 129.22  E-value: 6.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  79 DLYYPQTSKQAVPVVLWVHGGGYVGGDKSGMKEFATRLVADSSVAFISMNYELAPDAPYPSQLQQVDELVQFLLEKKQAY 158
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 159 PmLDLSKLFIGGDSAGAQIALQYATvqtnanYAKELGmtaalpASHLKGTLSYCGPVDLKqmanqqsdnrfmkffvktva 238
Cdd:COG0657   82 G-IDPDRIAVAGDSAGGHLAAALAL------RARDRG------GPRPAAQVLIYPVLDLT-------------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 239 wsllgtkdwqTSAELQEVSlvdkvtkEFPPTYLTDGNSFSFQEQGLALVQRLKTLNVPVSALFFKDKkatiTHEYQFDYQ 318
Cdd:COG0657  129 ----------ASPLRADLA-------GLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGG----GHGFGLLAG 187

                        250
                 ....*....|....*...
gi 488309613 319 TKEAKQCYQETVQFVNTY 336
Cdd:COG0657  188 LPEARAALAEIAAFLRRA 205
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 79-275 2.10e-25

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 101.49  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613   79 DLYYPQTSKQAVPVVLWVHGGGYVGGDKSGMKEFATRLVA---DSSVAFISMNYELAPDAPYPSQLQQVDELVQFLLEKK 155
Cdd:pfam20434   2 DIYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKallKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  156 QAYPmLDLSKLFIGGDSAGAQIALQYATVQTNANYAKELG---MTAALPASHLKGTLSYCGPVDLKQMANQQSDNrfmkf 232
Cdd:pfam20434  82 AKYG-IDTNKIALMGFSAGGHLALLAGLSNNNKEFEGNVGdytPESSKESFKVNAVVDFYGPTDLLDMDSCGTHN----- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488309613  233 FVKTVAWSLLGtKDWQTSAEL-QEVSLVDKVTKEFPPTYLTDGN 275
Cdd:pfam20434 156 DAKSPETLLLG-APPLENPDLaKSASPITYVDKNDPPFLIIHGD 198
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 93-304 6.85e-21

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


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 89.19  E-value: 6.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613   93 VLWVHGGGYVGGDKSGMKEFATRLVADSSVAFISMNYELAPDAPYPSQLQQVDELVQFLLEKKQAYPmLDLSKLFIGGDS 172
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELG-ADPSRIAVAGDS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  173 AGAQIALqyATvqtnANYAKELGMTAalpashLKGTLSYCGPVDLKQMANQQSDNRFMKFFVKTVAWSLLGTKDWQTSAE 252
Cdd:pfam07859  80 AGGNLAA--AV----ALRARDEGLPK------PAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGAD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488309613  253 LQE--VS-LVDKVTKEFPPTYLTDGNSFSFQEQGLALVQRLKTLNVPVSALFFKD 304
Cdd:pfam07859 148 RDDplASpLFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPG 202
PRK10162 PRK10162
acetyl esterase;
80-179 3.14e-12

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 66.28  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  80 LYYPQTSKQAVpvVLWVHGGGYVGGDKSGMKEFAtRLVADSS-VAFISMNYELAPDAPYPSQLQQVDELVQFLLEKKQAY 158
Cdd:PRK10162  73 LYYPQPDSQAT--LFYLHGGGFILGNLDTHDRIM-RLLASYSgCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDY 149

                         90       100
                 ....*....|....*....|.
gi 488309613 159 PmLDLSKLFIGGDSAGAQIAL 179
Cdd:PRK10162 150 G-INMSRIGFAGDSAGAMLAL 169
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
80-336 8.25e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 52.33  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  80 LYYPQTSKQAvPVVLWVHGGGyvGGDKSGMKEFATRLVAD--SSVAFISMNYELAPDAPYPSQLQQVDELVQFLLEKkqa 157
Cdd:COG1506   14 LYLPADGKKY-PVVVYVHGGP--GSRDDSFLPLAQALASRgyAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAAR--- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 158 yPMLDLSKLFIGGDSAGAQIALQYATVQTNAnyakelgmtaalpashLKGTLSYCGPVDLKQMANQQSDNRFMKFFVKtv 237
Cdd:COG1506   88 -PYVDPDRIGIYGHSYGGYMALLAAARHPDR----------------FKAAVALAGVSDLRSYYGTTREYTERLMGGP-- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 238 awsllgtkdWQTSAELQEVSL---VDKVTKefpPTYLT----DGNsFSFqEQGLALVQRLKTLNVPVSALFFKDKkatiT 310
Cdd:COG1506  149 ---------WEDPEAYAARSPlayADKLKT---PLLLIhgeaDDR-VPP-EQAERLYEALKKAGKPVELLVYPGE----G 210

                        250       260
                 ....*....|....*....|....*.
gi 488309613 311 HEYQFdyqtKEAKQCYQETVQFVNTY 336
Cdd:COG1506  211 HGFSG----AGAPDYLERILDFLDRH 232
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
79-279 1.17e-06

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 49.34  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  79 DLYYPQT------SKQAVPVVLWVHGGGyvgGDKSGMKEFATRLVA-----------DSSVAFISMNYELAPDAPYPSQL 141
Cdd:COG4188   45 DVWYPATapadapAGGPFPLVVLSHGLG---GSREGYAYLAEHLAShgyvvaapdhpGSNAADLSAALDGLADALDPEEL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 142 QQ--------VDELVQFLLEKKQAYPMLDLSKLFIGGDSAGAQIALQYAtvqtnanyakelGMT---AALPASHLKGTLS 210
Cdd:COG4188  122 WErpldlsfvLDQLLALNKSDPPLAGRLDLDRIGVIGHSLGGYTALALA------------GARldfAALRQYCGKNPDL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 211 YCGPVDLKQMANQQSDNRF----------MKFFVK------TVAWSLL-GTKDWQTSAELQEVSLVDKVTKefPPTYL-- 271
Cdd:COG4188  190 QCRALDLPRLAYDLRDPRIkavvalapggSGLFGEeglaaiTIPVLLVaGSADDVTPAPDEQIRPFDLLPG--ADKYLlt 267


                 ....*....
gi 488309613 272 -TDGNSFSF 279
Cdd:COG4188  268 lEGATHFSF 276
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 47-133 2.01e-05

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 46.17  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  47 EIKDSASYdkalPNVQLQENQTYPSSRKKN--------TFDLYYPQTSK--QAVPVVLWVHGGGYVGGDKS--GMKEFAT 114
Cdd:cd00312   46 DVLDATSY----PPSCMQWDQLGGGLWNAKlpgsedclYLNVYTPKNTKpgNSLPVMVWIHGGGFMFGSGSlyPGDGLAR 121

                         90
                 ....*....|....*....
gi 488309613 115 RlvaDSSVAFISMNYELAP 133
Cdd:cd00312  122 E---GDNVIVVSINYRLGV 137
COG4099 COG4099
Predicted peptidase [General function prediction only];
65-183 5.75e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 43.80  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  65 ENQTYPSSRKKNTFD--LYYPQ--TSKQAVPVVLWVHGGGYVGGD-----KSGMKEFATRLVADSSVAFIsmnyeLAPDA 135
Cdd:COG4099   20 EARTFTDPSDGDTLPyrLYLPKgyDPGKKYPLVLFLHGAGERGTDnekqlTHGAPKFINPENQAKFPAIV-----LAPQC 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488309613 136 P------YPSQLQQVDELVQFLLEKkqaYPMlDLSKLFIGGDSAGAQIALQYAT 183
Cdd:COG4099   95 PeddywsDTKALDAVLALLDDLIAE---YRI-DPDRIYLTGLSMGGYGTWDLAA 144
YpfH COG0400
Predicted esterase [General function prediction only];
86-182 7.77e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 7.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  86 SKQAVPVVLWVHGggyVGGDKSGMKEFATRLvADSSVAFISmnyelaPDAPYPS--------------------QLQQ-V 144
Cdd:COG0400    1 GGPAAPLVVLLHG---YGGDEEDLLPLAPEL-ALPGAAVLA------PRAPVPEgpggrawfdlsflegredeeGLAAaA 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488309613 145 DELVQFLLEKKQAYPmLDLSKLFIGGDSAGAQIALQYA 182
Cdd:COG0400   71 EALAAFIDELEARYG-IDPERIVLAGFSQGAAMALSLA 107
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 79-257 5.72e-04

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 41.05  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  79 DLYYPQTSKQAVPVVLWVHGGgyvGGDKSGMKEFATRLVADSSVAfismnyeLAPDAPY-------PSQL-----QQVDE 146
Cdd:COG1073   26 DLYLPAGASKKYPAVVVAHGN---GGVKEQRALYAQRLAELGFNV-------LAFDYRGygesegePREEgsperRDARA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613 147 LVQFLlekkQAYPMLDLSKLFIGGDSAGAQIALQYATVQTNAnyakelgmtaalpashlKGTLSYCGPVDLKQMANQQSD 226
Cdd:COG1073   96 AVDYL----RTLPGVDPERIGLLGISLGGGYALNAAATDPRV-----------------KAVILDSPFTSLEDLAAQRAK 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488309613 227 NRF-----MKFFVKTVAWSLLGTKDWQTSAELQEVS 257
Cdd:COG1073  155 EARgaylpGVPYLPNVRLASLLNDEFDPLAKIEKIS 190
COesterase pfam00135
Carboxylesterase family;
81-133 2.54e-03

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 39.60  E-value: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488309613   81 YYPQTSKQ---AVPVVLWVHGGGYVGGDKS--GMKEFATRLvadsSVAFISMNYELAP 133
Cdd:pfam00135  91 YTPKELKEnknKLPVMVWIHGGGFMFGSGSlyDGSYLAAEG----DVIVVTINYRLGP 144
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
91-131 5.88e-03

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 38.33  E-value: 5.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488309613  91 PVVLWVHGGGYVGGDkSGMKEF-ATRLVADSSVaFISMNYEL 131
Cdd:COG2272  106 PVMVWIHGGGFVSGS-GSEPLYdGAALARRGVV-VVTINYRL 145
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
77-182 7.91e-03

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 37.50  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488309613  77 TFDLYYP-QTSKQAVPVVLWVHGGgyvGGD------KSGMKEFAtrlvADSSVAFISMNYELAP---DAPYPSQLQQ--- 143
Cdd:COG0627   19 PVSVYLPpGYDGRPLPVLYLLHGL---TGThenwtrKTGAQRLA----AELGVIVVMPDGGQASfyvDWTQGPAGHYrwe 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488309613 144 ---VDELVQFLlekKQAYPMLDL-SKLFIGGDSAGAQIALQYA 182
Cdd:COG0627   92 tylTEELPPLI---EANFPVSADrERRAIAGLSMGGHGALTLA 131
 
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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