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Conserved domains on  [gi|515974959|ref|WP_017405542|]
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MULTISPECIES: alpha/beta hydrolase [Delftia]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

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
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 103-307 1.32e-82

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: 249.05  E-value: 1.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  103 LLYLHGGGFTVGSVATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDAWDALQWLASQGALLGADPARLAVGGDSA 182
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  183 GGTLAAACAIHARDAGL-KLALQLLIYPGTTAHQDTDSH--RRFAHGLVIDEPAITWFFAQYLnSPADREDWRFAPLLAP 259
Cdd:pfam07859  81 GGNLAAAVALRARDEGLpKPAGQVLIYPGTDLRTESPSYlaREFADGPLLTRAAMDWFWRLYL-PGADRDDPLASPLFAS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 515974959  260 DVDGVAPAWIGLAECDPLVDEGVEYADKLRMSGVPVDLEIYRGVTHEF 307
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 103-307 1.32e-82

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: 249.05  E-value: 1.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  103 LLYLHGGGFTVGSVATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDAWDALQWLASQGALLGADPARLAVGGDSA 182
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  183 GGTLAAACAIHARDAGL-KLALQLLIYPGTTAHQDTDSH--RRFAHGLVIDEPAITWFFAQYLnSPADREDWRFAPLLAP 259
Cdd:pfam07859  81 GGNLAAAVALRARDEGLpKPAGQVLIYPGTDLRTESPSYlaREFADGPLLTRAAMDWFWRLYL-PGADRDDPLASPLFAS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 515974959  260 DVDGVAPAWIGLAECDPLVDEGVEYADKLRMSGVPVDLEIYRGVTHEF 307
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
85-324 9.80e-61

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 193.17  E-value: 9.80e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  85 RLYAPEeraqAPASGLPVLLYLHGGGFTVGSVATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDAWDALQWLASQ 164
Cdd:COG0657    2 DVYRPA----GAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRAN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 165 GALLGADPARLAVGGDSAGGTLAAACAIHARDAGL-KLALQLLIYPGTtahqdtdshrrfahglvidepaitwffaqyln 243
Cdd:COG0657   78 AAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGpRPAAQVLIYPVL-------------------------------- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 244 spadreDWRFAPLLApDVDGVAPAWIGLAECDPLVDEGVEYADKLRMSGVPVDLEIYRGVTHEFVkMGRAIAEARRAHAD 323
Cdd:COG0657  126 ------DLTASPLRA-DLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFG-LLAGLPEARAALAE 197


                 .
gi 515974959 324 M 324
Cdd:COG0657  198 I 198
PRK10162 PRK10162
acetyl esterase;
16-320 1.14e-45

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 157.96  E-value: 1.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  16 PLPASLTHQMRDVL-RRMERAARTPMHQlGAEGARAAYEAGAGVLEIPKPVLPRvEDLQIPARDGALlPARLYAPEERAQ 94
Cdd:PRK10162   5 PVLDLISAEMKAVVnTQQPDLPDWPATG-DIAEQRQYYTLERRFWNAGAPEMAT-RAYMVPTPYGQV-ETRLYYPQPDSQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  95 ApasglpVLLYLHGGGFTVGSVATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDAWDALQWLASQGALLGADPAR 174
Cdd:PRK10162  82 A------TLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 175 LAVGGDSAGGTLAAACAIHARDAGL---KLALQLLIYpGTTAHQDTDSHRRFahGLVID---EPAITWFFAQYLNSPADR 248
Cdd:PRK10162 156 IGFAGDSAGAMLALASALWLRDKQIdcgKVAGVLLWY-GLYGLRDSVSRRLL--GGVWDgltQQDLQMYEEAYLSNDADR 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515974959 249 EDwRFAPLLAPDVD-GVAPAWIGLAECDPLVDEGVEYADKLRMSGVPVDLEIYRGVTHEFVKMGRAIAEARRA 320
Cdd:PRK10162 233 ES-PYYCLFNNDLTrDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMDTADDA 304
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 96-193 3.67e-06

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: 48.48  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  96 PASGLPVLLYLHGGGFTVGSvATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDA------WD---ALQWLASQGA 166
Cdd:cd00312   91 PGNSLPVMVWIHGGGFMFGS-GSLYPGDGLAREGDNVIVVSINYRLGVLGFLSTGDIELpgnyglKDqrlALKWVQDNIA 169

                         90       100
                 ....*....|....*....|....*..
gi 515974959 167 LLGADPARLAVGGDSAGGTLAAACAIH 193
Cdd:cd00312  170 AFGGDPDSVTIFGESAGGASVSLLLLS 196
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 103-307 1.32e-82

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: 249.05  E-value: 1.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  103 LLYLHGGGFTVGSVATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDAWDALQWLASQGALLGADPARLAVGGDSA 182
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  183 GGTLAAACAIHARDAGL-KLALQLLIYPGTTAHQDTDSH--RRFAHGLVIDEPAITWFFAQYLnSPADREDWRFAPLLAP 259
Cdd:pfam07859  81 GGNLAAAVALRARDEGLpKPAGQVLIYPGTDLRTESPSYlaREFADGPLLTRAAMDWFWRLYL-PGADRDDPLASPLFAS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 515974959  260 DVDGVAPAWIGLAECDPLVDEGVEYADKLRMSGVPVDLEIYRGVTHEF 307
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
85-324 9.80e-61

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 193.17  E-value: 9.80e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  85 RLYAPEeraqAPASGLPVLLYLHGGGFTVGSVATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDAWDALQWLASQ 164
Cdd:COG0657    2 DVYRPA----GAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRAN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 165 GALLGADPARLAVGGDSAGGTLAAACAIHARDAGL-KLALQLLIYPGTtahqdtdshrrfahglvidepaitwffaqyln 243
Cdd:COG0657   78 AAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGpRPAAQVLIYPVL-------------------------------- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 244 spadreDWRFAPLLApDVDGVAPAWIGLAECDPLVDEGVEYADKLRMSGVPVDLEIYRGVTHEFVkMGRAIAEARRAHAD 323
Cdd:COG0657  126 ------DLTASPLRA-DLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFG-LLAGLPEARAALAE 197


                 .
gi 515974959 324 M 324
Cdd:COG0657  198 I 198
PRK10162 PRK10162
acetyl esterase;
16-320 1.14e-45

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 157.96  E-value: 1.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  16 PLPASLTHQMRDVL-RRMERAARTPMHQlGAEGARAAYEAGAGVLEIPKPVLPRvEDLQIPARDGALlPARLYAPEERAQ 94
Cdd:PRK10162   5 PVLDLISAEMKAVVnTQQPDLPDWPATG-DIAEQRQYYTLERRFWNAGAPEMAT-RAYMVPTPYGQV-ETRLYYPQPDSQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  95 ApasglpVLLYLHGGGFTVGSVATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDAWDALQWLASQGALLGADPAR 174
Cdd:PRK10162  82 A------TLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 175 LAVGGDSAGGTLAAACAIHARDAGL---KLALQLLIYpGTTAHQDTDSHRRFahGLVID---EPAITWFFAQYLNSPADR 248
Cdd:PRK10162 156 IGFAGDSAGAMLALASALWLRDKQIdcgKVAGVLLWY-GLYGLRDSVSRRLL--GGVWDgltQQDLQMYEEAYLSNDADR 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515974959 249 EDwRFAPLLAPDVD-GVAPAWIGLAECDPLVDEGVEYADKLRMSGVPVDLEIYRGVTHEFVKMGRAIAEARRA 320
Cdd:PRK10162 233 ES-PYYCLFNNDLTrDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMDTADDA 304
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
73-318 1.45e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 69.28  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  73 QIPARDGALLPARLYAPEEraqapASGLPVLLYLHGGGFTvgSVATHDVLCRQLAHLsGAMVISLEYRRAPEHKFPTAHN 152
Cdd:COG1506    1 TFKSADGTTLPGWLYLPAD-----GKKYPVVVYVHGGPGS--RDDSFLPLAQALASR-GYAVLAPDYRGYGESAGDWGGD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 153 DAWD---ALQWLASQGallGADPARLAVGGDSAGGTLAAACAIHARDAGLKLALQLLIYPGTTAHQDTDSHRRFAHGLVI 229
Cdd:COG1506   73 EVDDvlaAIDYLAARP---YVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPW 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 230 DEPAITWFFaqylnSPADR-EDWRfAPLL--APDVDGVAPawiglaecdplVDEGVEYADKLRMSGVPVDLEIYRGVTHE 306
Cdd:COG1506  150 EDPEAYAAR-----SPLAYaDKLK-TPLLliHGEADDRVP-----------PEQAERLYEALKKAGKPVELLVYPGEGHG 212

                        250
                 ....*....|..
gi 515974959 307 FVKMGRAIAEAR 318
Cdd:COG1506  213 FSGAGAPDYLER 224
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 86-188 1.38e-09

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: 57.19  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959   86 LYAPEErAQAPasgLPVLLYLHGGGFTVGSV-ATHDVLCRQLAHL--SGAMVISLEYRRAPEHKFPTAHNDAWDALQWLA 162
Cdd:pfam20434   3 IYLPKN-AKGP---YPVVIWIHGGGWNSGDKeADMGFMTNTVKALlkAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLR 78

                          90       100
                  ....*....|....*....|....*.
gi 515974959  163 SQGALLGADPARLAVGGDSAGGTLAA 188
Cdd:pfam20434  79 ANAAKYGIDTNKIALMGFSAGGHLAL 104
COesterase pfam00135
Carboxylesterase family;
87-189 4.61e-09

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 57.32  E-value: 4.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959   87 YAPEERAQaPASGLPVLLYLHGGGFTVGSVATHD--VLCRQLahlsGAMVISLEYRRAPEHKFPTAHNDA------WD-- 156
Cdd:pfam00135  91 YTPKELKE-NKNKLPVMVWIHGGGFMFGSGSLYDgsYLAAEG----DVIVVTINYRLGPLGFLSTGDDEApgnyglLDqv 165

                          90       100       110
                  ....*....|....*....|....*....|....
gi 515974959  157 -ALQWLASQGALLGADPARLAVGGDSAGGTLAAA 189
Cdd:pfam00135 166 lALRWVQENIASFGGDPNRVTLFGESAGAASVSL 199
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 62-194 2.26e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 47.99  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  62 PKPVLPRVEDLQIPARDGALLPARLYAPEEraqaPASGLPVLLYLHGGGftvGSVATHDVLCRQLAHLsGAMVISLEYRR 141
Cdd:COG1073    3 PPSDKVNKEDVTFKSRDGIKLAGDLYLPAG----ASKKYPAVVVAHGNG---GVKEQRALYAQRLAEL-GFNVLAFDYRG 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515974959 142 ------APEHKFPTAHNDAWDALQWLasqGALLGADPARLAVGGDSAGGtlaaACAIHA 194
Cdd:COG1073   75 ygesegEPREEGSPERRDARAAVDYL---RTLPGVDPERIGLLGISLGG----GYALNA 126
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 96-193 3.67e-06

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: 48.48  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  96 PASGLPVLLYLHGGGFTVGSvATHDVLCRQLAHLSGAMVISLEYRRAPEHKFPTAHNDA------WD---ALQWLASQGA 166
Cdd:cd00312   91 PGNSLPVMVWIHGGGFMFGS-GSLYPGDGLAREGDNVIVVSINYRLGVLGFLSTGDIELpgnyglKDqrlALKWVQDNIA 169

                         90       100
                 ....*....|....*....|....*..
gi 515974959 167 LLGADPARLAVGGDSAGGTLAAACAIH 193
Cdd:cd00312  170 AFGGDPDSVTIFGESAGGASVSLLLLS 196
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
93-189 3.62e-05

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 45.26  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  93 AQAPASGLPVLLYLHGGGFTVGSVATHDVLCRQLAHlSGAMVISLEYR----------RAPEHKFPTAHN----DAWDAL 158
Cdd:COG2272   98 ALAAGAKLPVMVWIHGGGFVSGSGSEPLYDGAALAR-RGVVVVTINYRlgalgflalpALSGESYGASGNygllDQIAAL 176

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515974959 159 QWLASQGALLGADPARLAVGGDSAGGTLAAA 189
Cdd:COG2272  177 RWVRDNIAAFGGDPDNVTIFGESAGAASVAA 207
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
70-324 2.52e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 41.88  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  70 EDLQIPARDGALLPARLYAPEERAQAPAsglpvLLYLHGGGftvGSVATHDVLCRQLAHLsG--AMVISLEYRRAP---- 143
Cdd:COG0412    4 ETVTIPTPDGVTLPGYLARPAGGGPRPG-----VVVLHEIF---GLNPHIRDVARRLAAA-GyvVLAPDLYGRGGPgddp 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 144 --------EHKFPTAHNDAWDALQWLASQGallGADPARLAVGGDSAGGTLAAACAihARDAGLKLALqlLIYPGTTAHQ 215
Cdd:COG0412   75 dearalmgALDPELLAADLRAALDWLKAQP---EVDAGRVGVVGFCFGGGLALLAA--ARGPDLAAAV--SFYGGLPADD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 216 DTDSHRRFAhglvidepaitwffaqylnspadredwrfAPLLapdvdgvapawIGLAECDPLV--DEGVEYADKLRMSGV 293
Cdd:COG0412  148 LLDLAARIK-----------------------------APVL-----------LLYGEKDPLVppEQVAALEAALAAAGV 187

                        250       260       270
                 ....*....|....*....|....*....|....
gi 515974959 294 PVDLEIYRGVTHEFVKMGRAI---AEARRAHADM 324
Cdd:COG0412  188 DVELHVYPGAGHGFTNPGRPRydpAAAEDAWQRT 221
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
40-189 8.47e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 40.48  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  40 MHQLGAEGARAAYEAGAGvleiPKPVLPRVEDLQIPARDGALlPARLYAPEE-RAQAPASG-LPVLLYLHGGGftvGSVA 117
Cdd:COG4188    5 LALLLAAAAAASPLRQPG----PFAVGVQTLTLRDPSRDRPL-PVDVWYPATaPADAPAGGpFPLVVLSHGLG---GSRE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959 118 THDVLCRQLA-HlsGAMVISLEY--------RRAPEHKFPTAHNDAW-----------DALQWLASQGALLGA--DPARL 175
Cdd:COG4188   77 GYAYLAEHLAsH--GYVVAAPDHpgsnaadlSAALDGLADALDPEELwerpldlsfvlDQLLALNKSDPPLAGrlDLDRI 154

                        170
                 ....*....|....*.
gi 515974959 176 AVGGDSAGG--TLAAA 189
Cdd:COG4188  155 GVIGHSLGGytALALA 170
COG4099 COG4099
Predicted peptidase [General function prediction only];
76-191 1.27e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.57  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515974959  76 ARDGALLPARLYAPEEraQAPASGLPVLLYLHGGGftvgsvATHDVLCRQLAHlSGAMVISLEYRRapehKFP------- 148
Cdd:COG4099   27 PSDGDTLPYRLYLPKG--YDPGKKYPLVLFLHGAG------ERGTDNEKQLTH-GAPKFINPENQA----KFPaivlapq 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515974959 149 TAHNDAW-------DALQWLASQGALLGADPARLAVGGDSAGG--TLAAACA 191
Cdd:COG4099   94 CPEDDYWsdtkaldAVLALLDDLIAEYRIDPDRIYLTGLSMGGygTWDLAAR 145
 
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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