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Conserved domains on  [gi|1002293623|ref|XP_015651151|]
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2-hydroxyisoflavanone dehydratase [Oryza sativa Japonica Group]

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.
 151-364 1.50e-54

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: 178.94  E-value: 1.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 151 VVFFHGGAFFIESAgsETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSWAALQWAASAQDGWiaeHGDTARLFV 230
Cdd:pfam07859   1 LVYFHGGGFVLGSA--DTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAEL---GADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 231 AGDSAGANIAHEMLVRAAASGGrPRMEGAILLHPW----FGGSKEIEGEPEGGAAITAAM----WNYACPGaaAGADDPR 302
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDEGL-PKPAGQVLIYPGtdlrTESPSYLAREFADGPLLTRAAmdwfWRLYLPG--ADRDDPL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002293623 303 LNPLAAggpvlEELA-CERMLVCAGGKDVLAARNRAYYDAVAasAWRGSAAWLESEGEGHVFF 364
Cdd:pfam07859 153 ASPLFA-----SDLSgLPPALVVVAEFDPLRDEGEAYAERLR--AAGVPVELIEYPGMPHGFH 208
 
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.
 151-364 1.50e-54

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: 178.94  E-value: 1.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 151 VVFFHGGAFFIESAgsETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSWAALQWAASAQDGWiaeHGDTARLFV 230
Cdd:pfam07859   1 LVYFHGGGFVLGSA--DTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAEL---GADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 231 AGDSAGANIAHEMLVRAAASGGrPRMEGAILLHPW----FGGSKEIEGEPEGGAAITAAM----WNYACPGaaAGADDPR 302
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDEGL-PKPAGQVLIYPGtdlrTESPSYLAREFADGPLLTRAAmdwfWRLYLPG--ADRDDPL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002293623 303 LNPLAAggpvlEELA-CERMLVCAGGKDVLAARNRAYYDAVAasAWRGSAAWLESEGEGHVFF 364
Cdd:pfam07859 153 ASPLFA-----SDLSgLPPALVVVAEFDPLRDEGEAYAERLR--AAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
135-385 1.03e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 135.00  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 135 RLFLPKlqEPSKKLPVVVFFHGGAFFIESAgsETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSWAALQWAASA 214
Cdd:COG0657     2 DVYRPA--GAKGPLPVVVYFHGGGWVSGSK--DTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 215 QDGWiaeHGDTARLFVAGDSAGANIAHeMLVRAAASGGRPRMEGAILLHPWFggskeiegepeggaaitaamwnyacpga 294
Cdd:COG0657    78 AAEL---GIDPDRIAVAGDSAGGHLAA-ALALRARDRGGPRPAAQVLIYPVL---------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 295 aagadDPRLNPLAAggpVLEELAceRMLVCAGGKDVLAARNRAYYDAVAASawRGSAAWLESEGEGHVFFLGNSECEnAK 374
Cdd:COG0657   126 -----DLTASPLRA---DLAGLP--PTLIVTGEADPLVDESEALAAALRAA--GVPVELHVYPGGGHGFGLLAGLPE-AR 192

                         250
                  ....*....|.
gi 1002293623 375 QLMDRIVAFIA 385
Cdd:COG0657   193 AALAEIAAFLR 203
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 136-237 5.42e-11

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: 63.89  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 136 LFLPKLQEPSKKLPVVVFFHGGAFFIESAGSETYHNYVnslAAAAGVLVVSVDYRLAP-------EHPLP--AGYDDSWA 206
Cdd:cd00312    83 VYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLA---REGDNVIVVSINYRLGVlgflstgDIELPgnYGLKDQRL 159

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002293623 207 ALQwaasaqdgWIAEH-----GDTARLFVAGDSAGA 237
Cdd:cd00312   160 ALK--------WVQDNiaafgGDPDSVTIFGESAGG 187
PRK10162 PRK10162
acetyl esterase;
132-240 1.26e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 62.04  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 132 VSVRLFLPKLQEPSkklpVVVFFHGGAFFIESAgsETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSWAALQwa 211
Cdd:PRK10162   69 VETRLYYPQPDSQA----TLFYLHGGGFILGNL--DTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCC-- 140

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002293623 212 asaqdgWIAEHGD-----TARLFVAGDSAGANIA 240
Cdd:PRK10162  141 ------YFHQHAEdyginMSRIGFAGDSAGAMLA 168
 
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.
 151-364 1.50e-54

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: 178.94  E-value: 1.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 151 VVFFHGGAFFIESAgsETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSWAALQWAASAQDGWiaeHGDTARLFV 230
Cdd:pfam07859   1 LVYFHGGGFVLGSA--DTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAEL---GADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 231 AGDSAGANIAHEMLVRAAASGGrPRMEGAILLHPW----FGGSKEIEGEPEGGAAITAAM----WNYACPGaaAGADDPR 302
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDEGL-PKPAGQVLIYPGtdlrTESPSYLAREFADGPLLTRAAmdwfWRLYLPG--ADRDDPL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002293623 303 LNPLAAggpvlEELA-CERMLVCAGGKDVLAARNRAYYDAVAasAWRGSAAWLESEGEGHVFF 364
Cdd:pfam07859 153 ASPLFA-----SDLSgLPPALVVVAEFDPLRDEGEAYAERLR--AAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
135-385 1.03e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 135.00  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 135 RLFLPKlqEPSKKLPVVVFFHGGAFFIESAgsETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSWAALQWAASA 214
Cdd:COG0657     2 DVYRPA--GAKGPLPVVVYFHGGGWVSGSK--DTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 215 QDGWiaeHGDTARLFVAGDSAGANIAHeMLVRAAASGGRPRMEGAILLHPWFggskeiegepeggaaitaamwnyacpga 294
Cdd:COG0657    78 AAEL---GIDPDRIAVAGDSAGGHLAA-ALALRARDRGGPRPAAQVLIYPVL---------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 295 aagadDPRLNPLAAggpVLEELAceRMLVCAGGKDVLAARNRAYYDAVAASawRGSAAWLESEGEGHVFFLGNSECEnAK 374
Cdd:COG0657   126 -----DLTASPLRA---DLAGLP--PTLIVTGEADPLVDESEALAAALRAA--GVPVELHVYPGGGHGFGLLAGLPE-AR 192

                         250
                  ....*....|.
gi 1002293623 375 QLMDRIVAFIA 385
Cdd:COG0657   193 AALAEIAAFLR 203
COesterase pfam00135
Carboxylesterase family;
143-241 7.17e-12

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 66.56  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 143 EPSKKLPVVVFFHGGAFFIESAgsETY-HNYvnsLAAAAGVLVVSVDYRLAP--------EHpLP--AGYDDSWAALQwa 211
Cdd:pfam00135  98 ENKNKLPVMVWIHGGGFMFGSG--SLYdGSY---LAAEGDVIVVTINYRLGPlgflstgdDE-APgnYGLLDQVLALR-- 169

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002293623 212 asaqdgWIAEH-----GDTARLFVAGDSAGANIAH 241
Cdd:pfam00135 170 ------WVQENiasfgGDPNRVTLFGESAGAASVS 198
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 136-237 5.42e-11

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: 63.89  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 136 LFLPKLQEPSKKLPVVVFFHGGAFFIESAGSETYHNYVnslAAAAGVLVVSVDYRLAP-------EHPLP--AGYDDSWA 206
Cdd:cd00312    83 VYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLA---REGDNVIVVSINYRLGVlgflstgDIELPgnYGLKDQRL 159

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002293623 207 ALQwaasaqdgWIAEH-----GDTARLFVAGDSAGA 237
Cdd:cd00312   160 ALK--------WVQDNiaafgGDPDSVTIFGESAGG 187
PRK10162 PRK10162
acetyl esterase;
132-240 1.26e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 62.04  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 132 VSVRLFLPKLQEPSkklpVVVFFHGGAFFIESAgsETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSWAALQwa 211
Cdd:PRK10162   69 VETRLYYPQPDSQA----TLFYLHGGGFILGNL--DTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCC-- 140

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002293623 212 asaqdgWIAEHGD-----TARLFVAGDSAGANIA 240
Cdd:PRK10162  141 ------YFHQHAEdyginMSRIGFAGDSAGAMLA 168
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
132-385 7.11e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 58.87  E-value: 7.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 132 VSVRLFLPKlqePSKKLPVVVFFHGGAffiesAGSETYHNYVNSLAAAAGVLVVSVDYRLAPEHPLPAGYDDSW---AAL 208
Cdd:COG1506    10 LPGWLYLPA---DGKKYPVVVYVHGGP-----GSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDdvlAAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 209 QWAasAQDGWIaehgDTARLFVAGDSAGANIA------HEMLVRAAASGGrprmeGAILLHPWFGGSKEIEGEPEGGAAI 282
Cdd:COG1506    82 DYL--AARPYV----DPDRIGIYGHSYGGYMAllaaarHPDRFKAAVALA-----GVSDLRSYYGTTREYTERLMGGPWE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 283 TAAMWNYACPGAAAgaddPRLNplaagGPVleelacermLVCAGGKD--VLAARNRAYYDavAASAWRGSAAWLESEGEG 360
Cdd:COG1506   151 DPEAYAARSPLAYA----DKLK-----TPL---------LLIHGEADdrVPPEQAERLYE--ALKKAGKPVELLVYPGEG 210

                         250       260
                  ....*....|....*....|....*
gi 1002293623 361 HVFFLgnsecENAKQLMDRIVAFIA 385
Cdd:COG1506   211 HGFSG-----AGAPDYLERILDFLD 230
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 136-273 1.88e-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: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 136 LFLPKlqEPSKKLPVVVFFHGGAFFieSAGSETYHNYVNSLAAA---AGVLVVSVDYRLAPEHPLPAGYDDSWAALQWA- 211
Cdd:pfam20434   3 IYLPK--NAKGPYPVVIWIHGGGWN--SGDKEADMGFMTNTVKAllkAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLr 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002293623 212 ASAQdgwiAEHGDTARLFVAGDSAGANIAhEMlvrAAASGGRPRMEGAILLHPWFGGSKEIE 273
Cdd:pfam20434  79 ANAA----KYGIDTNKIALMGFSAGGHLA-LL---AGLSNNNKEFEGNVGDYTPESSKESFK 132
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
144-237 3.91e-09

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 57.98  E-value: 3.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 144 PSKKLPVVVFFHGGAFFIESAGSETYHnyVNSLaAAAGVLVVSVDYRLAPE----HP-LPAGYDDSW---------AALQ 209
Cdd:COG2272   101 AGAKLPVMVWIHGGGFVSGSGSEPLYD--GAAL-ARRGVVVVTINYRLGALgflaLPaLSGESYGASgnyglldqiAALR 177

                          90       100
                  ....*....|....*....|....*....
gi 1002293623 210 WaasAQDGwIAE-HGDTARLFVAGDSAGA 237
Cdd:COG2272   178 W---VRDN-IAAfGGDPDNVTIFGESAGA 202
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
120-385 9.31e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 49.23  E-value: 9.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 120 TSKDVVLDADTGVSVRLFLPKLQEPSKklPVVVFFHGGAffiesAGSETYHNYVNSLAAAaGVLVVSVDYRLAPEHPLPA 199
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRPAGSPR--GTVVLVHGLG-----EHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 200 GYDDSWAALQWAASAQDGWIAEHGDTaRLFVAGDSAGANIAhemlvRAAASGGRPRMEGAILLHPWFggskeiEGEPEGG 279
Cdd:COG2267    74 GHVDSFDDYVDDLRAALDALRARPGL-PVVLLGHSMGGLIA-----LLYAARYPDRVAGLVLLAPAY------RADPLLG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 280 AAiTAAMWNYACPGAAAGADDPrlnplaaggpvleelacerMLVCAGGKDVLAARNRAyydAVAASAWRGSAAWLESEGE 359
Cdd:COG2267   142 PS-ARWLRALRLAEALARIDVP-------------------VLVLHGGADRVVPPEAA---RRLAARLSPDVELVLLPGA 198

                         250       260
                  ....*....|....*....|....*.
gi 1002293623 360 GHVFFLgnseCENAKQLMDRIVAFIA 385
Cdd:COG2267   199 RHELLN----EPAREEVLAAILAWLE 220
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 118-261 5.83e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 47.22  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 118 GVTSKDVVLDADTGVSVR--LFLPKlqEPSKKLPVVVFFHGGAFFIESAGsetyhNYVNSLaAAAGVLVVSVDYR----- 190
Cdd:COG1073     7 KVNKEDVTFKSRDGIKLAgdLYLPA--GASKKYPAVVVAHGNGGVKEQRA-----LYAQRL-AELGFNVLAFDYRgyges 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002293623 191 --LAPEHPLPAGYdDSWAALQWAASAQDgwiaehGDTARLFVAGDSAGANIAhemlvrAAASGGRPRMEGAIL 261
Cdd:COG1073    79 egEPREEGSPERR-DARAAVDYLRTLPG------VDPERIGLLGISLGGGYA------LNAAATDPRVKAVIL 138
COG4099 COG4099
Predicted peptidase [General function prediction only];
122-249 1.63e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.73  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 122 KDVVLDADTGVSV--RLFLPKLQEPSKKLPVVVFFHGgaffiesaGSETYHNYVNSLAAAAGVLVVSVDYR------LAP 193
Cdd:COG4099    21 ARTFTDPSDGDTLpyRLYLPKGYDPGKKYPLVLFLHG--------AGERGTDNEKQLTHGAPKFINPENQAkfpaivLAP 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002293623 194 EHPLPAGYDDSwAALQWAASAQDGWIAEH-GDTARLFVAGDSAGANIAHEMLVR-----AAA 249
Cdd:COG4099    93 QCPEDDYWSDT-KALDAVLALLDDLIAEYrIDPDRIYLTGLSMGGYGTWDLAARypdlfAAA 153
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
119-355 6.29e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 40.72  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 119 VTSKDVVLDADTGVSVR--LFLPKLQEPskkLPVVVFFHggaffiESAGSETYHNYVNSLAAAAGVLVVSVDY------- 189
Cdd:COG0412     1 MTTETVTIPTPDGVTLPgyLARPAGGGP---RPGVVVLH------EIFGLNPHIRDVARRLAAAGYVVLAPDLygrggpg 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 190 -------RLAPEHPLPAGYDDSWAALQWAAsAQDGWiaehgDTARLFVAGDSAGANIAhemlVRAAASggRPRMEGAILL 262
Cdd:COG0412    72 ddpdearALMGALDPELLAADLRAALDWLK-AQPEV-----DAGRVGVVGFCFGGGLA----LLAAAR--GPDLAAAVSF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 263 HPWFGGskeiEGEPEGGAAITAAMWnyacpgAAAGADDPRLNP---------LAAGGPVLEelacerMLVCAGGKDVLAA 333
Cdd:COG0412   140 YGGLPA----DDLLDLAARIKAPVL------LLYGEKDPLVPPeqvaaleaaLAAAGVDVE------LHVYPGAGHGFTN 203

                         250       260
                  ....*....|....*....|...
gi 1002293623 334 RNRAYYDAVAAS-AWRGSAAWLE 355
Cdd:COG0412   204 PGRPRYDPAAAEdAWQRTLAFLA 226
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 134-240 1.04e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 40.52  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 134 VRLFLPKLQEPSKKLPVVVFFHGGAFFIESAGSETYHNYVNSLAAAAGVLVVS----VDYRLAPEHPLPAGYDDSWAALQ 209
Cdd:pfam00756  10 VQVYLPEDYPPGRKYPVLYLLDGTGWFQNGPAKEGLDRLAASGEIPPVIIVGSprggEVSFYSDWDRGLNATEGPGAYAY 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002293623 210 WAASAQD--GWIAEHGDTARLF--VAGDSAGANIA 240
Cdd:pfam00756  90 ETFLTQElpPLLDANFPTAPDGraLAGQSMGGLGA 124
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
 136-267 1.06e-03

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 40.56  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 136 LFLPKLQEPskkLPVVVFFHGgaffiesAGSETYHNYVNSLAAAAGVLVVSVDYR----LAPEHPLPAGYDDSWAALQW- 210
Cdd:COG3458    73 LLRPKGEGP---LPAVVEFHG-------YGGGRGLPHEDLDWAAAGYAVLVMDTRgqgsSWGDTPDPGGYSGGALPGYMt 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 211 -----------------------AASAQDGWiaehgDTARLFVAGDSAGANIAhemlvrAAASGGRPRMEGAILLHPWFG 267
Cdd:COG3458   143 rgiddpdtyyyrrvyldavravdALRSLPEV-----DGKRIGVTGGSQGGGLA------LAAAALDPRVKAAAADVPFLC 211
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 108-248 1.07e-03

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 40.37  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 108 VLPAGLDEATGVTSKDVVLDADTGVSVRLFLPKLQEPSKKLPVVVFFHG----GAFFIESAGsetyhnyVNSLAAAAGVL 183
Cdd:COG3509    13 LLALLPAAAAAGDFERTFTVGGGTRTYRLYVPAGYDGGAPLPLVVALHGcggsAADFAAGTG-------LNALADREGFI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 184 VVsvdyrlapehpLPAGYDD------SWAALQWAASAQD--GWI--------AEHG-DTARLFVAGDSAGANIAHEMLVR 246
Cdd:COG3509    86 VV-----------YPEGTGRapgrcwNWFDGRDQRRGRDdvAFIaalvddlaARYGiDPKRVYVTGLSAGGAMAYRLACE 154


                  ..
gi 1002293623 247 AA 248
Cdd:COG3509   155 YP 156
YpfH COG0400
Predicted esterase [General function prediction only];
149-305 1.74e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.12  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 149 PVVVFFHG-GAffiesagSETYHNYVNSLAAAAGVLVVSVDyrlAPEHPLPAGYddSWAALQWAASAQD----------- 216
Cdd:COG0400     6 PLVVLLHGyGG-------DEEDLLPLAPELALPGAAVLAPR---APVPEGPGGR--AWFDLSFLEGREDeeglaaaaeal 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293623 217 -----GWIAEHG-DTARLFVAGDSAGANIAHEMLVRAAAsggrpRMEGAILLHPWFGGSkEIEGEPEGGAAITAAMWnya 290
Cdd:COG0400    74 aafidELEARYGiDPERIVLAGFSQGAAMALSLALRRPE-----LLAGVVALSGYLPGE-EALPAPEAALAGTPVFL--- 144

                         170
                  ....*....|....*
gi 1002293623 291 cpgaAAGADDPRLNP 305
Cdd:COG0400   145 ----AHGTQDPVIPV 155
 
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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