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Conserved domains on  [gi|357514717|ref|XP_003627647|]
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probable carboxylesterase 8 [Medicago truncatula]

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

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.
82-304 2.47e-55

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: 179.33  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717   82 ILYFHGGGFFRYHPSSisFHQCCSTFAAQIPIVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQnpsvsdpwiRDNVD 161
Cdd:pfam07859   1 LVYFHGGGFVLGSADT--HDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAA---------ELGAD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  162 FDNCFLMGSSAGGNIAYFAGLRALDLDLSPLKIQGLIMnaPffGGVQRTKSELRFINDN----ILPLSASDLMWALSLPe 237
Cdd:pfam07859  70 PSRIAVAGDSAGGNLAAAVALRARDEGLPKPAGQVLIY--P--GTDLRTESPSYLAREFadgpLLTRAAMDWFWRLYLP- 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357514717  238 GTDRDHVYCNPkvsdvIHGEKIGRLPRCFVNGYGGDPLVDRQKELVKILEARGVHVESVFCEDGFHA 304
Cdd:pfam07859 145 GADRDDPLASP-----LFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHG 206
 
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.
82-304 2.47e-55

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: 179.33  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717   82 ILYFHGGGFFRYHPSSisFHQCCSTFAAQIPIVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQnpsvsdpwiRDNVD 161
Cdd:pfam07859   1 LVYFHGGGFVLGSADT--HDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAA---------ELGAD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  162 FDNCFLMGSSAGGNIAYFAGLRALDLDLSPLKIQGLIMnaPffGGVQRTKSELRFINDN----ILPLSASDLMWALSLPe 237
Cdd:pfam07859  70 PSRIAVAGDSAGGNLAAAVALRARDEGLPKPAGQVLIY--P--GTDLRTESPSYLAREFadgpLLTRAAMDWFWRLYLP- 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357514717  238 GTDRDHVYCNPkvsdvIHGEKIGRLPRCFVNGYGGDPLVDRQKELVKILEARGVHVESVFCEDGFHA 304
Cdd:pfam07859 145 GADRDDPLASP-----LFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
75-324 4.01e-31

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 116.13  E-value: 4.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  75 SAAKLPLILYFHGGGFFryHPSSISFHQCCSTFAAQIPIVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQnpsvsdp 154
Cdd:COG0657    9 AKGPLPVVVYFHGGGWV--SGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAA------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 155 wiRDNVDFDNCFLMGSSAGGNIAYFAGLRALDLDLSplKIQGLIMNAPFFGgvqrtkselrfindnilpLSASDLMWALS 234
Cdd:COG0657   80 --ELGIDPDRIAVAGDSAGGHLAAALALRARDRGGP--RPAAQVLIYPVLD------------------LTASPLRADLA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 235 lpegtdrdhvycnpkvsdvihgekigRLPRCFVnGYGG-DPLVDRQKELVKILEARGVHVESVFCEDGFHAVELFDPAK- 312
Cdd:COG0657  138 --------------------------GLPPTLI-VTGEaDPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPe 190
                        250
                 ....*....|..
gi 357514717 313 AQALLDYVKKFI 324
Cdd:COG0657  191 ARAALAEIAAFL 202
PRK10162 PRK10162
acetyl esterase;
82-304 1.63e-07

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 52.03  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  82 ILYFHGGGFFRyhpSSISFH-QCCSTFAAQIPIVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQnpsvsdpwiRDNV 160
Cdd:PRK10162  84 LFYLHGGGFIL---GNLDTHdRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAE---------DYGI 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 161 DFDNCFLMGSSAGGNIAYFAGLRALDLDLSPLKIQGLIMNAPFFGgvQRTKSELRFINDNILPLSASDL-MW-ALSLPEG 238
Cdd:PRK10162 152 NMSRIGFAGDSAGAMLALASALWLRDKQIDCGKVAGVLLWYGLYG--LRDSVSRRLLGGVWDGLTQQDLqMYeEAYLSND 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357514717 239 TDRDHVYCNPKVSDVIHGekigrLPRCFVNGYGGDPLVDRQKELVKILEARGVHVESVFCEDGFHA 304
Cdd:PRK10162 230 ADRESPYYCLFNNDLTRD-----VPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHA 290
 
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.
82-304 2.47e-55

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: 179.33  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717   82 ILYFHGGGFFRYHPSSisFHQCCSTFAAQIPIVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQnpsvsdpwiRDNVD 161
Cdd:pfam07859   1 LVYFHGGGFVLGSADT--HDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAA---------ELGAD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  162 FDNCFLMGSSAGGNIAYFAGLRALDLDLSPLKIQGLIMnaPffGGVQRTKSELRFINDN----ILPLSASDLMWALSLPe 237
Cdd:pfam07859  70 PSRIAVAGDSAGGNLAAAVALRARDEGLPKPAGQVLIY--P--GTDLRTESPSYLAREFadgpLLTRAAMDWFWRLYLP- 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357514717  238 GTDRDHVYCNPkvsdvIHGEKIGRLPRCFVNGYGGDPLVDRQKELVKILEARGVHVESVFCEDGFHA 304
Cdd:pfam07859 145 GADRDDPLASP-----LFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
75-324 4.01e-31

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 116.13  E-value: 4.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  75 SAAKLPLILYFHGGGFFryHPSSISFHQCCSTFAAQIPIVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQnpsvsdp 154
Cdd:COG0657    9 AKGPLPVVVYFHGGGWV--SGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAA------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 155 wiRDNVDFDNCFLMGSSAGGNIAYFAGLRALDLDLSplKIQGLIMNAPFFGgvqrtkselrfindnilpLSASDLMWALS 234
Cdd:COG0657   80 --ELGIDPDRIAVAGDSAGGHLAAALALRARDRGGP--RPAAQVLIYPVLD------------------LTASPLRADLA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 235 lpegtdrdhvycnpkvsdvihgekigRLPRCFVnGYGG-DPLVDRQKELVKILEARGVHVESVFCEDGFHAVELFDPAK- 312
Cdd:COG0657  138 --------------------------GLPPTLI-VTGEaDPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPe 190
                        250
                 ....*....|..
gi 357514717 313 AQALLDYVKKFI 324
Cdd:COG0657  191 ARAALAEIAAFL 202
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
77-182 6.32e-10

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: 58.35  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717   77 AKLPLILYFHGGGFF---RYHPSSISFHQCCSTFAAQIpiVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQNPsvsd 153
Cdd:pfam20434  11 GPYPVVIWIHGGGWNsgdKEADMGFMTNTVKALLKAGY--AVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKY---- 84
                          90       100
                  ....*....|....*....|....*....
gi 357514717  154 pwirdNVDFDNCFLMGSSAGGNIAYFAGL 182
Cdd:pfam20434  85 -----GIDTNKIALMGFSAGGHLALLAGL 108
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
78-324 5.00e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 52.71  E-value: 5.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  78 KLPLILYFHGGGFFRYHPSSISFHQccstFAAQiPIVVASVAHRLTPEHR---LPAAYDDAIDSLFWLRAqaqnpsvsdp 154
Cdd:COG1506   22 KYPVVVYVHGGPGSRDDSFLPLAQA----LASR-GYAVLAPDYRGYGESAgdwGGDEVDDVLAAIDYLAA---------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 155 wiRDNVDFDNCFLMGSSAGGNIAYFAGLRaldldlSPLKIQGLIMNAPFFGGVQRTKSELRFINDNI-LPLSASDLMWAL 233
Cdd:COG1506   87 --RPYVDPDRIGIYGHSYGGYMALLAAAR------HPDRFKAAVALAGVSDLRSYYGTTREYTERLMgGPWEDPEAYAAR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 234 SLpegtdRDHVycnPKVSD---VIHGEKigrlprcfvngyggDPLVDRQ--KELVKILEARGVHVESVFCEDGFHAV-EL 307
Cdd:COG1506  159 SP-----LAYA---DKLKTpllLIHGEA--------------DDRVPPEqaERLYEALKKAGKPVELLVYPGEGHGFsGA 216
                        250
                 ....*....|....*..
gi 357514717 308 FDPAKAQALLDYVKKFI 324
Cdd:COG1506  217 GAPDYLERILDFLDRHL 233
PRK10162 PRK10162
acetyl esterase;
82-304 1.63e-07

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 52.03  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  82 ILYFHGGGFFRyhpSSISFH-QCCSTFAAQIPIVVASVAHRLTPEHRLPAAYDDAIDSLFWLRAQAQnpsvsdpwiRDNV 160
Cdd:PRK10162  84 LFYLHGGGFIL---GNLDTHdRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAE---------DYGI 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 161 DFDNCFLMGSSAGGNIAYFAGLRALDLDLSPLKIQGLIMNAPFFGgvQRTKSELRFINDNILPLSASDL-MW-ALSLPEG 238
Cdd:PRK10162 152 NMSRIGFAGDSAGAMLALASALWLRDKQIDCGKVAGVLLWYGLYG--LRDSVSRRLLGGVWDGLTQQDLqMYeEAYLSND 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357514717 239 TDRDHVYCNPKVSDVIHGekigrLPRCFVNGYGGDPLVDRQKELVKILEARGVHVESVFCEDGFHA 304
Cdd:PRK10162 230 ADRESPYYCLFNNDLTRD-----VPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHA 290
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
80-175 2.47e-04

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 42.52  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717   80 PLILYFHGGGF-FRYHPSSISFHQCCSTFAAQIPIVVasvahrltPEHRLPAAYDDAIDslfWLRAQAQNPSVSDpWIRD 158
Cdd:pfam10340 123 PILLYYHGGGFaLKLIPVTLVFLNNLGKYFPDMAILV--------SDYTVTANCPQSYT---YPLQVLQCLAVYD-YLTL 190
                          90
                  ....*....|....*..
gi 357514717  159 NVDFDNCFLMGSSAGGN 175
Cdd:pfam10340 191 TKGCKNVTLMGDSAGGN 207
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
74-174 1.10e-03

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 40.64  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717  74 SSAAKLPLILYFHGGGFFRYHPSSISFHqcCSTFAAQiPIVVASVAHRL------------TPEHRLPAAYD--DAIDSl 139
Cdd:COG2272  100 AAGAKLPVMVWIHGGGFVSGSGSEPLYD--GAALARR-GVVVVTINYRLgalgflalpalsGESYGASGNYGllDQIAA- 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 357514717 140 fwLRaqaqnpsvsdpWIRDNV-----DFDNCFLMGSSAGG 174
Cdd:COG2272  176 --LR-----------WVRDNIaafggDPDNVTIFGESAGA 202
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
166-324 2.92e-03

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 38.44  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357514717 166 FLMGSSAGGNIAYFAGLRAldldlsPLKIQGLIMNAPFFGGVQRTKSELRFINDnilpLSASDLMWALSLPegtdrdhVY 245
Cdd:COG2267  102 VLLGHSMGGLIALLYAARY------PDRVAGLVLLAPAYRADPLLGPSARWLRA----LRLAEALARIDVP-------VL 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357514717 246 cnpkvsdVIHGEKigrlprcfvngyggDPLVDRqKELVKILEARGVHVESVFCEDGFHAVeLFDPAKAQAlLDYVKKFI 324
Cdd:COG2267  165 -------VLHGGA--------------DRVVPP-EAARRLAARLSPDVELVLLPGARHEL-LNEPAREEV-LAAILAWL 219
 
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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