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Conserved domains on  [gi|1061214223|ref|NP_001317648|]
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UDP-glucuronosyltransferase 2B7 isoform 2 precursor [Homo sapiens]

Protein Classification

UDP-glycosyltransferase family protein( domain architecture ID 11989770)

UDP-glycosyltransferase family protein similar to UDP-glucuronosyltransferase (UDPGT), which is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds

EC:  2.4.-.-
Gene Ontology:  GO:0008194|GO:0006486
SCOP:  3001586

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
24-363 0e+00

UDP-glucoronosyl and UDP-glucosyl transferase;


:

Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 579.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223  24 GKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRW-SDLPK 102
Cdd:pfam00201   1 GKVLVWPMDGSHWMNMKGILEELVQRGHEVTVLRPSASISIGPGKPSNLKFETYPTSATKEELENPFPKRQMQWfEEASF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 103 DTFWLYFSQVQEimsiFGDITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEK 182
Cdd:pfam00201  81 GTVWSYFSALQE----YSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 183 HSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDmKKWDQFYSEVLGRPTTLSETMGKADVWLIRNSW 262
Cdd:pfam00201 157 VSGGLPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFP-RKWDQFASEVLGRPVTLPELMSKASVWLIRSYW 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 263 NFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGN 342
Cdd:pfam00201 236 DLEFPRPLLPNMDFIGGLHCKPAKPLPQEMEAFVQSSGEHGVVVFSLGSMVSNIPEEKANAIASALAQIPQKVLWRFDGT 315
                         330       340
                  ....*....|....*....|.
gi 1061214223 343 KPDTLGLNTRLYKWIPQNDLL 363
Cdd:pfam00201 316 KPSTLGNNTRLVKWLPQNDLL 336
 
Name Accession Description Interval E-value
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
24-363 0e+00

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 579.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223  24 GKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRW-SDLPK 102
Cdd:pfam00201   1 GKVLVWPMDGSHWMNMKGILEELVQRGHEVTVLRPSASISIGPGKPSNLKFETYPTSATKEELENPFPKRQMQWfEEASF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 103 DTFWLYFSQVQEimsiFGDITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEK 182
Cdd:pfam00201  81 GTVWSYFSALQE----YSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 183 HSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDmKKWDQFYSEVLGRPTTLSETMGKADVWLIRNSW 262
Cdd:pfam00201 157 VSGGLPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFP-RKWDQFASEVLGRPVTLPELMSKASVWLIRSYW 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 263 NFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGN 342
Cdd:pfam00201 236 DLEFPRPLLPNMDFIGGLHCKPAKPLPQEMEAFVQSSGEHGVVVFSLGSMVSNIPEEKANAIASALAQIPQKVLWRFDGT 315
                         330       340
                  ....*....|....*....|.
gi 1061214223 343 KPDTLGLNTRLYKWIPQNDLL 363
Cdd:pfam00201 316 KPSTLGNNTRLVKWLPQNDLL 336
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
25-363 2.28e-34

UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.


Pssm-ID: 340817 [Multi-domain]  Cd Length: 404  Bit Score: 130.75  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223  25 KVLVWA-AEYSHWMNIKTILDELIQRGHEVTVLASSasILFDPNNSSAlKIEIYPTSLTKTELENFIMQQikrwsDLPKD 103
Cdd:cd03784     2 RILFVPfPGQGHVNPMLPLAKALAARGHEVTVATPP--FNFADLVEAA-GLTFVPVGDDPDELELDSETN-----LGPDS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 104 TFWLYFSQVQEIMSIFGDITRKFCKDvvsnkkfmkkvqeSRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEKH 183
Cdd:cd03784    74 LLELLRRLLKAADELLDDLLAALRSS-------------WKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 184 SGGFIFPPSYVPVVMSELTDQM--TFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSevlgrPTTLSEtmgkadvwlirns 261
Cdd:cd03784   141 HPFGVLNLLLSSLLEPELFLDPllEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIG-----PTFPSL------------- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 262 wnfqFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDG 341
Cdd:cd03784   203 ----PPDRPRLPSVLGGLRIVPKNGPLPDELWEWLDKQPPRSVVYVSFGSMVRDLPEELLELIAEALASLGQRFLWVVGP 278
                         330       340
                  ....*....|....*....|....*
gi 1061214223 342 NKPDTLGL---NTRLYKWIPQNDLL 363
Cdd:cd03784   279 DPLGGLERlpdNVLVVKWVPQDELL 303
egt PHA03392
ecdysteroid UDP-glucosyltransferase; Provisional
8-368 1.10e-09

ecdysteroid UDP-glucosyltransferase; Provisional


Pssm-ID: 223071 [Multi-domain]  Cd Length: 507  Bit Score: 59.59  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223   8 VILLIQLSFCFSSGNCGKVLvwaA-----EYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKiEIyPTSLT 82
Cdd:PHA03392    5 IIILLLLLLLLSGVRAARIL---AvfptpAYSHHSVFKVYVEALAERGHNVTVIKPTLRVYYASHLCGNIT-EI-DASLS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223  83 KTELENFIMQ-QIKRWSDLPKDTfwlyfSQV--QEIMSIFGDITRKFCKDVVsnKKFMKKvQESRFDVIFADAIFPCSEL 159
Cdd:PHA03392   80 VEYFKKLVKSsAVFRKRGVVADS-----STVtaDNYMGLVRMISDQFDLPNV--KNLIAN-KNNKFDLLVTEAFLDYPLV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 160 LAELF-NIPFVyslSFSPGY----TFEKhSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFD------ 228
Cdd:PHA03392  152 FSHLFgDAPVI---QISSGYglaeNFET-MGAVSRHPVYYPNLWRSKFGNLNVWETINEIYTELRLYNEFSLLAdeqnkl 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 229 MKKwdQFysevlGRPT-TLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLH--CKPAKPLPKEMEDFVQSSgENGVV 305
Cdd:PHA03392  228 LKQ--QF-----GPDTpTIRELRNRVQLLFVNVHPVFDNNRPVPPSVQYLGGLHlhKKPPQPLDDYLEEFLNNS-TNGVV 299
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1061214223 306 VFSLGSM--VSNMTEERANVIASALAQIPQKVLWRFDGNKP-DTLGLNTRLYKWIPQNDLLDIKRM 368
Cdd:PHA03392  300 YVSFGSSidTNDMDNEFLQMLLRTFKKLPYNVLWKYDGEVEaINLPANVLTQKWFPQRAVLKHKNV 365
 
Name Accession Description Interval E-value
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
24-363 0e+00

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 579.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223  24 GKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRW-SDLPK 102
Cdd:pfam00201   1 GKVLVWPMDGSHWMNMKGILEELVQRGHEVTVLRPSASISIGPGKPSNLKFETYPTSATKEELENPFPKRQMQWfEEASF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 103 DTFWLYFSQVQEimsiFGDITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEK 182
Cdd:pfam00201  81 GTVWSYFSALQE----YSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 183 HSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDmKKWDQFYSEVLGRPTTLSETMGKADVWLIRNSW 262
Cdd:pfam00201 157 VSGGLPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFP-RKWDQFASEVLGRPVTLPELMSKASVWLIRSYW 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 263 NFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGN 342
Cdd:pfam00201 236 DLEFPRPLLPNMDFIGGLHCKPAKPLPQEMEAFVQSSGEHGVVVFSLGSMVSNIPEEKANAIASALAQIPQKVLWRFDGT 315
                         330       340
                  ....*....|....*....|.
gi 1061214223 343 KPDTLGLNTRLYKWIPQNDLL 363
Cdd:pfam00201 316 KPSTLGNNTRLVKWLPQNDLL 336
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
25-363 2.28e-34

UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.


Pssm-ID: 340817 [Multi-domain]  Cd Length: 404  Bit Score: 130.75  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223  25 KVLVWA-AEYSHWMNIKTILDELIQRGHEVTVLASSasILFDPNNSSAlKIEIYPTSLTKTELENFIMQQikrwsDLPKD 103
Cdd:cd03784     2 RILFVPfPGQGHVNPMLPLAKALAARGHEVTVATPP--FNFADLVEAA-GLTFVPVGDDPDELELDSETN-----LGPDS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 104 TFWLYFSQVQEIMSIFGDITRKFCKDvvsnkkfmkkvqeSRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEKH 183
Cdd:cd03784    74 LLELLRRLLKAADELLDDLLAALRSS-------------WKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 184 SGGFIFPPSYVPVVMSELTDQM--TFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSevlgrPTTLSEtmgkadvwlirns 261
Cdd:cd03784   141 HPFGVLNLLLSSLLEPELFLDPllEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIG-----PTFPSL------------- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 262 wnfqFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDG 341
Cdd:cd03784   203 ----PPDRPRLPSVLGGLRIVPKNGPLPDELWEWLDKQPPRSVVYVSFGSMVRDLPEELLELIAEALASLGQRFLWVVGP 278
                         330       340
                  ....*....|....*....|....*
gi 1061214223 342 NKPDTLGL---NTRLYKWIPQNDLL 363
Cdd:cd03784   279 DPLGGLERlpdNVLVVKWVPQDELL 303
egt PHA03392
ecdysteroid UDP-glucosyltransferase; Provisional
8-368 1.10e-09

ecdysteroid UDP-glucosyltransferase; Provisional


Pssm-ID: 223071 [Multi-domain]  Cd Length: 507  Bit Score: 59.59  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223   8 VILLIQLSFCFSSGNCGKVLvwaA-----EYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKiEIyPTSLT 82
Cdd:PHA03392    5 IIILLLLLLLLSGVRAARIL---AvfptpAYSHHSVFKVYVEALAERGHNVTVIKPTLRVYYASHLCGNIT-EI-DASLS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223  83 KTELENFIMQ-QIKRWSDLPKDTfwlyfSQV--QEIMSIFGDITRKFCKDVVsnKKFMKKvQESRFDVIFADAIFPCSEL 159
Cdd:PHA03392   80 VEYFKKLVKSsAVFRKRGVVADS-----STVtaDNYMGLVRMISDQFDLPNV--KNLIAN-KNNKFDLLVTEAFLDYPLV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 160 LAELF-NIPFVyslSFSPGY----TFEKhSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFD------ 228
Cdd:PHA03392  152 FSHLFgDAPVI---QISSGYglaeNFET-MGAVSRHPVYYPNLWRSKFGNLNVWETINEIYTELRLYNEFSLLAdeqnkl 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214223 229 MKKwdQFysevlGRPT-TLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLH--CKPAKPLPKEMEDFVQSSgENGVV 305
Cdd:PHA03392  228 LKQ--QF-----GPDTpTIRELRNRVQLLFVNVHPVFDNNRPVPPSVQYLGGLHlhKKPPQPLDDYLEEFLNNS-TNGVV 299
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1061214223 306 VFSLGSM--VSNMTEERANVIASALAQIPQKVLWRFDGNKP-DTLGLNTRLYKWIPQNDLLDIKRM 368
Cdd:PHA03392  300 YVSFGSSidTNDMDNEFLQMLLRTFKKLPYNVLWKYDGEVEaINLPANVLTQKWFPQRAVLKHKNV 365
 
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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