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Conserved domains on  [gi|568990339|ref|XP_006520075|]
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UDP-glucuronosyltransferase 3A1 isoform X2 [Mus musculus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
24-281 3.21e-29

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member pfam00201:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 499  Bit Score: 116.74  E-value: 3.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339   24 KILTISTlSASHYILMNRVSQILQGGGHDVIKLLYEGGDIPDFRKEnSSYQVINWRLP---EDQQKTFENRWHRLIDEYA 100
Cdd:pfam00201   2 KVLVWPM-DGSHWMNMKGILEELVQRGHEVTVLRPSASISIGPGKP-SNLKFETYPTSatkEELENPFPKRQMQWFEEAS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  101 YGRSK--YHTLLKIHQYFADLCSHLLSRKDIMELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDF---- 174
Cdd:pfam00201  80 FGTVWsyFSALQEYSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEkvsg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  175 GLPNaPLSYAPVYGSGLTDQMDFWGRVKNILM--FFHFtkkrrdIFSQYGNTVQEHFAEGSQ-PV-LSDLLLKAELWFVN 250
Cdd:pfam00201 160 GLPS-PPSYVPVILSDLSDHMTFMERVKNMLImlYFDF------WFQCFPRKWDQFASEVLGrPVtLPELMSKASVWLIR 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 568990339  251 SDFALDFARPLFPNTVYVGGLLDKPVQPIPQ 281
Cdd:pfam00201 233 SYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQ 263
 
Name Accession Description Interval E-value
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
24-281 3.21e-29

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 116.74  E-value: 3.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339   24 KILTISTlSASHYILMNRVSQILQGGGHDVIKLLYEGGDIPDFRKEnSSYQVINWRLP---EDQQKTFENRWHRLIDEYA 100
Cdd:pfam00201   2 KVLVWPM-DGSHWMNMKGILEELVQRGHEVTVLRPSASISIGPGKP-SNLKFETYPTSatkEELENPFPKRQMQWFEEAS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  101 YGRSK--YHTLLKIHQYFADLCSHLLSRKDIMELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDF---- 174
Cdd:pfam00201  80 FGTVWsyFSALQEYSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEkvsg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  175 GLPNaPLSYAPVYGSGLTDQMDFWGRVKNILM--FFHFtkkrrdIFSQYGNTVQEHFAEGSQ-PV-LSDLLLKAELWFVN 250
Cdd:pfam00201 160 GLPS-PPSYVPVILSDLSDHMTFMERVKNMLImlYFDF------WFQCFPRKWDQFASEVLGrPVtLPELMSKASVWLIR 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 568990339  251 SDFALDFARPLFPNTVYVGGLLDKPVQPIPQ 281
Cdd:pfam00201 233 SYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQ 263
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
24-278 1.91e-09

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: 58.33  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  24 KILTISTLSASHYILMNRVSQILQGGGHDVIKLLYEGGDIPDFRKENSSYQVINWRLPEDQQKTFENRWHRLIDEYAYGR 103
Cdd:cd03784    2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLELLRRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339 104 SKYHTLLkihqyFADLCSHLLSrkdimellqKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDFGLPnaplsY 183
Cdd:cd03784   82 LKAADEL-----LDDLLAALRS---------SWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYLH-----P 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339 184 APVYGSGLTDQMDFWGRVKNILMFFHFTKKRRdifsqygntvqeHFAEGSQPVLSDLLLKAELWFVNSDFALDFARPLFP 263
Cdd:cd03784  143 FGVLNLLLSSLLEPELFLDPLLEVLDRLRERL------------GLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLP 210
                        250
                 ....*....|....*
gi 568990339 264 NTVYVGGLLDKPVQP 278
Cdd:cd03784  211 SVLGGLRIVPKNGPL 225
 
Name Accession Description Interval E-value
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
24-281 3.21e-29

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 116.74  E-value: 3.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339   24 KILTISTlSASHYILMNRVSQILQGGGHDVIKLLYEGGDIPDFRKEnSSYQVINWRLP---EDQQKTFENRWHRLIDEYA 100
Cdd:pfam00201   2 KVLVWPM-DGSHWMNMKGILEELVQRGHEVTVLRPSASISIGPGKP-SNLKFETYPTSatkEELENPFPKRQMQWFEEAS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  101 YGRSK--YHTLLKIHQYFADLCSHLLSRKDIMELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDF---- 174
Cdd:pfam00201  80 FGTVWsyFSALQEYSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEkvsg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  175 GLPNaPLSYAPVYGSGLTDQMDFWGRVKNILM--FFHFtkkrrdIFSQYGNTVQEHFAEGSQ-PV-LSDLLLKAELWFVN 250
Cdd:pfam00201 160 GLPS-PPSYVPVILSDLSDHMTFMERVKNMLImlYFDF------WFQCFPRKWDQFASEVLGrPVtLPELMSKASVWLIR 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 568990339  251 SDFALDFARPLFPNTVYVGGLLDKPVQPIPQ 281
Cdd:pfam00201 233 SYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQ 263
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
24-278 1.91e-09

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: 58.33  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339  24 KILTISTLSASHYILMNRVSQILQGGGHDVIKLLYEGGDIPDFRKENSSYQVINWRLPEDQQKTFENRWHRLIDEYAYGR 103
Cdd:cd03784    2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLELLRRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339 104 SKYHTLLkihqyFADLCSHLLSrkdimellqKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDFGLPnaplsY 183
Cdd:cd03784   82 LKAADEL-----LDDLLAALRS---------SWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYLH-----P 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990339 184 APVYGSGLTDQMDFWGRVKNILMFFHFTKKRRdifsqygntvqeHFAEGSQPVLSDLLLKAELWFVNSDFALDFARPLFP 263
Cdd:cd03784  143 FGVLNLLLSSLLEPELFLDPLLEVLDRLRERL------------GLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLP 210
                        250
                 ....*....|....*
gi 568990339 264 NTVYVGGLLDKPVQP 278
Cdd:cd03784  211 SVLGGLRIVPKNGPL 225
 
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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