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Conserved domains on  [gi|61608262|gb|AAX47027|]
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UDP-glucuronosyltransferase 1A8, partial [Homo sapiens]

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 ...
26-285 4.95e-107

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: 319.74  E-value: 4.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262    26 GKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLG--KSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVR 103
Cdd:pfam00201   1 GKVLVWPMDGSHWMNMKGILEELVQRGHEVTVLRPSASISIGpgKPSNLKFETYPTSATKEELENPFPKRQMQWFEEASF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262   104 SLFSLFLSSSNGFFNLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEGA-Q 182
Cdd:pfam00201  81 GTVWSYFSALQEYSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEKVSgG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262   183 CPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYP 262
Cdd:pfam00201 161 LPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFPRKWDQFASEVLGRPVTLPELMSKASVWLIRSYWDLEFP 240
                         250       260
                  ....*....|....*....|...
gi 61608262   263 KPVMPNMIFIGGINYHQGKPLPM 285
Cdd:pfam00201 241 RPLLPNMDFIGGLHCKPAKPLPQ 263
 
Name Accession Description Interval E-value
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
26-285 4.95e-107

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 319.74  E-value: 4.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262    26 GKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLG--KSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVR 103
Cdd:pfam00201   1 GKVLVWPMDGSHWMNMKGILEELVQRGHEVTVLRPSASISIGpgKPSNLKFETYPTSATKEELENPFPKRQMQWFEEASF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262   104 SLFSLFLSSSNGFFNLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEGA-Q 182
Cdd:pfam00201  81 GTVWSYFSALQEYSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEKVSgG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262   183 CPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYP 262
Cdd:pfam00201 161 LPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFPRKWDQFASEVLGRPVTLPELMSKASVWLIRSYWDLEFP 240
                         250       260
                  ....*....|....*....|...
gi 61608262   263 KPVMPNMIFIGGINYHQGKPLPM 285
Cdd:pfam00201 241 RPLLPNMDFIGGLHCKPAKPLPQ 263
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
28-267 4.31e-13

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: 68.73  E-value: 4.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262  28 LLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEvswqlgkslnctvktYSTSYTLEDLDREFMDFADAQWKAQVRSLFS 107
Cdd:cd03784   4 LFVPFPGQGHVNPMLPLAKALAARGHEVTVATPP---------------FNFADLVEAAGLTFVPVGDDPDELELDSETN 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262 108 LFLSSSNGFFNLFFSHCRSLFNDrkLVEYLKESS-FDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEegaqCPAP 186
Cdd:cd03784  69 LGPDSLLELLRRLLKAADELLDD--LLAALRSSWkPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSA----YLHP 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262 187 LSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIaseilqTPVTAYDLYSHTSIWLLRTDFVLDYPKPVM 266
Cdd:cd03784 143 FGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLL------RLVPPLYVIGPTFPSLPPDRPRLPSVLGGL 216

                .
gi 61608262 267 P 267
Cdd:cd03784 217 R 217
 
Name Accession Description Interval E-value
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
26-285 4.95e-107

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 319.74  E-value: 4.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262    26 GKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLG--KSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVR 103
Cdd:pfam00201   1 GKVLVWPMDGSHWMNMKGILEELVQRGHEVTVLRPSASISIGpgKPSNLKFETYPTSATKEELENPFPKRQMQWFEEASF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262   104 SLFSLFLSSSNGFFNLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEGA-Q 182
Cdd:pfam00201  81 GTVWSYFSALQEYSDGYRVTCKELVGNKKLMTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEKVSgG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262   183 CPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYP 262
Cdd:pfam00201 161 LPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFPRKWDQFASEVLGRPVTLPELMSKASVWLIRSYWDLEFP 240
                         250       260
                  ....*....|....*....|...
gi 61608262   263 KPVMPNMIFIGGINYHQGKPLPM 285
Cdd:pfam00201 241 RPLLPNMDFIGGLHCKPAKPLPQ 263
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
28-267 4.31e-13

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: 68.73  E-value: 4.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262  28 LLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEvswqlgkslnctvktYSTSYTLEDLDREFMDFADAQWKAQVRSLFS 107
Cdd:cd03784   4 LFVPFPGQGHVNPMLPLAKALAARGHEVTVATPP---------------FNFADLVEAAGLTFVPVGDDPDELELDSETN 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262 108 LFLSSSNGFFNLFFSHCRSLFNDrkLVEYLKESS-FDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEegaqCPAP 186
Cdd:cd03784  69 LGPDSLLELLRRLLKAADELLDD--LLAALRSSWkPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSA----YLHP 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61608262 187 LSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIaseilqTPVTAYDLYSHTSIWLLRTDFVLDYPKPVM 266
Cdd:cd03784 143 FGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLL------RLVPPLYVIGPTFPSLPPDRPRLPSVLGGL 216

                .
gi 61608262 267 P 267
Cdd:cd03784 217 R 217
 
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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