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Conserved domains on  [gi|767957330|ref|XP_011516940|]
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putative glycosyltransferase 6 domain-containing protein 1 isoform X3 [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 58-244 5.39e-91

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd02515:

Pssm-ID: 472172  Cd Length: 271  Bit Score: 269.20  E-value: 5.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330  58 EYLRPFLHSANKHFMTGYRVIFYIMVDAFFKLPDIEPSPLRTFKAFKVGTERWWLDGPLVHVKSLGEHIASHIQDEVDFL 137
Cdd:cd02515   48 EFLERFLESAEKHFMVGYRVIYYIFTDKPAAVPEVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330 138 FSMAANQVFQNEFGVETLGPLVAQLHAWWYFRNTKNFPYERRPTSAACIPFGQGDFYYGNLMVGGTPHNILDFIKEYLNG 217
Cdd:cd02515  128 FCMDVDMVFQGPFGVETLGDSVAQLHPWWYGKPRKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEG 207

                        170       180
                 ....*....|....*....|....*....
gi 767957330 218 VIHDIKNGL--NSTYEKHLNKYFYLNKPT 244
Cdd:cd02515  208 ILADKANGIeaRWHDESHLNKYFLLHKPT 236
 
Name Accession Description Interval E-value
Glyco_transf_6 cd02515
Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO ...
 58-244 5.39e-91

Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO blood group antigens; Glycosyltransferase family 6, GT_6, comprises enzymes with three known activities: alpha-1,3-galactosyltransferase, alpha-1,3 N-acetylgalactosaminyltransferase, and alpha-galactosyltransferase. UDP-galactose:beta-galactosyl alpha-1,3-galactosyltransferase (alpha3GT) catalyzes the transfer of galactose from UDP-alpha-d-galactose into an alpha-1,3 linkage with beta-galactosyl groups in glycoconjugates. The enzyme exists in most mammalian species but is absent from humans, apes, and old world monkeys as a result of the mutational inactivation of the gene. The alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase are responsible for the production of the human ABO blood group antigens. A N-acetylgalactosaminyltransferases use a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase uses a UDP-galactose donor to convert the H-antigen acceptor to the B antigen. Alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase differ only in the identity of four critical amino acid residues.


Pssm-ID: 133008  Cd Length: 271  Bit Score: 269.20  E-value: 5.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330  58 EYLRPFLHSANKHFMTGYRVIFYIMVDAFFKLPDIEPSPLRTFKAFKVGTERWWLDGPLVHVKSLGEHIASHIQDEVDFL 137
Cdd:cd02515   48 EFLERFLESAEKHFMVGYRVIYYIFTDKPAAVPEVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330 138 FSMAANQVFQNEFGVETLGPLVAQLHAWWYFRNTKNFPYERRPTSAACIPFGQGDFYYGNLMVGGTPHNILDFIKEYLNG 217
Cdd:cd02515  128 FCMDVDMVFQGPFGVETLGDSVAQLHPWWYGKPRKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEG 207

                        170       180
                 ....*....|....*....|....*....
gi 767957330 218 VIHDIKNGL--NSTYEKHLNKYFYLNKPT 244
Cdd:cd02515  208 ILADKANGIeaRWHDESHLNKYFLLHKPT 236
Glyco_transf_6 pfam03414
Glycosyltransferase family 6;
59-244 1.06e-65

Glycosyltransferase family 6;


Pssm-ID: 427285  Cd Length: 289  Bit Score: 205.38  E-value: 1.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330   59 YLRPFLHSANKHFMTGYRVIFYIMVDAFFKLPDIEPSPLRTFKAFKVGTERWWLDGPLVHVKSLGEHIASHIQDEVDFLF 138
Cdd:pfam03414  66 FLELFLESAEKYFMVGHRVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLF 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330  139 SMAANQVFQNEFGVETLGPLVAQLHAWWYFRNTKNFPYERRPTSAACIPFGQGDFYYGNLMVGGTPHNILDFIKEYLNGV 218
Cdd:pfam03414 146 CVDVDMVFRDHFGVETLGPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAI 225

                         170       180
                  ....*....|....*....|....*...
gi 767957330  219 IHDIKNGLNSTY--EKHLNKYFYLNKPT 244
Cdd:pfam03414 226 LADKANGIEAAWhdESHLNKYFLSHKPT 253
 
Name Accession Description Interval E-value
Glyco_transf_6 cd02515
Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO ...
 58-244 5.39e-91

Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO blood group antigens; Glycosyltransferase family 6, GT_6, comprises enzymes with three known activities: alpha-1,3-galactosyltransferase, alpha-1,3 N-acetylgalactosaminyltransferase, and alpha-galactosyltransferase. UDP-galactose:beta-galactosyl alpha-1,3-galactosyltransferase (alpha3GT) catalyzes the transfer of galactose from UDP-alpha-d-galactose into an alpha-1,3 linkage with beta-galactosyl groups in glycoconjugates. The enzyme exists in most mammalian species but is absent from humans, apes, and old world monkeys as a result of the mutational inactivation of the gene. The alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase are responsible for the production of the human ABO blood group antigens. A N-acetylgalactosaminyltransferases use a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase uses a UDP-galactose donor to convert the H-antigen acceptor to the B antigen. Alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase differ only in the identity of four critical amino acid residues.


Pssm-ID: 133008  Cd Length: 271  Bit Score: 269.20  E-value: 5.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330  58 EYLRPFLHSANKHFMTGYRVIFYIMVDAFFKLPDIEPSPLRTFKAFKVGTERWWLDGPLVHVKSLGEHIASHIQDEVDFL 137
Cdd:cd02515   48 EFLERFLESAEKHFMVGYRVIYYIFTDKPAAVPEVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330 138 FSMAANQVFQNEFGVETLGPLVAQLHAWWYFRNTKNFPYERRPTSAACIPFGQGDFYYGNLMVGGTPHNILDFIKEYLNG 217
Cdd:cd02515  128 FCMDVDMVFQGPFGVETLGDSVAQLHPWWYGKPRKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEG 207

                        170       180
                 ....*....|....*....|....*....
gi 767957330 218 VIHDIKNGL--NSTYEKHLNKYFYLNKPT 244
Cdd:cd02515  208 ILADKANGIeaRWHDESHLNKYFLLHKPT 236
Glyco_transf_6 pfam03414
Glycosyltransferase family 6;
59-244 1.06e-65

Glycosyltransferase family 6;


Pssm-ID: 427285  Cd Length: 289  Bit Score: 205.38  E-value: 1.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330   59 YLRPFLHSANKHFMTGYRVIFYIMVDAFFKLPDIEPSPLRTFKAFKVGTERWWLDGPLVHVKSLGEHIASHIQDEVDFLF 138
Cdd:pfam03414  66 FLELFLESAEKYFMVGHRVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLF 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957330  139 SMAANQVFQNEFGVETLGPLVAQLHAWWYFRNTKNFPYERRPTSAACIPFGQGDFYYGNLMVGGTPHNILDFIKEYLNGV 218
Cdd:pfam03414 146 CVDVDMVFRDHFGVETLGPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAI 225

                         170       180
                  ....*....|....*....|....*...
gi 767957330  219 IHDIKNGLNSTY--EKHLNKYFYLNKPT 244
Cdd:pfam03414 226 LADKANGIEAAWhdESHLNKYFLSHKPT 253
 
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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