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Conserved domains on  [gi|149039248|gb|EDL93468|]
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rCG45409 [Rattus norvegicus]

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 ...
47-334 4.84e-176

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 pfam03414:

Pssm-ID: 472172  Cd Length: 289  Bit Score: 489.27  E-value: 4.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248   47 VNRKAYPQPRVLTPTRTDVLVLTPWLAPIIWEGTFNIDILNEQFRLRNTTIGLTVFAIKKYVVFLKLFLETAEQHFMVGH 126
Cdd:pfam03414   3 LPRWFYPKPKLLEPKRPDVLTVTPWLAPIVWEGTFDPAILEDYYRPQNLTIGLTVFAVGKYVRFLELFLESAEKYFMVGH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  127 KVIYYVFTDRPADVPQVPLGAGRRLVVLTVRNYTRWQDVSMHRMEVISHFSEQRFRHEVDYLVCADVDMKFRDHVGVEIL 206
Cdd:pfam03414  83 RVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLFCVDVDMVFRDHFGVETL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  207 SALFGTLHPGFYRSRRESFTYERRPQSQAYIPWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESH 286
Cdd:pfam03414 163 GPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAILADKANGIEAAWHDESH 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 149039248  287 LNKYLLYHKPTKVLSPEYMWDQQlLGWPSIMKKLRYVAVPKNHQAIRN 334
Cdd:pfam03414 243 LNKYFLSHKPTKVLSPEYLWDYQ-IGRPSDLRLVRFAWVPKNYNWVRN 289
 
Name Accession Description Interval E-value
Glyco_transf_6 pfam03414
Glycosyltransferase family 6;
47-334 4.84e-176

Glycosyltransferase family 6;


Pssm-ID: 427285  Cd Length: 289  Bit Score: 489.27  E-value: 4.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248   47 VNRKAYPQPRVLTPTRTDVLVLTPWLAPIIWEGTFNIDILNEQFRLRNTTIGLTVFAIKKYVVFLKLFLETAEQHFMVGH 126
Cdd:pfam03414   3 LPRWFYPKPKLLEPKRPDVLTVTPWLAPIVWEGTFDPAILEDYYRPQNLTIGLTVFAVGKYVRFLELFLESAEKYFMVGH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  127 KVIYYVFTDRPADVPQVPLGAGRRLVVLTVRNYTRWQDVSMHRMEVISHFSEQRFRHEVDYLVCADVDMKFRDHVGVEIL 206
Cdd:pfam03414  83 RVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLFCVDVDMVFRDHFGVETL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  207 SALFGTLHPGFYRSRRESFTYERRPQSQAYIPWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESH 286
Cdd:pfam03414 163 GPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAILADKANGIEAAWHDESH 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 149039248  287 LNKYLLYHKPTKVLSPEYMWDQQlLGWPSIMKKLRYVAVPKNHQAIRN 334
Cdd:pfam03414 243 LNKYFLSHKPTKVLSPEYLWDYQ-IGRPSDLRLVRFAWVPKNYNWVRN 289
Glyco_transf_6 cd02515
Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO ...
62-333 4.98e-161

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: 450.63  E-value: 4.98e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  62 RTDVLVLTPWLAPIIWEGTFNIDILNEQFRLRNTTIGLTVFAIKKYVVFLKLFLETAEQHFMVGHKVIYYVFTDRPADVP 141
Cdd:cd02515    1 RPDVLTVTPWLAPIVWEGTFNPDVLDEYYRKQNITIGLTVFAVGKYTEFLERFLESAEKHFMVGYRVIYYIFTDKPAAVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248 142 QVPLGAGRRLVVLTVRNYTRWQDVSMHRMEVISHFSEQRFRHEVDYLVCADVDMKFRDHVGVEILSALFGTLHPGFYRSR 221
Cdd:cd02515   81 EVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYLFCMDVDMVFQGPFGVETLGDSVAQLHPWWYGKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248 222 RESFTYERRPQSQAYIPWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESHLNKYLLYHKPTKVLS 301
Cdd:cd02515  161 RKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEGILADKANGIEARWHDESHLNKYFLLHKPTKVLS 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 149039248 302 PEYMWDQQlLGWPSIMKKLRYVAVPKNHQAIR 333
Cdd:cd02515  241 PEYLWDDR-IGQAAEIRLPRLSWLPKNYQEVR 271
Gltr_6 NF041524
family 6 glucosyltransferase;
96-314 1.46e-46

family 6 glucosyltransferase;


Pssm-ID: 469409  Cd Length: 226  Bit Score: 157.40  E-value: 1.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  96 TIGLTVFAIKKYVVFLKLFLETAEQHFMVGHKVIYYVFTDRPAD----------VPQVPLGagrrlvvltvrnytrWQDV 165
Cdd:NF041524   2 KIGILYICTGKYSIFWKDFYLSCEKYFLPGAEKEYFVFTDPDDLyfkknnnvhvIYQENLG---------------WPLN 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248 166 SMHRMEVIShfseqRFRHEV---DYLVCADVDMKFRDHVGVEIL-----SALFGTLHPGFYRSRRESFTYERRPQSQAYI 237
Cdd:NF041524  67 TLLRFSMFL-----KIKEELkefDYLFFFNANALFVKPISAEILpteeeNGLVGVIHPGYYNKPPIEYPYERRKKSTAYI 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149039248 238 PWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESHLNKYLLYHKPtKVLSPEYMWDQqllGWP 314
Cdd:NF041524 142 PYGKGGYYFQGGLNGGKTKAYLKLIETCSLNIEKDLKNNIIAIWHDESHLNKYFLDKKP-KILSPAYGYPE---GWN 214
 
Name Accession Description Interval E-value
Glyco_transf_6 pfam03414
Glycosyltransferase family 6;
47-334 4.84e-176

Glycosyltransferase family 6;


Pssm-ID: 427285  Cd Length: 289  Bit Score: 489.27  E-value: 4.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248   47 VNRKAYPQPRVLTPTRTDVLVLTPWLAPIIWEGTFNIDILNEQFRLRNTTIGLTVFAIKKYVVFLKLFLETAEQHFMVGH 126
Cdd:pfam03414   3 LPRWFYPKPKLLEPKRPDVLTVTPWLAPIVWEGTFDPAILEDYYRPQNLTIGLTVFAVGKYVRFLELFLESAEKYFMVGH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  127 KVIYYVFTDRPADVPQVPLGAGRRLVVLTVRNYTRWQDVSMHRMEVISHFSEQRFRHEVDYLVCADVDMKFRDHVGVEIL 206
Cdd:pfam03414  83 RVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLFCVDVDMVFRDHFGVETL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  207 SALFGTLHPGFYRSRRESFTYERRPQSQAYIPWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESH 286
Cdd:pfam03414 163 GPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAILADKANGIEAAWHDESH 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 149039248  287 LNKYLLYHKPTKVLSPEYMWDQQlLGWPSIMKKLRYVAVPKNHQAIRN 334
Cdd:pfam03414 243 LNKYFLSHKPTKVLSPEYLWDYQ-IGRPSDLRLVRFAWVPKNYNWVRN 289
Glyco_transf_6 cd02515
Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO ...
62-333 4.98e-161

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: 450.63  E-value: 4.98e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  62 RTDVLVLTPWLAPIIWEGTFNIDILNEQFRLRNTTIGLTVFAIKKYVVFLKLFLETAEQHFMVGHKVIYYVFTDRPADVP 141
Cdd:cd02515    1 RPDVLTVTPWLAPIVWEGTFNPDVLDEYYRKQNITIGLTVFAVGKYTEFLERFLESAEKHFMVGYRVIYYIFTDKPAAVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248 142 QVPLGAGRRLVVLTVRNYTRWQDVSMHRMEVISHFSEQRFRHEVDYLVCADVDMKFRDHVGVEILSALFGTLHPGFYRSR 221
Cdd:cd02515   81 EVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYLFCMDVDMVFQGPFGVETLGDSVAQLHPWWYGKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248 222 RESFTYERRPQSQAYIPWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESHLNKYLLYHKPTKVLS 301
Cdd:cd02515  161 RKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEGILADKANGIEARWHDESHLNKYFLLHKPTKVLS 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 149039248 302 PEYMWDQQlLGWPSIMKKLRYVAVPKNHQAIR 333
Cdd:cd02515  241 PEYLWDDR-IGQAAEIRLPRLSWLPKNYQEVR 271
Gltr_6 NF041524
family 6 glucosyltransferase;
96-314 1.46e-46

family 6 glucosyltransferase;


Pssm-ID: 469409  Cd Length: 226  Bit Score: 157.40  E-value: 1.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248  96 TIGLTVFAIKKYVVFLKLFLETAEQHFMVGHKVIYYVFTDRPAD----------VPQVPLGagrrlvvltvrnytrWQDV 165
Cdd:NF041524   2 KIGILYICTGKYSIFWKDFYLSCEKYFLPGAEKEYFVFTDPDDLyfkknnnvhvIYQENLG---------------WPLN 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149039248 166 SMHRMEVIShfseqRFRHEV---DYLVCADVDMKFRDHVGVEIL-----SALFGTLHPGFYRSRRESFTYERRPQSQAYI 237
Cdd:NF041524  67 TLLRFSMFL-----KIKEELkefDYLFFFNANALFVKPISAEILpteeeNGLVGVIHPGYYNKPPIEYPYERRKKSTAYI 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149039248 238 PWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESHLNKYLLYHKPtKVLSPEYMWDQqllGWP 314
Cdd:NF041524 142 PYGKGGYYFQGGLNGGKTKAYLKLIETCSLNIEKDLKNNIIAIWHDESHLNKYFLDKKP-KILSPAYGYPE---GWN 214
 
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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