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Conserved domains on  [gi|2168836640|ref|XP_045419471|]
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inactive N-acetyllactosaminide alpha-1,3-galactosyltransferase isoform X6 [Lemur catta]

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 ...
91-373 2.85e-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: 491.59  E-value: 2.85e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640  91 QLWDWFNPK------KRPEVVTVTSWKAPVVWEGTYNKAILENYYAKQKITVGLTVFAVGRYIeHYLEEFITSANRYFMV 164
Cdd:pfam03414   2 QLPRWFYPKpkllepKRPDVLTVTPWLAPIVWEGTFDPAILEDYYRPQNLTIGLTVFAVGKYV-RFLELFLESAEKYFMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 165 GHKVIFYIMLDDISKMPLIELGPLRSFKVFEIKPEKRWQDISMMRMKTIGEHILAHIQHEVDFLFCMDVDQVFQDNFGVE 244
Cdd:pfam03414  81 GHRVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLFCVDVDMVFRDHFGVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 245 TLGQSVAQLQAWWYKADPDEFTYERRKESAAYIPFGEGDFYYHAAIFGGTPIQVLNITRECFKGILQDKKNDIEAEWHDE 324
Cdd:pfam03414 161 TLGPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAILADKANGIEAAWHDE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2168836640 325 SHLNKYFLLNKPSKILSPEYCWDFHIGLPSDIKIVKISWQTKQYNLVRN 373
Cdd:pfam03414 241 SHLNKYFLSHKPTKVLSPEYLWDYQIGRPSDLRLVRFAWVPKNYNWVRN 289
 
Name Accession Description Interval E-value
Glyco_transf_6 pfam03414
Glycosyltransferase family 6;
91-373 2.85e-176

Glycosyltransferase family 6;


Pssm-ID: 427285  Cd Length: 289  Bit Score: 491.59  E-value: 2.85e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640  91 QLWDWFNPK------KRPEVVTVTSWKAPVVWEGTYNKAILENYYAKQKITVGLTVFAVGRYIeHYLEEFITSANRYFMV 164
Cdd:pfam03414   2 QLPRWFYPKpkllepKRPDVLTVTPWLAPIVWEGTFDPAILEDYYRPQNLTIGLTVFAVGKYV-RFLELFLESAEKYFMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 165 GHKVIFYIMLDDISKMPLIELGPLRSFKVFEIKPEKRWQDISMMRMKTIGEHILAHIQHEVDFLFCMDVDQVFQDNFGVE 244
Cdd:pfam03414  81 GHRVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLFCVDVDMVFRDHFGVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 245 TLGQSVAQLQAWWYKADPDEFTYERRKESAAYIPFGEGDFYYHAAIFGGTPIQVLNITRECFKGILQDKKNDIEAEWHDE 324
Cdd:pfam03414 161 TLGPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAILADKANGIEAAWHDE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2168836640 325 SHLNKYFLLNKPSKILSPEYCWDFHIGLPSDIKIVKISWQTKQYNLVRN 373
Cdd:pfam03414 241 SHLNKYFLSHKPTKVLSPEYLWDYQIGRPSDLRLVRFAWVPKNYNWVRN 289
Glyco_transf_6 cd02515
Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO ...
101-372 2.71e-169

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: 472.97  E-value: 2.71e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 101 RPEVVTVTSWKAPVVWEGTYNKAILENYYAKQKITVGLTVFAVGRYIEhYLEEFITSANRYFMVGHKVIFYIMLDDISKM 180
Cdd:cd02515     1 RPDVLTVTPWLAPIVWEGTFNPDVLDEYYRKQNITIGLTVFAVGKYTE-FLERFLESAEKHFMVGYRVIYYIFTDKPAAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 181 PLIELGPLRSFKVFEIKPEKRWQDISMMRMKTIGEHILAHIQHEVDFLFCMDVDQVFQDNFGVETLGQSVAQLQAWWYKA 260
Cdd:cd02515    80 PEVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYLFCMDVDMVFQGPFGVETLGDSVAQLHPWWYGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 261 DPDEFTYERRKESAAYIPFGEGDFYYHAAIFGGTPIQVLNITRECFKGILQDKKNDIEAEWHDESHLNKYFLLNKPSKIL 340
Cdd:cd02515   160 PRKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEGILADKANGIEARWHDESHLNKYFLLHKPTKVL 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2168836640 341 SPEYCWDFHIGLPSDIKIVKISWQTKQYNLVR 372
Cdd:cd02515   240 SPEYLWDDRIGQAAEIRLPRLSWLPKNYQEVR 271
Gltr_6 NF041524
family 6 glucosyltransferase;
144-358 4.94e-36

family 6 glucosyltransferase;


Pssm-ID: 469409  Cd Length: 226  Bit Score: 130.82  E-value: 4.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 144 GRYIEhYLEEFITSANRYFMVGHKVIFYIMLDDISkmplieLGPLRSFKVFEIKPEKR-WQDISMMRMktigeHILAHIQ 222
Cdd:NF041524   11 GKYSI-FWKDFYLSCEKYFLPGAEKEYFVFTDPDD------LYFKKNNNVHVIYQENLgWPLNTLLRF-----SMFLKIK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 223 HEV---DFLFCMDVDQVFQDNFGVETLGQS-----VAQLQAWWYKADPDEFTYERRKESAAYIPFGEGDFYYHAAIFGGT 294
Cdd:NF041524   79 EELkefDYLFFFNANALFVKPISAEILPTEeenglVGVIHPGYYNKPPIEYPYERRKKSTAYIPYGKGGYYFQGGLNGGK 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168836640 295 PIQVLNITRECFKGILQDKKNDIEAEWHDESHLNKYFLLNKPsKILSPEYCWDFHIGLPSDIKI 358
Cdd:NF041524  159 TKAYLKLIETCSLNIEKDLKNNIIAIWHDESHLNKYFLDKKP-KILSPAYGYPEGWNLPFEPKI 221
 
Name Accession Description Interval E-value
Glyco_transf_6 pfam03414
Glycosyltransferase family 6;
91-373 2.85e-176

Glycosyltransferase family 6;


Pssm-ID: 427285  Cd Length: 289  Bit Score: 491.59  E-value: 2.85e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640  91 QLWDWFNPK------KRPEVVTVTSWKAPVVWEGTYNKAILENYYAKQKITVGLTVFAVGRYIeHYLEEFITSANRYFMV 164
Cdd:pfam03414   2 QLPRWFYPKpkllepKRPDVLTVTPWLAPIVWEGTFDPAILEDYYRPQNLTIGLTVFAVGKYV-RFLELFLESAEKYFMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 165 GHKVIFYIMLDDISKMPLIELGPLRSFKVFEIKPEKRWQDISMMRMKTIGEHILAHIQHEVDFLFCMDVDQVFQDNFGVE 244
Cdd:pfam03414  81 GHRVIYYVFTDDPAAVPRVPLGPGRQLSVFEIGRYKRWQDISMRRMETISEHIAQRIQHEVDYLFCVDVDMVFRDHFGVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 245 TLGQSVAQLQAWWYKADPDEFTYERRKESAAYIPFGEGDFYYHAAIFGGTPIQVLNITRECFKGILQDKKNDIEAEWHDE 324
Cdd:pfam03414 161 TLGPLVAQLHPWWYAADRQKFTYERRPLSAAYIPFGEGDFYYHGAIFGGTVARVYNLTRACHKAILADKANGIEAAWHDE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2168836640 325 SHLNKYFLLNKPSKILSPEYCWDFHIGLPSDIKIVKISWQTKQYNLVRN 373
Cdd:pfam03414 241 SHLNKYFLSHKPTKVLSPEYLWDYQIGRPSDLRLVRFAWVPKNYNWVRN 289
Glyco_transf_6 cd02515
Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO ...
101-372 2.71e-169

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: 472.97  E-value: 2.71e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 101 RPEVVTVTSWKAPVVWEGTYNKAILENYYAKQKITVGLTVFAVGRYIEhYLEEFITSANRYFMVGHKVIFYIMLDDISKM 180
Cdd:cd02515     1 RPDVLTVTPWLAPIVWEGTFNPDVLDEYYRKQNITIGLTVFAVGKYTE-FLERFLESAEKHFMVGYRVIYYIFTDKPAAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 181 PLIELGPLRSFKVFEIKPEKRWQDISMMRMKTIGEHILAHIQHEVDFLFCMDVDQVFQDNFGVETLGQSVAQLQAWWYKA 260
Cdd:cd02515    80 PEVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYLFCMDVDMVFQGPFGVETLGDSVAQLHPWWYGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 261 DPDEFTYERRKESAAYIPFGEGDFYYHAAIFGGTPIQVLNITRECFKGILQDKKNDIEAEWHDESHLNKYFLLNKPSKIL 340
Cdd:cd02515   160 PRKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEGILADKANGIEARWHDESHLNKYFLLHKPTKVL 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2168836640 341 SPEYCWDFHIGLPSDIKIVKISWQTKQYNLVR 372
Cdd:cd02515   240 SPEYLWDDRIGQAAEIRLPRLSWLPKNYQEVR 271
Gltr_6 NF041524
family 6 glucosyltransferase;
144-358 4.94e-36

family 6 glucosyltransferase;


Pssm-ID: 469409  Cd Length: 226  Bit Score: 130.82  E-value: 4.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 144 GRYIEhYLEEFITSANRYFMVGHKVIFYIMLDDISkmplieLGPLRSFKVFEIKPEKR-WQDISMMRMktigeHILAHIQ 222
Cdd:NF041524   11 GKYSI-FWKDFYLSCEKYFLPGAEKEYFVFTDPDD------LYFKKNNNVHVIYQENLgWPLNTLLRF-----SMFLKIK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168836640 223 HEV---DFLFCMDVDQVFQDNFGVETLGQS-----VAQLQAWWYKADPDEFTYERRKESAAYIPFGEGDFYYHAAIFGGT 294
Cdd:NF041524   79 EELkefDYLFFFNANALFVKPISAEILPTEeenglVGVIHPGYYNKPPIEYPYERRKKSTAYIPYGKGGYYFQGGLNGGK 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168836640 295 PIQVLNITRECFKGILQDKKNDIEAEWHDESHLNKYFLLNKPsKILSPEYCWDFHIGLPSDIKI 358
Cdd:NF041524  159 TKAYLKLIETCSLNIEKDLKNNIIAIWHDESHLNKYFLDKKP-KILSPAYGYPEGWNLPFEPKI 221
 
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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