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Conserved domains on  [gi|21751080|dbj|BAC03899|]
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unnamed protein product [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 ...
 82-177 7.72e-10

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 cd04194:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 248  Bit Score: 56.07  E-value: 7.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751080  82 FNSGVMLLNLEAMRQSPLYSRLLEpaqvqqLADKYHFRGHLGDQDFFTMIgMEHPKLFhvLDCTWNRQLCTWWRDHGYSD 161
Cdd:cd04194 152 FNSGVLLINLKKWREENITEKLLE------LIKEYGGRLIYPDQDILNAV-LKDKILY--LPPRYNFQTGFYYLLKKKSK 222

                        90
                ....*....|....*.
gi 21751080 162 VFEAYFRCEGHVKIYH 177
Cdd:cd04194 223 EEQELEEARKNPVIIH 238
 
Name Accession Description Interval E-value
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
 82-177 7.72e-10

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 56.07  E-value: 7.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751080  82 FNSGVMLLNLEAMRQSPLYSRLLEpaqvqqLADKYHFRGHLGDQDFFTMIgMEHPKLFhvLDCTWNRQLCTWWRDHGYSD 161
Cdd:cd04194 152 FNSGVLLINLKKWREENITEKLLE------LIKEYGGRLIYPDQDILNAV-LKDKILY--LPPRYNFQTGFYYLLKKKSK 222

                        90
                ....*....|....*.
gi 21751080 162 VFEAYFRCEGHVKIYH 177
Cdd:cd04194 223 EEQELEEARKNPVIIH 238
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
 82-177 2.87e-08

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 52.28  E-value: 2.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751080  82 FNSGVMLLNLEAMRQSPLYSRLLEpaqvqqLADKYHFRGHLGDQDFFTMIGMEHpklFHVLDCTWNRQlCTWWRDHGYSD 161
Cdd:COG1442 158 FNSGVLLINLKKWREENITEKALE------FLKENPDKLKYPDQDILNIVLGGK---VKFLPPRYNYQ-YSLYYELKDKS 227

                        90
                ....*....|....*.
gi 21751080 162 VFEAYFRCEGHVKIYH 177
Cdd:COG1442 228 NKKELLEARKNPVIIH 243
 
Name Accession Description Interval E-value
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
 82-177 7.72e-10

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 56.07  E-value: 7.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751080  82 FNSGVMLLNLEAMRQSPLYSRLLEpaqvqqLADKYHFRGHLGDQDFFTMIgMEHPKLFhvLDCTWNRQLCTWWRDHGYSD 161
Cdd:cd04194 152 FNSGVLLINLKKWREENITEKLLE------LIKEYGGRLIYPDQDILNAV-LKDKILY--LPPRYNFQTGFYYLLKKKSK 222

                        90
                ....*....|....*.
gi 21751080 162 VFEAYFRCEGHVKIYH 177
Cdd:cd04194 223 EEQELEEARKNPVIIH 238
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
 82-177 2.87e-08

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 52.28  E-value: 2.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751080  82 FNSGVMLLNLEAMRQSPLYSRLLEpaqvqqLADKYHFRGHLGDQDFFTMIGMEHpklFHVLDCTWNRQlCTWWRDHGYSD 161
Cdd:COG1442 158 FNSGVLLINLKKWREENITEKALE------FLKENPDKLKYPDQDILNIVLGGK---VKFLPPRYNYQ-YSLYYELKDKS 227

                        90
                ....*....|....*.
gi 21751080 162 VFEAYFRCEGHVKIYH 177
Cdd:COG1442 228 NKKELLEARKNPVIIH 243
GT8_like_2 cd06430
GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of ...
 83-179 1.35e-05

GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.


Pssm-ID: 133052  Cd Length: 304  Bit Score: 44.38  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751080  83 NSGVMLLNLEAMRQSPLYSRLLEPA-----QVQQLADKYHFRGHLGDQDFFTMIGMEHPKLFHVLDCTWNrqlctwWR-D 156
Cdd:cd06430 158 NSGVMLMNLTRMRRKYFKNDMTPVGlrweeILMPLYKKYKLKITWGDQDLINIIFHHNPEMLYVFPCHWN------YRpD 231

                        90       100
                ....*....|....*....|....
gi 21751080 157 HG-YSDVFEAyfRCEGHVKIYHGN 179
Cdd:cd06430 232 HCmYGSNCKA--AEEEGVFILHGN 253
GT8_LARGE_C cd06431
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ...
 82-150 1.45e-05

LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis.


Pssm-ID: 133053  Cd Length: 280  Bit Score: 44.00  E-value: 1.45e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21751080  82 FNSGVMLLNLEAMRQsplysrlLEPAQVQQL-ADKY---HFRGHLGDQDFFTMIGMEHPKLFHVLDCTWNRQL 150
Cdd:cd06431 158 FNTGVILLDLDKLRK-------MKWESMWRLtAERElmsMLSTSLADQDIFNAVIKQNPFLVYQLPCAWNVQL 223
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
 82-182 1.20e-03

Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.


Pssm-ID: 132996 [Multi-domain]  Cd Length: 246  Bit Score: 38.19  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751080  82 FNSGVMLLNLEAMRQSPLYSRLLEPAQVQQLAdkyhfrGHLGDQDFFTMIGMEHPKLFHVLDCTWNrqlctwWRDHGYSD 161
Cdd:cd00505 153 FNSGVFVVNLSKERRNQLLKVALEKWLQSLSS------LSGGDQDLLNTFFKQVPFIVKSLPCIWN------VRLTGCYR 220

                        90       100
                ....*....|....*....|.
gi 21751080 162 VFEAYFRCEGHVKIYHGNCNT 182
Cdd:cd00505 221 SLNCFKAFVKNAKVIHFNGPT 241
 
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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