NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907118890|ref|XP_036015930|]
View 

beta-1,4-galactosyltransferase 4 isoform X2 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 122-298 5.29e-89

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 cd00899:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 219  Bit Score: 264.44  E-value: 5.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890 122 QRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQTGSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPEN 201
Cdd:cd00899     2 HKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPEN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890 202 DFNLYTCGDQPKHLVVGRNSTGY-----------------------------------------RVELHKMKISRPKPDV 240
Cdd:cd00899    82 DRNLYGCEEGPRHLSVPLDKFHYklpyktyfggvlaltreqfrkvngfsnaywgwggedddlynRIKAAGLKITRPSGDT 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907118890 241 GKYTMIFHTRDKGNEVNMGRMKLLQQMSRVWKTDGLSSCSYRLLSVEHNPLYANITVD 298
Cdd:cd00899   162 GRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 122-298 5.29e-89

Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen.


Pssm-ID: 132999 [Multi-domain]  Cd Length: 219  Bit Score: 264.44  E-value: 5.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890 122 QRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQTGSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPEN 201
Cdd:cd00899     2 HKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPEN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890 202 DFNLYTCGDQPKHLVVGRNSTGY-----------------------------------------RVELHKMKISRPKPDV 240
Cdd:cd00899    82 DRNLYGCEEGPRHLSVPLDKFHYklpyktyfggvlaltreqfrkvngfsnaywgwggedddlynRIKAAGLKITRPSGDT 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907118890 241 GKYTMIFHTRDKGNEVNMGRMKLLQQMSRVWKTDGLSSCSYRLLSVEHNPLYANITVD 298
Cdd:cd00899   162 GRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 85-208 3.47e-83

N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 463972  Cd Length: 125  Bit Score: 246.22  E-value: 3.47e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890  85 RGQSKLVFKPDLTLEEIEAENPKV-SRGRYHPEECKALQRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQT 163
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVqPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907118890 164 GSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPENDFNLYTC 208
Cdd:pfam13733  81 GNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 122-298 5.29e-89

Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen.


Pssm-ID: 132999 [Multi-domain]  Cd Length: 219  Bit Score: 264.44  E-value: 5.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890 122 QRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQTGSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPEN 201
Cdd:cd00899     2 HKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPEN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890 202 DFNLYTCGDQPKHLVVGRNSTGY-----------------------------------------RVELHKMKISRPKPDV 240
Cdd:cd00899    82 DRNLYGCEEGPRHLSVPLDKFHYklpyktyfggvlaltreqfrkvngfsnaywgwggedddlynRIKAAGLKITRPSGDT 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907118890 241 GKYTMIFHTRDKGNEVNMGRMKLLQQMSRVWKTDGLSSCSYRLLSVEHNPLYANITVD 298
Cdd:cd00899   162 GRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 85-208 3.47e-83

N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 463972  Cd Length: 125  Bit Score: 246.22  E-value: 3.47e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907118890  85 RGQSKLVFKPDLTLEEIEAENPKV-SRGRYHPEECKALQRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQT 163
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVqPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907118890 164 GSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPENDFNLYTC 208
Cdd:pfam13733  81 GNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 225-248 5.67e-04

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 37.98  E-value: 5.67e-04
                          10        20
                  ....*....|....*....|....
gi 1907118890 225 RVELHKMKISRPKPDVGKYTMIFH 248
Cdd:pfam02709  54 RLLLAGLEIERPPGDIGRYYMLYH 77
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH