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Conserved domains on  [gi|2080470226|ref|XP_042832201|]
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beta-1,4-galactosyltransferase 3 isoform X1 [Panthera tigris]

Protein Classification

beta-1,4-galactosyltransferase( domain architecture ID 10097028)

beta-1,4-galactosyltransferase is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids

CAZY:  GT7
EC:  2.4.1.-
Gene Ontology:  GO:0016758
PubMed:  15465321
SCOP:  4000687

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 125-344 9.01e-125

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: 359.20  E-value: 9.01e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 125 RSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPE 204
Cdd:cd00899     1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 205 NDHNLYVCdPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPT 284
Cdd:cd00899    81 NDRNLYGC-EEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 285 SVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITAD 344
Cdd:cd00899   160 DTGRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 125-344 9.01e-125

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: 359.20  E-value: 9.01e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 125 RSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPE 204
Cdd:cd00899     1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 205 NDHNLYVCdPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPT 284
Cdd:cd00899    81 NDRNLYGC-EEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 285 SVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITAD 344
Cdd:cd00899   160 DTGRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 88-212 9.35e-72

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: 220.41  E-value: 9.35e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226  88 VGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQA 167
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVQPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2080470226 168 GNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVC 212
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 ...
 125-344 9.01e-125

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: 359.20  E-value: 9.01e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 125 RSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPE 204
Cdd:cd00899     1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 205 NDHNLYVCdPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPT 284
Cdd:cd00899    81 NDRNLYGC-EEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 285 SVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITAD 344
Cdd:cd00899   160 DTGRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 88-212 9.35e-72

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: 220.41  E-value: 9.35e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226  88 VGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQA 167
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVQPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2080470226 168 GNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVC 212
Cdd:pfam13733  81 GNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 218-295 2.14e-35

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: 124.65  E-value: 2.14e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080470226 218 RHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHR 295
Cdd:pfam02709   1 RHLSVALDKFGYKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGDIGRYYMLYHK 78
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 163-278 1.47e-03

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 39.10  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080470226 163 VIH--QAGNGtFNRAKLLNVGVREAlrdeEWDCLFLHDVDLLPEND----H------NLYVcdpRGPRhVAVAMNKfgys 230
Cdd:cd06420    55 IKHvwQEDEG-FRKAKIRNKAIAAA----KGDYLIFIDGDCIPHPDfiadHielaepGVFL---SGSR-VLLNEKL---- 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2080470226 231 lpYPQYF-GGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMK 278
Cdd:cd06420   122 --TERGIrGCNMSFWKKDLLAVNGFDEEFTGWGGEDSELVARLLNSGIK 168
 
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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