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Conserved domains on  [gi|1034656331|ref|XP_016867937|]
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glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 isoform X1 [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 229488)

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
Galactosyl_T super family cl21608
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 107-221 1.91e-09

Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2.


The actual alignment was detected with superfamily member pfam02434:

Pssm-ID: 473923  Cd Length: 248  Bit Score: 57.71  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656331 107 VKATWAQRCNKVLFMSSeenkDFPAVGLKTKEG-------------RDQLYWKTIKAFqyvhEHYLE-DADWFLKADDDT 172
Cdd:pfam02434  24 LLKTWISRAKHQTYIFT----DGEDEGLPTRTGghlintncsaghcRKALSCKMAVEY----DRFLEsGKKWFCHVDDDN 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034656331 173 YVILDNLRWLLSKYDPEEPIYFGRR-----FKPYVKQG--------YMSGGAGYVLSKE-ALK 221
Cdd:pfam02434  96 YVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGlALK 158
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 107-221 1.91e-09

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 57.71  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656331 107 VKATWAQRCNKVLFMSSeenkDFPAVGLKTKEG-------------RDQLYWKTIKAFqyvhEHYLE-DADWFLKADDDT 172
Cdd:pfam02434  24 LLKTWISRAKHQTYIFT----DGEDEGLPTRTGghlintncsaghcRKALSCKMAVEY----DRFLEsGKKWFCHVDDDN 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034656331 173 YVILDNLRWLLSKYDPEEPIYFGRR-----FKPYVKQG--------YMSGGAGYVLSKE-ALK 221
Cdd:pfam02434  96 YVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGlALK 158
PLN03153 PLN03153
hypothetical protein; Provisional
 159-225 3.95e-07

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 51.84  E-value: 3.95e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034656331 159 LEDADWFLKADDDTYVILDNLRWLLSKYDPEEPIYFGRRFKPYVKQGYMS-----GGAGYVLS---KEALKRFVD 225
Cdd:PLN03153  208 LPDVRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGIAISyplAEALSRILD 282
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 107-221 1.91e-09

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 57.71  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656331 107 VKATWAQRCNKVLFMSSeenkDFPAVGLKTKEG-------------RDQLYWKTIKAFqyvhEHYLE-DADWFLKADDDT 172
Cdd:pfam02434  24 LLKTWISRAKHQTYIFT----DGEDEGLPTRTGghlintncsaghcRKALSCKMAVEY----DRFLEsGKKWFCHVDDDN 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034656331 173 YVILDNLRWLLSKYDPEEPIYFGRR-----FKPYVKQG--------YMSGGAGYVLSKE-ALK 221
Cdd:pfam02434  96 YVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGlALK 158
PLN03153 PLN03153
hypothetical protein; Provisional
 159-225 3.95e-07

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 51.84  E-value: 3.95e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034656331 159 LEDADWFLKADDDTYVILDNLRWLLSKYDPEEPIYFGRRFKPYVKQGYMS-----GGAGYVLS---KEALKRFVD 225
Cdd:PLN03153  208 LPDVRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGIAISyplAEALSRILD 282
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 117-252 5.62e-05

Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 43.47  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656331 117 KVLFMSSEENK---DFpaVGLKTKEGRDQLYWKTIKAFQYVHEhYLEDADWFLKADDDTYVILDNLRWLLSKYD------ 187
Cdd:pfam01762  36 KVADLVMEEAKlygDI--VVVDFEDTYENLTFKTLTGLLWAVS-KCPSAKYIGKIDDDVYFFPDKLLSLLDNGNidpses 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656331 188 -------PEEPIYFGRRFKPYVKQGYMS--------GGAGYVLSKEALKRFvdaFKTDKCTHSSSIEDLALGRCMEIMNV 252
Cdd:pfam01762 113 sfygyvmEEGPVIRNKKSKWYVSPSDYKcsryppyaSGPFYVLSRDAAEKL---LKASKHRRFLQIEDVYVGILANDLGI 189
 
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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