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Conserved domains on  [gi|81868592|sp|Q9JJ06|]
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RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1; AltName: Full=Core 1 O-glycan T-synthase; Short=T-syn; AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1; AltName: Full=Core 1 beta1,3-galactosyltransferase 1; Short=C1GalT1; Short=Core 1 beta3-Gal-T1

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: ...
 107-248 1.37e-13

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: 69.65  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81868592   107 VKATWAQRCNKVLFMSSeenqDFPTVGLKTKEG-------------REQLYWKTIKAFqyvhDHYLE-DADWFMKADDDT 172
Cdd:pfam02434  24 LLKTWISRAKHQTYIFT----DGEDEGLPTRTGghlintncsaghcRKALSCKMAVEY----DRFLEsGKKWFCHVDDDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81868592   173 YVIVDNLRWLLSKYNPEQPIYFGRR-----FKPYVKQG--------YMSGGAGYVLSKEALRRFVNAFKTEKCTHSSSI- 238
Cdd:pfam02434  96 YVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGGRFMSTSEKi 175

                         170
                  ....*....|...
gi 81868592   239 ---EDLALGRCME 248
Cdd:pfam02434 176 rlpDDCTLGYIIE 188
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 107-248 1.37e-13

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: 69.65  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81868592   107 VKATWAQRCNKVLFMSSeenqDFPTVGLKTKEG-------------REQLYWKTIKAFqyvhDHYLE-DADWFMKADDDT 172
Cdd:pfam02434  24 LLKTWISRAKHQTYIFT----DGEDEGLPTRTGghlintncsaghcRKALSCKMAVEY----DRFLEsGKKWFCHVDDDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81868592   173 YVIVDNLRWLLSKYNPEQPIYFGRR-----FKPYVKQG--------YMSGGAGYVLSKEALRRFVNAFKTEKCTHSSSI- 238
Cdd:pfam02434  96 YVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGGRFMSTSEKi 175

                         170
                  ....*....|...
gi 81868592   239 ---EDLALGRCME 248
Cdd:pfam02434 176 rlpDDCTLGYIIE 188
PLN03153 PLN03153
hypothetical protein; Provisional
 159-222 2.53e-05

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 46.06  E-value: 2.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81868592  159 LEDADWFMKADDDTYVIVDNLRWLLSKYNPEQPIYFGRRFKPYVKQGYMS-----GGAGYVLS---KEALRR 222
Cdd:PLN03153 208 LPDVRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGIAISyplAEALSR 279
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 107-248 1.37e-13

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: 69.65  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81868592   107 VKATWAQRCNKVLFMSSeenqDFPTVGLKTKEG-------------REQLYWKTIKAFqyvhDHYLE-DADWFMKADDDT 172
Cdd:pfam02434  24 LLKTWISRAKHQTYIFT----DGEDEGLPTRTGghlintncsaghcRKALSCKMAVEY----DRFLEsGKKWFCHVDDDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81868592   173 YVIVDNLRWLLSKYNPEQPIYFGRR-----FKPYVKQG--------YMSGGAGYVLSKEALRRFVNAFKTEKCTHSSSI- 238
Cdd:pfam02434  96 YVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGGRFMSTSEKi 175

                         170
                  ....*....|...
gi 81868592   239 ---EDLALGRCME 248
Cdd:pfam02434 176 rlpDDCTLGYIIE 188
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 136-248 2.29e-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: 44.62  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81868592   136 TKEGREQLYWKTIKAFQYVHDhYLEDADWFMKADDDTYVIVDNLRWLLSKYN-------------PEQPIYFGRRFKPYV 202
Cdd:pfam01762  56 FEDTYENLTFKTLTGLLWAVS-KCPSAKYIGKIDDDVYFFPDKLLSLLDNGNidpsessfygyvmEEGPVIRNKKSKWYV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 81868592   203 KQGYMS--------GGAGYVLSKEALRRFVNAFKTEKCTHsssIEDLALGRCME 248
Cdd:pfam01762 135 SPSDYKcsryppyaSGPFYVLSRDAAEKLLKASKHRRFLQ---IEDVYVGILAN 185
PLN03153 PLN03153
hypothetical protein; Provisional
 159-222 2.53e-05

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 46.06  E-value: 2.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81868592  159 LEDADWFMKADDDTYVIVDNLRWLLSKYNPEQPIYFGRRFKPYVKQGYMS-----GGAGYVLS---KEALRR 222
Cdd:PLN03153 208 LPDVRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGIAISyplAEALSR 279
 
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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