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Conserved domains on  [gi|116517242|ref|NP_001070842|]
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glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1-A [Danio rerio]

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: ...
 169-292 1.10e-08

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: 55.40  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517242  169 WFLKADDDTFVVVDNLRWILSNYTPEQPIYFGKR-----FKPYTKQG--------YMSGGAGYVLSKEALRRFVEGFSTK 235
Cdd:pfam02434  87 WFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGG 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116517242  236 VCTHTTPV----EDLAMGQCLE-KMGVLAGDSrDSLH--RETFHPFIPE---HHLTGKFSKTFWYWN 292
Cdd:pfam02434 167 RFMSTSEKirlpDDCTLGYIIEnLLGVPLTHS-PLFHshLENLQDLPPEtlhEQVTLSYGKFWNKRN 232
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 169-292 1.10e-08

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: 55.40  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517242  169 WFLKADDDTFVVVDNLRWILSNYTPEQPIYFGKR-----FKPYTKQG--------YMSGGAGYVLSKEALRRFVEGFSTK 235
Cdd:pfam02434  87 WFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGG 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116517242  236 VCTHTTPV----EDLAMGQCLE-KMGVLAGDSrDSLH--RETFHPFIPE---HHLTGKFSKTFWYWN 292
Cdd:pfam02434 167 RFMSTSEKirlpDDCTLGYIIEnLLGVPLTHS-PLFHshLENLQDLPPEtlhEQVTLSYGKFWNKRN 232
PLN03153 PLN03153
hypothetical protein; Provisional
 169-280 2.24e-04

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 43.37  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517242 169 WFLKADDDTFVVVDNLRWILSNYTPEQPIYFGKRFKPYTKQGYMS-----GGAGYVLS---KEALRRFVEGFSTKVctHT 240
Cdd:PLN03153 213 WFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGIAISyplAEALSRILDDCLDRY--PK 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116517242 241 TPVEDLAMGQCLEKMGV------------LAGDSRDSLHRETFHPFIPEHHL 280
Cdd:PLN03153 291 LYGSDDRLHACITELGVplsrepgfhqwdIRGNAHGLLSSHPIAPFVSIHHV 342
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 169-292 1.10e-08

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: 55.40  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517242  169 WFLKADDDTFVVVDNLRWILSNYTPEQPIYFGKR-----FKPYTKQG--------YMSGGAGYVLSKEALRRFVEGFSTK 235
Cdd:pfam02434  87 WFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGG 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116517242  236 VCTHTTPV----EDLAMGQCLE-KMGVLAGDSrDSLH--RETFHPFIPE---HHLTGKFSKTFWYWN 292
Cdd:pfam02434 167 RFMSTSEKirlpDDCTLGYIIEnLLGVPLTHS-PLFHshLENLQDLPPEtlhEQVTLSYGKFWNKRN 232
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 143-257 3.36e-06

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: 47.32  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517242  143 EGRDQLYWKTIRAFHYALKnHGHEADWFLKADDDTFVVVDNLRWILSNYT-------------PEQPIYFGKRFKPYTKQ 209
Cdd:pfam01762  58 DTYENLTFKTLTGLLWAVS-KCPSAKYIGKIDDDVYFFPDKLLSLLDNGNidpsessfygyvmEEGPVIRNKKSKWYVSP 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116517242  210 GYMS--------GGAGYVLSKEALRRFVEgfSTKVcTHTTPVEDLAMGQCLEKMGV 257
Cdd:pfam01762 137 SDYKcsryppyaSGPFYVLSRDAAEKLLK--ASKH-RRFLQIEDVYVGILANDLGI 189
PLN03153 PLN03153
hypothetical protein; Provisional
 169-280 2.24e-04

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 43.37  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517242 169 WFLKADDDTFVVVDNLRWILSNYTPEQPIYFGKRFKPYTKQGYMS-----GGAGYVLS---KEALRRFVEGFSTKVctHT 240
Cdd:PLN03153 213 WFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGIAISyplAEALSRILDDCLDRY--PK 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116517242 241 TPVEDLAMGQCLEKMGV------------LAGDSRDSLHRETFHPFIPEHHL 280
Cdd:PLN03153 291 LYGSDDRLHACITELGVplsrepgfhqwdIRGNAHGLLSSHPIAPFVSIHHV 342
 
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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