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Conserved domains on  [gi|392919115|ref|NP_504520|]
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N-acetylgalactosaminide beta-1,3-galactosyltransferase [Caenorhabditis elegans]

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: ...
 231-424 2.09e-41

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: 147.47  E-value: 2.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115  231 VKTFEGHHVNRLEVLKNTWASDVSRIEYC-SDKEDPAIPTI---NLGVDNTDRGHCAKTWEI-----FRRFLGSsgnGAK 301
Cdd:pfam02434  10 VKTTKKFHKTRLPLLLKTWISRAKHQTYIfTDGEDEGLPTRtggHLINTNCSAGHCRKALSCkmaveYDRFLES---GKK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115  302 WLVVADDDTLMNFKRLKQMLELYDSGDKIIIGERYGYGF-------SLNGDSGYDYPTGGSGMIFTRSAVESLLAQC--P 372
Cdd:pfam02434  87 WFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPSLYRPieatervKGNRKVGFWFATGGAGFCISRGLALKMSPWAsgG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392919115  373 SCIANTD----PDDMTIGICaLTA--GIPIVHESRLHQARP--LDYAPEYI--KYPISFHKF 424
Cdd:pfam02434 167 RFMSTSEkirlPDDCTLGYI-IENllGVPLTHSPLFHSHLEnlQDLPPETLheQVTLSYGKF 227
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 231-424 2.09e-41

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: 147.47  E-value: 2.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115  231 VKTFEGHHVNRLEVLKNTWASDVSRIEYC-SDKEDPAIPTI---NLGVDNTDRGHCAKTWEI-----FRRFLGSsgnGAK 301
Cdd:pfam02434  10 VKTTKKFHKTRLPLLLKTWISRAKHQTYIfTDGEDEGLPTRtggHLINTNCSAGHCRKALSCkmaveYDRFLES---GKK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115  302 WLVVADDDTLMNFKRLKQMLELYDSGDKIIIGERYGYGF-------SLNGDSGYDYPTGGSGMIFTRSAVESLLAQC--P 372
Cdd:pfam02434  87 WFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPSLYRPieatervKGNRKVGFWFATGGAGFCISRGLALKMSPWAsgG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392919115  373 SCIANTD----PDDMTIGICaLTA--GIPIVHESRLHQARP--LDYAPEYI--KYPISFHKF 424
Cdd:pfam02434 167 RFMSTSEkirlPDDCTLGYI-IENllGVPLTHSPLFHSHLEnlQDLPPETLheQVTLSYGKF 227
PLN03153 PLN03153
hypothetical protein; Provisional
 301-404 7.24e-03

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 38.74  E-value: 7.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115 301 KWLVVADDDTLMNFKRLKQMLELYDSGDKIIIGERyGYGFSLNGDSGYDYPTGGSGMIFTRSAVESLLAQCPSCIANTDP 380
Cdd:PLN03153 212 RWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGP-SESHSANSYFSHNMAFGGGGIAISYPLAEALSRILDDCLDRYPK 290

                         90       100
                 ....*....|....*....|....*..
gi 392919115 381 ---DDMTIGICALTAGIPIVHESRLHQ 404
Cdd:PLN03153 291 lygSDDRLHACITELGVPLSREPGFHQ 317
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 231-424 2.09e-41

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: 147.47  E-value: 2.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115  231 VKTFEGHHVNRLEVLKNTWASDVSRIEYC-SDKEDPAIPTI---NLGVDNTDRGHCAKTWEI-----FRRFLGSsgnGAK 301
Cdd:pfam02434  10 VKTTKKFHKTRLPLLLKTWISRAKHQTYIfTDGEDEGLPTRtggHLINTNCSAGHCRKALSCkmaveYDRFLES---GKK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115  302 WLVVADDDTLMNFKRLKQMLELYDSGDKIIIGERYGYGF-------SLNGDSGYDYPTGGSGMIFTRSAVESLLAQC--P 372
Cdd:pfam02434  87 WFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPSLYRPieatervKGNRKVGFWFATGGAGFCISRGLALKMSPWAsgG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392919115  373 SCIANTD----PDDMTIGICaLTA--GIPIVHESRLHQARP--LDYAPEYI--KYPISFHKF 424
Cdd:pfam02434 167 RFMSTSEkirlPDDCTLGYI-IENllGVPLTHSPLFHSHLEnlQDLPPETLheQVTLSYGKF 227
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 298-398 2.55e-03

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: 38.84  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115  298 NGAKWLVVADDDTLMNFKRLkqmLELYDSGDKIIIGER-YGY----GFSLNGD------SGYDYP-------TGGSGMIF 359
Cdd:pfam01762  79 PSAKYIGKIDDDVYFFPDKL---LSLLDNGNIDPSESSfYGYvmeeGPVIRNKkskwyvSPSDYKcsryppyASGPFYVL 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 392919115  360 TRSAVESLLAQcpscIANTDP---DDMTIGICALTAGIPIVH 398
Cdd:pfam01762 156 SRDAAEKLLKA----SKHRRFlqiEDVYVGILANDLGISRVN 193
PLN03153 PLN03153
hypothetical protein; Provisional
 301-404 7.24e-03

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 38.74  E-value: 7.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919115 301 KWLVVADDDTLMNFKRLKQMLELYDSGDKIIIGERyGYGFSLNGDSGYDYPTGGSGMIFTRSAVESLLAQCPSCIANTDP 380
Cdd:PLN03153 212 RWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGP-SESHSANSYFSHNMAFGGGGIAISYPLAEALSRILDDCLDRYPK 290

                         90       100
                 ....*....|....*....|....*..
gi 392919115 381 ---DDMTIGICALTAGIPIVHESRLHQ 404
Cdd:PLN03153 291 lygSDDRLHACITELGVPLSREPGFHQ 317
 
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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