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Conserved domains on  [gi|133903791|ref|NP_493146|]
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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: ...
130-254 7.80e-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 pfam01762:

Pssm-ID: 473923 [Multi-domain]  Cd Length: 195  Bit Score: 54.64  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133903791  130 NLEDSFFDLFRKSIFGFYY--SYMHisnSFDWYLKADDDTYFAMDHLREYL--NTLDPSKPLYLGYVIKSGLKN------ 199
Cdd:pfam01762  55 DFEDTYENLTFKTLTGLLWavSKCP---SAKYIGKIDDDVYFFPDKLLSLLdnGNIDPSESSFYGYVMEEGPVIrnkksk 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133903791  200 GYNS-------------GGAGYILSNAAvkifVEKLYHDEYGCPYDWAEDRGMGRCLARVGIYPTDTR 254
Cdd:pfam01762 132 WYVSpsdykcsryppyaSGPFYVLSRDA----AEKLLKASKHRRFLQIEDVYVGILANDLGISRVNLP 195
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
130-254 7.80e-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.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 54.64  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133903791  130 NLEDSFFDLFRKSIFGFYY--SYMHisnSFDWYLKADDDTYFAMDHLREYL--NTLDPSKPLYLGYVIKSGLKN------ 199
Cdd:pfam01762  55 DFEDTYENLTFKTLTGLLWavSKCP---SAKYIGKIDDDVYFFPDKLLSLLdnGNIDPSESSFYGYVMEEGPVIrnkksk 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133903791  200 GYNS-------------GGAGYILSNAAvkifVEKLYHDEYGCPYDWAEDRGMGRCLARVGIYPTDTR 254
Cdd:pfam01762 132 WYVSpsdykcsryppyaSGPFYVLSRDA----AEKLLKASKHRRFLQIEDVYVGILANDLGISRVNLP 195
PLN03153 PLN03153
hypothetical protein; Provisional
159-248 1.22e-04

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 43.75  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133903791 159 WYLKADDDTYFAMDHLREYLNTLDPSKPLYLGYVIKSGLKNGYNS-----GGAG----YILSNAAVKIFVEKL--YHDEY 227
Cdd:PLN03153 213 WFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGiaisYPLAEALSRILDDCLdrYPKLY 292
                         90       100
                 ....*....|....*....|.
gi 133903791 228 GcpydwAEDRgMGRCLARVGI 248
Cdd:PLN03153 293 G-----SDDR-LHACITELGV 307
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
130-254 7.80e-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.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 54.64  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133903791  130 NLEDSFFDLFRKSIFGFYY--SYMHisnSFDWYLKADDDTYFAMDHLREYL--NTLDPSKPLYLGYVIKSGLKN------ 199
Cdd:pfam01762  55 DFEDTYENLTFKTLTGLLWavSKCP---SAKYIGKIDDDVYFFPDKLLSLLdnGNIDPSESSFYGYVMEEGPVIrnkksk 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133903791  200 GYNS-------------GGAGYILSNAAvkifVEKLYHDEYGCPYDWAEDRGMGRCLARVGIYPTDTR 254
Cdd:pfam01762 132 WYVSpsdykcsryppyaSGPFYVLSRDA----AEKLLKASKHRRFLQIEDVYVGILANDLGISRVNLP 195
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
79-215 3.48e-06

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: 47.31  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133903791   79 QIFCFVETSERYYNDRVPSIAATWLRRCDNGRF-FSKTP---LPSA------NMTYSTVY--KNLE---DSFFDLFRKSi 143
Cdd:pfam02434   5 DIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYiFTDGEdegLPTRtgghliNTNCSAGHcrKALSckmAVEYDRFLES- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133903791  144 fgfyysymhisnSFDWYLKADDDTYFAMDHLREYLNTLDPSKPLYLG--YV---------IKSGLKNGYN--SGGAGYIL 210
Cdd:pfam02434  84 ------------GKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGkpSLyrpieaterVKGNRKVGFWfaTGGAGFCI 151

                  ....*
gi 133903791  211 SNAAV 215
Cdd:pfam02434 152 SRGLA 156
PLN03153 PLN03153
hypothetical protein; Provisional
159-248 1.22e-04

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 43.75  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133903791 159 WYLKADDDTYFAMDHLREYLNTLDPSKPLYLGYVIKSGLKNGYNS-----GGAG----YILSNAAVKIFVEKL--YHDEY 227
Cdd:PLN03153 213 WFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFShnmafGGGGiaisYPLAEALSRILDDCLdrYPKLY 292
                         90       100
                 ....*....|....*....|.
gi 133903791 228 GcpydwAEDRgMGRCLARVGI 248
Cdd:PLN03153 293 G-----SDDR-LHACITELGV 307
 
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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