NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17507715|ref|NP_493101|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Galactosyl_T super family cl21608
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
127-254 1.62e-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 pfam01762:

Pssm-ID: 473923 [Multi-domain]  Cd Length: 195  Bit Score: 53.87  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507715   127 VYLNLKDSYYDLFRKTTFGFYY--SYMHiskSFDWYLKADDDTYFAMDHLKEYL--STLDPTKPLYLGYVLK---PYFKN 199
Cdd:pfam01762  52 VVVDFEDTYENLTFKTLTGLLWavSKCP---SAKYIGKIDDDVYFFPDKLLSLLdnGNIDPSESSFYGYVMEegpVIRNK 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17507715   200 G---YNS-------------GGSGYILSNAAVKLFVEKLYHDeytcPYDWAEDRGMGRCMARAGIFPTDTR 254
Cdd:pfam01762 129 KskwYVSpsdykcsryppyaSGPFYVLSRDAAEKLLKASKHR----RFLQIEDVYVGILANDLGISRVNLP 195
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
127-254 1.62e-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.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 53.87  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507715   127 VYLNLKDSYYDLFRKTTFGFYY--SYMHiskSFDWYLKADDDTYFAMDHLKEYL--STLDPTKPLYLGYVLK---PYFKN 199
Cdd:pfam01762  52 VVVDFEDTYENLTFKTLTGLLWavSKCP---SAKYIGKIDDDVYFFPDKLLSLLdnGNIDPSESSFYGYVMEegpVIRNK 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17507715   200 G---YNS-------------GGSGYILSNAAVKLFVEKLYHDeytcPYDWAEDRGMGRCMARAGIFPTDTR 254
Cdd:pfam01762 129 KskwYVSpsdykcsryppyaSGPFYVLSRDAAEKLLKASKHR----RFLQIEDVYVGILANDLGISRVNLP 195
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
127-254 1.62e-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.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 53.87  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507715   127 VYLNLKDSYYDLFRKTTFGFYY--SYMHiskSFDWYLKADDDTYFAMDHLKEYL--STLDPTKPLYLGYVLK---PYFKN 199
Cdd:pfam01762  52 VVVDFEDTYENLTFKTLTGLLWavSKCP---SAKYIGKIDDDVYFFPDKLLSLLdnGNIDPSESSFYGYVMEegpVIRNK 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17507715   200 G---YNS-------------GGSGYILSNAAVKLFVEKLYHDeytcPYDWAEDRGMGRCMARAGIFPTDTR 254
Cdd:pfam01762 129 KskwYVSpsdykcsryppyaSGPFYVLSRDAAEKLLKASKHR----RFLQIEDVYVGILANDLGISRVNLP 195
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
79-215 1.66e-03

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: 39.22  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507715    79 QLFCFVETSAVHYDDRVPSIASTWLPKCDNGRFF----------TKTPL----PNSNMTYSTVYLNLKDSY-YDLFrktt 143
Cdd:pfam02434   5 DIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIftdgedeglpTRTGGhlinTNCSAGHCRKALSCKMAVeYDRF---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507715   144 fgfyysymhISKSFDWYLKADDDTYFAMDHLKEYLSTLDPTKPLYLGyvlKPYF--------------KNGYN--SGGSG 207
Cdd:pfam02434  81 ---------LESGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLG---KPSLyrpieatervkgnrKVGFWfaTGGAG 148

                  ....*...
gi 17507715   208 YILSNAAV 215
Cdd:pfam02434 149 FCISRGLA 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure