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Conserved domains on  [gi|221331199|ref|NP_001097611|]
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uncharacterized protein Dmel_CG34452, isoform B [Drosophila melanogaster]

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: ...
 72-183 1.59e-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.


The actual alignment was detected with superfamily member pfam02434:

Pssm-ID: 473923  Cd Length: 248  Bit Score: 39.22  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331199   72 IHRTWVRHCDHYLFV-SDDIDNHLEPAVFMNM------PDKWHRMRAYLEYVYKYHFHQGD--WFLYCNDDNFVVVDNLR 142
Cdd:pfam02434  24 LLKTWISRAKHQTYIfTDGEDEGLPTRTGGHLintncsAGHCRKALSCKMAVEYDRFLESGkkWFCHVDDDNYVNVPRLV 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221331199  143 HMLKTYSPKELIYFG----------CKLRTTNGLV---FMLEGSGIVFS-AAALK 183
Cdd:pfam02434 104 RLLSCYNHTQDVYLGkpslyrpieaTERVKGNRKVgfwFATGGAGFCISrGLALK 158
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 72-183 1.59e-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: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331199   72 IHRTWVRHCDHYLFV-SDDIDNHLEPAVFMNM------PDKWHRMRAYLEYVYKYHFHQGD--WFLYCNDDNFVVVDNLR 142
Cdd:pfam02434  24 LLKTWISRAKHQTYIfTDGEDEGLPTRTGGHLintncsAGHCRKALSCKMAVEYDRFLESGkkWFCHVDDDNYVNVPRLV 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221331199  143 HMLKTYSPKELIYFG----------CKLRTTNGLV---FMLEGSGIVFS-AAALK 183
Cdd:pfam02434 104 RLLSCYNHTQDVYLGkpslyrpieaTERVKGNRKVgfwFATGGAGFCISrGLALK 158
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 72-183 1.59e-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: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331199   72 IHRTWVRHCDHYLFV-SDDIDNHLEPAVFMNM------PDKWHRMRAYLEYVYKYHFHQGD--WFLYCNDDNFVVVDNLR 142
Cdd:pfam02434  24 LLKTWISRAKHQTYIfTDGEDEGLPTRTGGHLintncsAGHCRKALSCKMAVEYDRFLESGkkWFCHVDDDNYVNVPRLV 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221331199  143 HMLKTYSPKELIYFG----------CKLRTTNGLV---FMLEGSGIVFS-AAALK 183
Cdd:pfam02434 104 RLLSCYNHTQDVYLGkpslyrpieaTERVKGNRKVgfwFATGGAGFCISrGLALK 158
 
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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