Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Unreviewed, UniProtKB/TrEMBL Q8T8L8 (Q8T8L8_DROME)

Last modified June 16, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Alpha 3 glucosyltransferase EMBL AAF50086.2
    EC=2.4.1.-
Submitted name:
    Putative alpha 3 glucosyltransferase EMBL CAD24126.1
Gene names
Name: Alg10 FlyBase FBgn0052076
Synonyms: ALG10 EMBL CAD24126.1
ORF Names: CG32076 FlyBase FBgn0052076, Dmel_CG32076 EMBL AAF50086.2
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome] EMBL CAD24126.1
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Ontologies

Keywords
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: InterPro

   Molecular functiontransferase activity, transferring hexosyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q8T8L8-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 879E231B5D047BB7

FASTA44951,783
        10         20         30         40         50         60 
MNGSWKLILP VGFVLYSLPL FLRVNGTSDY VIDEEFHIPQ GLAFCRKEFD VWDPKITTFP 

        70         80         90        100        110        120 
GLYLIALLLN PLSLCTVTGL RMLSLAGAGI NILLLYKIRR RILAGSGGNS YAAHEAITMS 

       130        140        150        160        170        180 
VLPPLYFFSH LYYTDTLSLT MVLLFYNYWQ QEAHLPAAVF GAASVLMRQT NIVWVCMATG 

       190        200        210        220        230        240 
MTVLDTLVNQ CARTGRVPKE NVRLMGKELW LQLVSSPQLL CNCILSILAK CCFYASIILP 

       250        260        270        280        290        300 
FVGFLFINGS IVVGDKSAHE ASLHVPQLFY FAIFAAGFGI SNTIRQFRPA AELIRRNRVL 

       310        320        330        340        350        360 
SLLALLLILV VVHLNTEVHP YLLADNRHYT FYIWSRLYGR FWWFRYAMAP AYLLSICVLF 

       370        380        390        400        410        420 
CGLRHMPESF KLMFPLSLFL VLCFQRLLEL RYFLVPYILF RLNTRHTRKG YAEWLELGAH 

       430        440 
LLLNVATFYV YFTKEFYWKN YRTPQRIIW 

« Hide

References

« Hide 'large scale' references
[1]"Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate."
Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.

Cross-references

Sequence databases

AE014296 Genomic DNA. Translation: AAF50086.2.
AJ431376 mRNA. Translation: CAD24126.1.
RefSeqNP_729680.1.
UniGeneDm.31152

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT59. Glycosyltransferase Family 59.

Proteomic databases

PRIDEQ8T8L8.

Genome annotation databases

EnsemblFBgn0052076. Drosophila melanogaster. [Contig view]
GeneID326193.
KEGGdme:Dmel_CG32076.
NMPDRfig|7227.3.peg.9324.

Organism-specific databases

FlyBaseFBgn0052076. Alg10.

Phylogenomic databases

OMAQ8T8L8. HEYLLAD.

Gene expression databases

ArrayExpressQ8T8L8.

Family and domain databases

InterProIPR016900. Alpha1_2_glucosyltferase_Alg10.
IPR007006. Glycosyltransferase_ALG10.
[Graphical view]
PANTHERPTHR12989. DIE2_ALG10. 1 hit.
PfamPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNetSearch...

Other Resources

NextBio847561.

Entry information

Entry nameQ8T8L8_DROME
AccessionPrimary (citable) accession number: Q8T8L8
Secondary accession number(s): Q9VTG3
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information