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Unreviewed, UniProtKB/TrEMBL Q9V9T9 (Q9V9T9_DROME)

Last modified June 16, 2009. Version 68. 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:
    CG2135 EMBL AAF57195.1
    EC=3.2.1.31
Submitted name:
    LD10588p EMBL AAQ22542.1
Gene names
ORF Names: CG2135 FlyBase FBgn0039874, Dmel_CG2135 EMBL AAF57195.1
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length686 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionbeta-glucuronidase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q9V9T9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 570CAFBF0D92E022

FASTA68679,302
        10         20         30         40         50         60 
MKSHWMPVTC LLLGSLQVLL AYTENDFLVN ANRKELTDSP LFEYDNVRKP TPTKGLLYPR 

        70         80         90        100        110        120 
DSETREVRSL DGMWQLVRSD PYDPLQGIRE KWFMDALRKT GREIISMPVP ASYNDITTDN 

       130        140        150        160        170        180 
LRDHVGTVWY ERTFFVPRSW KTMQRTWLRF SSVHYSAVVW INGRNATSHS IGHLPFESEI 

       190        200        210        220        230        240 
SGLLSFGGDN RITVMCDNRL SNRTIPQGSV YKVATDDGTV PIQSYTFDFF NYAGIHRSVH 

       250        260        270        280        290        300 
LYTTPLLHIS DLEVTTQLTK EGLGRIDYRV WLDASKEGLQ IQPIQLRVQL RDKDGHVAAQ 

       310        320        330        340        350        360 
QINKAVYHGT LLVPNATPWW PYLMHSDPGY LYNLQFELFV ASNEKELESL QDTYRLPVGI 

       370        380        390        400        410        420 
RSLSWDNDSL LLNGKPLYLR GFGRHEDSDI RGKGLDNALL ARDFNLLKWT GANAYRTSHY 

       430        440        450        460        470        480 
PYSEESMQFA DQHGIMIIDE CPAVNIDIFE PQLLENHMSS LEQLIHRDRN HPSVVAWSVA 

       490        500        510        520        530        540 
NEPRSNKQGA LKYFEFLVNY VREIAHGRPL TAAINANSSS CHLAQFLDIV GFNRYNSWYQ 

       550        560        570        580        590        600 
NSGRTDMILN LLTIEAQSWR DRFGKPVIQF EYGGDTMEGM HSLPAFIWSE EYQVELFSRH 

       610        620        630        640        650        660 
FKAFDELRGR GWFIGEFVWN FADFRTAQTI TRVGGNKKGV FTRNRQPKEV AHILRRRYFA 

       670        680 
LAKELDMFGL PEDLTVYISK HIHNEL 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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.
[3]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Berkeley EMBL AAQ22542.1.

Cross-references

Sequence databases

AE014297 Genomic DNA. Translation: AAF57195.1.
BT010073 mRNA. Translation: AAQ22542.1.
RefSeqNP_651893.1.
UniGeneDm.29815

3D structure databases

HSSPHSSP built from PDB template 1BHG based on UniProtKB P08236.
ModBaseSearch...

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDEQ9V9T9.

Genome annotation databases

EnsemblFBgn0039874. Drosophila melanogaster. [Contig view]
GeneID43746.
KEGGdme:Dmel_CG2135.
NMPDRfig|7227.3.peg.15649.

Organism-specific databases

FlyBaseFBgn0039874. CG2135.

Phylogenomic databases

HOGENOMQ9V9T9.
OMAQ9V9T9. AINANSS.

Gene expression databases

ArrayExpressQ9V9T9.

Family and domain databases

InterProIPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006104. Glyco_hydro_2_carb-bd.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio835573.

Entry information

Entry nameQ9V9T9_DROME
AccessionPrimary (citable) accession number: Q9V9T9
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 68 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