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Q9VHF2 (PTER_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphotriesterase-related protein
EC=3.1.-.-
Alternative name(s):
Parathion hydrolase-related protein
Gene names
ORF Names:CG18473
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Cofactor

Binds 2 divalent metal cations per subunit By similarity.

Sequence similarities

Belongs to the phosphotriesterase family.

Ontologies

Keywords
   LigandMetal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcatabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionhydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Phosphotriesterase-related protein
PRO_0000205367

Sites

Metal binding221Divalent metal cation 1 By similarity
Metal binding241Divalent metal cation 1 By similarity
Metal binding1691Divalent metal cation 1 By similarity
Metal binding1691Divalent metal cation 2 By similarity
Metal binding2011Divalent metal cation 2 By similarity
Metal binding2301Divalent metal cation 2 By similarity
Metal binding2981Divalent metal cation 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VHF2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5DD9833F68F97746

FASTA35039,297
        10         20         30         40         50         60 
MSTVQTVLGT ITPNLLGRTL THEHVALDFE HFYRPPPPDF ESELKAKISM STLGYVRLYP 

        70         80         90        100        110        120 
YSSKENVRFY DGEALEAAKK DVLLYKKHGG GSIVENSSYG LKRNLEFIVE LAKSTGVHFI 

       130        140        150        160        170        180 
AGTGHYIHAM QDASHASLTV EQMSDLYSKD IITGLQVNGK VVKCGFIGEV ASVYPIHDFE 

       190        200        210        220        230        240 
KNAIKAAGEI QEVLGCGVSM HPHRVTKAPF EIMRLYLEAG GRADKCVMSH LDRTIFDIDE 

       250        260        270        280        290        300 
LLEFAKLGCY IQYDLFGTEC SFYQLNTSVD MISDGQRIDN LIKLIKEGLV DKLLMSHDIH 

       310        320        330        340        350 
TKHRLTSYGG HGYHHIHTNI LPRMFDRGVT LEQVEQMTVT NPAKWLAFDP

« Hide

References

« Hide 'large scale' references
[1]"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.
[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: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014297 Genomic DNA. Translation: AAF54363.1.
AY071616 mRNA. Translation: AAL49238.1.
RefSeqNP_731339.1. NM_169272.1.
UniGeneDm.5836.

3D structure databases

ProteinModelPortalQ9VHF2.
SMRQ9VHF2. Positions 1-348.
ModBaseSearch...

Proteomic databases

PRIDEQ9VHF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082025; FBpp0081503; FBgn0037683.
GeneID41116.
KEGGdme:Dmel_CG18473.
NMPDRfig|7227.3.peg.11856.
UCSCCG18473-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0037683. CG18473.

Phylogenomic databases

eggNOGinNOG04978.
GeneTreeEMGT00050000017998.
InParanoidQ9VHF2.
OMAGETGCSW.
OrthoDBEOG4S4MXK.
PhylomeDBQ9VHF2.

Gene expression databases

ArrayExpressQ9VHF2.
BgeeQ9VHF2.
GermOnlineCG18473. Drosophila melanogaster.

Family and domain databases

InterProIPR017947. AryldialkylPase_Zn-BS.
IPR001559. Aryldialkylphosphatase.
[Graphical view]
KOK07048.
PANTHERPTHR10819. PTE. 1 hit.
PfamPF02126. PTE. 1 hit.
[Graphical view]
PROSITEPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio822258.

Entry information

Entry namePTER_DROME
AccessionPrimary (citable) accession number: Q9VHF2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents