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Reviewed, UniProtKB/Swiss-Prot Q9VXN4 (SYRC_DROME)

Last modified February 9, 2010. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable arginyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.19
Alternative name(s):
    Arginine--tRNA ligase
      Short name=ArgRS
Gene names
Name: Aats-arg
ORF Names: CG9020
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

SUMO binding

Inferred from physical interaction. Source: FlyBase

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665Probable arginyl-tRNA synthetase, cytoplasmic
PRO_0000151662

Regions

Motif205 – 21612"HIGH" region

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Sequences

Sequence LengthMass (Da)Tools
Q9VXN4-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CCC31E337EBBDA54

FASTA66575,577
        10         20         30         40         50         60 
MSELNMELKK LRELELKTQG LAARIQTAKS GEQLDVDLVQ LQIENKKLKN RLFILKKSIA 

        70         80         90        100        110        120 
EESTAAGGDV SKPKESSSIT EHLESVFRQA IASAFPEFRD TPVIIAPVNS TSAKFGDYQC 

       130        140        150        160        170        180 
NNAMGLSKKL KEKGINKAPR DIATELKGHC PASPIIEKLE IAGAGFVNVF LSKDYASLAL 

       190        200        210        220        230        240 
SNLLRNGVKP PEVIKKRVLV DFSSPNIAKQ MHVGHLRSTI IGESLCRLLE FLQHDVIRIN 

       250        260        270        280        290        300 
HLGDWGTQFG MLIAHLEDRF PNYLNESPPI SDLQLFYKES KKRFDEDEEF KKRAYSRVVS 

       310        320        330        340        350        360 
LQKGVPNSIK AWELICNVSR KEFQTIYERL DISVKERGES FYQSRMLSVV EYLRGKGLLE 

       370        380        390        400        410        420 
VDEGREIMWP DDTKTGIPLT IVKSDGGFTY DTSDMAAIRH RLEEELCDWI IYVVDSGQST 

       430        440        450        460        470        480 
HFNTIFKAAE RSAILNPLSH RVDHVQFGVV LGEDGKKFKT RSGDTVKLSD LLDEGMKRSL 

       490        500        510        520        530        540 
QQLESRGRDK VLTPQELKDA QESLAYGCIK YSDLCHNRIS DYIFSFDKML EDRGNTAVYL 

       550        560        570        580        590        600 
LYTYTRICSI ARNSGEDFTN LPEILKKTNI VLDHEKEWKL AKTLLKLHDI LIKCSKELFL 

       610        620        630        640        650        660 
HFLCEFCFEV CTVFTEFYDS CYCIEKNKQG DIIGVNHSRI LLCEATAAVL RQCFYILGLK 


PVSKM

« Hide

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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.
[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.
Tissue: Embryo.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014298 Genomic DNA. Translation: AAF48524.1.
AY070924 mRNA. Translation: AAL48546.1.
RefSeqNP_573081.1.
UniGeneDm.1574

3D structure databases

SMRQ9VXN4. Positions 76-665.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-23738N.
IntActQ9VXN4. 1 interaction.
STRINGQ9VXN4.

Proteomic databases

PRIDEQ9VXN4.

Genome annotation databases

EnsemblFBtr0074178; FBpp0073965; FBgn0027093; Drosophila melanogaster. [Genome view]
GeneID32539.
KEGGdme:Dmel_CG9020.
NMPDRfig|7227.3.peg.18032.

Organism-specific databases

CTD32539.
FlyBaseFBgn0027093. Aats-arg.

Phylogenomic databases

eggNOGinNOG05509.
InParanoidQ9VXN4.
OMAHMGFGTM.
OrthoDBEOG9M0F75.
PhylomeDBQ9VXN4.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-002060-MONOMER.
BRENDA6.1.1.19. 48.

Gene expression databases

ArrayExpressQ9VXN4.
BgeeQ9VXN4.
GermOnlineCG9020. Drosophila melanogaster.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-synth_Ic.
IPR015945. Arg-tRNA-synth_Ic_core.
IPR005148. Arg-tRNA-synth_Ic_N.
IPR008909. DALR_anticod_bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11956. Arg_tRNA-synt_1c. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM00836. DALR_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio779008.

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Entry information

Entry nameSYRC_DROME
AccessionPrimary (citable) accession number: Q9VXN4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents