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A1AVC2 (SYR_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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

Names and origin

Protein namesRecommended name:
Arginine--tRNA ligase

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:argS
Ordered Locus Names:Rmag_0079
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00123

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00123.

Sequence similarities

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

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: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018109

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A1AVC2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: E273AB13E14B4E8F

FASTA56764,097
        10         20         30         40         50         60 
MKEQLQKILK QSLNLLENEG VLESAPENIR IDHTKDKTQG DFASNIAMVL AKRSGLIPKV 

        70         80         90        100        110        120 
LAQKIIDNLG DNTQIDKVQI ADPGFINFFI SQGESVQIIE QIINQAEHYG KADVGKGQRI 

       130        140        150        160        170        180 
LLEFVSANPT GPLHVGHGRV AAYGATVASL LRAVGFEVDN EYYVNDAGRQ MDILAISVYL 

       190        200        210        220        230        240 
RYVETEQFPD NGYKGDYIFD IAKKISGVKK LDIFISQRSV KKNAGNKEKH IDRLIANCKF 

       250        260        270        280        290        300 
QLGHDYKKIL DLAINNILSG IKIDLVEFGV KYQQWFSEQS LMDSGLSKEI VKKLQDSGYI 

       310        320        330        340        350        360 
YEKEGALWFK TTDFGDDLDR VVVRKNGKYT YFASDIAYHL EKFERGYDKI INIWGVDHHG 

       370        380        390        400        410        420 
YIARIKASIK ALNHNSNKLE ILLVQFVNLF RNGKKASMST RSGSFITLEE LREEVGNDAA 

       430        440        450        460        470        480 
RFFYILSKSG QHMNFDLDLA KSKSNENPVF YIQYAHARIC SVLKQAKSPS MVDIDLSVLN 

       490        500        510        520        530        540 
NESEALLIKE LNRYKDILQS SALNYEPHVL ACYLRELAGH FHSYYNNSKF LVDDDKLRNA 

       550        560 
RLFLIIAVKQ ILVNGLNLLG VSAPDSM 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL01879.1.
RefSeqYP_903350.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AVC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413404.Rmag_0079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL01879; ABL01879; Rmag_0079.
GeneID4554702.
KEGGrma:Rmag_0079.
PATRIC31999723. VBICanRut45856_0094.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycCRUT413404:GHM7-83-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_RUTMC
AccessionPrimary (citable) accession number: A1AVC2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries