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P59483 (SYR_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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:bbp_224
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length578 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 – 578578Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151541

Regions

Motif125 – 13511"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
P59483 [UniParc].

Last modified April 4, 2003. Version 1.
Checksum: FF6F76245F6D1AB4

FASTA57867,542
        10         20         30         40         50         60 
MTIKSIISKH IKKVLNIIKI FITHEDLAIV RTSDKKVWDY QVNGIIKLAN NLNKNPYVLS 

        70         80         90        100        110        120 
KYIISNMRYY EYKMYKKITA SKLGFINIFI NKTWLEKELT KKIKSFRLGI KKVTPKNIII 

       130        140        150        160        170        180 
DYSSPNVAKK MHVGHLRSTI LGDATARILE FLGHNVMRIN HIGDWGTHFG MIIAYLKQNF 

       190        200        210        220        230        240 
ISYNEINQLD LNELYQKAKV NFDLDSEFSK KTRNYVVKLQ KKDKECIRIW KKIVKKTITE 

       250        260        270        280        290        300 
NQKIYKKLNV TLTNKHIVGE SFYNDMLPDI IQDLKTKKIA KQCNGAYIVF LNKFKNRDGA 

       310        320        330        340        350        360 
PMGVIIQKQD GAFLYSTIDL ACLKYRCEVL RADQILYFID SRQKEYLKQI LEIAKKAGYI 

       370        380        390        400        410        420 
SNNIIIRHNE FGMICSKNKR PFSTRSGNNI ILSDLINEAI KRAKKIAKNK NKNLSNKELE 

       430        440        450        460        470        480 
YLSEKIGIGA IKYFDLSKNR LTDYIFKWDE ILTFDGNTAP YMQYAYIRIL SIFKKLNISM 

       490        500        510        520        530        540 
LKLSGNIILT ELLENKLAIK LFQFEEIILE SLQHSAPHII CKYLYELSKI FSKFYEKCSI 

       550        560        570 
YKSKNTKIRK NRLLLSLLTA RTLKKGLFII GISTIKYM 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26955.1.
RefSeqNP_777850.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59483.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp224.

Proteomic databases

PRIDEP59483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26955; AAO26955; bbp_224.
GeneID1058239.
KEGGbab:bbp224.
PATRIC21245229. VBIBucAph80364_0221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-224-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_BUCBP
AccessionPrimary (citable) accession number: P59483
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: April 4, 2003
Last modified: April 16, 2014
This is version 78 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