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Q477C4 (SYR_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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:Reut_A0127
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length595 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 – 595595Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242075

Regions

Motif132 – 14211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q477C4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 645BD50B6A69D79E

FASTA59564,495
        10         20         30         40         50         60 
MLPVQTSNLA AAFTDAVRAL APADAALPAV TFERPKAAAH GDLACNIAMQ VARALKSNPR 

        70         80         90        100        110        120 
ELAQRIVAMV QADPRAAELV AGMEIAGPGF INLRLTPAAK ADVLRAVLSE GDGYGAQERG 

       130        140        150        160        170        180 
MHGNVLVEFV SANPTGPLHV GHGRQAALGD ALANLLSWQG YDVHREFYYN DAGVQIQNLA 

       190        200        210        220        230        240 
VSVQARTRGF KPGDANWPEA AYNGDYIGDI AADFLAGKTV SASDGEPVTA SGNPEDLDSI 

       250        260        270        280        290        300 
RKFAVTYLRN EQDIDLQAFG VKFDHYYLES SLYTDGRVEA AVQGLVGKGK TYESEGALWL 

       310        320        330        340        350        360 
RTTDDGDDKD RVMKKTDGTY TYFVPDVAYH TTKWERGFTK VINVQGSDHH GTIARVRAGL 

       370        380        390        400        410        420 
QGLDIGIPKG YPDYVLHKMV TVMKNGEEVK ISKRAGSYVT VRDLIEWSNG GDETIRGCLD 

       430        440        450        460        470        480 
AGVADWPEHF TRGRDAVRFF LLSRKADTEF VFDVDLALKQ NDENPVYYVQ YAHARICSIF 

       490        500        510        520        530        540 
ESWGGADWES RLAELAGTDL AAVTGADASP QALALGQRLA EFPEMLAAAA GELAPHAVAF 

       550        560        570        580        590 
YLRDLAGDFH AFYNADRVLV DDEAVKRARL ALLAATRQVL RNGLAVIGVS APRRM 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ59509.1.
RefSeqYP_294353.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ477C4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A0127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59509; AAZ59509; Reut_A0127.
GeneID3610940.
KEGGreu:Reut_A0127.
PATRIC20225685. VBIRalEut24049_0721.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMARFIMLTR.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-127-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_CUPPJ
AccessionPrimary (citable) accession number: Q477C4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 55 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