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C3PMA4 (SYR_RICAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:RAF_ORF0089
OrganismRickettsia africae (strain ESF-5) [Complete proteome] [HAMAP]
Taxonomic identifier347255 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length576 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 – 576576Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000203104

Regions

Motif126 – 13611"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
C3PMA4 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: B7DDF87C4FEF0729

FASTA57665,220
        10         20         30         40         50         60 
MNIFNQLKQD IIVASRQLYN NQEIANTATI EIPKDSFNGD LSSNIAMIIA AKESIAPREV 

        70         80         90        100        110        120 
ALKFKEVLIT LPYIASIEIA GPGFINFTIK ADSWQASIKD ILQHEEKFFE IDIDKSKNIN 

       130        140        150        160        170        180 
IEYVSANPTG PMHIGHARGA IYGDVLARIL QKVSYSVTKE YYVNDAGSQI NDLVSTVLLR 

       190        200        210        220        230        240 
YKEALGEQIT IPAGLYPGEY LIPLGQILAK EYGNKLLTMN YAERFKIIKS FAVEKMLDLN 

       250        260        270        280        290        300 
RKDLADLGIK HDIFFSEQSL HDKGEIEETV KLLERMGLIY EGTLPAPKGK IHEEWDNRVQ 

       310        320        330        340        350        360 
KLFKSTKYGD SQDRPIEKAD GSWSYFASDL AYAKDKIERG ANHLIYVLGA DHSGYVKRIE 

       370        380        390        400        410        420 
AIVKALGKEQ VKVDVKICQL VNFVENGVPV KMSKRLGSFA SVQDVNHEVG KDIIRFMMLT 

       430        440        450        460        470        480 
RQNDKPLDFD LVKVKEQSRE NPIFYVQYAH VRTISILSKA KELMPESYNN FESGKYDLSL 

       490        500        510        520        530        540 
LSSEEEIEII KLLASWTKTL EASAKYFEPH RIAFYLINLA SKFHSMWNFG KENSDYRFVI 

       550        560        570 
ESNKELTLAR LALASAIQKV IASGLEVIGV EPMNKM 

« Hide

References

[1]"Analysis of the Rickettsia africae genome reveals that virulence acquisition in Rickettsia species may be explained by genome reduction."
Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.
BMC Genomics 10:166-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ESF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001612 Genomic DNA. Translation: ACP53064.1.
RefSeqYP_002844807.1. NC_012633.1.

3D structure databases

ProteinModelPortalC3PMA4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347255.RAF_ORF0089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP53064; ACP53064; RAF_ORF0089.
GeneID7815340.
KEGGraf:RAF_ORF0089.
PATRIC17871909. VBIRicAfr6986_0103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAIRNTIND.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycRAFR347255:GJCT-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_RICAE
AccessionPrimary (citable) accession number: C3PMA4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 35 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