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Q3YRX1 (SYR_EHRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:Ecaj_0498
OrganismEhrlichia canis (strain Jake) [Complete proteome] [HAMAP]
Taxonomic identifier269484 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

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_0000242017

Regions

Motif132 – 14211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q3YRX1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: EECF47FF2801758D

FASTA57665,487
        10         20         30         40         50         60 
MNLINTIKDC IVERLHVLNA KKLIILDDVI LSKLVVDYPN NHDYGDLYTN AALILSKYVK 

        70         80         90        100        110        120 
KDPLDVAEIL LRELSNIKEI SNISVVKPGF INFNLSLYVW YEVISSINML KEDFANVNIG 

       130        140        150        160        170        180 
NGRKVNIEFV SANPTGPMHI GHARGAIFGD VLANLLTKVG YQVVREYYIN DAGTQIDVLV 

       190        200        210        220        230        240 
ESVYLRYKEA AGQDIVIGSG LYPGLYLKEI GQLLYEKYGT DLLEMNSAQK MKIIRDISLK 

       250        260        270        280        290        300 
HLLDLIKQDL VLLGIKHDVF TSEAELLRNN VVEKCVKLLE DKKLIYYGVL DQPKGTENNN 

       310        320        330        340        350        360 
WQPRKQMLFK STDFGDDVDR ALQKVDGSWT YFASDIAYHF DKISRGFQHM ILELGSDHIG 

       370        380        390        400        410        420 
YVKRLKAAVK ALSDNTATID IKLHNIVNFL NNGVQVKMSK RSGEFLTIKD VIEEVGIDVV 

       430        440        450        460        470        480 
RFIMLTRKSD AVLDFDFVKV VEQSKNNPIF YVQYAHARVC SLMRNAPNIL KIEDTDFSVL 

       490        500        510        520        530        540 
SSKEEILLIK LLAKWSNVIE LSAKTAEPHR ITFYLIEVAE TFHMLWGYGN KDVNRRFIID 

       550        560        570 
DDINLTSARI YLARAVAYVI SSGLKIFSIV PLEEMK 

« Hide

References

[1]"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
J. Bacteriol. 188:4015-4023(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Jake.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000107 Genomic DNA. Translation: AAZ68534.1.
RefSeqYP_303132.1. NC_007354.1.

3D structure databases

ProteinModelPortalQ3YRX1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269484.Ecaj_0498.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ68534; AAZ68534; Ecaj_0498.
GeneID3618507.
KEGGecn:Ecaj_0498.
PATRIC20574582. VBIEhrCan118076_0544.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMALCNVLAK.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycECAN269484:GI02-526-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_EHRCJ
AccessionPrimary (citable) accession number: Q3YRX1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 27, 2005
Last modified: May 14, 2014
This is version 61 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