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Q2JK96 (SYR_SYNJB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. 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:CYB_1944
OrganismSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321332 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length598 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 – 598598Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242106

Regions

Motif140 – 15011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q2JK96 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 52A66720E45B7841

FASTA59866,874
        10         20         30         40         50         60 
MATQPVSTSL IRFLTAAVAE SIRRASEAGQ LGSLAPQQAT AIAPVIQIPS DPRYGDYACP 

        70         80         90        100        110        120 
TPLGMAKLCR LAPAQIAQTL QKHLDLPDIE TQVAGGGYLN FRLGDPFLAK RLQELLHLGE 

       130        140        150        160        170        180 
NFGKTAIPHP ERILLEFVSA NPTGPLHVGH GRWAAVGSTL ANLLHWTGHQ VEREFYINDA 

       190        200        210        220        230        240 
GNQMRLLGQS LEVRVRQLQG EEVALPEDAY HGSYLVDIAR RLLGQVKAGI RPLPTTLEEY 

       250        260        270        280        290        300 
TDFAYGEMLA WQKQTLQQLR TEFDHWFSER RLHTPDPQTG LSAIQQALQE LQERGFLYKA 

       310        320        330        340        350        360 
KAPRGEDPKP GAEEAVYFKT QEFGDDKDRV VQKADGSFTY LAADIAYHRD KVQRGYHRLI 

       370        380        390        400        410        420 
NILGSDHHGY IGRLKAAVGA FSPDVKLEIL IGQFVKLFKT DPQTGEKTEV RMSKRTGNFV 

       430        440        450        460        470        480 
SLNDLIEDPE IGVGVDAARW FLLSSSMDSP INFDLDLAVK QTFDNPVVYV HYSHARCCTL 

       490        500        510        520        530        540 
LRRLQEEEKV ELTNKVPLTE QQKLPYKEPE ERALLLRLLA LPDELIAAAE ERAPHKIIRY 

       550        560        570        580        590 
AEAIAADFNK FYDNCRILPL LKEDPLLAQA RIQLVQATQQ VLFNVLTGIL GLSAPESM 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000240 Genomic DNA. Translation: ABD02899.1.
RefSeqYP_478162.1. NC_007776.1.

3D structure databases

ProteinModelPortalQ2JK96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321332.CYB_1944.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD02899; ABD02899; CYB_1944.
GeneID3900167.
KEGGcyb:CYB_1944.
PATRIC23806236. VBISynSp29577_1957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBCLSK423190.

Enzyme and pathway databases

BioCycSSP321332:GH1B-1944-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_SYNJB
AccessionPrimary (citable) accession number: Q2JK96
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 54 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