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Q478Y7 (SYR_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:Daro_3866
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length587 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 – 587587Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242011

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q478Y7 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 7AF447B9564215ED

FASTA58764,776
        10         20         30         40         50         60 
MAQDVKTQLT ALLQQALASV APAATDTPIH LERPRDPTHG DFATNLAMQL AKALKKNPRE 

        70         80         90        100        110        120 
IANQLLAELP PSRLVTKAEV AGAGFINFTL DAGFKTDVVK AVLAEGDNFG RSNQGGWQKV 

       130        140        150        160        170        180 
QVEFVSANPT GPLHVGHGRG AAYGASLSSL LTFAGWDVTR EYYVNDAGRQ MDILGLSTWL 

       190        200        210        220        230        240 
RYLEQHGVDV PFLPNAYQGD YVRDMAKQMT VAHGDKFVRP AADVLAGTPG LPEAERADDE 

       250        260        270        280        290        300 
AKRQRDLHLD ALIANAKVLL GPDWTYVHQH ALSEQLADGR DDLEEFGVHF DVWFSEQALF 

       310        320        330        340        350        360 
DTGLVARCVD LLEKNGHLYV QNGARWFKST TFGDEKDRVV QRENGLYTYF ASDIAYHLNK 

       370        380        390        400        410        420 
FERGFDKVIN IWGADHHGYI ARVNGAITAL GLDASKLQVA LVQFAVLYRN GQKASMSTRS 

       430        440        450        460        470        480 
GEFVTLRELR GEVGNDACRF FYALRKSDQH LDFDLDLAKS QTNENPVYYI QYAHARVCSV 

       490        500        510        520        530        540 
INQWGGDLAT LADANLALLD NPRELAIASK LAEFRDVIDG AARELAPHLI AFYLKDLAGE 

       550        560        570        580 
FHGWYNAERM LVDDAALRDA RVALAAAVRQ TIRNGMTILG VSCPDSM 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ48594.1.
RefSeqYP_287064.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ478Y7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_3866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ48594; AAZ48594; Daro_3866.
GeneID3567750.
KEGGdar:Daro_3866.
PATRIC21606426. VBIDecAro89105_3853.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycDARO159087:GI5B-3944-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. 2 hits.
[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_DECAR
AccessionPrimary (citable) accession number: Q478Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: April 16, 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