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B5RME6 (SYR_BORDL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. 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:BDU_595
OrganismBorrelia duttonii (strain Ly) [Complete proteome] [HAMAP]
Taxonomic identifier412419 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorrelia

Protein attributes

Sequence length585 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 – 585585Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095335

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B5RME6 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: CE96893EF201D2AE

FASTA58567,249
        10         20         30         40         50         60 
MIKTIKADLK NKIQKTIKEL ALSSNIKLDK INIVMQKPPK SEMGDLSILI FEFSKILKLS 

        70         80         90        100        110        120 
IPVITQEIIK QIGNEYKTKS MGPYLNIKFN RKEYIQNTIK KVNKEKENYG ANNSLQNKKT 

       130        140        150        160        170        180 
IIEFSSPNTN KPLHVGHLRN DIIGESLSRI LKASGSKVTK INLINDRGTH ICKSMLAYKK 

       190        200        210        220        230        240 
FGNNITPEIA QKKGDHLIGD FYVKYNEYAS QNSEIAENEI QQLLCQWEQG DEKTVQLWTK 

       250        260        270        280        290        300 
LNKWAIDGIK ETYNTTNITF DKIYLESEIF KIGREVVING LKEGLCYKRE DGAICINIPT 

       310        320        330        340        350        360 
EKNNIDNQNF KQKVLLRANG TSIYLTQDLG NIVARKNEFD FDEMIYVVGS EQIHHFKTLF 

       370        380        390        400        410        420 
YVADKLGVTN ENNLIHLSYG MVNLPEGKMK SREGNIIDAD NLIHDLSQST MLELKKRYEN 

       430        440        450        460        470        480 
EQNLQKLALN ISLGAIHYYL LKTAIHKDIL FNKTESLSFT GNSGPYIQYV GARINSILDK 

       490        500        510        520        530        540 
YNNLNLANKN TNFDLLVNEN EWEIIKIISE FEEYIIKASK DRNPSIIANY SYLLAKNFST 

       550        560        570        580 
YYQDTKIIDK DNLELTHARI DLAKAVLQTI KNCMHLLNIP YIQKM 

« Hide

References

[1]"The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."
Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 4:E1000185-E1000185(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ly.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000976 Genomic DNA. Translation: ACH93532.1.
RefSeqYP_002222238.1. NC_011229.1.

3D structure databases

ProteinModelPortalB5RME6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412419.BDU_595.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH93532; ACH93532; BDU_595.
GeneID6917821.
KEGGbdu:BDU_595.
PATRIC20563304. VBIBorDut9941_0611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycBDUT412419:GJ78-595-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_BORDL
AccessionPrimary (citable) accession number: B5RME6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 38 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