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B2S0U2 (SYR_BORHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:BH0594
OrganismBorrelia hermsii (strain HS1 / DAH) [Complete proteome] [HAMAP]
Taxonomic identifier314723 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorrelia

Protein attributes

Sequence length584 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 – 584584Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095336

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B2S0U2 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 4536CDFA4D5D8658

FASTA58467,429
        10         20         30         40         50         60 
MNSKIKKDLK DIISKTIKEL ALRESIKLEE INIIMQKPPK SELGDLSILI FEFSKILKLN 

        70         80         90        100        110        120 
TSIITEEIIK QIGDKYATKA MGPYLNIKFN RKEYIKDTIK KVNEQKEKYG INNVLKNKRI 

       130        140        150        160        170        180 
IIEFSSPNTN KPLHIGHLRN DIIGESLSRI LKASGAQVTK INLINDRGTH ICKSMLAYKK 

       190        200        210        220        230        240 
FGNNTTPELS LKKGDHLIGD FYVKYNEYAK NNEMAEDEIQ QLLCKWEEGD EKTVQLWKKL 

       250        260        270        280        290        300 
NQWAIEGIKA TYKLTNITFD KIYLESEIFK IGREIILKGL EEGLCYKRED GAICIDIPTE 

       310        320        330        340        350        360 
KNEISEQQFK QKVLLRANGT SIYLTQDLGN IVTRKNEFDF DEMIYVVGSE QIHHFKTLFY 

       370        380        390        400        410        420 
VANKLGITKE NNLVHLSYGM VNLPEGKMKS REGNVIDADN LIHDLSESII LEIKKRNSDK 

       430        440        450        460        470        480 
KDYQEIALNI SLGAIHYYLL KTAIHKDILF NKEESLSFTG NSGPYIQYVG ARINSILEKY 

       490        500        510        520        530        540 
DELNLSNETI NFDLLVNENE WEIIKIISEF EEHIIKASKD RNPSVIANYS YLLAKSFSTY 

       550        560        570        580 
YQDTKIIDKN KPELTHARID LSKAVLQTIK NCMHLLNIPY MKKM 

« Hide

References

[1]"The genome sequence of Borrelia hermsii and Borrelia turicatae: comparative analysis of two agents of endemic N. America relapsing fever."
Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T., Schwan T.G.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS1 / DAH.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000048 Genomic DNA. Translation: AAX17098.1.
RefSeqYP_001884018.1. NC_010673.1.

3D structure databases

ProteinModelPortalB2S0U2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314723.BH0594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX17098; AAX17098; BH0594.
GeneID6276894.
KEGGbhr:BH0594.
PATRIC20568544. VBIBorHer61105_0596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMAPDIAYHI.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBHER314723:GJES-592-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_BORHD
AccessionPrimary (citable) accession number: B2S0U2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 42 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