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Q052J1 (SYR_LEPBL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:LBL_1256
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]
Taxonomic identifier355276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length586 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 – 586586Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198917

Regions

Motif133 – 14311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q052J1 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: F40E628488804D1E

FASTA58666,833
        10         20         30         40         50         60 
MKENETLKQI VLKSLEEGVD SLIVSFPDVE KSSLRIKIEY SRDEKFGDYS TSFSLENSKL 

        70         80         90        100        110        120 
LKRNPIQVSK ELVEILQKRT DLFEKVDFTP PGFVNFKISP SYLLEYIEKS ILSGDHFPKV 

       130        140        150        160        170        180 
EHPLKINLEF VSANPTGPLN IVSARAAANG DTMASLLKAI GHNVDKEFYI NDYGNQVFLL 

       190        200        210        220        230        240 
GVSTLVRIRE IKGEFSTRQE ADDTTPIDTI LEKNILPAEG YRGEYIKDIA NALLNEPKKS 

       250        260        270        280        290        300 
SQIETLLKEK KYRELAELCS IWTVENNLDW QRKDLDSFGV EFDNYFRERT LHESDKVLAV 

       310        320        330        340        350        360 
MKDLERVGKI FEEDGKKIFR STEYGDDKDR VVVRDDGRPT YLLADIAYHK DKIERGYDRI 

       370        380        390        400        410        420 
YDIWGPDHHG YISRLSGAVQ TLGYKKENFK VIISQQVNLL ESGQKVKMSK RAGSFQTMSD 

       430        440        450        460        470        480 
LIGFLGKHGK DVGRYFFVMR SLDAPLDFDL DLAQDQSDKN PVFYLQYAHA RICSIFREVG 

       490        500        510        520        530        540 
TESSAEAAES LEMSEERKRL LFWIARFPEE IFDSANSMEP HRVANYLQSF AKAFTGFYLG 

       550        560        570        580 
KNNRLKDATP EVRLGLARIC LAARSVLAEG LGLIGVSAPE KMEKES 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L550.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000348 Genomic DNA. Translation: ABJ78754.1.
RefSeqYP_797687.1. NC_008508.1.

3D structure databases

ProteinModelPortalQ052J1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355276.LBL_1256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ78754; ABJ78754; LBL_1256.
GeneID4407308.
KEGGlbl:LBL_1256.
PATRIC22366286. VBILepBor75619_1606.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAIRNTIND.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycLBOR355276:GHUQ-1244-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.
InterProIPR001278. 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.
ProtoNetSearch...

Entry information

Entry nameSYR_LEPBL
AccessionPrimary (citable) accession number: Q052J1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 53 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