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B9DW76 (SYR_STRU0) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. 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:SUB1789
OrganismStreptococcus uberis (strain ATCC BAA-854 / 0140J) [Complete proteome] [HAMAP]
Taxonomic identifier218495 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length562 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 – 562562Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198939

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B9DW76 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: A4BF3D251F969E74

FASTA56263,982
        10         20         30         40         50         60 
MDTKTLIAND IAKVVPELDQ ETIYNLLETP KNSDMGDVAF PAFSLAKVLR KAPQMIAGEL 

        70         80         90        100        110        120 
AEKIDAAQYE KVMAVGPYIN FFLDKSSISK EVLEAVIKEK ANYGQQHIGD GQNVTLDMSS 

       130        140        150        160        170        180 
PNIAKPFSVG HLRSTVIADA IGHIYSKLGY NSIRINHLGD WGKQFGMLIV AYKLWGDRAT 

       190        200        210        220        230        240 
VEANPIDELL KLYVRINAEA EENPELDEQA RQWFKKLEDG DKEAWDLWQW FRDESLVEFN 

       250        260        270        280        290        300 
RIYDKLDVSF DHFHGEAFYN DKMDEGIQIL EDKNLLKESK GAQIVDLEKY NLPPALIKKS 

       310        320        330        340        350        360 
DGATLYITRD MATAMYRQRT FNFVKNIYVV GQEQSHHFKQ LKAVLKEMGF DWSDDMIHVS 

       370        380        390        400        410        420 
FGLVTKNKKK LSTRKGNIIR LEPTLDEAVS RALTQIEAKN PDLENKEDVA HAVGVGAVKF 

       430        440        450        460        470        480 
YDLKTDRDNG YDFDLEAMVS FEGETGPYVQ YTYARIQSIL RKADFTPNEE TPYSLNDAES 

       490        500        510        520        530        540 
WEIIKLLQGF AANIERAAEK YDPSIIAKFA IQLAQSFNRY YAHTRILDES EERDSRLALC 

       550        560 
YATAVVLKES LRLLGVQAPE KM 

« Hide

References

[1]"Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis."
Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D., Parkhill J.
BMC Genomics 10:54-54(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-854 / 0140J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM946015 Genomic DNA. Translation: CAR43791.1.
RefSeqYP_002563061.1. NC_012004.1.

3D structure databases

ProteinModelPortalB9DW76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218495.SUB1789.

Proteomic databases

PRIDEB9DW76.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR43791; CAR43791; SUB1789.
GeneID7393023.
KEGGsub:SUB1789.
PATRIC19809293. VBIStrUbe20775_1748.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSUBE218495:GJ7D-1826-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_STRU0
AccessionPrimary (citable) accession number: B9DW76
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 39 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