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B5XJ77 (SYR_STRPZ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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:Spy49_1762
OrganismStreptococcus pyogenes serotype M49 (strain NZ131) [Complete proteome] [HAMAP]
Taxonomic identifier471876 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length563 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 – 563563Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095414

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B5XJ77 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 98E9A71AF85A13C6

FASTA56362,993
        10         20         30         40         50         60 
MDTKTLIASE IAKVVPELEQ DAIFNLLETP KNSDMGDLAF PAFSLAKVLR KAPQMIASEL 

        70         80         90        100        110        120 
AEQIDESQFE KVVAVGPYIN FFLDKVKISS QVLEQVITAG SDYAQQDEGQ GRNVAIDMSS 

       130        140        150        160        170        180 
PNIAKPFSIG HLRSTVIGDS LANIFAKMGY QPVKINHLGD WGKQFGMLIV AYKKWGDEAA 

       190        200        210        220        230        240 
VQAHPIDELL KLYVRINAEA EIDPTVDEEA REWFRKLEDG DKEATELWQW FRDESLLEFN 

       250        260        270        280        290        300 
RLYDQLHVTF DSYNGEAFYN DKMDEVLALL EAKNLLVESK GAQVVTLEKY GIAPPPLIKK 

       310        320        330        340        350        360 
SDGATLHITR ALAPALYRKR TYDFAKSVYV VGNEQAAHFK QLKAVLKEMG YDWSDDMTHV 

       370        380        390        400        410        420 
AFGLVTKGGA KLSTRKGNVI LLEPTVAEAI NRAASQIEAK NPNLADKEAV AHAVGVGAIK 

       430        440        450        460        470        480 
FYDLKTDRMN GYDFDLEAMV SFEGETGPYV QYAHARIQSI LRKADFTPSA TTTYSLADAE 

       490        500        510        520        530        540 
SWEIIKLIQD FPRIIKRTSD NFEPSIMAKF AINLAQSFNK YYAHTRILDD NSERDNRLVL 

       550        560 
CYATATVLKE ALRLLGVDAP NEM 

« Hide

References

[1]"Genome sequence of a nephritogenic and highly transformable M49 strain of Streptococcus pyogenes."
McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B., Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.
J. Bacteriol. 190:7773-7785(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NZ131.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000829 Genomic DNA. Translation: ACI62011.1.
RefSeqYP_002286706.1. NC_011375.1.

3D structure databases

ProteinModelPortalB5XJ77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471876.Spy49_1762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI62011; ACI62011; Spy49_1762.
GeneID6985445.
KEGGsoz:Spy49_1762.
PATRIC19758670. VBIStrPyo129711_1821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

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_STRPZ
AccessionPrimary (citable) accession number: B5XJ77
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 41 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