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C0MGC8 (SYR_STRS7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:SZO_18760
OrganismStreptococcus equi subsp. zooepidemicus (strain H70) [Complete proteome] [HAMAP]
Taxonomic identifier553483 [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_1000203106

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
C0MGC8 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 298C08BC41E72E23

FASTA56362,955
        10         20         30         40         50         60 
MDTKTLIAAE IAKVVPELEQ AAIFNLLETP KNSDMGDLAF PAFSLAKALR KAPQAIASDL 

        70         80         90        100        110        120 
AERIDASQFE KVAAVGPYVN FFLDKASISA QVLTQVIADG ADYAQQDEGQ GRHIAIDMSS 

       130        140        150        160        170        180 
PNIAKPFSIG HLRSTVIGDS LAHIFAKMGY KPVKINHLGD WGKQFGMLIV AYKKWGNEAA 

       190        200        210        220        230        240 
VQAHPIDELL KLYVRINAEA ETDPSLDEEA REWFRRLEEG DQEATELWQW FRDESLIEFN 

       250        260        270        280        290        300 
RLYDQLGVSF DSYNGEAFYN DKMDEVLELL EDKGLLVESK GAKVVNLEKY GIEHPALIKK 

       310        320        330        340        350        360 
SDGATLYITR DLAAALYRKR TYDFAKSVYV VGNEQAAHFK QLKAVLKEMG YDWSDDMTHV 

       370        380        390        400        410        420 
AFGLVTKGGA KLSTRKGNVI LLEPTVAEAI SRAANQIEAK NPKLANKEAV AHAVGVGAIK 

       430        440        450        460        470        480 
FYDLKTDRMN GYDFDLEAMV SFEGETGPYV QYAHARIQSI LRKASFTPAV DTSYSLNDPE 

       490        500        510        520        530        540 
SWEIIKLIQD FPRIIKRAFD NFEPSIMAKF AIHLAQSFNK YYAHTRILED DPERDNRLAL 

       550        560 
CYATAIVLKE ALRLLGVEAP NEM 

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204884 Genomic DNA. Translation: CAX00816.1.
RefSeqYP_002745372.1. NC_012470.1.

3D structure databases

ProteinModelPortalC0MGC8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING553483.SZO_18760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAX00816; CAX00816; SZO_18760.
GeneID7694622.
KEGGseq:SZO_18760.
PATRIC19653641. VBIStrEqu35012_2014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycSEQU40041:GC8B-1989-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_STRS7
AccessionPrimary (citable) accession number: C0MGC8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: May 14, 2014
This is version 37 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