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Q8E2R1 (SYR_STRA3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:gbs2056
OrganismStreptococcus agalactiae serotype III (strain NEM316) [Complete proteome] [HAMAP]
Taxonomic identifier211110 [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_0000151613

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q8E2R1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 50520F4FFA657A77

FASTA56363,188
        10         20         30         40         50         60 
MDTKHLIASE IQKVVPDMEQ STILSLLETP KNSSMGDLAF PAFSLAKTLR KAPQIIASDI 

        70         80         90        100        110        120 
AEQIKSDQFE KVEAVGPYVN FFLDKAAISS QVLKQVLSDG SAYATQNIGE GRNVAIDMSS 

       130        140        150        160        170        180 
PNIAKPFSIG HLRSTVIGDS LANIFDKIGY HPVKINHLGD WGKQFGMLIV AYKKWGNEEA 

       190        200        210        220        230        240 
VRAHPIDELL KLYVRINAEA ETDPSVDEEA REWFRKLEAN DPEATELWQW FRDESLLEFN 

       250        260        270        280        290        300 
RLYDQMNVTF DSYNGEAFYN DKMDEVLELL ESKNLLVESK GAQVVNLEKY GIEHPALIKK 

       310        320        330        340        350        360 
SDGATLYITR DLAAALYRKR TYDFAKSIYV VGNEQSAHFK QLKAVLKEMD YDWSDDMTHV 

       370        380        390        400        410        420 
PFGLVTKGGA KLSTRKGNVI LLEPTVAEAI NRAASQIEAK NPNLADKDKV AQAVGVGAIK 

       430        440        450        460        470        480 
FYDLKTDRTN GYDFDLEAMV SFEGETGPYV QYAHARIQSI LRKANFNPSN SDNYSLNDVE 

       490        500        510        520        530        540 
SWEIIKLIQD FPRIIVRAAD NFEPSIIAKF AINLAQCFNK YYAHTRILDE DAEISSRLAL 

       550        560 
CYATATVLKE SLRLLGVDAP NEM 

« Hide

References

[1]"Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease."
Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.
Mol. Microbiol. 45:1499-1513(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NEM316.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL766856 Genomic DNA. Translation: CAD47715.1.
RefSeqNP_736489.1. NC_004368.1.

3D structure databases

ProteinModelPortalQ8E2R1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211110.gbs2056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD47715; CAD47715; CAD47715.
GeneID1031682.
KEGGsan:gbs2056.
PATRIC19640047. VBIStrAga3577_2108.

Organism-specific databases

GenoListgbs2056.
CMRSearch...

Phylogenomic databases

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

Family and domain databases

Gene3D3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001278. Arg-tRNA-ligase_Ia.
IPR015945. Arg-tRNA-synth_Ia_core.
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_STRA3
AccessionPrimary (citable) accession number: Q8E2R1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 70 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