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Q5M6I4 (SYR_STRT2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. 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:stu0047
OrganismStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]
Taxonomic identifier264199 [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_0000242101

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5M6I4 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 3E7C200F1058C816

FASTA56362,892
        10         20         30         40         50         60 
MNTKELIAAE IAKVVPELEQ ENIQNLLEIP KNADMGDLAF PAFSLAKVLR KAPQMIAADI 

        70         80         90        100        110        120 
AEKIDASNFE KVEAVGPYIN IFLDKSKISA DVLGQVIAQG SHYADQNIGN GRNIAFDMSS 

       130        140        150        160        170        180 
PNIAKPFSIG HLRSTVIADA LANIVAKQGY KPVRINHLGD WGKQFGMLIV AYKKWGSEEA 

       190        200        210        220        230        240 
VKANPINELL QLYVRINAEA EEDPSVDEEA REWFRKLEAG DEEATALWQW FRDESLVEFN 

       250        260        270        280        290        300 
RLYDELGVSF DSYNGEAFYN DKMDEVVDIL TKKGLLQESQ GAQVVNLEKY GIEHPALIKK 

       310        320        330        340        350        360 
SDGATLYITR DLAAALYRKR TYDFAKAIYV VGNEQSAHFK QLKAVLKEMG YNWSDDMTHV 

       370        380        390        400        410        420 
AFGLVTKNGK KLSTRKGNVI LLEPTIAEAV NRAQAQIEAK NPNLPNKEAI AHAVGVGAIK 

       430        440        450        460        470        480 
FYDLKTDRMN GYDFDLDAMV SFEGETGPYV QYAHARIQSI LRKADFTPSA DATYSLNDVE 

       490        500        510        520        530        540 
SWEIIKLLQD FPRIINRASD NFEPSIVAKF AISLAQAFNK YYAHTRILDE SPERDSRLAL 

       550        560 
CYATATVLKE ALRLLGVEAP DEM 

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-250 / LMG 18311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000023 Genomic DNA. Translation: AAV59777.1.
RefSeqYP_138592.1. NC_006448.1.

3D structure databases

ProteinModelPortalQ5M6I4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264199.stu0047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV59777; AAV59777; stu0047.
GeneID3164079.
KEGGstl:stu0047.
PATRIC19801584. VBIStrThe97850_0049.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSTHE264199:GI6K-68-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_STRT2
AccessionPrimary (citable) accession number: Q5M6I4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 1, 2005
Last modified: April 16, 2014
This is version 64 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