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C4ZD15 (SYR_EUBR3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 32. 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:EUBREC_2239
OrganismEubacterium rectale (strain ATCC 33656 / VPI 0990) [Complete proteome] [HAMAP]
Taxonomic identifier515619 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length597 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 – 597597Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000203094

Regions

Motif124 – 13411"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
C4ZD15 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: C0B7B15F19EABD3A

FASTA59766,744
        10         20         30         40         50         60 
MKKLINLISE EVTKAFVSAG YDEKYGKVTL SNRPDLCEFQ CNGAMAAAKE YKCAPFMISD 

        70         80         90        100        110        120 
KVAALLESDE MFESVESVKP GFLNIKMDTA FLAKYMNDMK DDEGRYGLEK AKKPLTIVVD 

       130        140        150        160        170        180 
YGGPNVAKPL HVGHLRSAVI GESVKRIAKF MGHNVIGDVH LGDWGLQMGL IITELRERKP 

       190        200        210        220        230        240 
DLVYFDESYT GEYPKEAPFT ISELEDIYPT ASGKSKSDES FKEAALLATK ELQGGRRGYQ 

       250        260        270        280        290        300 
ALLSHIMNVS VTDLKRNYEN LNVHFELWKG ESDAQPYVPG MVEMMKEKGF AHMSEGALVV 

       310        320        330        340        350        360 
DVKEDTDTKE IPPCIILKSD GASLYSTTDL ATLVMRMKEN NPDRVIYLAD ARQSMHFIQV 

       370        380        390        400        410        420 
FRCARKTGIV PDTTELVHIG FGTMNGKDGK PFKTRDGGVM RLEYLLKEID DEMLNKIKEN 

       430        440        450        460        470        480 
QKEKENLNID EAEAEQTAKT VALAAVKYGD LSNQASKDYI FDIDRFTSFE GNTGPYILYT 

       490        500        510        520        530        540 
IVRIKSILSK YEAKGGDISA LKDAIMPAVN AGQKNLMLSL AKFNATIESA YEESAPHKIC 

       550        560        570        580        590 
AYIYELANAF NGFYHDTKIL SEENEELKKS YISLLVLTKE ILEACIDMLG FSAPDRM 

« Hide

References

[1]"Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla."
Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., Hettich R.L., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33656 / VPI 0990.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001107 Genomic DNA. Translation: ACR75978.1.
RefSeqYP_002938112.1. NC_012781.1.

3D structure databases

ProteinModelPortalC4ZD15.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING515619.EUBREC_2239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR75978; ACR75978; EUBREC_2239.
GeneID7965871.
KEGGere:EUBREC_2239.
PATRIC21872609. VBIEubRec107985_1950.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAPDITKAW.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycEREC515619:GHMX-2230-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.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. 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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_EUBR3
AccessionPrimary (citable) accession number: C4ZD15
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 32 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