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P0CL51 (SYR_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:STM1909
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length577 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 term3D-structure
Complete proteome
Reference 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 – 577577Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151602

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Secondary structure

............................................................................................. 577
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CL51 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 842D46DD38EB44B7

FASTA57764,275
        10         20         30         40         50         60 
MNIQALLSEK VSQAMIAAGA PADCEPQVRQ SAKVQFGDYQ ANGMMAVAKK LGMAPRQLAE 

        70         80         90        100        110        120 
QVLTHLDLSG IASKVEIAGP GFINIFLEPA FLAEQVQQAL ASDRLGVSQP TRQTIVVDYS 

       130        140        150        160        170        180 
APNVAKEMHV GHLRSTIIGD AAVRTLEFLG HHVIRANHVG DWGTQFGMLI AWLEKQQQEN 

       190        200        210        220        230        240 
AGDMALADLE GFYRDAKKHY DEDEAFAERA RNYVVKLQSG DTYFREMWRK LVDITMTQNQ 

       250        260        270        280        290        300 
ITYDRLNVTL TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EFKNKEGDPM 

       310        320        330        340        350        360 
GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWT IVRKAGYVPD 

       370        380        390        400        410        420 
SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER ARRLVAEKNP DMPADELEKL 

       430        440        450        460        470        480 
ANAVGIGAVK YADLSKNRTT DYIFDWDNML AFEGNTAPYM QYAYTRVLSV FRKANIDEQA 

       490        500        510        520        530        540 
LASAPVIISE DREAQLAARL LQFEETLTVV AREGTPHVMC AYLYDVAGLF SGFYEHCPIL 

       550        560        570 
SAENDAVRNS RLKLAQLTAK TLKLGLDTLG IETVERM 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL20825.1.
RefSeqNP_460866.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LLEmodel-A1-577[»]
ProteinModelPortalP0CL51.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP0CL51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20825; AAL20825; STM1909.
GeneID1253430.
KEGGstm:STM1909.
PATRIC32382373. VBISalEnt20916_2025.

Phylogenomic databases

HOGENOMHOG000247212.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1921-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_SALTY
AccessionPrimary (citable) accession number: P0CL51
Secondary accession number(s): P74871
Entry history
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 8, 2011
Last modified: April 16, 2014
This is version 24 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries