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Q3Z2Q4 (SYR_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. 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:SSON_1242
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length578 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 – 578578Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242092

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q3Z2Q4 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: B50A559519071827

FASTA57864,852
        10         20         30         40         50         60 
MNIQALLSEK VRQAMIAAGA PADCEPQVRH SAKVQFGDYQ ANGMMAVAKK LGMTPRQLAE 

        70         80         90        100        110        120 
QVLTHLDLNG IASKVEIAGP GFINIFLDPA FLAEHVQQAL ASDRLGVSTP EKQTIVVDYS 

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

       190        200        210        220        230        240 
AGDEMELADL EGFYRDAKKH YDEDEEFAER ARNYVVKLQS GDEYFREMWR KLVDITMTQN 

       250        260        270        280        290        300 
QITYDRLNVT LTRDDVMGES LYNPMLPGIV ADLKAKGLAV ESEGATVVFL DEFKNKEGEP 

       310        320        330        340        350        360 
MGVIIQKKDG GYLYTTTDIA CAKYRYETLH ADRVLYYIDS RQHQHLMQAW AIVRKAGYVP 

       370        380        390        400        410        420 
ESVPLEHHMF GMMLGKDGKP FKTRAGGTVK LADLLDEALE RARRLVAEKN PDMPADELEK 

       430        440        450        460        470        480 
LANAVGIGAV KYADLSKNRT TDYIFDWDNM LAFEGNTAPY MQYAYTRVLS VFRKAEINEE 

       490        500        510        520        530        540 
QLAAAPVIIR EDREAQLAAR LLQFEETLTV VAREGTPHVM CAYLYDLAGL FSGFYEHCPI 

       550        560        570 
LSAENEEVRN SRLKLAQLTA KTLKLGLDTL GIETVERM 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000038 Genomic DNA. Translation: AAZ87958.1.
RefSeqYP_310193.1. NC_007384.1.

3D structure databases

ProteinModelPortalQ3Z2Q4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300269.SSON_1242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ87958; AAZ87958; SSON_1242.
GeneID3666444.
KEGGssn:SSON_1242.
PATRIC18736239. VBIShiSon107113_1472.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycSSON300269:GJJF-1238-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_SHISS
AccessionPrimary (citable) accession number: Q3Z2Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 60 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