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B7J3R6 (SYR_ACIF2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 35. 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:AFE_0170
OrganismAcidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) [Complete proteome] [HAMAP]
Taxonomic identifier243159 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length579 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 – 579579Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198863

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B7J3R6 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 733F5D6CCB2118DC

FASTA57964,520
        10         20         30         40         50         60 
MKAFVSQALQ GALQQLHAQG RIPGIPATLE LDRPKQVEHG HLASNVALLL AKAVGRKPRD 

        70         80         90        100        110        120 
IADDIVAALP ASDWIARTEI AGPGFINFFL QPAAFHAVIH RVRTEKEHFG ANRNGAGQRL 

       130        140        150        160        170        180 
QMEFVSANPT GPLHVGHGRG AAYGASLANI LRFNGFDIFC EYYVNDAGRQ MDILAASVYL 

       190        200        210        220        230        240 
RYLEADKALP WPFPENGYRG DYVREIAAHL REQVGDRLRH AAVGLPNLPQ MSDGDIAIDT 

       250        260        270        280        290        300 
LIAHLKQSLG EDYRTLHSAG LDEILADIRD DLEGFGVHYE RWYSEGSLMD TGAVDSAVAA 

       310        320        330        340        350        360 
LEKAGHCYTQ EGALWFRATA FDDDKDRVLR RDNGAYTYFA SDVAYHAEKF ARGFTHVIDM 

       370        380        390        400        410        420 
WGADHHGYVP RVKAALRALG LDDQQLEVVL VQFAILYRGT EKISMSTRAG EFVTLRELRE 

       430        440        450        460        470        480 
EVGNDAARFF YVLRRADQHL DFDLELAKKH SEENPVFYIQ YAHARVYSLL RQSVEKGLSL 

       490        500        510        520        530        540 
PPADGVGLEI LQESREIALA DALWRFPEVV ATAARDREPH QIAFYLRELA AAFHTYYNST 

       550        560        570 
RILVEETPLR HARLTLCLAV AQSIANGLRL LGVSAPEQM 

« Hide

References

[1]"Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications."
Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S.
BMC Genomics 9:597-597(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23270 / DSM 14882 / NCIB 8455.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001219 Genomic DNA. Translation: ACK78518.1.
RefSeqYP_002424679.1. NC_011761.1.

3D structure databases

ProteinModelPortalB7J3R6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243159.AFE_0170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK78518; ACK78518; AFE_0170.
GeneID7134449.
KEGGafr:AFE_0170.
PATRIC20651679. VBIAciFer29821_0164.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycAFER243159:GH3S-170-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_ACIF2
AccessionPrimary (citable) accession number: B7J3R6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: April 16, 2014
This is version 35 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