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Q3SF80 (SYR_THIDA) 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:Tbd_2782
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length557 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 – 557557Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242113

Regions

Motif128 – 13811"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q3SF80 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 90F27FD24BC1CE27

FASTA55761,607
        10         20         30         40         50         60 
MSSTHPLKDQ LALLIEAALE ALAPDAPVSL EIERPKNPTH GDFSSNAAMQ LARPLKRNPR 

        70         80         90        100        110        120 
ELAQLIVTEL PASTLVAKAD IAGAGFINFH LTPAAWHGIV RQVRTAGAQF GRAQRETPQR 

       130        140        150        160        170        180 
VLIEFVSANP TGPLHVGHGR QAALGDALCN LYAAQGWDVY REFYYNDAGV QIATLAASVQ 

       190        200        210        220        230        240 
ARARGLQPGD ATWPEAAYNG DYIADIARDF LAGKTVKSDD REFTASGDVD DLDSIRQFAV 

       250        260        270        280        290        300 
AYLRHEQDLD LRAFAVHFDN YYLESSLYTD GRVDATVQRL VAAGKTYEQD GALWLRTTEY 

       310        320        330        340        350        360 
GDDKDRVMKK SDGTYTYFVP DVAYHIAKWE RGFARAINIQ GTDHHGTIAR VRAGLQAASV 

       370        380        390        400        410        420 
GIPEGYPDYL LHTMVRVMRG GEEVKISKRA GSYVTLRDLI EWTSKDAVRF FLLSRKADTE 

       430        440        450        460        470        480 
YVFDIDLALA RNNDNPVYYV QYAHARICRV FEEWSGDVAT LADADLAPLE AAHELALMQR 

       490        500        510        520        530        540 
LAEYPETVAS AARDLAPHLL VHYLQMLAGD FHAWYNAEKF LVADEATKRA RLALADATRI 

       550 
VIVNGLALLG VDAPEKM 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ98735.1.
RefSeqYP_316540.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SF80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_2782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ98735; AAZ98735; Tbd_2782.
GeneID3672848.
KEGGtbd:Tbd_2782.
PATRIC23971767. VBIThiDen82923_2768.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTDEN292415:GHWG-2834-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_THIDA
AccessionPrimary (citable) accession number: Q3SF80
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 11, 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