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Q9HLE7 (SYR_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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:Ta0281
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length546 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

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
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 – 546546Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151658

Regions

Motif117 – 12711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q9HLE7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EB72B6D59406E078

FASTA54663,004
        10         20         30         40         50         60 
MLLFQDLRKD IYEIVSKRFR ISENDVYLDD TGHSDITIRV FRILKSPDGG ENAVMEIVRS 

        70         80         90        100        110        120 
ISEKDYVEKA LSEGGYINVW IKRTYMLREV LESIEKSGTY PDVFQEAERV SVEHTSANPT 

       130        140        150        160        170        180 
GPLHIGRARN SIIGDSIYRI LSRYGYRTVR QYFVNDSGKQ MISLYTAYIK YGGPITIENL 

       190        200        210        220        230        240 
LENYQKIYRE MEKDQSIEKE IEKNIERYEN ADPEVFGTLR KIAGVMLDGI ASTLKRIGIE 

       250        260        270        280        290        300 
FDEFDWESDL LLNGSVRKAI DMLETKEEDS ARYIEISGKK VFLTRKDGTT LYFARDIAYH 

       310        320        330        340        350        360 
LFKAENSEWI IDVLGEDHKD HAKSLNHVLK EMLKLENRVS FMYYSFITLE TGKMSTRRGN 

       370        380        390        400        410        420 
IVTLQDLVDR TYDEALKIVN EKRPDLSEEE RKKIAEVIAS SAVRYSIIRV SAPKPITFRW 

       430        440        450        460        470        480 
EEALNFESNS APFIMYSHAR AASILDKAPE PEQSYGMDMP KEEADLVKAM YVYPYYLKDA 

       490        500        510        520        530        540 
AQDLKPDLIA AYLISLVQKF NDFYGACRVI GTDPLTYARR IRIVKAYKQI LSDAGDLIGI 


KMLDQM 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445063 Genomic DNA. Translation: CAC11426.1.
RefSeqNP_393761.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HLE7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0281.

Proteomic databases

PRIDEQ9HLE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC11426; CAC11426; CAC11426.
GeneID1455910.
KEGGtac:Ta0281.

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247213.
KOK01887.
OMANPNGPLH.
ProtClustDBPRK01611.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001278. Arg-tRNA-ligase.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYR_THEAC
AccessionPrimary (citable) accession number: Q9HLE7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 71 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