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Q8U149 (SYR_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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:PF1380
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length629 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 – 629629Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151652

Regions

Motif128 – 13811"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q8U149 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 9AEA216208AB71DF

FASTA62972,281
        10         20         30         40         50         60 
MMETIKSEIK RTIEGIVREM APDWSEDIQF VDTPSPELGD FGTPVAFQLA RLLRKSPLII 

        70         80         90        100        110        120 
AQEIAEKFNK NKPKEVKKAI AVNGYVNFFL DYPQISKLVI EAILGYGTEY GRSEIGKGKK 

       130        140        150        160        170        180 
VIVEHTSVNP TKPLHMGHAR NAILGDTVAR ILRFLGYQVE VQNYIDDLGV QFAQVYWGYL 

       190        200        210        220        230        240 
NLKRKFDELM KELKEKIPKN NPIDHVLGLL YVEVNKKIEE SSEVEKEIRE LMKKLEEREL 

       250        260        270        280        290        300 
NGRKLAEEVV KAQMETLYSL NIYYDLLVWE SDIVSTRLFE KTIKLLEKNE NFYTPKEGKY 

       310        320        330        340        350        360 
KGAFVMDLSK LFPDMKNPYL VLRRSDGTAT YTGKDIAYHL WKFGKIDIDL MYKKWDEHTW 

       370        380        390        400        410        420 
TTAPDGEPIP GKFGAGDIVI NVIGAEQRHP QLAIKYALEL LGYKDAAENF HHLAYEHVES 

       430        440        450        460        470        480 
PEGKFSGRKG TWVGFTVDEV IAEAINKAKS LIEEKNPNLT EEEKEEIAKK VAVGAIRYTL 

       490        500        510        520        530        540 
IKYSPEKKIV FRWEDVLNFE GESAPYIQYA HARCSSILRK AEELGISTDW KSLLKVANFN 

       550        560        570        580        590        600 
QITEKERELI MLLSRFPEIV QQAGTDLKPH LIAWYANEVA STFNKFYMDH PVIKAEEGVR 

       610        620 
EARLLLVMAT RQVLRNSLWL MGIEAPDKM 

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL81504.1.
RefSeqNP_579109.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1380.

Proteomic databases

PRIDEQ8U149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81504; AAL81504; PF1380.
GeneID1469256.
KEGGpfu:PF1380.

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247213.
KOK01887.
OMANPNGPLH.
ProtClustDBPRK01611.

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. 2 hits.
[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_PYRFU
AccessionPrimary (citable) accession number: Q8U149
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 75 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