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Q17X54 (SYR_HELAH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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:Hac_1002
OrganismHelicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]
Taxonomic identifier382638 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length541 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 – 541541Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018040

Regions

Motif119 – 12911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q17X54 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 9FCD83A0E07A9DA1

FASTA54162,118
        10         20         30         40         50         60 
MHTLIKSVLE EILEAEVIIE HPKDREHGHY ATPIAFNLAK IFKKSPLVIA EELALKISTH 

        70         80         90        100        110        120 
AKTQGFFDSV VACKGYINFT LSLDFLERFT QKALELKEKF GSKFKSENSQ KIFLEFVSAN 

       130        140        150        160        170        180 
PTGPLHIGHA RGAVFGDSLA KIARFLGHEV LCEYYVNDMG SQIRLLGLSV WLAYREHVLK 

       190        200        210        220        230        240 
EGVTYPEVFY KGEYIIEIAK KAHNDLEPSL FKENEETIIE VLSSYAKDLM LLEIKDNLDS 

       250        260        270        280        290        300 
LGIHFDSYAS EKEIFKHKDA VFKNLEKANA LYEKDSKIWL KSSLYQDESD RVLVKEDKNY 

       310        320        330        340        350        360 
TYLAGDIVYH NEKFKQNYTK YINIWGADHH GYIARVKASL KFLGYDSNKL EVLLAQMVGL 

       370        380        390        400        410        420 
LKDNEPYKMS KRAGNFILIK DVVDDIGKDA LRFIFLSKRL DTHLEFDVNT LKKQDSSNPI 

       430        440        450        460        470        480 
YYIHYANSRI HTMLEKSPFS KEEILQTPLK NLNAEEKYLL FSALSLPKII EASFEEYGLQ 

       490        500        510        520        530        540 
KMCEYAKTLA SEFHRFYNAG KILDTPKTKE LLKICLMVSL SLTNAFKLLG IEIKTKISAK 


D 

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References

[1]"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sheeba.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260522 Genomic DNA. Translation: CAJ99772.1.
RefSeqYP_664771.1. NC_008229.1.

3D structure databases

ProteinModelPortalQ17X54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382638.Hac_1002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ99772; CAJ99772; Hac_1002.
GeneID4176931.
KEGGhac:Hac_1002.
PATRIC20585849. VBIHelAci71660_0939.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAYNARENG.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycHACI382638:GJAU-927-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_HELAH
AccessionPrimary (citable) accession number: Q17X54
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: April 16, 2014
This is version 55 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