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B6JKP5 (SYR_HELP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 33. 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:HPP12_0316
OrganismHelicobacter pylori (strain P12) [Complete proteome] [HAMAP]
Taxonomic identifier570508 [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_1000095369

Regions

Motif119 – 12911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B6JKP5 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 0C9BD44F6491439C

FASTA54162,099
        10         20         30         40         50         60 
MHTLIKGVLE EILEEEVIIE YPKDREHGHY ATPIAFNLAK VFKKSPLVIA EELALKISTH 

        70         80         90        100        110        120 
EKTQGLFDSV VACKGYINFT LSLDFLERFT QKALELKERF GSQIKSERSQ KIFLEFVSAN 

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

       190        200        210        220        230        240 
ESVTYPEVFY KGEYIIEIAK KANNDLEPSL FKENEETIIE ILSGYAKDLM LLEIKDNLDA 

       250        260        270        280        290        300 
LGIHFDSYAS EKEVFKHKDA VFERLEKANA LYEKDSKIWL KSSLYQDESD RVLIKEDKSC 

       310        320        330        340        350        360 
TYLAGDIVYH DEKFKQNYTK YINIWGADHH GYIARVKASL EFLGHDSNKL EVLLAQMVRL 

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

       430        440        450        460        470        480 
YYIHYANSRI HTMLEKSPFS KEEVLQTPLT NLNAEEKYLL FSALSLPKAV ESSFEEYGLQ 

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


D 

« Hide

References

[1]"The complete genome sequence of Helicobacter pylori strain P12."
Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001217 Genomic DNA. Translation: ACJ07473.1.
RefSeqYP_002300953.1. NC_011498.1.

3D structure databases

ProteinModelPortalB6JKP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING570508.HPP12_0316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ07473; ACJ07473; HPP12_0316.
GeneID7010688.
KEGGhpp:HPP12_0316.
PATRIC20608578. VBIHelPyl2824_0333.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAPRVKGAI.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycHPYL570508:GJ8D-325-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_HELP2
AccessionPrimary (citable) accession number: B6JKP5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 33 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