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Q9PNC0 (SYR_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:Cj1175c
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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 – 530530Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242001

Regions

Motif113 – 12311"HIGH" region HAMAP-Rule MF_00123

Secondary structure

................................................................... 530
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9PNC0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D2C9B35AF857B2B8

FASTA53060,190
        10         20         30         40         50         60 
MKSIIFNEIK KILECDFALE NPKDKNLAHF ATPLAFSLAK ELKKSPMLIA SDLASKFQNH 

        70         80         90        100        110        120 
DCFESVEAVN GYLNFRISKT FLNELANQAL TNPNDFTKGE KKQESFLLEY VSANPTGPLH 

       130        140        150        160        170        180 
IGHARGAVFG DTLTRLARHL GYKFNTEYYV NDAGNQIYLL GLSILLSVKE SILHENVEYP 

       190        200        210        220        230        240 
EQYYKGEYIV DLAKEAFEKF GKEFFSEENI PSLADWAKDK MLVLIKQNLE QAKIKIDSYV 

       250        260        270        280        290        300 
SERSYYDALN ATLESLKEHK GIYEQEGKIW LASSQKGDEK DRVIIREDGR GTYLAADIVY 

       310        320        330        340        350        360 
HKDKMSRGYG KCINIWGADH HGYIPRMKAA MEFLGFDSNN LEIILAQMVS LLKDGEPYKM 

       370        380        390        400        410        420 
SKRAGNFILM SDVVDEIGSD ALRYIFLSKK CDTHLEFDIS DLQKEDSSNP VYYINYAHAR 

       430        440        450        460        470        480 
IHQVFAKAGK KIDDVMKADL QSLNQDGVNL LFEALNLKAV LNDAFEARAL QKIPDYLKNL 

       490        500        510        520        530 
AANFHKFYNE NKVVGSANEN DLLKLFSLVA LSIKTAFSLM GIEAKNKMEH 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35290.1.
PIRA81323.
RefSeqYP_002344566.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FNRX-ray2.20A78-530[»]
ProteinModelPortalQ9PNC0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9PNC0. 3 interactions.
STRING192222.Cj1175c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35290; CAL35290; Cj1175c.
GeneID905465.
KEGGcje:Cj1175c.
PATRIC20059306. VBICamJej33762_1156.

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMARFIMLTR.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-1146-MONOMER.

Family and domain databases

Gene3D3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase_Ia.
IPR015945. Arg-tRNA-synth_Ia_core.
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...

Other

EvolutionaryTraceQ9PNC0.

Entry information

Entry nameSYR_CAMJE
AccessionPrimary (citable) accession number: Q9PNC0
Secondary accession number(s): Q0P981
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 80 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries