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Q5HTT9 (SYR_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:CJE1309
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length530 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 – 530530Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242002

Regions

Motif113 – 12311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5HTT9 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: C36AB8867A4445BB

FASTA53060,160
        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 
EQYYKGEYIA DLAKEAFEKF GKEFFSQENI 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 SDVVNEIGSD 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]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35630.1.
RefSeqYP_179296.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HTT9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE1309.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW35630; AAW35630; CJE1309.
GeneID3231816.
KEGGcjr:CJE1309.
PATRIC20044418. VBICamJej134361_1327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAIRNTIND.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-1335-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_CAMJR
AccessionPrimary (citable) accession number: Q5HTT9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 62 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