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Q2KTN9 (SYR_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:BAV3361
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length561 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 – 561561Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000241992

Regions

Motif129 – 13911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q2KTN9 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: B606CF5844884694

FASTA56161,604
        10         20         30         40         50         60 
MLPEQQQHLI SLLARAVAGI LPEASPDILL ERPKVAAHGD VATNVAMQLA KPAKRNPREL 

        70         80         90        100        110        120 
AQGIVDALLA DPQARAIVDS AEIAGPGFIN LRFTAQARQA VVAAVSAQGA AFGRAARRDE 

       130        140        150        160        170        180 
KVLVEFVSAN PTGPLHVGHA RQAALGDAIC RLFDASGWDV TREFYYNDAG NQIQNLAISV 

       190        200        210        220        230        240 
QARARGIGPD APEWPADGYK GDYIADIARD YLAQASVQAA DGEPVQASGN IDDLEDIRAF 

       250        260        270        280        290        300 
AVAYLRREQD LDLQAFGLKF DNFFLESSLY TSGRVERTVE TLIAKGHTYE QDGALWLRTT 

       310        320        330        340        350        360 
ELGTGDDKDR VMRKSEGGYT YFVPDVAYHL AKWERGFHHA INIQGSDHHG TVARVRAGLQ 

       370        380        390        400        410        420 
GLEEGIPKEF PAYVLHKMVK VMRGGEEVKI SKRAGSYVTM RDLIEWVGRD AVRYFLIQRR 

       430        440        450        460        470        480 
ADTEFVFDID LALSKSDENP VYYIQYAHAR ICSMIASSGL DDATIAAADA ARLTAPSEFA 

       490        500        510        520        530        540 
LMQRLAEFPN VVKLAAQELA PHHIAFWLRD CASDFHGWYN AERVLVDDEG LKQARLRLAA 

       550        560 
TTRQVLANGL ALLGVTALER M 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ50971.1.
RefSeqYP_787856.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2KTN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV3361.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6266525.
KEGGbav:BAV3361.
PATRIC21133051. VBIBorAvi43433_3400.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAPRVKGAI.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBAVI360910:GCKI-3440-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_BORA1
AccessionPrimary (citable) accession number: Q2KTN9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 53 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