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A9KH27 (SYR_COXBN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:CBUD_2109
OrganismCoxiella burnetii (strain Dugway 5J108-111) [Complete proteome] [HAMAP]
Taxonomic identifier434922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length592 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 – 592592Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198890

Regions

Motif134 – 14411"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A9KH27 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 94B7C490266795D4

FASTA59266,806
        10         20         30         40         50         60 
MIDLSTMKQQ IETLLNQAIE RLKTKGVLKP EVTPVIKITH TTDPQHGDFA TNLALTLSKA 

        70         80         90        100        110        120 
AGMRPHALAE KIVEALPPSG QITEVEIAGP GFINFFVTEG SYQTVVSSIL KAGKDYGRSE 

       130        140        150        160        170        180 
MGKGQRVHME YVSANPTGPL HVGHGRGAAY GACVANLLNA AGFEVHREYY VNDAGRQMGI 

       190        200        210        220        230        240 
LALSVWVRYL QGYEASIELP KNAYQGEYII DIAEALKAKY GKQFYHSVES IQAKIPEEID 

       250        260        270        280        290        300 
SNADPEAYLD AWVTAQKDLL GPKDFECVFQ AALDSILNDI KNDLEEFGVT YDDWFPESRL 

       310        320        330        340        350        360 
VREGLIQEGL DLLTKHGYVY EKNGAQWFRA TALGDEKDRV LIRKNGLPTY FAADVAYHLH 

       370        380        390        400        410        420 
KFNQGYDQII DIFGADHHGY IPRIRGFLKG LGKAPEKLHI LLVQFAILYR GNEKVSMSTR 

       430        440        450        460        470        480 
GGTFVTLREL RHEVGNDAAR FFYIMRKPDQ HLDFDLELAK SQSNENPVYY IQYAHARICS 

       490        500        510        520        530        540 
VFRQLKTTQK NWDRPRGMEN LSLLSTNYEK ELLATLGRYP EVIKRAAMNY APHLLAHYLQ 

       550        560        570        580        590 
TLANQFHTYY NAERFLIEDD NLRNARLNLI NAVQQIIRNG LTLLGVSAPE EM 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Dugway 5J108-111.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000733 Genomic DNA. Translation: ABS77583.2.
RefSeqYP_001425414.2. NC_009727.1.

3D structure databases

ProteinModelPortalA9KH27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434922.CBUD_2109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS77583; ABS77583; CBUD_2109.
GeneID5458316.
KEGGcbd:CBUD_2109.
PATRIC17924011. VBICoxBur32972_2078.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCBUR434922:GJTP-2216-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. 2 hits.
[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_COXBN
AccessionPrimary (citable) accession number: A9KH27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 25, 2008
Last modified: May 14, 2014
This is version 47 of the entry and version 2 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