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Q5X3M1 (SYR_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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:lpp2013
OrganismLegionella pneumophila (strain Paris) [Complete proteome] [HAMAP]
Taxonomic identifier297246 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length589 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 – 589589Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242038

Regions

Motif131 – 14111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5X3M1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 8C6DAF46BF0F8CF5

FASTA58966,082
        10         20         30         40         50         60 
MRSMKAIIEY LLKQALINLQ QSGEMPIDLE VEIKVENAKD PSHGDYATNL ALVLAKPCRQ 

        70         80         90        100        110        120 
APKVLAERLV AVIPADPSVE KIEIAGAGFI NFFMRSTARS LIISEILNKG KEFGRGNLGQ 

       130        140        150        160        170        180 
SQKVLIEFVS ANPTGPLHVG HGRGAAFGAT LGNVLKAAGY DVTLEYYVND AGRQMNILAV 

       190        200        210        220        230        240 
SVWLRYLELA GEPIVFPTNG YKGQYVYEIA QEMWSEQGNQ FVHPWISVVE NLPADEPEGG 

       250        260        270        280        290        300 
DKETYIDAII ARAQSLLGKD GFANFHQHAL KTVLDDIKDD LQAFGVRFDS WFSEQSLFED 

       310        320        330        340        350        360 
GSIEKGIQAL KDRGHTYERE GALWFRATDF GDEKDRVLVR ANGQTTYFAS DVAYHWNKYD 

       370        380        390        400        410        420 
RGFDRVIDIF GADHHGYVTR IKTAVKALGH DESALDVILV QFAILYRGGD RVQMSTRSGS 

       430        440        450        460        470        480 
FVTLRELREE VGNDAARYFY VARKPEQHMD FDLDLAKSES SDNPVYYIQY AHARICSVLR 

       490        500        510        520        530        540 
QLKERGLKWD KDMGLKNLDL LEQQHETTLI SLIARYPEVI QSAAASCEPH QLAYYLRELA 

       550        560        570        580 
NGLHSYYNAI QLLCEQEQLR CARLCLLESV RQVLNNGLAI LGVSAPESM 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628336 Genomic DNA. Translation: CAH13165.1.
RefSeqYP_124327.1. NC_006368.1.

3D structure databases

ProteinModelPortalQ5X3M1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297246.lpp2013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH13165; CAH13165; lpp2013.
GeneID3116398.
KEGGlpp:lpp2013.
PATRIC22324511. VBILegPne27771_2301.

Organism-specific databases

LegioListlpp2013.
CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

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_LEGPA
AccessionPrimary (citable) accession number: Q5X3M1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 65 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