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A4VH02 (SYR_PSEU5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:PST_0547
OrganismPseudomonas stutzeri (strain A1501) [Complete proteome] [HAMAP]
Taxonomic identifier379731 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length579 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 – 579579Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018095

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A4VH02 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 3435F8CBF4D744B1

FASTA57964,116
        10         20         30         40         50         60 
MKDSIRHLIQ QALVRLTSEG VLPEGLTPAI QVENTKDKSH GDFASNIAMM LAKPAGMKPR 

        70         80         90        100        110        120 
ELAEKLIAAL PQDAQISKVE IAGPGFLNFF QNSDALAQRL ETALADAQLA VHKASAKQRV 

       130        140        150        160        170        180 
VIDLSSPNLA KEMHVGHLRS TIIGDAVGRV LEFLGDEVIR QNHVGDWGTQ FGMLLAYLEE 

       190        200        210        220        230        240 
KPAAAESELA DLEQFYRAAK QRFDESPEFA DRARELVVKL QAGDAQCLSL WTRFNDISLS 

       250        260        270        280        290        300 
HCQKIYDRLN VKLTPADVKG ESAYNADLAD IVEALREKGL LTEDNGAQCV FLDEFKNAEG 

       310        320        330        340        350        360 
NPLPVIVQKA GGGYLYATTD LAAMRYRSQQ LHADRVLYFV DQRQALHFQM AFEVARRAGF 

       370        380        390        400        410        420 
VHEGMQLEHM GFGTMNGADG RPFKTRDGGT VKLIDLLDEA EQRAYTLVKG KNPELDEAEL 

       430        440        450        460        470        480 
RQIARAVGIS AVKYADLSKH RTSDYRFNFE LMLSFEGNTA PYLLYAYTRV ASVFRKLGKG 

       490        500        510        520        530        540 
IDEISGQIQL DAEQELALAA KLAQFGEVLN SVGEKGEPHL LCAYLYDLAG LFSSFYEHCP 

       550        560        570 
ILGAEQEAQK QSRLRLAALT GRTLKQGLEL LGLEPLERM 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y. expand/collapse author list , Elmerich C., Lin M., Jin Q.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A1501.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000304 Genomic DNA. Translation: ABP78253.1.
RefSeqYP_001171095.1. NC_009434.1.

3D structure databases

ProteinModelPortalA4VH02.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING379731.PST_0547.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP78253; ABP78253; PST_0547.
GeneID5094774.
KEGGpsa:PST_0547.
PATRIC19961537. VBIPseStu31643_0564.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycPSTU379731:GJER-547-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_PSEU5
AccessionPrimary (citable) accession number: A4VH02
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 47 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