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C1D5W4 (SYR_LARHH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 36. 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:LHK_01003
OrganismLaribacter hongkongensis (strain HLHK9) [Complete proteome] [HAMAP]
Taxonomic identifier557598 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeLaribacter

Protein attributes

Sequence length573 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 – 573573Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198912

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
C1D5W4 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 963EDDE0EF099AD2

FASTA57363,639
        10         20         30         40         50         60 
MTLTQLLHDK LAAALIAAGV PDAQPLLQPA SRPEFGDFQA NGVMAAAKQR KMNPRELAQQ 

        70         80         90        100        110        120 
VIDKLDLAGI ASKIEIAGPG FINITLAPDF LAKRLDTVLD DARLGVRSVT EPQRVMVEYS 

       130        140        150        160        170        180 
SPNLAKEMHV GHLRSTIIGD TLARVVEFLG NNMVRGNHVG DWGTQFGMLT AYLVETRQAG 

       190        200        210        220        230        240 
KADLELSDLE TFYRNAKIRF DEDPVFADTA RNYVVRLQGG DADVLKLWEQ FVDVSLAHCE 

       250        260        270        280        290        300 
AVYRKLGVGL TRADVRGESA YNDDLPVIVD ELAAKNLLSE DDGAKVVYLD EFRNHDGDPM 

       310        320        330        340        350        360 
GVIVQKKDGG FLYTTTDLGA VRYRHKELNL DRVIYVVDAR QSQHFQQMFT ICRKAGFAPE 

       370        380        390        400        410        420 
AMSLEHVGFG TMMGDDGKPF KTRSGGTVKL IELLDEAEER AYALVSEKNP DLPEEEKRKI 

       430        440        450        460        470        480 
AHAVGIGAVK YADLSKNRNS DYIFNWDLML AFEGNTAPYL QYAYTRVASI FRKVDRFDAS 

       490        500        510        520        530        540 
APLLITEPAE KQLALMLAQF SDVLNEVART CFPHLLTQYL YQVATQFMRF YEACPILKSE 

       550        560        570 
GATQASRLKL ARITADTLKT GLGLLGIEVL ESM 

« Hide

References

[1]"The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats."
Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.
PLoS Genet. 5:E1000416-E1000416(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLHK9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001154 Genomic DNA. Translation: ACO73995.1.
RefSeqYP_002795004.1. NC_012559.1.

3D structure databases

ProteinModelPortalC1D5W4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557598.LHK_01003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO73995; ACO73995; LHK_01003.
GeneID7756625.
KEGGlhk:LHK_01003.
PATRIC22299089. VBILarHon49832_0946.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycLHON557598:GHO5-1030-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_LARHH
AccessionPrimary (citable) accession number: C1D5W4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 36 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