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Q87RD6 (SYR_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:VP0861
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length577 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 – 577577Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151633

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q87RD6 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 8BF8273F071A48D2

FASTA57763,871
        10         20         30         40         50         60 
MNIQALINDK VSQALEAAGA PAGSPAAVRQ SAKPQFGDYQ ANGVMGVAKK LGTNPREFAQ 

        70         80         90        100        110        120 
KVLDVLDLDG IASKTEIAGP GFINIFLSEE FLAKQADAAL ADSRLGVAAE EAQTIVADYS 

       130        140        150        160        170        180 
APNVAKEMHV GHLRSTIIGD AVVRTLEFLG HKVIRANHIG DWGTQFGMLI ANLERVQQES 

       190        200        210        220        230        240 
GEVSMELADL EGFYRESKKL YDEDEEFAVK ARNYVVKLQS GDEFCAEMWK KLVDVTMIQN 

       250        260        270        280        290        300 
QRNYDRLNVS LTRDDVMGES MYNDMLPKIV ADLKAQGLAV EDDGAQVVFL EEFKNKDGEA 

       310        320        330        340        350        360 
MGVIVQKRDG GFLYTTTDIA CAKYRYEELG ADRVLYFIDS RQHQHLMQAW TIVRKAGYVP 

       370        380        390        400        410        420 
ESVSLEHHAF GMMLGKDGKP FKTRAGGTVR LADLLDEAEV RAAQLIESKN PELDAEEKEK 

       430        440        450        460        470        480 
ISKTVAMAAV KYSDLSKHRT TDYVFDWDNM LAFEGNTAPY MQYAYTRVAS IFAKAGVAMD 

       490        500        510        520        530        540 
ELQGDIQITD EKEKALIAKL LQFEEAVQSV AREGQPHIMC SYLFELAGQF SSFYEACPIL 

       550        560        570 
VAEDEAVKQS RLKLAALTAK TIKQGLSLLG IETLERM 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC59124.1.
RefSeqNP_797240.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87RD6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP0861.

Protocols and materials databases

DNASU1188358.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC59124; BAC59124; BAC59124.
GeneID1188358.
KEGGvpa:VP0861.
PATRIC20139940. VBIVibPar50997_0815.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycVPAR223926:GHK4-902-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_VIBPA
AccessionPrimary (citable) accession number: Q87RD6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: April 16, 2014
This is version 72 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