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Q5E6L2 (SYR_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:VF_0839
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

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
Reference 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_0000242119

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5E6L2 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: D8828B87E812FA1B

FASTA57764,101
        10         20         30         40         50         60 
MNIQSLINDK VSQALEAAGA PAGSPAAVRQ SAKAQFGDYQ ANGVMGVAKR LGTNPREFAQ 

        70         80         90        100        110        120 
KVLDVLDLDG IASKTEIAGP GFINIFLSEE FLAKQAEAAL ADERLGVAKE EQQNIVADYS 

       130        140        150        160        170        180 
APNVAKEMHV GHLRSTIIGD AVVRTLEFLG HNVTRANHIG DWGTQFGMLI ANLERIQKEK 

       190        200        210        220        230        240 
GEVSMELSDL EGFYRESKKL YDEDEEFAVT ARGYVVKLQS GDEFCAEMWK KLVDVTMVQN 

       250        260        270        280        290        300 
QRNYDRLNVS LTRDNVMGES MYNSMLAPIV ADLQKQGLAV ESEGAQVVFL DEYKNKDGEP 

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

       370        380        390        400        410        420 
ESVSLEHHAF GMMLGKDGRP FKTRAGGTVR LADLLDEAEE RATKLIEEKN KDLSAEEKAK 

       430        440        450        460        470        480 
IATTVAMAAV KYSDLSKHRT TDYIFDWDNM LAFEGNTAPY MQYAYTRVAS IFSKAGLSMD 

       490        500        510        520        530        540 
ELTGEVKITD EKEKALVAKL MQFEEAVQAV ASEGQPHLMC AYLFELAGQF SSFYEACPIL 

       550        560        570 
NNEDDAVKQS RLKLAALTAK TIKQGLELLG IETLERM 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW85334.1.
RefSeqYP_204222.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E6L2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_0839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW85334; AAW85334; VF_0839.
GeneID3277453.
KEGGvfi:VF_0839.
PATRIC20112252. VBIVibFis127983_0832.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycAFIS312309:GIWP-888-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_VIBF1
AccessionPrimary (citable) accession number: Q5E6L2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 61 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