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A1VEG5 (SYR_DESVV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:Dvul_1814
OrganismDesulfovibrio vulgaris subsp. vulgaris (strain DP4) [Complete proteome] [HAMAP]
Taxonomic identifier391774 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length551 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 – 551551Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018021

Regions

Motif125 – 13511"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A1VEG5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 820AB17CA4856C10

FASTA55160,537
        10         20         30         40         50         60 
MRAKKQLLAA LQDIVKDMGL AWPEKATIDT PKATGFGDLA ANIALVLAKQ AGQNPRELAT 

        70         80         90        100        110        120 
RIADALRNRD ADITAIDIAG PGFLNVTYSQ DFWRETILRA QEAGSAFGSS DTGAGRKVQV 

       130        140        150        160        170        180 
EYVSANPTGP LHIGHGRGAA VGDSLARIMR FAGYDVSTEY YINDAGRQMR LLGLSVWVRA 

       190        200        210        220        230        240 
KELAGRPVTL PEDFYRGDYI KDIARELMEK EPGLLDLDDA AGEDRCFAYA MNSILDGIKQ 

       250        260        270        280        290        300 
DLADFRVEHQ VWFSERSLVE GGAVEKTFNR LKEAGLAFEQ DGALWFRTTD FGDDKDRVLR 

       310        320        330        340        350        360 
KSDGTLTYFS SDIAYHDNKY DRGFDLVVDI WGADHHGYIP RMRAAVAALG RKPEAFDVVL 

       370        380        390        400        410        420 
IQLVNLLRGG ELVAMSTRAG QFETLADVVK ETGADAARFM FLSRKSDSPL DFDLELVKQR 

       430        440        450        460        470        480 
TMDNPVYYVQ YAHARVCSVL RKAAERGIEM PAQLDGASLA PLSGDDEMEL LRLLDRFEET 

       490        500        510        520        530        540 
VAGAATALAP HHISHYLMEV AGALHSYYAR QPILNATEQD VIVPRLALLR AVGCVLANGL 

       550 
SLLGVSAPES M 

« Hide

References

[1]"Contribution of mobile genetic elements to Desulfovibrio vulgaris genome plasticity."
Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S., He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P., Stahl D.A.
Environ. Microbiol. 11:2244-2252(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000527 Genomic DNA. Translation: ABM28831.1.
RefSeqYP_967258.1. NC_008751.1.

3D structure databases

ProteinModelPortalA1VEG5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391774.Dvul_1814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM28831; ABM28831; Dvul_1814.
GeneID4662105.
KEGGdvl:Dvul_1814.
PATRIC21767508. VBIDesVul62463_2027.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycDVUL391774:GHS0-1871-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_DESVV
AccessionPrimary (citable) accession number: A1VEG5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 52 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