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Q7NWM1 (SYR_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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:CV_1962
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium

Protein attributes

Sequence length572 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 – 572572Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151549

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q7NWM1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 8818CA5CE234A80A

FASTA57263,582
        10         20         30         40         50         60 
MTIHQLINER VQAALAAAGA PDAPAVVQPA SKPEFGDYQA NGVMGAAKAL KTNPRALAEK 

        70         80         90        100        110        120 
VVAALDLAGI ADKVEIAGPG FINIHLAPEY LARRSEAALK DDKLGIAPVK PLRVMVEYSS 

       130        140        150        160        170        180 
PNLAKEMHVG HLRSSIIGDA LARVMEYVGH DVVRANHVGD WGTQFGMLVA YLVETRHAGD 

       190        200        210        220        230        240 
ADLQLSDLET FYRNAKIRFD ESEDFANTAR DYVVKLQGGD EEVLKLWRQF VDVSLKHCED 

       250        260        270        280        290        300 
VYEKLNVGLK REHVRGESSY NDDLPVIVQE LREKGLLTED DGAQVVFLDE FRTQEDKPMG 

       310        320        330        340        350        360 
VIVQKKDGGF IYTTTDIGAV RYRHRELKLD RVIYVVDARQ SQHFAQMFTI CRKAGFAPEA 

       370        380        390        400        410        420 
MKLEHVGFGV MMGDDGKPFK TRSGGTVKLI ELLNEAEERA YALVSEKNPD LSDAQKREIA 

       430        440        450        460        470        480 
NAVGIGAVKY ADLSKNRMSD YIFNWDTMLA FEGNTAPYLQ YAYTRVQSVF RKAEDYDANA 

       490        500        510        520        530        540 
RIVITEPAEK QLAAALAQFE DTLNSVVEGC YPHYLSLYLY QIATLFSRFY EACPILKSEG 

       550        560        570 
EVRASRLQLA ALTAKTLRTG LDLLGIKVLE SM 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ59634.1.
RefSeqNP_901632.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NWM1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_1962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ59634; AAQ59634; CV_1962.
GeneID2549042.
KEGGcvi:CV_1962.
PATRIC21438710. VBIChrVio67196_1911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAPHIIFEN.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-2017-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_CHRVO
AccessionPrimary (citable) accession number: Q7NWM1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 76 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