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A9WNA7 (SYR_RENSM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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:RSal33209_1427
OrganismRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP]
Taxonomic identifier288705 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeRenibacterium

Protein attributes

Sequence length549 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 – 549549Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000076225

Regions

Motif132 – 14211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A9WNA7 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: A03BADE8C2B731C5

FASTA54959,074
        10         20         30         40         50         60 
MTPDELSVAL TACLKAAVEA GELVVPTEAV PAEVRVERPK NRDHGDWATN IALQLAKPAG 

        70         80         90        100        110        120 
LNPRAVAEIL KSRLEAIEGV AAVDIAGPGF LNITLDAAAA GALAKNIVHA GSQYGENQAL 

       130        140        150        160        170        180 
TGQVINVEFV SANPTGPLHL AHTRWAAVGD SVARLLKASG ATVTSEYYIN DAGSQMNNFG 

       190        200        210        220        230        240 
ASVLAAIKGE PTPEGGYPGA YITELAQQVV RDHPYVTELT DEAALPVVRA AAYLAQLADI 

       250        260        270        280        290        300 
KETLNDFGVH FDVFFSEQEL HSTGAVEKAV DRLRGQGHVF YQDGAIWLRT TDFTDDKDRV 

       310        320        330        340        350        360 
LIRANGEPTY FAADAAYYLS KKDRGFVEKI YLLGADHHGY IGRLKAIAAC AGDDPARNIE 

       370        380        390        400        410        420 
VLIGQMVSVN GARLSKRAGN IVELRDLLNW LGADALRYSL GRSPADSPLA LEPEQLQKAS 

       430        440        450        460        470        480 
NDNPVFYVQY AHARTKAVDR NAEAAGVDRS AFEASLLTHP TESNLLAQLG AFPSVVAEAA 

       490        500        510        520        530        540 
KFREPHRVAR HLEVVAGTYH RWYDACRVTP FAGEEITDLN RTRLWLNDAT GQVLANGLDL 


LGVSAPERM 

« Hide

References

[1]"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000910 Genomic DNA. Translation: ABY23163.1.
RefSeqYP_001624577.1. NC_010168.1.

3D structure databases

ProteinModelPortalA9WNA7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288705.RSal33209_1427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY23163; ABY23163; RSal33209_1427.
GeneID5821312.
KEGGrsa:RSal33209_1427.
PATRIC23076111. VBIRenSal21953_1475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycRSAL288705:GHX1-1427-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.
InterProIPR001278. 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.
ProtoNetSearch...

Entry information

Entry nameSYR_RENSM
AccessionPrimary (citable) accession number: A9WNA7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 41 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