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Q2S3W3 (SYR_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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:SRU_0986
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP]
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length562 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 – 562562Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242087

Regions

Motif126 – 13611"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q2S3W3 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 08A98C82AEAAA7ED

FASTA56262,397
        10         20         30         40         50         60 
MKDYLRTQIR RVLDALGDVP DDFEIELEAP DRPEHGDLAT NTALRLASVL GDNPRSIAET 

        70         80         90        100        110        120 
LAERLRERVD PARIKSVEVA GPGFVNFRFA QDYLFDGLAD LLAQGDTFGQ TDAGAGERAL 

       130        140        150        160        170        180 
VEYVSANPTG PLNVGHGRNA VLGDTIANLL AWTGYDVTRE YYYNDAGRQM RVLAQSVRAR 

       190        200        210        220        230        240 
YEALAGNVPT TTLTLDDDTT VEVPETFPED GYLGQYIVEI AQALYDEHGD ALCATDDLAP 

       250        260        270        280        290        300 
FRAAAETAIF GDIEATLRAL NIDMDGYANE QALHDEGRVD AVLDGLADAG YTYEEDGALW 

       310        320        330        340        350        360 
FKTTEFGTED DTVLVKQTGE PTYRTPDIAY HTAKFERGFD LMVDVFGADH HAAYPDVLSA 

       370        380        390        400        410        420 
LDVLGYDTDR VDVILYQFVT LVRGDEPVKM STRRANYVTL DDLIEQVGAD VTRFFFLMRS 

       430        440        450        460        470        480 
PDTHLNFDLE LAEEESEKNP VFYLQYAHAR ICSVLDKAEE VGFSHDEDAD LALLTHEDEI 

       490        500        510        520        530        540 
ALIKELLRFP RELQNAADAR APHFVPNYLR DVATAFSQFY DNCRIIGEEQ ELASARMRLA 

       550        560 
LAAKTVLKNG LTVLGISAPR QM 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC46058.1.
RefSeqYP_445118.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S3W3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_0986.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC46058; ABC46058; SRU_0986.
GeneID3851895.
KEGGsru:SRU_0986.
PATRIC23424357. VBISalRub86502_1023.

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
PhylomeDBQ2S3W3.
ProtClustDBCLSK2775157.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-984-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_SALRD
AccessionPrimary (citable) accession number: Q2S3W3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 63 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