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B8FCL2 (SYR_DESAA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 32. 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:Dalk_4496
OrganismDesulfatibacillum alkenivorans (strain AK-01) [Complete proteome] [HAMAP]
Taxonomic identifier439235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfatibacillum

Protein attributes

Sequence length556 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 – 556556Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198894

Regions

Motif129 – 13911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B8FCL2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: DF31DB5AFFE31720

FASTA55662,972
        10         20         30         40         50         60 
MKEILAEMIT RAAFKAHEQG VLPSDAIPQP GLEEPKQEAH GDFSTNIAMV MAKVQKMAPR 

        70         80         90        100        110        120 
KIAEAIVDNL EDPENFLVKT EIAGPGFINF YLRPSLWQRV VKGILDKGDE YGRSQIGAGQ 

       130        140        150        160        170        180 
KVQVEFVSAN PTGPLHVGHG RGAAVGDALA ALLDMCGFEV EREYYINDSG RQIRTLGLST 

       190        200        210        220        230        240 
WLRYCELKGK EIDFPKDCYQ GDYIKDLAKR IQDENLADLD SMEEEDAVLW CARFAANDIL 

       250        260        270        280        290        300 
DGIKQDLKDF RVVHDVWFSE QSLYDDNSVQ NALEHFEKTG DIYEKDGAKW FKTEDRGDEK 

       310        320        330        340        350        360 
DRVVVRNNGL TTYFASDIAY HKNKFDRGFD RVIDVWGADH HGYVARMKAA VDAVGRDKDA 

       370        380        390        400        410        420 
FEVVLVKLVN LLRDGEPLAM TTRGGTFETL ADVVNEVGAD AARFIFLSRH YESPLDFDLE 

       430        440        450        460        470        480 
LAKKQTNENP VWYVQYVHAR ICSIEAKAKD FPVSLDFDWD RDEEILKEIE EIRLMKALAR 

       490        500        510        520        530        540 
YPEVVEGAAR TLEPHRIVFY LRELASAFHS FYHDHMVLKE DQTPVLTKAR LDLVTTVRQV 

       550 
IRNGLALLGV SAPESM 

« Hide

References

[1]"Complete sequence of Desulfatibacillum alkenivorans AK-01."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Wawrik B., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AK-01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001322 Genomic DNA. Translation: ACL06175.1.
RefSeqYP_002433643.1. NC_011768.1.

3D structure databases

ProteinModelPortalB8FCL2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439235.Dalk_4496.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL06175; ACL06175; Dalk_4496.
GeneID7168459.
KEGGdal:Dalk_4496.
PATRIC21655926. VBIDesAlk8144_4790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDALK439235:GHP2-4552-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_DESAA
AccessionPrimary (citable) accession number: B8FCL2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 32 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