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B1KYT1 (SYR_CLOBM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:CLK_0517
OrganismClostridium botulinum (strain Loch Maree / Type A3) [Complete proteome] [HAMAP]
Taxonomic identifier498214 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length563 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 – 563563Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095353

Regions

Motif120 – 13011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B1KYT1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 1089717F4CA2B743

FASTA56363,917
        10         20         30         40         50         60 
MDYKNLVAER IKENTELEVD LIEKLIEIPP KKDMGDYAFP CFQLAKTFRK APNLIAEELK 

        70         80         90        100        110        120 
EKINKEGFEK VVTVGPYLNF FVDKTVLIKD VLEKVLNEKE KYGSSKVGEG KNVVVEYSSP 

       130        140        150        160        170        180 
NIAKPFHIGH LFTTAIGNAL YKILSFEGYN CIGINHLGDW GTQFGKLISA YRRWVDEEAL 

       190        200        210        220        230        240 
EKDAIGELLR IYVKFHEEAE KNPELEKEAR LNFKKLEDGS EEETELWNRF KDLSLKEFNK 

       250        260        270        280        290        300 
VYDMLGIKFD SLAGESFYSD KMDAVVQEID DKGLLVDSNG AKVVMLDDYN MPPCMIKKSD 

       310        320        330        340        350        360 
GATIYATRDL AAAMYRKKTY DFHKCIYVVG TPQALHFKQV FTTLKLMGHD WADDCKHVGF 

       370        380        390        400        410        420 
GLVKLANKKL STRNGDVVFL EDLLNQSVEE TLKIINEKNP NLKDKEGTAK KLGIGAVVFT 

       430        440        450        460        470        480 
YLKNNRERDI VFDWKEILSF DGETGPYVEY SYARGKSILR KAGELTGEAD YSKLSSKEEF 

       490        500        510        520        530        540 
ELAKLLGGFN DAIMNAIDKL EPAMVTRYVI EVAKAFNKFY NAHGILNAED NDVKLARVKL 

       550        560 
VEATCQVIKN ALNLLGIDVV EEM 

« Hide

References

[1]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Loch Maree / Type A3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000962 Genomic DNA. Translation: ACA55304.1.
RefSeqYP_001786465.1. NC_010520.1.

3D structure databases

ProteinModelPortalB1KYT1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498214.CLK_0517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA55304; ACA55304; CLK_0517.
GeneID6152185.
KEGGcbl:CLK_0517.
PATRIC19387654. VBICloBot822_1440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCBOT498214:GH05-1179-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_CLOBM
AccessionPrimary (citable) accession number: B1KYT1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 39 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