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C1FK28 (SYR_CLOBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:CLM_1232
OrganismClostridium botulinum (strain Kyoto / Type A2) [Complete proteome] [HAMAP]
Taxonomic identifier536232 [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_1000198885

Regions

Motif120 – 13011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
C1FK28 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 1EA8D08F50243986

FASTA56364,027
        10         20         30         40         50         60 
MDYKNLVAER IKENTELEVD LIEKLIEIPP KKEMGDYAFP CFQLAKTFRK APNLIAEELK 

        70         80         90        100        110        120 
EKINKEGFEK VVTVGPYLNF FVDKTILIKD VLEKVLSEKE KYGSSKVGEG KNVVVEYSSP 

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

       190        200        210        220        230        240 
EKDAIGELLR IYVKFHEEAE KDPELEKEAR LNFKRLEEGS EEETELWNRF KDLSLKEFNK 

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

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

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

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

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

       550        560 
VEATCQVIKN ALNLLGIDVV EEM 

« Hide

References

[1]"Genome sequence of Clostridium botulinum A2 Kyoto."
Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Kyoto / Type A2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001581 Genomic DNA. Translation: ACO86384.1.
RefSeqYP_002803441.1. NC_012563.1.

3D structure databases

ProteinModelPortalC1FK28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING536232.CLM_1232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO86384; ACO86384; CLM_1232.
GeneID7765890.
KEGGcby:CLM_1232.
PATRIC19379013. VBICloBot91161_1132.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCBOT536232:GCO3-1189-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_CLOBJ
AccessionPrimary (citable) accession number: C1FK28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 35 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