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A5N8F9 (SYR_CLOK5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:CKL_1548
OrganismClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) [Complete proteome] [HAMAP]
Taxonomic identifier431943 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length566 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 – 566566Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000076210

Regions

Motif120 – 13011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A5N8F9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 6FAE822C077322CC

FASTA56665,277
        10         20         30         40         50         60 
MDFKKLAAEE IKKNIDLELN FIEGLIEVPP KPEMGDYAFP CFQLAKVLKK APNIISKELK 

        70         80         90        100        110        120 
DKLHSKYFEK IENLGPYVNF FVDKKIFTEY TLKEILLKGD SYGSSDMGEG KNVVVEYSSP 

       130        140        150        160        170        180 
NIAKPFHVGH LFSTSIGNAL YKMINFQGYN CTRINHLGDW GTQFGKLIAA YNRWCNAEEL 

       190        200        210        220        230        240 
NRDPIKELLR IYVKFHEEAE KDPSLNEEGR MYFKKLEDGS EEEIKLWKKF KDLSLREFKK 

       250        260        270        280        290        300 
VYDLLKVDFD SYAGESFYTD KMDAVVEEID KKGLLVESNG AKVVLLDEYN IPPCIVKKSD 

       310        320        330        340        350        360 
GTTIYATRDL AAAIYRKKTY DFYKSIYVVG LDQSLHFKQV FTTLKLMGKD WADSCKHVGF 

       370        380        390        400        410        420 
GLVRFANKKL STRKGDVIFL EELLNKSVER TLEIINEKNP KLENKEEAAK KIGIGAVIFT 

       430        440        450        460        470        480 
YLKNNREKDI VFDWNEMLSF EGETGPYVQY SYARGKSILR KSEEASYDEN QIDYSKLGSK 

       490        500        510        520        530        540 
EEFELVKILE NFNKSIINAI NRLEPFIVTR YVIDVAKAFN KFYNAHSIMN AADENIKKAR 

       550        560 
LYLVKCTCQV LKNGLNLMGI EVVEKM 

« Hide

References

[1]"The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features."
Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., Hagemeier C., Thauer R.K., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8527 / DSM 555 / NCIMB 10680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000673 Genomic DNA. Translation: EDK33590.1.
RefSeqYP_001394938.1. NC_009706.1.

3D structure databases

ProteinModelPortalA5N8F9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING431943.CKL_1548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEDK33590; EDK33590; CKL_1548.
GeneID5391058.
KEGGckl:CKL_1548.
PATRIC19464559. VBICloKlu111549_1614.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAARLHLFK.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycCKLU431943:GJF1-1548-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_CLOK5
AccessionPrimary (citable) accession number: A5N8F9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 50 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