A9NEI9 · SYC_ACHLI

Function

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

143450100150200250300350400
TypeIDPosition(s)Description
Binding site28Zn2+ (UniProtKB | ChEBI)
Binding site207Zn2+ (UniProtKB | ChEBI)
Binding site232Zn2+ (UniProtKB | ChEBI)
Binding site236Zn2+ (UniProtKB | ChEBI)
Binding site267ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functioncysteine-tRNA ligase activity
Molecular Functionzinc ion binding
Biological Processcysteinyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cysteine--tRNA ligase
  • EC number
  • Alternative names
    • Cysteinyl-tRNA synthetase
      (CysRS
      )

Gene names

    • Name
      cysS
    • Ordered locus names
      ACL_0143

Organism names

Accessions

  • Primary accession
    A9NEI9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003327761-434Cysteine--tRNA ligase

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif30-40'HIGH' region
Motif264-268'KMSKS' region

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    434
  • Mass (Da)
    50,682
  • Last updated
    2008-02-05 v1
  • Checksum
    CC4ABAEEE848A63A
MLKIYNSLSNKIEEFKPIHEKKVNMYVCGPTVYDDIHIGNGRPVVFFDVVKRYLQYLDYGVKYASNITDVDDKIIDRAQKLHITEKELATTYTNNFFEIAKKIGGYNFDVTPHATNYIEEMIKFIGELISDGFAYKTQSGVYFRVDKIKDYGILSNQQVKDLKTGVRIDLETDKEKDYDFALWKNTEEGIKYHAPWGDGRPGWHTECVVMTNEIFGGEIDIHGGGFDLKFPHHENEIAQSVAKHDHHLAKYWMHVGRLDLANEKMSKSLGNDIKLKDLVQVYNPNAYRLMLLAHHYRAPIQFSDDLIEQYQKAYDKISYTLNKWHFHMILNNINENGLDHESMEYFEGFMNDDFATPRVISLIDKLIKDLNKAFKVENYNTIIQILSTLGINPNILEVLEDDIQNYNNWQQARLEKNYEKADIYRKPLLDKGFI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000896
EMBL· GenBank· DDBJ
ABX80769.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp