P58156 · CBPX2_SACS2

Function

function

Can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Features

Showing features for binding site, active site.

139350100150200250300350
TypeIDPosition(s)Description
Binding site104Zn2+ (UniProtKB | ChEBI)
Binding site109Zn2+ (UniProtKB | ChEBI)
Binding site245Zn2+ (UniProtKB | ChEBI)
Active site302Proton donor
Active site373Nucleophile

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
Molecular Functioncarboxypeptidase activity
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding
Molecular Functionmetallopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Thermostable carboxypeptidase 2
  • EC number

Gene names

    • Name
      cpsA2
    • Synonyms
      cpsA-2
    • Ordered locus names
      SSO1952

Organism names

Accessions

  • Primary accession
    P58156

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000619481-393Thermostable carboxypeptidase 2

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase M20 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    393
  • Mass (Da)
    42,993
  • Last updated
    2001-06-01 v1
  • Checksum
    AFBDE9F0A3469B63
MDLVEKLKNDVKEIEDWIIQIRRKIHENPELSYKEYSTSKLVAETLRKLGIEVEEGVGLPTAVVGKIRGNKPGKTVALRADMDALPVEETSDVEFKSKVKGVMHACGHDTHVAMLLGGAYLLVKNKDLISGEIRLIFQPAEEDGGLGGAKPMIEAGVMNGVDYVFGIHISSSYPSGVFATRKGPIMATPDAFKIVVHGKGGHGSAPHETIDPIFISLQIANAIYGITARQIDPVQPFVISITTIHSGTKDNIIPDDAEMQGTIRSLDENVRSKAKDYMRRIVSSICGIYGATCEVKFMEDVYPITVNNPEVTDEVMKILSSISTVVETEPVLGAEDFSRFLQKAPGMYFFLGTRNEKKGCIYPNHSSKFCVDEDVLKLGALAHALLAIKFSNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE006641
EMBL· GenBank· DDBJ
AAK42144.1
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