D0MYK8 · D0MYK8_PHYIT

Function

Catalytic activity

  • Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
    EC:3.4.21.62 (UniProtKB | ENZYME | Rhea)

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.

Features

Showing features for active site, binding site.

169150100150200250300350400450500550600650
TypeIDPosition(s)Description
Active site254Charge relay system
Active site258Charge relay system
Active site485Charge relay system
Binding site530Ca2+ (UniProtKB | ChEBI)
Binding site531Ca2+ (UniProtKB | ChEBI)
Binding site555Ca2+ (UniProtKB | ChEBI)
Binding site557Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular Functionmetal ion binding
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    subtilisin
  • EC number

Gene names

    • ORF names
      PITG_03813

Organism names

Accessions

  • Primary accession
    D0MYK8

Proteomes

    • Identifier
    • Component
      Partially assembled WGS sequence

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane614-638Helical

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_500301152123-691subtilisin

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain182-577Peptidase S53
Compositional bias648-676Polar residues
Region648-691Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    691
  • Mass (Da)
    74,304
  • Last updated
    2009-12-15 v1
  • Checksum
    4365431FE5A3C585
MSGLWLLSLAVVLCSLSGGTIAATYEPPSRFSGFSSDRYVRQSRVDPEQVVPLVIGLHPDDFNGMERVFYRVSDPAHTTYGQYLTQEQTDHLSRPAHGALGAVRHWVREFAHENNAGAFSTTSNLFKIPMKRRRLMRAATDVSVPEHLQDFVSFLSVNAHPLGLRALGAATSETAESTNNGGGTLAQVRQTYGIPDNLVVTNPSNTQCVPSFYDESYDPADLKTFFSQYLPGENPPPIIEKGSRVNNPEHASTEASLDVQYITGVGRNATTFVWTMNGSNPYSSEDEPFVEFVQDVLALENPPLVVSISYSDDEEHIFDVSPGYARTLDTLLIKMGLRGITVLIAGGDDGVTGLRPEFEKVPVEEMCKKSGPQWPSSSPYITTVGATMLLTKAQQAAKSFFHTKEEVICSVENGGIITSGGGFSNIYAMPEYQRTSVERYLATRNIPNTAGFFNASGRAYPDVAALGAGFLVYMNGRLSSVSGTSASTPVLGAMVTLWNDMRLNAGKSPLGFINPLLYYLAETNPNAFNDVVVGNNGAPRGGNTPCDDSFSAAAGWDSVSGVGTPNFPVISEFITNLEDHFNVSQLGGTNNSAMSDVNNNAVATTSGIGEMSTFTMVLLVAAVVANVAIGIVVVVTLVKRWRNQYTPLDDVASGNTTPTAPVDSTATPTARMQRLGSNSEDDVELSEINLN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias648-676Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS028121
EMBL· GenBank· DDBJ
EEY66256.1
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