A0A8K0WU41 · A0A8K0WU41_9HYPO

  • Protein
    tripeptidyl-peptidase II
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Release of an N-terminal tripeptide from a polypeptide.
    EC:3.4.14.10 (UniProtKB | ENZYME | Rhea)

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.

Features

Showing features for active site, binding site.

114682004006008001,0001,2001,400
TypeIDPosition(s)Description
Active site268Charge relay system
Active site272Charge relay system
Active site489Charge relay system
Binding site532Ca2+ (UniProtKB | ChEBI)
Binding site533Ca2+ (UniProtKB | ChEBI)
Binding site555Ca2+ (UniProtKB | ChEBI)
Binding site557Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionmetal ion binding
Molecular FunctionNAD+ binding
Molecular Functionserine-type endopeptidase activity
Molecular Functiontransferase activity
Molecular Functiontripeptidyl-peptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    tripeptidyl-peptidase II
  • EC number

Gene names

    • ORF names
      B0I35DRAFT_348637

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MPI-CAGE-CH-0235
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Stachybotryaceae > Stachybotrys

Accessions

  • Primary accession
    A0A8K0WU41

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_503547686223-1468tripeptidyl-peptidase II

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain191-577Peptidase S53
Domain613-1171Deacetylase sirtuin-type
Region670-847Disordered
Compositional bias674-707Basic and acidic residues
Compositional bias714-756Polar residues
Compositional bias774-792Polar residues
Compositional bias793-807Pro residues
Compositional bias808-847Polar residues
Region929-993Disordered
Compositional bias930-970Polar residues
Compositional bias971-993Basic and acidic residues
Region1167-1199Disordered
Compositional bias1168-1184Basic and acidic residues
Region1218-1440Disordered
Compositional bias1244-1263Basic and acidic residues
Compositional bias1266-1291Polar residues
Compositional bias1315-1335Basic and acidic residues
Compositional bias1345-1391Pro residues

Sequence similarities

Belongs to the sirtuin family. Class I subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,468
  • Mass (Da)
    160,038
  • Last updated
    2022-08-03 v1
  • Checksum
    D999594B4A1DFFFF
MSSTVLGQIVALAGLGFGAASAVRQPSSFIPGGWQALDDQVKPSEPLRLSIALRQPGIGQVWGRIGSREHLSRGEVAALRAPDEQDADDVMRWLATHGITNAKVQKDWIHVQTTVGQAEPLLQMKMQYYAFEDKEPILRTREYSIPDSLSQAIQFVHPIDNFITPKRELSATSPPLEEGGLDVREAACRTGTSPNCIRELYNFNYTGSGPSDIRFGVAGFLEEWANYQDAHQFLQMAAPNIASTSYNFSVELVNGGENSQNVRYAGLEAALDIDYAMALGYPAKVTYYSTGGRGVELGDDGEPLEGDLVDNEPYLELLEYLLDKDDSELPHVLSVSYADDELSVPRHYAERVCDLFGLLTSRGTTILGGSGDGGARGARNSTCRTNDGTNQEVAMAVFPATCPWVTAVGAVSNAFDPPQGATYSGGGFSQYFARERWQDAAVQGYVKALGSHMGSKYNASMRATPDISAIGSQFMVVIASQITRLQGTSASTPVIAAMMVQINDARVRQGKKPLGWINGLLYSDEVRKTLRDVTVGESEPCPFSGGEAGWPAKEGYDAITGLGVPGDFEALMQVLSAWGAAVLNASSRWRATGLSQPVSKLRRARTMPTQHVEPASDDLLQQIADSLLKARKVVVVTGAGISTNSGIPDFRSENGLYSLIQAQFDAAARQARPVESADSDKDEASFQEPPAKRRSTDVKREPPSEESQDDSEACADGTVVNSNHEANEEVDGTSPPSPNAQLLSTPQPKFKHPSPTTSPLSSPPPEDFILTPRGFQDSTRSRLYKTTIPLSSSPLSSPPPGLFDPYPPSSPSDSSTTQNSTSPSELDDSPPSSNNFSSQSSTKSTLPNMKGKDLFDASIWSDPLRTSVFYTFATTLRQKVKEVTPTPSHHFISHLRDRGKLVRCYTQNIDQIEEKVGLSTCLTAGPGSRGRFSRRSTANTSQLNKMVEEASDSSKSQTDASQSQDTEDSQPKTNSEGDTTEQEKHEPPAIKREPSRTGVECVFLHGSLEQLRCFLCGRVCSWDEAGRQEETLSGQQPECPHCAGATARREERGKRALGVGKLRPDIVLYGEDHPNSHLISPIVTHDLALQPDMLLILGTSLRVHGLKVMVREFAKAVHNRAGKVVFVNFTKPPESAWGDIIDYWIQWDCDAWVDNLQGRIPKLWQALEPPKPKKKRDSAGKSDIETKKPPAANPVAQRDTKATGAYWSLKIINELHRITGTPPLPSQPRRASLPTTETTSEPRPQPPKAERTKPKRPRKSAPGALEKQQKPSTLNPNHGRPRRQQDTADSVPATPVVKKELPSIPISSILDSVKSNPRVRKRKMIDGEEVVMPKIGRRRTANSTPAPTFPPPLPELKLAPLNPQPASPSSPYGRPEPLEPQSPPPGPPLASISANPRNWLHDAFAMTGSPIQWPEHPMTARPLRLLPAQEEDKSQAAARALAELRDSWNVRRPPQDQRASMPINVKAM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias674-707Basic and acidic residues
Compositional bias714-756Polar residues
Compositional bias774-792Polar residues
Compositional bias793-807Pro residues
Compositional bias808-847Polar residues
Compositional bias930-970Polar residues
Compositional bias971-993Basic and acidic residues
Compositional bias1168-1184Basic and acidic residues
Compositional bias1244-1263Basic and acidic residues
Compositional bias1266-1291Polar residues
Compositional bias1315-1335Basic and acidic residues
Compositional bias1345-1391Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGPNK010000003
EMBL· GenBank· DDBJ
KAH7324886.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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