ID   PRTT_PARAQ              Reviewed;         293 AA.
AC   P20015;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Proteinase T;
DE            EC=3.4.21.-;
DE   Flags: Precursor; Fragment;
GN   Name=PROT;
OS   Parengyodontium album (Tritirachium album).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Parengyodontium.
OX   NCBI_TaxID=37998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=ATCC 22563 / Limber;
RX   PubMed=2697641; DOI=10.1016/0378-1119(89)90425-3;
RA   Samal B.B., Karan B., Boone T.C., Chen K.K., Rohde M.F., Stabinsky Y.;
RT   "Cloning and expression of the gene encoding a novel proteinase from
RT   Tritirachium album limber.";
RL   Gene 85:329-333(1989).
CC   -!- FUNCTION: Serine proteinase.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; M54900; AAA34204.1; -; mRNA.
DR   EMBL; M54901; AAA34205.1; -; Genomic_DNA.
DR   PIR; JQ0380; JQ0380.
DR   AlphaFoldDB; P20015; -.
DR   SMR; P20015; -.
DR   MEROPS; S08.061; -.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Protease; Serine protease.
FT   PROPEP          <1..12
FT                   /id="PRO_0000027148"
FT   CHAIN           13..293
FT                   /note="Proteinase T"
FT                   /id="PRO_0000027149"
FT   DOMAIN          19..293
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        51
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        83
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DISULFID        46..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..262
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   293 AA;  29722 MW;  F4CF215EDC71B93B CRC64;
     EFIEQDAVVT ISATQEDAPW GLARISSQEP GGTTYTYDDS AGTGTCAYII DTGIYTNHTD
     FGGRAKFLKN FAGDGQDTDG NGHGTHVAGT VGGTTYGVAK KTSLFAVKVL DANGQGSNSG
     VIAGMDFVTK DASSQNCPKG VVVNMSLGGP SSSAVNRAAA EITSAGLFLA VAAGNEATDA
     SSSSPASEES ACTVGATDKT DTLAEYSNFG SVVDLLAPGT DIKSTWNDGR TKIISGTSMA
     SPHVAGLGAY FLGLGQKVQG LCDYMVEKGL KDVIQSVPSD TANVLINNGE GSA