ID   PRTR_PARAQ              Reviewed;         387 AA.
AC   P23653;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Proteinase R;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=PROR;
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 [MRNA].
RC   STRAIN=ATCC 22563 / Limber;
RX   PubMed=2077361; DOI=10.1111/j.1365-2958.1990.tb00558.x;
RA   Samal B.B., Karan B., Boone T.C., Osslund T.D., Chen K.K., Stabinsky Y.;
RT   "Isolation and characterization of the gene encoding a novel, thermostable
RT   serine proteinase from the mould Tritirachium album Limber.";
RL   Mol. Microbiol. 4:1789-1792(1990).
CC   -!- FUNCTION: Serine proteinase.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; X56116; CAA39584.1; -; mRNA.
DR   PIR; S11985; S11985.
DR   AlphaFoldDB; P23653; -.
DR   SMR; P23653; -.
DR   MEROPS; S08.054; -.
DR   PRIDE; P23653; -.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.70.80; -; 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   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
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   Calcium; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..108
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027140"
FT   CHAIN           109..387
FT                   /note="Proteinase R"
FT                   /id="PRO_0000027141"
FT   DOMAIN          42..107
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          115..387
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        177
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        332
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   BINDING         124
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         368
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   DISULFID        142..231
FT                   /evidence="ECO:0000250"
FT   DISULFID        286..357
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   387 AA;  40927 MW;  66E9B953FADDA188 CRC64;
     MRLSILLGLL PLAPRPPAVD AVEQRSEPAP LIEAQGEMIA DKYIVKLKEG SALASLDAAM
     EKLSGKADHV YKNIFKGFAA SLDEKMVEVL RAHPDVEYIE QDAIVNINAE QRNAPWGLAR
     ISSTSPGTST YRYDDSAGQG TCVYVIDTGV EASHPEFEGR AQMVKTYYAS SRDGNGHGTH
     CAGTIGSRTY GVAKKTQIFG VKVLNDQGSG QYSTIISGMD FVANDYRNRN CPNGVVASMS
     IGGGYSSSVN SAAANLQQSG VMVAVAAGNN NADARNYSPA SESSICTVGA TDRYDRRSSF
     SNYGSVLDIF APGTDILSTW IGGSTRSISG TSMATPHVAG LAAYLMTLGR ATASNACRYI
     AQTANQGDLS NISFGTVNLL AYNNYQG