ID   ALP_HYPAT               Reviewed;         409 AA.
AC   Q03420;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Alkaline proteinase;
DE            Short=ALP;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=prb1;
OS   Hypocrea atroviridis (Trichoderma atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=63577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=IMI 206040;
RX   PubMed=8326868; DOI=10.1111/j.1365-2958.1993.tb01604.x;
RA   Geremia R.A., Goldman G.H., Jacobs D., Ardiles W., Vila S.B.,
RA   van Montagu M., Herrera-Estrella A.;
RT   "Molecular characterization of the proteinase-encoding gene, prb1, related
RT   to mycoparasitism by Trichoderma harzianum.";
RL   Mol. Microbiol. 8:603-613(1993).
CC   -!- FUNCTION: Serine protease, secreted specifically during the
CC       mycoparasitic process, which is involved in the degradation of
CC       phytopathogen cell walls, membranes and of the proteins released after
CC       lysis of the host.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: By mycelia, fungal cell walls, and chitin, but only in the
CC       absence of glucose.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; M87518; AAA34211.1; -; Genomic_DNA.
DR   EMBL; M87516; AAA34209.1; -; mRNA.
DR   PIR; S32905; S32905.
DR   AlphaFoldDB; Q03420; -.
DR   SMR; Q03420; -.
DR   MEROPS; S08.066; -.
DR   PRIDE; Q03420; -.
DR   OMA; INWRTAS; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..120
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026990"
FT   CHAIN           121..409
FT                   /note="Alkaline proteinase"
FT                   /id="PRO_0000026991"
FT   DOMAIN          35..112
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          129..409
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        353
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   409 AA;  42271 MW;  D0F548EA236C5E63 CRC64;
     MTSIRRLALY LGALLPAVLA APAALHKKPE AVPNKFIVTL KEGASIDTDS HLAWVTDIHT
     RSLTKRSTAG VEKTYNIHTW NAYAGEFDEE TIEQIKSNPD VASVEPDYIM HLSDIVEDKR
     ALTTQSGAPW GLGTVSHRTS GSTSYIYDSS AGAGTFAYVV DSGINTSHQQ FGGRASLGYN
     AAGGQHVDTL GHGTHVSGTI GGSTYGVAKQ ASLISVKVFA GESASTSVIL DGYNWAVNDI
     VSKSRASKSA INMSLGGPAS STWTTAINAA FNQGVLTIVA AGNGDSLGNP QPVSGTSPAN
     VPNAITVAAL DINWRTASFT NYGAGVDVFA PGVNILSSWI GSNTATNTIS GTSMATPHVV
     GLALYLQSLE GLTSPTAVTN RIKALATSGR VTGSLNGSPN VIIFNGNSS