ID   CUDP_METAN              Reviewed;         388 AA.
AC   P29138;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cuticle-degrading protease;
DE            EC=3.4.21.-;
DE   AltName: Full=Chymoelastase;
DE   AltName: Full=PR1;
DE   Flags: Precursor;
GN   Name=PR1;
OS   Metarhizium anisopliae (Entomophthora anisopliae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=5530;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 108-115.
RC   STRAIN=ME1 / ARSEF 2575;
RX   PubMed=1551399; DOI=10.1111/j.1432-1033.1992.tb16721.x;
RA   St Leger R.J., Frank D.C., Roberts D.W., Staples R.C.;
RT   "Molecular cloning and regulatory analysis of the cuticle-degrading-
RT   protease structural gene from the entomopathogenic fungus Metarhizium
RT   anisopliae.";
RL   Eur. J. Biochem. 204:991-1001(1992).
CC   -!- FUNCTION: Capable of breaching the insect cuticle.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; M73795; AAA33417.1; -; mRNA.
DR   PIR; S22387; S22387.
DR   AlphaFoldDB; P29138; -.
DR   SMR; P29138; -.
DR   MEROPS; S08.056; -.
DR   PHI-base; PHI:4615; -.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..107
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027006"
FT   CHAIN           108..388
FT                   /note="Cuticle-degrading protease"
FT                   /id="PRO_0000027007"
FT   DOMAIN          41..106
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          116..388
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        179
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        334
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..233
FT                   /evidence="ECO:0000250"
FT   DISULFID        288..360
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  40331 MW;  4CAF735D3FA39352 CRC64;
     MHLSALLTLL PAVLAAPATI GRRAEPAPLF TPQAESIIAD KYIVKFKDDI ARIATDDTVS
     ALTSKADFVY EHAFHGFAGS LTKEELKMLR EHPGVDFIEK DAVMRISGIT EQSGAPWGLG
     RISHRSKGST TYRYDDSAGQ GTCVYIIDTG IEASHPEFEG RATFLKSFIS GQNTDGHGHG
     THCAGTIGSK TYGVAKKAKL YGVKVLDNQG SGSYSGIISG MDYVAQDSKT RGCPNGAIAS
     MSLGGGYSAS VNQGAAALVN SGVFLAVAAG NDNRDAQNTS PASEPSACTV GASAENDSRS
     SFSNYGRVVD IFAPGSNVLS TWIVGRTNSI SGTSMATPHI AGLAAYLSAL QGKTTPAALC
     KKIQDTATKN VLTGVPSGTV NYLAYNGA