ID   PCH18_PENCH             Reviewed;         494 AA.
AC   P9WEW6; Q9HF04;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Subtilisin-like serine protease EN45_078720 {ECO:0000250|UniProtKB:P9WEW5};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749};
DE   AltName: Full=Vacuolar serine protease {ECO:0000250|UniProtKB:P9WEW5};
DE   Flags: Precursor;
GN   ORFNames=EN45_078720;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P2niaD18;
RX   PubMed=25059858; DOI=10.1128/genomea.00577-14;
RA   Specht T., Dahlmann T.A., Zadra I., Kuernsteiner H., Kueck U.;
RT   "Complete sequencing and chromosome-scale genome assembly of the industrial
RT   progenitor strain P2niaD18 from the penicillin producer Penicillium
RT   chrysogenum.";
RL   Genome Announc. 2:E0057714-E0057714(2014).
CC   -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q9Y749}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; CM002799; KZN89274.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEW6; -.
DR   SMR; P9WEW6; -.
DR   Proteomes; UP000076449; Chromosome ii.
DR   GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
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; 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; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; IgE-binding protein; Protease; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..136
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P9WEW5"
FT                   /id="PRO_0000451345"
FT   CHAIN           137..453
FT                   /note="Subtilisin-like serine protease EN45_078720"
FT                   /evidence="ECO:0000250|UniProtKB:P9WEW5"
FT                   /id="PRO_0000451346"
FT   PROPEP          454..494
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000451440"
FT   DOMAIN          43..136
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          146..448
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          180..198
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P8G3"
FT   REGION          209..231
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P9WEW5"
FT   ACT_SITE        182
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        376
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            311
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JIZ5"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   494 AA;  52309 MW;  5F6A37AF0DAEA894 CRC64;
     MKGFLSLTLL PLLVAASPVA VNSIHNDAAP ILSSMTSKDI PDSYIVVFKK HVDPSSASAH
     QSWLQEVHTA HTGRMELKKR SLFGFDFEAF MGLKHTFHIA GSLLGYAGHF HEDVIEQIRR
     HPDVDYIEKD SEVRTMSEGS VEKNAPWGLA RISHRESLSF GNFNKYLYAE EGGEGVDAYV
     IDTGANVKHV DFEGRANWGK TIPQGDADED GNGHGTHCSG TIAGKKFGVA KKANVYAVKV
     LRSNGSGTMS DVVKGVEWAA EAHIKKSKKG DKKFKGSVAN MSLGGGSSRT LDLAVNAAVD
     AGIHFAVAAG NDNADACNYS PAAAEKAITV GASTLADERA YFSNYGKCTD IFAPGLNILS
     TWVGSDHATN TISGTSMASP HIAGLLAYYV SLAPAKDSAY AVADVTPKQL KAALISVATE
     GTLTDIPSDT PNLLAWNGGG SANYTKILAD GGYKAHNAET TVEDRIGGII DSAEKAFHKE
     LGAIYSEIKD AVSA