ID   SMP1_MAGPO              Reviewed;         404 AA.
AC   Q9Y778;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Subtilisin-like proteinase Mp1;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Magnaporthiopsis poae (Kentucky bluegrass fungus) (Magnaporthe poae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX   NCBI_TaxID=148304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RC   STRAIN=ATCC 64411 / 73-15;
RX   PubMed=10415340; DOI=10.1016/s0378-1119(99)00201-2;
RA   Sreedhar L., Kobayashi D.Y., Bunting T.E., Hillman B.I., Belanger F.C.;
RT   "Fungal proteinase expression in the interaction of the plant pathogen
RT   Magnaporthe poae with its host.";
RL   Gene 235:121-129(1999).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AF118126; AAD26255.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y778; -.
DR   SMR; Q9Y778; -.
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; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..112
FT                   /evidence="ECO:0000269|PubMed:10415340"
FT                   /id="PRO_0000027163"
FT   CHAIN           113..404
FT                   /note="Subtilisin-like proteinase Mp1"
FT                   /id="PRO_0000027164"
FT   DOMAIN          33..111
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          121..404
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        186
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        347
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   404 AA;  42352 MW;  BD99430F8CE6D0FE CRC64;
     MVGFKTLALH LAAVLPALAA PVDKQATQVV PNSYIITLKQ GASAASFHNH LSWVGDVHRR
     SVSKRDTTGV DKVFDLDGFT AYSGSFDAAT LQEIKKSDEV AFVEPDQVWD LYTLSTQSGA
     PWGLGSISHR KPNSTDYVYD PAGLGADHYA YIIDTGLDTE HVEFEGRGTL GYNAYPNSQF
     IDKIGHGTHV AGTIAGKTYG VAKKASIVSV RVFDTGSVTR QSTTAIVLDG FSWAVKDITA
     KGRQAKSVIS MSLGGGRSEA FNAAVEAAYQ ANILTVAAAG NSAWDASQYS PASAPNAITV
     GAIDVDNVMA WFSNYGPVVD VFAPGVAVES AWIGSSHAEH DVLDGTSMAT PHVSGLVLYL
     KSLEGFASAA AVTDRIKALG TNDVVTGLEG TDSPNLIAFN GVTA