ID   SUB7D_COCP7             Reviewed;         394 AA.
AC   C5P9H3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Subtilisin-like protease CPC735_005570;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   ORFNames=CPC735_005570;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; ACFW01000030; EER26385.1; -; Genomic_DNA.
DR   RefSeq; XP_003068530.1; XM_003068484.1.
DR   AlphaFoldDB; C5P9H3; -.
DR   SMR; C5P9H3; -.
DR   EnsemblFungi; EER26385; EER26385; CPC735_005570.
DR   GeneID; 9694013; -.
DR   KEGG; cpw:CPC735_005570; -.
DR   VEuPathDB; FungiDB:CPC735_005570; -.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..114
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407024"
FT   CHAIN           115..394
FT                   /note="Subtilisin-like protease CPC735_005570"
FT                   /id="PRO_0000407025"
FT   DOMAIN          37..110
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          123..394
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        155
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        340
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   394 AA;  41203 MW;  194D5BF864DF3A10 CRC64;
     MRAIISVALF LSLSLLSAVN AAEILSAGDT DDVIPDSYIV VMRDGLSTDA FNSHTTQISG
     FRNEDRNVKA SLKKTFDLNG LKGYSGTFDE ATIRQIANDP AVKYIEHDRI ANARGLVEQQ
     DAGWNLARIS HKKTGARTYV YDKSAGAGIS VCLVDTGVDV DNPDLGGRAT WGANFVDNDD
     SDGNGHGTFL ASLIAGQKHG VAKKAKIIAV KVLDANGSGS YSNVISGIDW CVKYAKEHGI
     SERMVVNLSL GGGYSQAVNQ AAENAVLAGM FVSAAVGGSN RDARNDSPAS ARGVCAIAAS
     TMDDKAALFS NYGSIVAVYA PGQNIMAAGR MGSVTLSGTS FAAGHASGVG AYLLALEKIT
     GDRVCTRIKE LAIPVIRNSP SNTTRLLLYN GSGR