ID   SUB8_COCP7              Reviewed;         497 AA.
AC   C5P4Z8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Subtilisin-like protease CPC735_031240;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   ORFNames=CPC735_031240;
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; ACFW01000025; EER27788.1; -; Genomic_DNA.
DR   RefSeq; XP_003069933.1; XM_003069887.1.
DR   AlphaFoldDB; C5P4Z8; -.
DR   SMR; C5P4Z8; -.
DR   PRIDE; C5P4Z8; -.
DR   EnsemblFungi; EER27788; EER27788; CPC735_031240.
DR   GeneID; 9695428; -.
DR   KEGG; cpw:CPC735_031240; -.
DR   VEuPathDB; FungiDB:CPC735_031240; -.
DR   HOGENOM; CLU_011263_1_4_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; 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; Protease; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..136
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407026"
FT   CHAIN           137..497
FT                   /note="Subtilisin-like protease CPC735_031240"
FT                   /id="PRO_0000407027"
FT   DOMAIN          43..134
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          146..452
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
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        380
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  52875 MW;  D548E4B61A25BEB6 CRC64;
     MKGVLSLSLL PLLAAPSPIL VDTIHRDAAP ILSSHNSKEV PDSYIVVFKK NVSPASAAAH
     QVWVQDLHTT VMAKRSLRKR NQFPFKNDAF DGLKHTYDIA GSIMGYSGHF DEEVIEQVRR
     HPDVQYIEKD SEVHAWDEPV TENNAPWGLA RVSHRDSLTM GTFNKYLYAA NGGEGVDVYV
     IDTGTNIEHV DFEGRAHWGK TIPTGDDDVD GNGHGTHCSG TVAGKKYGVA KKANVYAVKV
     LRSNGSGTMS DVVKGVEWAA GAHLSKMVEA RKKGNKAFKG SAANMSLGGG KSFTLDLAVN
     AAVDAGIHFA VAAGNDNADA CNYSPAAAEK AVTVGASTLA DERAYFSNYG KCTDIFAPGL
     NILSTWIGSK YAVNTISGTS MASPHVAGLL AYFLSLQPEQ DSAFAVSPIS PAKLKKDMIA
     IATKNALTDI PADTPNILAW NGGGSSNYTA IIQQGGYEAT RPGNKAAQLT EKIEKLGQNT
     ASQLGAIYSE IKDAFTI