ID   SUB9_COCP7              Reviewed;         399 AA.
AC   C5P5Q3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Subtilisin-like protease CPC735_033790;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   ORFNames=CPC735_033790;
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; EER28043.1; -; Genomic_DNA.
DR   RefSeq; XP_003070188.1; XM_003070142.1.
DR   AlphaFoldDB; C5P5Q3; -.
DR   SMR; C5P5Q3; -.
DR   MEROPS; S08.115; -.
DR   EnsemblFungi; EER28043; EER28043; CPC735_033790.
DR   GeneID; 9695683; -.
DR   KEGG; cpw:CPC735_033790; -.
DR   VEuPathDB; FungiDB:CPC735_033790; -.
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; 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; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..117
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407028"
FT   CHAIN           118..399
FT                   /note="Subtilisin-like protease CPC735_033790"
FT                   /id="PRO_0000407029"
FT   DOMAIN          37..116
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          127..399
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        159
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        190
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   399 AA;  42066 MW;  89C515EE67F451F6 CRC64;
     MGFLSSAILL LITAFPAAQA GEMINAAAGA TDVIPDSYIV VMNEGISESD FESHRTWATS
     MNSKSRKRAG AFSGVSRTWS ATGMKGYSGS FARETIEQIA NNSAVAYVEP DRMVNITAFV
     TQRNAPSYGL GRISNKRPGN RDYIFDESAG RGITIYGVDT GIDIRHPEFE GRATWGTNEI
     NDVNQDENGH GTHTAGTFAG RNFGVAKRAN IVAVKVLNAE GSGSTSGIIS GINWCVDHAR
     RNNILGRAVM NLSLGGTGAR AFNQVATNAA NAGIFLAVAA GNDGEDAANT SPASARGVCT
     VSASTERDTR ADFSNFGSVV DIYAPGDQIP SVFPNNARRV LSGTSMAAPH VAGVGAYLMA
     LEGISSGQVC NRIKRLSQPR IRNPGRDTTN RLLYNNSGV