ID   SU11A_COCP7             Reviewed;         403 AA.
AC   C5P1W9;
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_035780;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   ORFNames=CPC735_035780;
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; ACFW01000012; EER28872.1; -; Genomic_DNA.
DR   RefSeq; XP_003071017.1; XM_003070971.1.
DR   AlphaFoldDB; C5P1W9; -.
DR   SMR; C5P1W9; -.
DR   EnsemblFungi; EER28872; EER28872; CPC735_035780.
DR   GeneID; 9696512; -.
DR   KEGG; cpw:CPC735_035780; -.
DR   VEuPathDB; FungiDB:CPC735_035780; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..117
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407002"
FT   CHAIN           118..403
FT                   /note="Subtilisin-like protease CPC735_035780"
FT                   /id="PRO_0000407003"
FT   DOMAIN          35..116
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          127..403
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        349
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        233
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        399
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   403 AA;  42069 MW;  B56B3F774623544C CRC64;
     MSIMKIATLF FAALSAVEAA KLLTPSDKRD IVPDSYIVVM KDNVSPLKFD SHMSWATNVH
     HANLARQGST ATGGLKHVYR IDGWQGYSGS FARETIDRIL ENDDVDYVEP DRRVHLTALT
     TQPNAPSWGL GRISHRNNGN SNFVYDDRAG EGITFYGVDT GIDINHPDFG GRAVWGTNTA
     GGSDSDGHGH GTHTAGTVAG ASYGIAKKAK LVAVKVLSEG GTGQWSGIIE GINWSVNHAR
     ANNALGKAVM NMSLGGRLST SVNQATTRAQ RAGIFIAVAA GNEDPSVQSD AANTSPASAE
     DVCTVAASTE QDGRASFSNW GSMVEIYAPG TNIVSTTPGG NTGKMSGTSM AAPHVAGVGA
     AIMASEGISP SEVCSRLVEI GLEQISNPGS GTTNKLLYNN SGR