ID   PEPA_COCP7              Reviewed;         443 AA.
AC   C5PEI9; Q3HYC4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Aspartic protease PEP3 {ECO:0000305};
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=PEP3 {ECO:0000303|PubMed:16369008}; ORFNames=CPC735_058790;
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 [GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=16369008; DOI=10.1128/iai.74.1.516-527.2006;
RA   Tarcha E.J., Basrur V., Hung C.Y., Gardner M.J., Cole G.T.;
RT   "A recombinant aspartyl protease of Coccidioides posadasii induces
RT   protection against pulmonary coccidioidomycosis in mice.";
RL   Infect. Immun. 74:516-527(2006).
RN   [2]
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 aspartic endopeptidase that allows assimilation of
CC       proteinaceous substrates. The scissile peptide bond is attacked by a
CC       nucleophilic water molecule activated by two aspartic residues in the
CC       active site. Shows a broad primary substrate specificity. Favors
CC       hydrophobic residues at the P1 and P1' positions.
CC       {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
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DR   EMBL; DQ176860; ABA54908.1; -; Genomic_DNA.
DR   EMBL; ACFW01000049; EER24509.1; -; Genomic_DNA.
DR   RefSeq; XP_003066654.1; XM_003066608.1.
DR   AlphaFoldDB; C5PEI9; -.
DR   SMR; C5PEI9; -.
DR   MEROPS; A01.079; -.
DR   EnsemblFungi; EER24509; EER24509; CPC735_058790.
DR   GeneID; 9692124; -.
DR   KEGG; cpw:CPC735_058790; -.
DR   VEuPathDB; FungiDB:CPC735_058790; -.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Secreted; Signal; Virulence; Zymogen.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   PROPEP          37..107
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q12567"
FT                   /id="PRO_0000407046"
FT   CHAIN           108..443
FT                   /note="Aspartic protease PEP3"
FT                   /id="PRO_0000407047"
FT   DOMAIN          123..440
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        363..403
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   443 AA;  47804 MW;  466E602D1F48ED6B CRC64;
     MQNRPRVFDS AMNLSPNMHF LSLMPGLLLL SLQVHTSPTP LKKTIRSVRI ERIRQPNYVP
     DGPGALKKAY AKFGIIPSGI SFDSFEDFTP FSSDNVRNTV SKAMQANETG IVTNTPTNND
     VEYLSPVTIG GQKFVMNLDT GSSDTWVFNT QLSEDAKRGH SIFDPAKSKA FSDLEDATFN
     ITYGDASFAF GRVGIDTVDI GGATVQKQAV GLPTDVSGSF ILDQASDGLI GLGFDELNTV
     EPQQQKSFFT NLAANLDEPV LAAQLKKGAP GSYEFGSIDE TKFKGDLVTI PVNNSRGFWE
     VKSTMFKVGK DEQLHRITKG VGSAIADTGT TLMLVNEEIV NSYYDQVDNA RSVYAAGGFI
     FPCNATLPDL YVSLGDTHLA RIPGDLMNFS KVGLSTETGE ELCFGGVQSN SGSGLQVFGD
     VLFKAIFVVF DLRGPSLHVA GHA