ID   MEP9_COCP7              Reviewed;         639 AA.
AC   C5NZT1; Q3KRQ4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Extracellular metalloproteinase 9;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP9;
DE   AltName: Full=Fungalysin MEP9;
DE   Flags: Precursor;
GN   Name=MEP9; ORFNames=CPC735_012920;
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=16177346; DOI=10.1128/iai.73.10.6689-6703.2005;
RA   Hung C.Y., Seshan K.R., Yu J.J., Schaller R., Xue J., Basrur V.,
RA   Gardner M.J., Cole G.T.;
RT   "A metalloproteinase of Coccidioides posadasii contributes to evasion of
RT   host detection.";
RL   Infect. Immun. 73:6689-6703(2005).
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 metalloproteinase that allows assimilation of
CC       proteinaceous substrates and probably acts as a virulence factor.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY45759.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY987813; AAY45759.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; ACFW01000001; EER29974.1; -; Genomic_DNA.
DR   RefSeq; XP_003072119.1; XM_003072073.1.
DR   AlphaFoldDB; C5NZT1; -.
DR   SMR; C5NZT1; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EER29974; EER29974; CPC735_012920.
DR   GeneID; 9697614; -.
DR   KEGG; cpw:CPC735_012920; -.
DR   VEuPathDB; FungiDB:CPC735_012920; -.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   PRINTS; PR00999; FUNGALYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..250
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407170"
FT   CHAIN           251..639
FT                   /note="Extracellular metalloproteinase 9"
FT                   /id="PRO_0000407171"
FT   REGION          293..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  70268 MW;  301B8F4514CC90E0 CRC64;
     MHGLLLAAGL LSLPLRALGH PNPNPQMHTL SRRGAVDLDA FRLGQNAEYS NTASVASNPP
     ALSIRSTQSY VDVAKDLVKT TLPDATFRVV NDHYVGTNGV AHVHLRQTVH GIDVDNADFN
     VNVKDGKVFS FGNSFYKGKI PEENPMVKRD HADPVKALKG VVSALKLPVK TEKASAAISA
     QSQGQDAVVF KGTSGALSDP KGELVYLIKP DGELSLTWKV ETDVGDNWLL SYIDAKDGKN
     IHGVVDYVAD ATYQVYPWGI NDPTEGEREV FTDPWDGNAS EFTWISDGRT RYPTTRGNNG
     IAQDNPSGGN QYENNYRPMS DDLRFEYPYS TDMSPPDSYI DASITQLFYT ANVYHDLLYI
     LGFTERAGNF EYNNNNQGGR GNDYVILNSQ DGSGTNNANF ATPPDGQPGR MRMYTWTTSR
     PNRDGSFEAG IVIHEYTHGL SNRLCGGPSN SRCLNALESG GMGEGWGDFM ATAIRLKAGD
     TRETDYTMGE WAANQQGGIR QHPYSTNLQT NPLVYTTVNQ YREVHDIGTV WASMLYEVLW
     NLIDKHGKND GPKPELRDGV PTDGKYLTMK LVIDGMALQP CNPNFVQARD AILDADEALT
     GGENKCEIWA GFAKRELGTG ARYDRSRRTG STDVPQECQ