ID   MEP7_COCP7              Reviewed;         363 AA.
AC   C5P3T4; Q3KRQ6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Neutral protease 2 homolog MEP7;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MEP7;
DE   AltName: Full=Metalloproteinase 7;
DE   Flags: Precursor;
GN   Name=MEP7; ORFNames=CPC735_062250;
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. Shows high activities on basic nuclear
CC       substrates such as histone and protamine. May be involved in virulence
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.;
CC         EC=3.4.24.39;
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 M35 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY45757.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY987811; AAY45757.1; ALT_INIT; Genomic_DNA.
DR   EMBL; ACFW01000015; EER28352.1; -; Genomic_DNA.
DR   RefSeq; XP_003070497.1; XM_003070451.1.
DR   AlphaFoldDB; C5P3T4; -.
DR   SMR; C5P3T4; -.
DR   MEROPS; M35.001; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EER28352; EER28352; CPC735_062250.
DR   GeneID; 9695992; -.
DR   KEGG; cpw:CPC735_062250; -.
DR   VEuPathDB; FungiDB:CPC735_062250; -.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   BRENDA; 3.4.24.39; 9184.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Signal; Virulence;
KW   Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..181
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407076"
FT   CHAIN           182..363
FT                   /note="Neutral protease 2 homolog MEP7"
FT                   /id="PRO_0000407077"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        187..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  39903 MW;  83C6840D362F9345 CRC64;
     MLLCSMVAAL AALATPAFSC ALPHLDLPED NSGLDIKLDS LSNTRVKATI TNKADRPLNL
     LKFNTFFDDG PTEKVGIFKD GNPIKFDGIM RRIQTFDLPI SAFVPISPGE SIEREFDIAS
     TSDLTVGGAF DILSEGAIPY AEANQTTLTG AMVFKSNALQ LKIDGEMAAT VARAIQPLDR
     RSDVHVCRNS AKRKALMKAL RNSAHLAGTA ASAAYRNPRK VQEYFHTTDR TAVRSVAARL
     KAISRESGST RNGATRYACE DHWNRCEPGV LAYTLPSHNL VVNCPSFYNL PALTNRCHGQ
     DQATTVLHEF AHAPGVHEPF CKDHAYGYRS IRRLSTRLAL NNADSFSLFA NGRFRRRFRV
     IST