ID   MEP5_COCP7              Reviewed;         356 AA.
AC   C5NZY5; Q3KRQ8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Neutral protease 2 homolog MEP5;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MEP5;
DE   AltName: Full=Metalloproteinase 5;
DE   Flags: Precursor;
GN   Name=MEP5; ORFNames=CPC735_000180;
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=AAY45755.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EER29762.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY987809; AAY45755.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; ACFW01000004; EER29762.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003071907.1; XM_003071861.1.
DR   AlphaFoldDB; C5NZY5; -.
DR   SMR; C5NZY5; -.
DR   EnsemblFungi; EER29762; EER29762; CPC735_000180.
DR   GeneID; 9697412; -.
DR   KEGG; cpw:CPC735_000180; -.
DR   HOGENOM; CLU_039313_1_1_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; IPR029463; Lys_MEP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   SMART; SM01351; Aspzincin_M35; 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..179
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407072"
FT   CHAIN           180..356
FT                   /note="Neutral protease 2 homolog MEP5"
FT                   /id="PRO_0000407073"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        187..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  38867 MW;  1BB88E56A099A9BD CRC64;
     MRVSSSLIAL AALAVQALAL PVNELAERDT GLDVKLIPIG NTRVKAIITN NADHEMSFVK
     YNTLFDSSPV RKVQISKDGS IVPFNGMRLY YDINNLPKEA YKTLAPGASA EAEFDIAETS
     DLSAGGSFEI SAEGSIPVID GQGTKPTGSI RFKANVLTMD IDGEMASKVA SAIPELDKRT
     RVDGQTCTGQ YAQLLQGGLR NCVTYAQRAA QAASGGNAQK FQEYFKTTSQ QARQSVARRF
     QAIAQECSSA NQGRTIYFCQ DIYRNCQRGL IAYTIPARSH VVNCPDYWRL PPVVNRGLDP
     DHGYVVVHEF THATSIFSPG TVDHAYGYEQ CRRLNAQQSL SNADNYSLFA ADVTRN