ID   MEP10_COCP7             Reviewed;         629 AA.
AC   C5P7A7; Q3KRQ3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Extracellular metalloproteinase 10;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP10;
DE   AltName: Full=Fungalysin MEP10;
DE   Flags: Precursor;
GN   Name=MEP10; ORFNames=CPC735_026430;
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}.
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DR   EMBL; AY987814; AAY45760.1; -; Genomic_DNA.
DR   EMBL; ACFW01000025; EER27307.1; -; Genomic_DNA.
DR   RefSeq; XP_003069452.1; XM_003069406.1.
DR   AlphaFoldDB; C5P7A7; -.
DR   SMR; C5P7A7; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EER27307; EER27307; CPC735_026430.
DR   GeneID; 9694947; -.
DR   KEGG; cpw:CPC735_026430; -.
DR   VEuPathDB; FungiDB:CPC735_026430; -.
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; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..629
FT                   /note="Extracellular metalloproteinase 10"
FT                   /id="PRO_0000407148"
FT   PROPEP          20..240
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407149"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         424
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   629 AA;  69424 MW;  DD5EEA451AEB6116 CRC64;
     MHGLLLAAGL LSLPLYTIAH TQPSGALSRR GVDLDAYRLP EKSSYTNTND VQENSAILSL
     NAGSYVDVAT KLVKQTIPSA TFRVVDDHYI SDTGLGHVYF RQTINGLDVD NADFNVNVGK
     DGKIFSFGNS FYTGKVPSAS LTRDHSDPIQ ALNGARKALK LPVKTEKATA RATNRGEYMF
     KGTSGALSEP TAKLVYIVKD DGSLALTWRV ETDIGDNWLL SYVDAKDSDK VHNVVDYVAH
     ATYQVYPWGI NDPTEGSRQV FKDPWELPAS PFTWISDGRQ NYTTTRGNNG IAQNNPDGGT
     EYLNNYRPNS RNLRFEYRYS PSMNPPKSYT NASITQLFYS ANTYHDLLYT LGFTEEAGNF
     QVSNGNRGGK GNDYVILNAQ DGSGTNNANF ATPPDGRPGR MRMYIWTRAN PPRDGCFEAG
     IVIHEYTHGL SNRLTGGPDN TRCLNGLESG GMGEGWGDFY ATAVRLKRND TRNTVYAKSA
     WASNNPGGVR AYPYSTDFEI NPLTYTSVNQ LNEVHAVGTV WATMLYELLW NLIDKHGKND
     GPKPVFRDGV PTDGKYLAMK IVLDGMKIQP CNPNFVQARD AILDADKALT GGENKCEIWT
     AFAKRELGTG ARYNRNNRTG SKEVPNECK