ID   MEP10_UNCRE             Reviewed;         637 AA.
AC   C4JX59;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 43.
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=UREG_06232;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
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. {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; CH476618; EEP81367.1; -; Genomic_DNA.
DR   RefSeq; XP_002583265.1; XM_002583219.1.
DR   AlphaFoldDB; C4JX59; -.
DR   SMR; C4JX59; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EEP81367; EEP81367; UREG_06232.
DR   GeneID; 8441585; -.
DR   KEGG; ure:UREG_06232; -.
DR   VEuPathDB; FungiDB:UREG_06232; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; C4JX59; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000002058; 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   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..245
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407150"
FT   CHAIN           246..637
FT                   /note="Extracellular metalloproteinase 10"
FT                   /id="PRO_0000407151"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   637 AA;  70622 MW;  441AC4AE1D9E00EF CRC64;
     MHGLLLAATL LSLPFNAVAH VPPTTGLVRR GVDLDSFRLN ERSQFKISEQ VEKDSGVSAL
     HSRNYVDVAT RLVKRVAPKA TFRLVDDHYI GDTGVGHVYF RQTINGVDVD NGDFNVNIGR
     NGRVFSYGNS FHTGDVPESN LRVKEDPSNP VQALHGALKA LRIPIKAERA VAEATNEEDD
     EDFVLKGTSG ALADPTAKLV YLMKNDGSLA LTWRVETDIG DNWLLTYVDA EDTTKVHNVV
     DYVAHATYKV YRWGIADPTE GELEVISDPW NLRTSEFTWH GNGTTRFSTT IGNNGIAQSN
     PTGGSEYLNN YRPQPADLKF EYDYSPSMNP PSTYIDASIT QLWYSANTYH DLLYMLGFNE
     RSGNFETNNN NQGGKGNDYV ILNAQDGSGT NNANFATPPD GRPGRMRMYI WTRANPPRDV
     CFEEGTVVHE YTHGLSNRLT GGPANSRCLN ALESGGMGEG WSDFFATAVR LKPKDTRHTD
     YPKGAWVANN PRGVRQYVYS TNMTTNPLVY TTVNSLNQVH AIGTVWATIL YEVLWNLIDK
     HGKNDGPTPK FRNGVPTDGK YLAMKLVLDG LALQPCNPNF VQARDAILDA DKILTGGRNQ
     CELWKGFAKR ELGTGAKWDP RNRVGSTRVP VICRIFT