ID   MEP9_UNCRE              Reviewed;         635 AA.
AC   C4JR56;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
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=UREG_03538;
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; CH476616; EEP78692.1; -; Genomic_DNA.
DR   RefSeq; XP_002544021.1; XM_002543975.1.
DR   AlphaFoldDB; C4JR56; -.
DR   SMR; C4JR56; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EEP78692; EEP78692; UREG_03538.
DR   GeneID; 8437440; -.
DR   KEGG; ure:UREG_03538; -.
DR   VEuPathDB; FungiDB:UREG_03538; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; C4JR56; -.
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..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407172"
FT   CHAIN           247..635
FT                   /note="Extracellular metalloproteinase 9"
FT                   /id="PRO_0000407173"
FT   REGION          279..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  69593 MW;  F938924810450CD7 CRC64;
     MHGLLLAAGL LTLPLRALAH PGHQSTSILS RRGAVDLDAY RVSAKAEYSN VNDVAENPPA
     VSLMSSGSYV DIATELVKTT LPGVTFRVVN DHYVGTNGVA HVHFRQTIHG VDVDNADFNV
     NVKDGKVFSF GNGFYKGEIP KENPMVKRDF SDPVHALKGA CNALKIPIKT NKVSVKSGKG
     QESVVFKGTS GALSEPKGDL VYFVKPDGKL SLTWRVETDV GDNWLSSYVD AKDSSKIHGV
     TDYVADATFQ VYPWGLNDPT EGSRQTLTDP WERNASEFTW HSDGNTRYPT TRGNNGIAQD
     NPSGGTGYLN NYRPQSSALR FEYPYSTSMS PPTSYKDASI TQLFYTANTF HDLTYLLGFT
     ERAGNFEVNN NNQGGRGNDF VILNAQDGSG VNNANFATPP DGQPGRMRMY TWNRSQPNRD
     GCFEAGIVIH EYAHGLSNRL CGGPANSRCL SALESGGMGE GWGDFLATAI RLKANDTRRT
     SYTMGEWASN QRGGIRQYPY STSTTTNPLV YTTVNRYNRV HDIGTVWATM LYEVLWNLID
     KHGKNDGPRP EFRNGVPTDG KYLTMKLVID GMALMPCNPN FVQARDAIID ADEALTGGQN
     KCEIWAGFAK RQLGTGARYG RTNRVGSTEV PSECR