ID   MEP_FUSV7               Reviewed;         637 AA.
AC   C7Z3B7;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Extracellular metalloproteinase MEP;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP;
DE   AltName: Full=Fungalysin MEP;
DE   Flags: Precursor;
GN   Name=MEP; ORFNames=NECHADRAFT_87892;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(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   -!- INDUCTION: Expression is controlled by the prtT transcription factor.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; GG698907; EEU41806.1; -; Genomic_DNA.
DR   RefSeq; XP_003047519.1; XM_003047473.1.
DR   AlphaFoldDB; C7Z3B7; -.
DR   SMR; C7Z3B7; -.
DR   STRING; 660122.C7Z3B7; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; NechaT87892; NechaP87892; NechaG87892.
DR   GeneID; 9675951; -.
DR   KEGG; nhe:NECHADRAFT_87892; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; C7Z3B7; -.
DR   OMA; IRKDSYT; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000005206; 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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407187"
FT   CHAIN           247..637
FT                   /note="Extracellular metalloproteinase MEP"
FT                   /id="PRO_0000407188"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   637 AA;  68995 MW;  AC96B72629813434 CRC64;
     MRSVDSLLLL GLTGLASQAN AHPAKRQPND SPLSKRGVDL DAFRLPELAK YVPQDEVPDI
     SNARIAPSSD YTKTAEEFVK SVVGKATFRL VSDHYVGTNG VAHVRFKQTV NDIDVDNADF
     NVNIGADGKV FSYGNSFYTG KIPGPLVKRD TSDPVTALKS TVEVLDLPVD ASDAKAEPKG
     DEHYTFTDTS GTVKKPEAKL VYLIDGEQNL KLTWRVETDV LDNWLLTYVD ADKTEKVVGV
     VDYVADLATY EVYPWGVNDP SKGSRSVVED PWNIATSEFT WISDGSANYT TTRGNNAIAQ
     VNPSGGTAYL NNYRPSSSSL EFEYTFSTTQ TDPVSYRDAS ITQLFYTANK YHDLLHLLGF
     NEAAGNFEVN NNGQGGAGND FVILNSQDGS GTNNANFATP ADGSPGRMRM YLWTYSTPRR
     DSSFDAGVVI HEYTHGLSNR LTGGPANAGC LSGTESGGMG EGWSDFMATA VHLGARDTRS
     TNHVIGDWVY NNANGIRAYP YSTSLTTNPY TYRSVNSLSG VHAVGTYWAT ALYEVLWNLI
     DKHGKNDADT PTFDSNGVPT DGKYLAMKLV IDGMALQPCN PNMVQARDAI LDADVALTGG
     DNQCELWTGF AKRGLGTGAR YSSTSRTESF ALPSGVC