ID   MEP_COLGM               Reviewed;         639 AA.
AC   E3QKL1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 37.
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=GLRG_06543;
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212;
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697355; EFQ31399.1; -; Genomic_DNA.
DR   RefSeq; XP_008095419.1; XM_008097228.1.
DR   AlphaFoldDB; E3QKL1; -.
DR   SMR; E3QKL1; -.
DR   STRING; 645133.E3QKL1; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFQ31399; EFQ31399; GLRG_06543.
DR   GeneID; 24411908; -.
DR   VEuPathDB; FungiDB:GLRG_06543; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000008782; 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..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..248
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407181"
FT   CHAIN           249..639
FT                   /note="Extracellular metalloproteinase mep"
FT                   /id="PRO_0000407182"
FT   ACT_SITE        434
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   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  69318 MW;  405CE23844D50056 CRC64;
     MYRSMKSLAL LGLLGPTSQV FAHPATGHAH NIGRRGVDIE AFRLPQVGSY TNATEIETTP
     PIALLKRESY VETATELVKK LAPNSEFRLV GDHYVGTNGI GHVNFKQTVH GLDIDNGDFN
     VNIGKDGKVF SYGNNFFKGE APEASPLKKR DFKDPVSALK GAKDVLQLPV EAASASAEPK
     EGTEVYSIKG TSGTVSDPEA RLVYFVKADG SLALSWRVET DITENWLLTY VDAETGTDVH
     GVVDYVSDLA NYRVYPWGVN DPTEGDRVLV TDPWDISASP LTWQSDGTTN YTTTRGNNGI
     AQSNPSGGTA YLNNYRPTSA ARNFDYQYTT SLTTPSSYID ASIAQLYYTA NHYHDLLYTL
     GFTESAGNFQ INNNGKGGVG NDFVVLFAQD GSGTNNANFL TPPDGSNGRM RMYLWTMSTP
     RRDCSFEAGV VIHEYTHGLS TRLTGGPANS NCLNALESGG MGEGWGDFFA TAIRLKPTDT
     RATDYSMGAW VYNNPAGIRS VLYSTSMTTT PNTYSTINGV SSVHRIGETW ATTLYEVLWN
     LIDKHGKNDG PRPEFDSNGV PTDGKYLTLK LVLDGMALQP CSPNFIQARD AILDADKALT
     GGDNLCELWT AFAKRGLGSN AVYSSSNRRD GFNVPAGVC