ID   MEP1_COLGM              Reviewed;         280 AA.
AC   E3QJV4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Extracellular metalloprotease GLRG_06286;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=GLRG_06286;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; GG697353; EFQ31142.1; -; Genomic_DNA.
DR   RefSeq; XP_008095162.1; XM_008096971.1.
DR   AlphaFoldDB; E3QJV4; -.
DR   SMR; E3QJV4; -.
DR   EnsemblFungi; EFQ31142; EFQ31142; GLRG_06286.
DR   GeneID; 24411651; -.
DR   VEuPathDB; FungiDB:GLRG_06286; -.
DR   eggNOG; ENOG502RYKG; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   OrthoDB; 1569419at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04275; ZnMc_pappalysin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   Pfam; PF05572; Peptidase_M43; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..280
FT                   /note="Extracellular metalloprotease GLRG_06286"
FT                   /id="PRO_0000407201"
FT   REGION          217..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        232..259
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   280 AA;  30109 MW;  05FFB3EE54BC5349 CRC64;
     MQVTFTLVAA LAGMASAAVA GERGSFGCAT HEPTLEHIEI SKKLAEEEAT NATLFGLAAA
     ATITVPTYFH VVASSQTVAN GYITDKMLSD QLAVMNEDFA PHGISFNLVQ TTRTINPTWA
     RDGDELAMKR SLRKGDYGAL NLYFLRDIGG AFGYCYFPTT ASPGSASYIR DGCTILSSTV
     PGGSSTNYNL GRTVTHEVGH WFGLYHTFQG GCTGSGDSIA DTPAQSSPSS GCPVGRDSCP
     NQPGVDPIHN YMDYSIDSCY EEFTPNQQTR MYSFFNQYRA