ID   MEP_NEOFI               Reviewed;         634 AA.
AC   A1DBW0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=NFIA_099860;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates and probably acts as a virulence factor.
CC       {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; DS027694; EAW20350.1; -; Genomic_DNA.
DR   RefSeq; XP_001262247.1; XM_001262246.1.
DR   AlphaFoldDB; A1DBW0; -.
DR   SMR; A1DBW0; -.
DR   STRING; 331117.A1DBW0; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; A1DBW0; -.
DR   EnsemblFungi; EAW20350; EAW20350; NFIA_099860.
DR   GeneID; 4588767; -.
DR   KEGG; nfi:NFIA_099860; -.
DR   VEuPathDB; FungiDB:NFIA_099860; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; IRKDSYT; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000006702; 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   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..245
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407189"
FT   CHAIN           246..634
FT                   /note="Extracellular metalloproteinase MEP"
FT                   /id="PRO_0000407190"
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"
SQ   SEQUENCE   634 AA;  68721 MW;  D3416CD05C214970 CRC64;
     MRGLLLAGAL ALPASVFAHP AHQSYGLNRR TVDLNAFRLK SLAKYVNATE TVIEAPSSFA
     PFKQQSYVEA ATQHVKMIAP DATFRVVDDH YVGDNGVAHV HFRQTANGLD IDNADFNVNV
     GKDGKVFSYG NSFYTGQIPS SAALTKRDFS DPVTALKGTT NTLQLPITVD SASSESTEGK
     ESYVFKGVSG TVSDPKANLV YFVKDDGTLA LTWRVETDID SNWLLTYIDA KSGEQIHGVV
     DYVAEADYQV YAWGINDPTE GERTVVKDPW DSAASEFTWI SDGSTKYTTS RGNNGIAQSN
     PNGGSSYLNN YRPSSSSLSF KYPYSPSSSP PSSYIDASII QLFYTANTYH DLLYTLGFNE
     KAGNFEYNTN GQGGRGNDYV ILNAQDGSGT NNANFATPPD GQPGRMRMYV WTESTPYRDG
     SFEAGIVIHE YTHGLSTRLT GGPANSNCLN ALESGGMGEG WGDFMATAIR LKPGDKRSTD
     YTMGEWAANR PGGIRQYPYS TSMSTNPLTY TSVNSLNAVH AIGTVWATML YEVMWNLIDK
     HGKNDAPKPT LRDGVPTDGK YLAMKLVIDG MALQPCNPNF VQARDAILDA DTALTGGENQ
     CEIWKAFAKR GLGAGAQYSS RNRVGSTEVP SGVC