ID   MEP2_TRIVH              Reviewed;         632 AA.
AC   D4D2D2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor;
GN   Name=MEP2; ORFNames=TRV_01237;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Secreted metalloproteinase probably acting as a virulence
CC       factor. {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; ACYE01000067; EFE43987.1; -; Genomic_DNA.
DR   RefSeq; XP_003024598.1; XM_003024552.1.
DR   AlphaFoldDB; D4D2D2; -.
DR   SMR; D4D2D2; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFE43987; EFE43987; TRV_01237.
DR   GeneID; 9579926; -.
DR   KEGG; tve:TRV_01237; -.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   Proteomes; UP000008383; 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   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397728"
FT   CHAIN           245..632
FT                   /note="Probable extracellular metalloproteinase 2"
FT                   /id="PRO_0000397729"
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"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  69836 MW;  06B76A188521A3EA CRC64;
     MHGLLLAGLA AALPLGVAGL PARQQSGLSP RGIDINPYRF ASMAKYSEHK ATSQMVHSFS
     YSKDDDYVAT ATKLVKSTFP NMTFRTVKDH YIGTNGIGHV HFKQTAHGID IDNADFNVNI
     GRDGKVFTFG NSFYEGEMPK TNPLTKRDFS DPVKALHGAI KTLKLPVKPQ SAKAMPMKEA
     ETFKFEGTSG ALSDPMAKLV YIQKDGKLHL TWRVETDVGD NWLLSYVDSK ETETVHNVVD
     YVASADYKVF AWGLNDPTEG QPTMIKDPWN TTGTGSPFTW HGDGQMDYTV TRGNNIAAQD
     NPSGGEQWEN NYRPDSPELS FVYEYNEQME PEQYKDFAIT QLFYTTNTFH DVLYSLGFTE
     EAGNFQMNNN GKGGEGNDFA ICNAQDGSGT NNANFATPPD GQNGRMRMYT WTTAQPSRDG
     DLEAGIVIHE YTHGLSNRLC GGPANSNCLT ELEAGGMGEG WGDFYATAIR LKQDDTHDTD
     YTMGEWAANM QGGIREYPYS TNMQTNPYTY ADVQGMDEVH GIGTVWATIL YEVLWNLIDE
     HGMSKNIMPK FVNGAPSDGR NLAMKLVLDG MTLMPCNPNF MQARDAIIDA DQALTNGQNK
     CALMKAFSKR GLGANYKHGK TRVNNFDMPA DC