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 22-FEB-2023, entry version 44.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 GlyCosmos; D4D2D2; 2 sites, No reported glycans.
DR GeneID; 9579926; -.
DR KEGG; tve:TRV_01237; -.
DR HOGENOM; CLU_012703_3_0_1; -.
DR OrthoDB; 2786251at2759; -.
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 CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
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
//
