ID   M28P2_TRIVH             Reviewed;         497 AA.
AC   D4D8N9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable zinc metalloprotease TRV_03476;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=TRV_03476;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; ACYE01000180; EFE41794.1; -; Genomic_DNA.
DR   RefSeq; XP_003022412.1; XM_003022366.1.
DR   AlphaFoldDB; D4D8N9; -.
DR   SMR; D4D8N9; -.
DR   EnsemblFungi; EFE41794; EFE41794; TRV_03476.
DR   GeneID; 9580959; -.
DR   KEGG; tve:TRV_03476; -.
DR   HOGENOM; CLU_047420_0_0_1; -.
DR   Proteomes; UP000008383; 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:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; PTHR12147; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..497
FT                   /note="Probable zinc metalloprotease TRV_03476"
FT                   /id="PRO_0000411763"
FT   DOMAIN          411..497
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  54890 MW;  A750C76D5DF243A3 CRC64;
     MRFLISSLLS GLALLTSLHA FVLALPREYT IAMSNPFHES LFSCPAASWP RVKLGSENTP
     QEPSKDLRKI LSQISPKRIE ATIRKLVSFG TRHTLSTQTN ATYGIGAARD WIESEFQRYA
     NASDGRLTVK VVGYDQQPDG NRIPFPVRIS DVVATLKGEG DPERVYVVSG HYDSRNSDPL
     DYKGIAPGAN DDASGVAVSL ELARVMSQRD LPRPKATIVF AAVAGEEQGL YGANFLAQSF
     RNSSTNVEGM FTNDIIGSST ADDGTKEPHV IRLFAQGIPP LNVENQAMRE RRIMIGGDND
     TPARQLARFV KETAENKHTD MEVSVIYRLD RYLRGGDHRP FLEAGYPAAR FTEPNENYAH
     QHQDIRIDKD PKTGKDIQYG DLPEFCDFDF ISRVGKVNAA ALWNLAMSPG MPRNVRVNTN
     ALSNDSKFSW DPPAGGNALV GGYEIVWRST TAPFWTHKMD VGMVQEATID LSKDNVIFGI
     RARGKNGERG VAVLPFP