ID   Y6366_TRIVH             Reviewed;         430 AA.
AC   D4DGR1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Probable aspartic-type endopeptidase TRV_06366;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   ORFNames=TRV_06366;
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: Probable secreted aspartic-type endopeptidase which
CC       contributes to virulence. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; ACYE01000362; EFE38962.1; -; Genomic_DNA.
DR   RefSeq; XP_003019607.1; XM_003019561.1.
DR   AlphaFoldDB; D4DGR1; -.
DR   SMR; D4DGR1; -.
DR   MEROPS; A01.079; -.
DR   PRIDE; D4DGR1; -.
DR   EnsemblFungi; EFE38962; EFE38962; TRV_06366.
DR   GeneID; 9578379; -.
DR   KEGG; tve:TRV_06366; -.
DR   HOGENOM; CLU_013253_0_0_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Glycoprotein; Hydrolase; Protease; Secreted; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..87
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397716"
FT   CHAIN           88..430
FT                   /note="Probable aspartic-type endopeptidase TRV_06366"
FT                   /id="PRO_0000397717"
FT   DOMAIN          109..427
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          61..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   430 AA;  46757 MW;  2B16674808C2BCD8 CRC64;
     MHVSTLLVAV LLPLALSKPT PRKKTSSFKV HLARRGETEY YRDGPTDLQR AYAKYGIPTT
     HEMEGYHPQP ISKLPGNSKA TAGSGKEGVE SQDEKGEVVN NPTDHDIQFL SPVTIGGQPF
     IMNFDTGSSD TWVMNTQMTD EEAKKDHHLY DPSKSKTASK LVDQNFDIKY GDKTHASGPV
     YSDVMDIGGA TVRNQAIGLP SKVAASLAED KTSDGLVGLA MTKLNTIRPV KQKTFFENLA
     EDLDEPVFTA QLRHGKMGSY EFGAIDKSKY HGDLIKVPVI NENGFWEIPC SLYSVGKLDK
     IQTIQNGTGT AILDTGTTLL VLDEKIVKAY YAQVPGARYD PTRFAGWVYP CNSPMPSLFL
     AVGTDHMAII PSSLLTFQSY GPGPDGVETC YGGLQSNNAG GIQILGDVFF KALFVVFDQR
     GPSISLAPHA