ID   Y7403_ARTBC             Reviewed;         430 AA.
AC   D4AT39;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable aspartic-type endopeptidase ARB_07403;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   ORFNames=ARB_07403;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE33939.1; Type=Erroneous gene model prediction; Evidence={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; ABSU01000008; EFE33939.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003014842.1; XM_003014796.1.
DR   AlphaFoldDB; D4AT39; -.
DR   SMR; D4AT39; -.
DR   STRING; 663331.D4AT39; -.
DR   MEROPS; A01.079; -.
DR   EnsemblFungi; EFE33939; EFE33939; ARB_07403.
DR   GeneID; 9520379; -.
DR   KEGG; abe:ARB_07403; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   Proteomes; UP000008866; 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; Reference proteome;
KW   Secreted; Signal; 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_0000397718"
FT   CHAIN           88..430
FT                   /note="Probable aspartic-type endopeptidase ARB_07403"
FT                   /id="PRO_0000397719"
FT   DOMAIN          109..427
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          66..105
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;  46693 MW;  07016BC41046239D CRC64;
     MHVSTLLVAV LLPLALSKPT PRKKTGSFKV HLARRGETEY SRDGPTDLQR AYAKYGIPTT
     HEMDGYHPQH ISKLPGNSKA TAGSGKEGVE SQDEKGEVVN NPTNHDIQFL SPVTIGGQPF
     IMNFDTGSSD TWVMNTQMTD EEAKKDHHLY DPSKSKTASK LVDQTFDIKY GDKTHASGPV
     YSDVMDIGGA TVRNQAIGLP SKVAASLAED KTSDGLVGLA MTKLNTIRPV KQKTFFENLA
     EDLDEPVFTA QLRHGKMGSY EFGTIDKSKY HGDLIKVPVI NENGFWEIPC SLYSVGKLDK
     IQTIQNGTGT AILDTGTTLL VLDEKIVKAY YAQVPGARYD PTRFAGWVYP CNSPMPSLFL
     AVGTDHMAII PSSLLTFQSY GPGPDGVETC YGGLQSNNAG GIQILGDVFF KALFVVFDQR
     GPSISLAPHA