ID   Y4018_ARTBC             Reviewed;         370 AA.
AC   D4AIC4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable aspartic-type endopeptidase ARB_04018;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   ORFNames=ARB_04018;
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 aspartic-type endopeptidase which contributes to
CC       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; ABSU01000001; EFE36497.1; -; Genomic_DNA.
DR   RefSeq; XP_003017142.1; XM_003017096.1.
DR   AlphaFoldDB; D4AIC4; -.
DR   SMR; D4AIC4; -.
DR   STRING; 663331.D4AIC4; -.
DR   EnsemblFungi; EFE36497; EFE36497; ARB_04018.
DR   GeneID; 9527107; -.
DR   KEGG; abe:ARB_04018; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   OMA; HRIYHPE; -.
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; 2.
DR   Pfam; PF00026; Asp; 2.
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.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..370
FT                   /note="Probable aspartic-type endopeptidase ARB_04018"
FT                   /id="PRO_0000406414"
FT   DOMAIN          94..367
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   370 AA;  41458 MW;  FF572A747F03C327 CRC64;
     MWHSPFSTAF TLFLGFFTLT LALPTNSLAT TGHFTIEQRL INTIKSDWPP KELWRGLRKH
     HRPLPPAVSR ISRHGGSFAN GTVKVTPDEY DTEFVNEITI GNDTLFVDID TGSSDFWVFS
     SQLPEQSQRN HRIYHPEKTG IKLPKQIWET SYGDGTGAAG NVFLDKVNLA GLEVSSQVTP
     KKQKTWFGNI MERLEKPIFT ACLKHKAPGF YDFGFIDKTK HIGNPSYLPV DNSRGWWETT
     FNGFSTGPSD NSTYRFRAVV DTGTTFMLLP REITEQYYSS ITGSAFDREN GGWTFPCNAT
     LPEFAIHVND YKAIVPGEHI NWAQIPGTNT CFGGIQPVDR SPAVLGGSFL KSQFVIFDHD
     GPKMGFAAQR