ID   F2RYB7_TRIT1            Unreviewed;       495 AA.
AC   F2RYB7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Aspartyl protease {ECO:0000313|EMBL:EGD96316.1};
GN   ORFNames=TESG_03769 {ECO:0000313|EMBL:EGD96316.1};
OS   Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=647933;
RN   [1] {ECO:0000313|EMBL:EGD96316.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112818 {ECO:0000313|EMBL:EGD96316.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA   Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA   Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA   Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA   Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; GG698493; EGD96316.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2RYB7; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000009172; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000313|EMBL:EGD96316.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EGD96316.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..495
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003285691"
FT   TRANSMEM        476..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..408
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          449..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   495 AA;  51729 MW;  759446BE34856BE7 CRC64;
     MRGDAFIWSL ATAIPLLSTA VESLQVVKRD NPSVLGFDIE RFQAAKPIHR DIIAKRASTK
     TISQDLDNQK NLYFCNLTLG TPPQTIRAHI DTGSSDLWVN TADSRFCSSR RSPCSQGGTY
     DSSSSSTYQL VNNDFNISYV DGSGASGDYV TDFINIGGIK LKDFQFAIGH TSSSPLGVLG
     IGYEAGEAQV TRSGDESYPN LPAALVKAGH IRSNAYSLWL NDLGASRGQI LFGGIDTGKF
     QGKLQTIPVL HTSRGDYTSL VVALTGVGIR TGSDGSIDTF PSQPVAVAMD SGSSLSYLPD
     ALAAKVYNAV DAVFDPANNL AFVPCSMASD NRKLVFTFSS PQIAVGMDEL VIDLGPDANG
     NEATFRDGSK ACVFGIAPAG GSISILGDTV LRSAYLVYDL DNNEISIAPT LFNSTETNIL
     EIGTGENSVP DATGVPNAVT SAQVTQATGL PGVETGVPGS RPPSSKAAGQ AKRPDFILGI
     AAVGLAGAGL LFAAM
//