ID   CTSD_TRIVH              Reviewed;         509 AA.
AC   D4D8U6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable aspartic-type endopeptidase CTSD;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=CTSD; ORFNames=TRV_03534;
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 GPI-anchored aspartic-type endopeptidase which
CC       contributes to virulence. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; ACYE01000183; EFE41705.1; -; Genomic_DNA.
DR   RefSeq; XP_003022323.1; XM_003022277.1.
DR   AlphaFoldDB; D4D8U6; -.
DR   SMR; D4D8U6; -.
DR   MEROPS; A01.077; -.
DR   EnsemblFungi; EFE41705; EFE41705; TRV_03534.
DR   GeneID; 9580870; -.
DR   KEGG; tve:TRV_03534; -.
DR   HOGENOM; CLU_013253_10_1_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_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; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Protease; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..485
FT                   /note="Probable aspartic-type endopeptidase CTSD"
FT                   /id="PRO_0000397700"
FT   PROPEP          486..509
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397701"
FT   DOMAIN          102..408
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          451..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   LIPID           485
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   509 AA;  54631 MW;  2EA12E9D2B261853 CRC64;
     MQFLWLCLLS AVTLQFTGTL AFYPIKLPDF TKGLVSNHGS IDRRFFTFPG LYKHAHTGST
     TLNIRRGPSN YRRDNNYPAQ IASPPTAPNT LGINNDGYDF SYFSEVKVGS EGQKMWMLID
     TGASGTWVFG SDCTSKACGR HNTFGKEDSK TIKVTDEKWG VTYGTGKVSG VIVNDTMSFA
     GFELVTPFGS ASTASDDFLN YPMDGILGIG PQDPNAKTPT VVQLLMQQKL LKSNVIGINL
     QRASEGATDG QITFGDIDKS KFSGELIYSN VVPDGYQWEI AMDDLIMDGK SLNLKGRTGI
     IDTGTSFLIL PPADADLIHS MIPQANKGSG FYTLPCSTKV DIKLSIGGVE YTIQPDDYVG
     NETATKGTCN SLIVGRQILG PKQWLVGDVF LKNVYSVFDF DKNRVGLAAR KYAGTKNPPS
     STPSPGMFLL HAILCPKTIS VLMLHIDPTS NKAPSGGSPG LPAESGSDST TNGEATNGAT
     SSPNSSSSVL TPTWLTLAVF FAIGSSLWS