ID   CTSD_ARTBC              Reviewed;         509 AA.
AC   D4AZK1;
DT   05-OCT-2010, 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 CTSD;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=CTSD; ORFNames=ARB_01619;
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 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; ABSU01000021; EFE31471.1; -; Genomic_DNA.
DR   RefSeq; XP_003012111.1; XM_003012065.1.
DR   AlphaFoldDB; D4AZK1; -.
DR   SMR; D4AZK1; -.
DR   STRING; 663331.D4AZK1; -.
DR   MEROPS; A01.077; -.
DR   EnsemblFungi; EFE31471; EFE31471; ARB_01619.
DR   GeneID; 9519598; -.
DR   KEGG; abe:ARB_01619; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_10_0_1; -.
DR   OMA; PFLELFC; -.
DR   Proteomes; UP000008866; 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; Reference proteome; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..485
FT                   /note="Probable aspartic-type endopeptidase CTSD"
FT                   /id="PRO_0000397698"
FT   PROPEP          486..509
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397699"
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;  54651 MW;  B73C15FA25EB0931 CRC64;
     MQFLWLCLLS AVTLQFTGTL AFYPIKLPDF TKGIISHHGS VGRRFFTFPG LYKHAHTGST
     TLNIRRGPSN YRRDNNYPAQ IASPPTAPNT LGINNDGYDF SYFSEVKVGS EGQKMWMLID
     TGASGTWVFG SDCTSKACGR HNTFGKEDSK TIKVTDEKWG VTYGTGKVSG VIVNDTMSFA
     GFELVTPFGS ASTASDDFLN YPMDGILGIG PQDPNAKTPT VVQLLMQQKL LKSNVIGINL
     QRASEGATDG QITFGDIDKS KFSGELIYSN VVPNGYQWEI AMDDLIMDGK SLNLKGRTGI
     IDTGTSFLIL PPADADLIHS MIPQADKGSG FYTLPCSTKV DIKLSIGGVE YTIQPDDYVG
     NETATKGTCN SLIVGRQILG PKQWLVGDVF LKNVYSVFDF DKNRVGLAAR KYAGTKNPPS
     STPSPGMFLL HAIHCQKTIS VLMLHIDPTS NKAPSGGSPG LPAESGSDST TNGEATNGAT
     SSPNSSSSVL TPTWLTLAVF FAIGSSLWS