ID   CTSD_ARTOC              Reviewed;         377 AA.
AC   C5FEK4;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Probable aspartic-type endopeptidase CTSD;
DE            EC=3.4.23.-;
DE   Flags: Precursor; Fragment;
GN   Name=CTSD; ORFNames=MCYG_01216;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Secreted aspartic-type endopeptidase which is secreted and
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEQ28328.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DS995701; EEQ28328.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002851112.1; XM_002851066.1.
DR   AlphaFoldDB; C5FEK4; -.
DR   SMR; C5FEK4; -.
DR   STRING; 63405.XP_002851112.1; -.
DR   MEROPS; A01.077; -.
DR   EnsemblFungi; EEQ28328; EEQ28328; MCYG_01216.
DR   GeneID; 9228653; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_10_0_1; -.
DR   OrthoDB; 753343at2759; -.
DR   Proteomes; UP000002035; 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; Virulence.
FT   CHAIN           <1..350
FT                   /note="Probable aspartic-type endopeptidase CTSD"
FT                   /id="PRO_0000390766"
FT   PROPEP          351..377
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390767"
FT   DOMAIN          <1..292
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          296..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   LIPID           350
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   377 AA;  39731 MW;  1F2C39CD6BB5997F CRC64;
     SLIDTGASRT WVFGSDCTSK SCGAHNTFGK EDSKTIKVTD EKWDVAYGTG KVAGVIVNDT
     MSFAGFELDT PFGSATTASD DFMSYPMDGI LGIGPQDSKA KVPTVIQLLM QQKLLKSNII
     GINLQRNSDG ATDGQITFGD VDKSKFSGEL AYSNVVSGGY QWEIAVDDII VDGKPLNFQG
     RSGIVDTGTS FLLLPPDDAD LIHSKIPKSA KSSVFYTVPC STTTNIELSI SGVKYAIKPK
     DYVGYESTTK GICNSLIIGR QAIGPKQWLL GDVFLKNVYS VYDFDKNRVG LAARKYGETK
     DPPSSSHPPP APTSNKASGG SPGLPEQSGT SSATTSTTGE PSSGSTASPS AASSVSMSAW
     LSLAVFLSTA SSLILWD