ID   SUB1_ARTOC              Reviewed;         485 AA.
AC   C5FPS1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Subtilisin-like protease 1;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB1; ORFNames=MCYG_04495;
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 subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; DS995704; EEQ31676.1; -; Genomic_DNA.
DR   RefSeq; XP_002846758.1; XM_002846712.1.
DR   AlphaFoldDB; C5FPS1; -.
DR   SMR; C5FPS1; -.
DR   STRING; 63405.XP_002846758.1; -.
DR   MEROPS; S08.062; -.
DR   EnsemblFungi; EEQ31676; EEQ31676; MCYG_04495.
DR   GeneID; 9229872; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   OMA; PKVMFVE; -.
DR   OrthoDB; 921536at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..116
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384063"
FT   CHAIN           117..485
FT                   /note="Subtilisin-like protease 1"
FT                   /id="PRO_0000384064"
FT   DOMAIN          34..116
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..400
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          377..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..454
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        190
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   485 AA;  51283 MW;  231B1116582E1532 CRC64;
     MGIFRFISIS LAAVSAANAG HILSMGHAKT IPNSYIVVMK DGTTEEDFTH HQSWVQSIHT
     HNVTRRGLLD NAGVRHKYGF GSMMGYAGLF DEDTIKDISD DPKVMFVEPD TTITIHGELT
     QNDVPSWGLA RISSQRPGTE DYTYDSSAGE GITVYSVDTG VDIHHEDFEG RASWGTNMIE
     DGYDKDGNGH GTHTAGTMVG KTFGIAKKAK VVAVKVLDNN GSGPTSGIIA GINWCAQHAS
     QNGGTDKAVI NMSLGGGSSS ALNRAAAQAV QKGMFLAVAA GNDNQDARTS SPASEDTVCT
     VGASAENDER SSFSNWGPAV DLFAPGSNIV STRPGGGSQS MSGTSMASPH VAGLGAYIMA
     LEGISGSAVC DRLKQLGTSS VTNPGPGTRT NILINNGDAK NGGKKPSQPS QPPKPSQPSK
     PQQPSEPQEP SEPQEPAPGQ PAPAPAPVPQ HPHTPFPNDD FNFDDFWKKY FGTDHWRKTF
     GRFWN