ID   SUB8_ARTOC              Reviewed;         490 AA.
AC   C5FII2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Subtilisin-like protease 8;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB8; ORFNames=MCYG_02070;
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; DS995702; EEQ29251.1; -; Genomic_DNA.
DR   RefSeq; XP_002849136.1; XM_002849090.1.
DR   AlphaFoldDB; C5FII2; -.
DR   SMR; C5FII2; -.
DR   STRING; 63405.XP_002849136.1; -.
DR   PRIDE; C5FII2; -.
DR   EnsemblFungi; EEQ29251; EEQ29251; MCYG_02070.
DR   GeneID; 9229190; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   OMA; SNYGKCN; -.
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; IPR022398; Peptidase_S8_His-AS.
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; PS00137; SUBTILASE_HIS; 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..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..134
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000406380"
FT   CHAIN           135..490
FT                   /note="Subtilisin-like protease 8"
FT                   /id="PRO_0000406381"
FT   DOMAIN          43..133
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          144..450
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        180
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        378
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   490 AA;  52480 MW;  6D09396BF1F3E7E0 CRC64;
     MKGLLSLSVL PVLAYASPMI VDSIHQDAAP ILSSTNAKDI PDSYIVVFKK GVSSSSALAH
     QTWVQEIHTS TESKRLKKRN QFTFKNEAFD GLKHTFDIAG GLLGYSGHFD EEVIEQVRRH
     PDVEYIERDS EVRALESVTE NGAPWGLARI SHRKRLNFGT FNKYIYAAQG GEGVDAYVID
     TGTNIEHVDF EGRASWGKTI PENDDDIDGN GHGTHCSGTI AGKKYGVAKK AHVHAVKVLR
     TSGSGTMSDV VKGVQWAAES HLKQVGETKK GNRKGFKGSV ANMSLGGGKS VTLDRVVDQA
     VAVGMHFAVA AGNDNADACN YSPAASQNSI TVGASTLTDE RAYFSNYGKC TDIFAPGLNI
     QSTWIGSKYA VNTISGTSMA SPHICGLLAY FLSLQPASDS AFAVAEITPA EMKENMISIA
     SKNALTDIPA DTPNLLAWNG GGSDNYKEIV GGKDNATKEH ISSTLTEKLE QLAEEGLTAI
     YNELKDVVVA