ID   SUB6_ARTGP              Reviewed;         408 AA.
AC   E4V4J8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Subtilisin-like protease 6;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB6; ORFNames=MGYG_07924;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS989829; EFR04922.1; -; Genomic_DNA.
DR   RefSeq; XP_003169757.1; XM_003169709.1.
DR   AlphaFoldDB; E4V4J8; -.
DR   SMR; E4V4J8; -.
DR   STRING; 63402.XP_003169757.1; -.
DR   EnsemblFungi; EFR04922; EFR04922; MGYG_07924.
DR   GeneID; 10024988; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   InParanoid; E4V4J8; -.
DR   OMA; CEGSGSN; -.
DR   OrthoDB; 308083at2759; -.
DR   Proteomes; UP000002669; 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; IPR023827; Peptidase_S8_Asp-AS.
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; PS00136; SUBTILASE_ASP; 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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..123
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000406374"
FT   CHAIN           124..408
FT                   /note="Subtilisin-like protease 6"
FT                   /id="PRO_0000406375"
FT   DOMAIN          36..119
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          131..408
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        163
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        354
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   408 AA;  42209 MW;  8C1BAA03D6A9666B CRC64;
     MGFITKAIPI VLAALSTVDG AKILEAGPHA ETIPNKYIVV MKQDVSHEAF NAHATWVGNN
     FSRRPMRRGG SFKPMAGMQH KFSLGGTFKA YTGEFDEAMI KDISNHDDVD FIERDTVVKA
     TAITQQDNVP SWGLARVGSK EAGGSTYYYD DTAGKGVTAY IIDTGIDIHH GDFGGRAKWG
     KNFVDKMDED CNGHGSHVAG TVGGTKFGVA KGVNLVAVKV LDCEGSGSNS GVIMGMEWAM
     KEASGGGNST AKAAGKSVMN MSLGGPRSEA SNKAAKAIAD AGIFMAVAAG NDNMDAQHSS
     PASEPSICTV AASSEDDSKA DFSNYGAVVD IYAPGNEITS VKPGNGTDTL SGTSMASPHV
     CGLGAYLIGL GKEGGPGLCD TIKEMATDAI KNPGEGTTGK LIYNGSGK