ID   SUB11_ARTGP             Reviewed;         400 AA.
AC   E4V5C5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Subtilisin-like protease 11;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB11; ORFNames=MGYG_08213;
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}.
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DR   EMBL; DS989829; EFR05199.1; -; Genomic_DNA.
DR   RefSeq; XP_003170034.1; XM_003169986.1.
DR   AlphaFoldDB; E4V5C5; -.
DR   SMR; E4V5C5; -.
DR   STRING; 63402.XP_003170034.1; -.
DR   EnsemblFungi; EFR05199; EFR05199; MGYG_08213.
DR   GeneID; 10025269; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   InParanoid; E4V5C5; -.
DR   OMA; GWHAYSG; -.
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; 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.
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..117
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000406400"
FT   CHAIN           118..400
FT                   /note="Subtilisin-like protease 11"
FT                   /id="PRO_0000406401"
FT   DOMAIN          35..116
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          127..400
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        159
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  41693 MW;  F316061E2E36FEED CRC64;
     MGLFTVVFTA IAALSAVDAA ELLRSPNSKD IVPNSYLVVM KDSVSSADLD SHVSWVTDLH
     SESITKPGVK NLDGFKHSYK INGWHAYSGS FDSETLASIL DNDQVDFVEH DRYVYIDGLV
     TQKDAPSWGL GRVSHRMNGT RDYVYDETAG SGITFYGVDT GIDIRHPDFG GRAVWGTNVV
     SGTGDNDRHG HGTHTAATAT GTKYGLAKKA NVVAVKALND HGAGLWSNIM KALEWCVDDA
     RKKNALGKAV LNLSISGGKV VAANQAITNA ANAGIFVSVA AGNDNQDATN KSPASAENVC
     CAAASTIRDE KASISNYGSV VKLYAPGQGI TSATPNNSTG VMTGTSMAAP HVGGVGATLM
     ASKHIAPSAV CAELIKMATG AVRNPGANTT NKLLYNGSGQ