ID   SUB2_ARTOT              Reviewed;         424 AA.
AC   Q8J0D8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Subtilisin-like protease 2;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB2;
OS   Arthroderma otae (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=63405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IHEM 15221;
RX   PubMed=12406327; DOI=10.1046/j.1523-1747.2002.01784.x;
RA   Descamps F., Brouta F., Monod M., Zaugg C., Baar D., Losson B., Mignon B.;
RT   "Isolation of a Microsporum canis gene family encoding three subtilisin-
RT   like proteases expressed in vivo.";
RL   J. Invest. Dermatol. 119:830-835(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAD24009.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ431179; CAD24009.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q8J0D8; -.
DR   SMR; Q8J0D8; -.
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; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..123
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380767"
FT   CHAIN           124..424
FT                   /note="Subtilisin-like protease 2"
FT                   /id="PRO_5000068279"
FT   DOMAIN          37..123
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          132..424
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        170
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        359
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   424 AA;  45738 MW;  F284C0DD0B221775 CRC64;
     MQLLNLGLLL LLPFVAGEIA PQPEPLRAGP SDIVPGQYIV TLKEGLASAQ IREHKKWVSS
     VHQANLDSFA AGASGVETVG IMKNFHIHNL NMYSGGFDDK TAEDLRRSPD VKSVHPDQHV
     YLAKTVTQPQ ARWGLGYMSS KGMPVPLHST LVDYLYDDKA GEGVWAYVLD TGINVDHIEF
     EDRGILGHNA IPNKPHTDEF EHGTYVAGII AGKTYGVAKK ANVVSAKAFD TGSSTYNYIL
     ETYDWIVKNI TDSNRKNKAV INLSISGAKY QPFDDAVENA FKAGITAVVA AGNDGKDAKN
     NTPASSPNAI TVGAVRWENT RPSLASNYGK IVDIWAPGEL IKSCWKGGNN ATSTQSGTSA
     ASPHVAGLVA YLMSLENLPS PSAVTARVLN LTIPNLVKDA KDSPNRVVYN GIQERKFTLP
     KNTK