ID   SUB2_ARTBC              Reviewed;         421 AA.
AC   D4AZ75;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Subtilisin-like protease 2;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB2; ORFNames=ARB_01495;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   INDUCTION.
RX   PubMed=19942661; DOI=10.1099/mic.0.033464-0;
RA   Staib P., Zaugg C., Mignon B., Weber J., Grumbt M., Pradervand S.,
RA   Harshman K., Monod M.;
RT   "Differential gene expression in the pathogenic dermatophyte Arthroderma
RT   benhamiae in vitro versus during infection.";
RL   Microbiology 156:884-895(2010).
CC   -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Expression is up-regulated during infection.
CC       {ECO:0000269|PubMed:19942661}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE31595.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000020; EFE31595.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003012235.1; XM_003012189.1.
DR   AlphaFoldDB; D4AZ75; -.
DR   SMR; D4AZ75; -.
DR   STRING; 663331.D4AZ75; -.
DR   EnsemblFungi; EFE31595; EFE31595; ARB_01495.
DR   GeneID; 9519803; -.
DR   KEGG; abe:ARB_01495; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   Proteomes; UP000008866; 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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..122
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397782"
FT   CHAIN           123..421
FT                   /note="Subtilisin-like protease 2"
FT                   /id="PRO_0000397783"
FT   DOMAIN          36..122
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          131..421
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        357
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        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  45608 MW;  0A144F717D1DB978 CRC64;
     MQLLNFGLLL LPFVAGDLAP QPEPLLAGPS DVVPGQYIVT LKEGLTSAQI RDHKKWVSSV
     HRANLDSFAA GASGVETEGI MKHFHIHDLN MYSGGFDEKT VEDLSRNPYV KSVHPDQHVY
     LAKTVTQRQA RWGLGYMSSK GKPVPLHSTL VDYSYDDKAG EGVWAYVLDT GINVNHVEFE
     GRGILGHNAI PNKPHTDEFG HGTYVAGIIA GKTYGVAKKA NVVSAKAFDT GSSTYNYILE
     TYDWIVRNIT DSNRKNKAVI NLSISGAKYQ PFDDAVEKAF KAGITTVVAA GNDGKDAKNN
     TPASSPNAIT VGAVRWENTR PSFSNYGKLV DIWAPGELIK SCWKGGNNAT STQSGTSAAS
     PHVAGLVAYL MSIENLPSPS AVTARVLNLT IPNLVKDAKD SPNRVAYNGI QERKFTLPKY
     Y