ID   SUB8_ARTBC              Reviewed;         490 AA.
AC   D4AX50;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Subtilisin-like protease 8;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB8; ORFNames=ARB_00777;
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).
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; ABSU01000016; EFE32255.1; -; Genomic_DNA.
DR   RefSeq; XP_003012895.1; XM_003012849.1.
DR   AlphaFoldDB; D4AX50; -.
DR   SMR; D4AX50; -.
DR   STRING; 663331.D4AX50; -.
DR   EnsemblFungi; EFE32255; EFE32255; ARB_00777.
DR   GeneID; 9522973; -.
DR   KEGG; abe:ARB_00777; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   OMA; SNYGKCN; -.
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; 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_0000406378"
FT   CHAIN           135..490
FT                   /note="Subtilisin-like protease 8"
FT                   /id="PRO_0000406379"
FT   DOMAIN          43..134
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        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   490 AA;  52335 MW;  DEDD1BBEE492D88F CRC64;
     MKGLLSLSVL PVLAYASPMI VDSIHQNAAP ILSSTNAKDI PDSYIVVFKK GVTSTSALAH
     QNWVQDIHTS VESKRMKKRN QFTFKNEAFD GLKHTFDFAG GFLGYSGHFD EEVIEQVRRH
     PDVEYIERDS EVHTLKAATE NGAPWGLARI SHRDKLNFGT FNKYIYASQG GEGVDAYVID
     TGTNIDHVDF EGRASWGKTI PQGDDDVDGN GHGTHCSGTI AGKKYGVAKK ANVYAVKVLR
     TSGSGTMSDV VKGVQWAAES HLKSVGEAKK GNRKGFKGSV ANMSLGGGKS VTLDRVVDQA
     VAVGMHFAVA AGNDNADACN YSPAGSKNSI TVGASTLADE RAYFSNFGKC TDIFAPGLNI
     QSTWIGSKHA VNTISGTSMA SPHICGLLAY FLSLQPASDS AFAVAEITPA EMKDNMISIA
     SKDLLSDIPS DTPNLLAWNG GGSDDYKKII GGARENDTTE FSSTLTEKLE KLAEEGLTAI
     YNELKDAVVA