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 27-MAR-2024, entry version 55.
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}.
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DR EMBL; DS989829; EFR04922.1; -; Genomic_DNA.
DR RefSeq; XP_003169757.1; XM_003169709.1.
DR AlphaFoldDB; E4V4J8; -.
DR SMR; E4V4J8; -.
DR STRING; 535722.E4V4J8; -.
DR GlyCosmos; E4V4J8; 4 sites, No reported glycans.
DR GeneID; 10024988; -.
DR VEuPathDB; FungiDB:MGYG_07924; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_3_1; -.
DR InParanoid; E4V4J8; -.
DR OMA; AMDWAVK; -.
DR OrthoDB; 380531at2759; -.
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; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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
//
