ID SUB6_ARTOC Reviewed; 406 AA.
AC C5FQI3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Subtilisin-like protease 6;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB6; ORFNames=MCYG_04955;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995704; EEQ32136.1; -; Genomic_DNA.
DR RefSeq; XP_002847218.1; XM_002847172.1.
DR AlphaFoldDB; C5FQI3; -.
DR SMR; C5FQI3; -.
DR STRING; 554155.C5FQI3; -.
DR GlyCosmos; C5FQI3; 5 sites, No reported glycans.
DR GeneID; 9223824; -.
DR VEuPathDB; FungiDB:MCYG_04955; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_3_1; -.
DR OMA; AMDWAVK; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000002035; 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; 3.40.50.200; 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 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..122
FT /evidence="ECO:0000250"
FT /id="PRO_0000384073"
FT CHAIN 123..406
FT /note="Subtilisin-like protease 6"
FT /id="PRO_0000384074"
FT DOMAIN 36..119
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 130..406
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 42160 MW; A7B72E70C741A667 CRC64;
MGFITKALPL ALAAFSTVNG AKILEASPGA DTIPDSYIVV MKAGVTSETF SAHTDWVGRT
YQRRPMRRGA NSQPMAGLQH SLSFGGNFMY AGQFDQAMID DIAKNDDVDF IEPDYKVTLS
SITEQKDVPS WGLSRLSTKE PGGTTYFYDE SAGEGTTAYI VDTGIDVNNG DFGGRAKWGN
NFVDHQDTDC NGHGTHVAGT VGGKNFGVAK KTNLIAVKVL DCNGSGSNSG VIKGMEWVMR
DASGGGNSTS KASKSVMNMS LGGPRSEATN RAAKAISDAG IFLAVAAGND NADSQHDSPA
SEPSVCTVAA SAEDDTKASF SNWGQAVDVF APGMHITSDK PGNGTAVLSG TSMASPHVCG
IGAYLIGLGK KGGPGLCDTI KDMARPVIKN PGQGTTNKLI YNGSGK
//
