ID SUB3_ARTOC Reviewed; 397 AA.
AC C5FMY5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Subtilisin-like protease 3;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB3; ORFNames=MCYG_04040;
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}.
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DR EMBL; DS995704; EEQ31221.1; -; Genomic_DNA.
DR RefSeq; XP_002846303.1; XM_002846257.1.
DR AlphaFoldDB; C5FMY5; -.
DR SMR; C5FMY5; -.
DR STRING; 554155.C5FMY5; -.
DR GlyCosmos; C5FMY5; 2 sites, No reported glycans.
DR GeneID; 9224372; -.
DR VEuPathDB; FungiDB:MCYG_04040; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_3_1; -.
DR OMA; GHINRTV; -.
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; 3.30.70.80; 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; 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:SF68; ALKALINE PROTEASE 1; 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; 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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000384067"
FT CHAIN 117..397
FT /note="Subtilisin-like protease 3"
FT /id="PRO_0000384068"
FT DOMAIN 35..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 126..397
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 344
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 40855 MW; BB09E91E4D987B31 CRC64;
MGCIKVISVF LAAVAAVDAR AFFHNRGGND VIPNSYIVVM KDGVTAEDFD SHISSVATTH
SINKAKRGSE TVGHKDSFNI NGWRAYNGHF DEATIESILN DDKVDYVEHD RVVKLAALTT
QPNAPTWGLG RVSHKAPGNK DFVYDSSAGQ GVTIYGVDTG IDINHPEFRG RIRWGTNTVD
NDNTDGNGHG THTAGTFAGT TYGVAKKANI VAVKVLSAGG SGSTAGVIKG IDWCVTDAKA
KGALGKAALN LSLGGAFSQA NNDAVTRAQN AGIFVAVAAG NDNKDAKNSS PASAPAVCTA
ASSTIDDQKS SFSNWGTIVD IYAPGSNILS AAPGGGTRTL SGTSMASPHV CGVGAAMLAQ
GVSVAQACDR IKQIANAVIK NPGTGTTNKL LYNGSGR
//
