ID A0A179UBS5_BLAGS Unreviewed; 496 AA.
AC A0A179UBS5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cerevisin {ECO:0000313|EMBL:OAT04739.1};
GN ORFNames=BDBG_01242 {ECO:0000313|EMBL:OAT04739.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT04739.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
CC -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC activity that contributes to pathogenicity.
CC {ECO:0000256|ARBA:ARBA00002101}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; GG657449; OAT04739.1; -; Genomic_DNA.
DR RefSeq; XP_002628334.1; XM_002628288.1.
DR AlphaFoldDB; A0A179UBS5; -.
DR STRING; 559298.A0A179UBS5; -.
DR GeneID; 8510469; -.
DR KEGG; bgh:BDBG_01242; -.
DR VEuPathDB; FungiDB:BDBG_01242; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; 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; SSF52743; Subtilisin-like; 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 {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002038};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008107286"
FT DOMAIN 43..137
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 174..422
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 496 AA; 52760 MW; 04F918403B5BAA31 CRC64;
MKGLLALSIF PLLAASSPLV IDSIHQDAAP VLSSVNSKHV EDSYIIVFKK HVTSASAAAH
QSWVQNLHTT ALAKRSQLNK RNQFPFKNDV FSGLKHTYDI AGSLLGYSGS FDEEVIEQVR
KHPDVDFIEK DSEVHTMEKH KIEHNAPWGL ARISHRDSLS FGTFNKYLYA AAGGEGVDVY
VIDTGTNVDH VDFEGRAFWG KTIPIGDEDV DGNGHGTHCS GTVAGKKFGV AKKAHVYAVK
VLKSNGSGTM SDVVKGVEWA TTRHLRQVEA AKSGKGRKGF KGSAANMSLG GGKSMTLDLA
VNAAVDAGIH FAVAAGNDNA DSCSYSPAAA EKAVTVGAST LADERAYFSN YGPCNDIFAP
GLNILSTWIG SKYAVNTISG TSMASPHVAG LLAYFLSLQP AEESAFAVAP LTPEKLKATL
IDIGTWGVLT QVPADTENVL AWNGGGSSNY SAIVAKGGYK VASFQEQAQD TLDRLETAAN
HELHAIYSEL KSAFVL
//
