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Database: UniProt
Entry: W9W2I9_9EURO
LinkDB: W9W2I9_9EURO
Original site: W9W2I9_9EURO 
ID   W9W2I9_9EURO            Unreviewed;       495 AA.
AC   W9W2I9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   28-JUN-2023, entry version 41.
DE   SubName: Full=Subtilisin-like serine protease pepC {ECO:0000313|EMBL:EXJ62277.1};
GN   ORFNames=A1O7_02710 {ECO:0000313|EMBL:EXJ62277.1};
OS   Cladophialophora yegresii CBS 114405.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ62277.1, ECO:0000313|Proteomes:UP000019473};
RN   [1] {ECO:0000313|EMBL:EXJ62277.1, ECO:0000313|Proteomes:UP000019473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ62277.1,
RC   ECO:0000313|Proteomes:UP000019473};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ62277.1}.
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DR   EMBL; AMGW01000002; EXJ62277.1; -; Genomic_DNA.
DR   RefSeq; XP_007754931.1; XM_007756741.1.
DR   AlphaFoldDB; W9W2I9; -.
DR   STRING; 1182544.W9W2I9; -.
DR   GeneID; 19177316; -.
DR   VEuPathDB; FungiDB:A1O7_02710; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000019473; Unassembled WGS sequence.
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:SF11; 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; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
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:UP000019473};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..495
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013062453"
FT   DOMAIN          42..137
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          182..427
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        184
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        216
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   495 AA;  52618 MW;  0A2FCF749B0C0AC4 CRC64;
     MKGLLLSLLP LLAAGSPVLV DTIHNDAAPI VSSSNAKEIP DSYMVVFKKH VTERDASAHH
     SWVLDTHSSH EARKLELRKR SQVSLADDTV FEGLRHTYNI PGGFLGYAGH FDEGVIELVR
     RHPDVEYIER DSQVQTMNHT PALEKNAPWG LARISHRDAL GFGDFNKYLY SEDGGEGVDA
     YVIDTGTNID HVDFEGRASW GKTIPAGDED IDGNGHGTHC SGTIAGKKFG VAKKANIYAV
     KVLKSNGSGT MSDVVKGVEW AANAHSESIS AAKKGKKKNF KGSVANMSLG GGKSRILDLA
     VNAAVDAGLH FAVAAGNDNA DSCNYSPAAA EKAVTVGAST LADERAYFSN YGTCNDIFAP
     GLNILSTWIG SKYATNIISG TSMASPHICG LLAYFLSLQP ANDSAYAVAA ITPKQLKANI
     IAIATEGALS NVPSDTANIL AWNGGGKSNF TEIVDDGGYS VNKFTPEDYL SEKASELKAE
     LKQIATELEA LIEKS
//
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