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Database: UniProt
Entry: A0A072PNK1_9EURO
LinkDB: A0A072PNK1_9EURO
Original site: A0A072PNK1_9EURO 
ID   A0A072PNK1_9EURO        Unreviewed;       496 AA.
AC   A0A072PNK1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Cerevisin {ECO:0000313|EMBL:KEF61292.1};
GN   ORFNames=A1O9_02857 {ECO:0000313|EMBL:KEF61292.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF61292.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF61292.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF61292.1,
RC   ECO:0000313|Proteomes:UP000027920};
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 Exophiala aquamarina CBS 119918.";
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:KEF61292.1}.
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DR   EMBL; AMGV01000002; KEF61292.1; -; Genomic_DNA.
DR   RefSeq; XP_013263882.1; XM_013408428.1.
DR   AlphaFoldDB; A0A072PNK1; -.
DR   STRING; 1182545.A0A072PNK1; -.
DR   GeneID; 25277798; -.
DR   VEuPathDB; FungiDB:A1O9_02857; -.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000027920; 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: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   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:UP000027920};
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..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..496
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001681806"
FT   DOMAIN          43..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   496 AA;  52536 MW;  19C6E99A51438208 CRC64;
     MKSFLGLSLL PLLAAGSPVI VETIHKDAAP VISSSNAKEI PDSYMVVFKQ HVSNADAVAH
     HSWIQDLHLT NQVNKQELRK RSFGFSEDTI FEGLRHTYNI PGGLLGYAGH FDQDVIEQVR
     RHPDVEYIER DSEVHTMKET PALEKNAPWG LARISHRKSL GFGDFNKYLY SEDGGEGVDA
     YVIDTGTNTE HVDFEGRASW GKTIPQGDED VDGNGHGTHC SGTIAGKKFG VAKKANIYAV
     KVLKSNGSGT MSDVVKGVEW AATAHSGSVS AAKKGKKKGF KGSVANMSLG GGKSRVLDLA
     VNAAVDAGLH FAVAAGNDNA DSCNYSPAAA ENAVTVGAST LADERAYFSN FGACNDIFAP
     GLNVLSTWIG SKYATNTISG TSMASPHIAG LLAYLLSLQP SNDSAYAVAE ITPKKLKANI
     IAIATEGALT NVPADTANIL AWNGGGKSNY TEIIKDGGYT LDNAAGTESY LSEKAQELKL
     ELKKIAAELE ALVEAS
//
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