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Database: UniProt
Entry: B6HLS3_PENRW
LinkDB: B6HLS3_PENRW
Original site: B6HLS3_PENRW 
ID   B6HLS3_PENRW            Unreviewed;       494 AA.
AC   B6HLS3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   SubName: Full=Vacuolar serine proteinase AAG44693-Penicillium chrysogenum {ECO:0000313|EMBL:CAP96594.1};
GN   ORFNames=Pc21g16970 {ECO:0000313|EMBL:CAP96594.1}, PCH_Pc21g16970
GN   {ECO:0000313|EMBL:CAP96594.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP96594.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP96594.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; AM920436; CAP96594.1; -; Genomic_DNA.
DR   RefSeq; XP_002568697.1; XM_002568651.1.
DR   AlphaFoldDB; B6HLS3; -.
DR   SMR; B6HLS3; -.
DR   STRING; 500485.B6HLS3; -.
DR   Allergome; 525; Pen ch 18.
DR   GeneID; 8310066; -.
DR   KEGG; pcs:Pc21g16970; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g16970; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   OMA; NADSCNY; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
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:UP000000724};
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..494
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002845775"
FT   DOMAIN          43..136
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          180..421
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        182
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        376
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   494 AA;  52309 MW;  5F6A37AF0DAEA894 CRC64;
     MKGFLSLTLL PLLVAASPVA VNSIHNDAAP ILSSMTSKDI PDSYIVVFKK HVDPSSASAH
     QSWLQEVHTA HTGRMELKKR SLFGFDFEAF MGLKHTFHIA GSLLGYAGHF HEDVIEQIRR
     HPDVDYIEKD SEVRTMSEGS VEKNAPWGLA RISHRESLSF GNFNKYLYAE EGGEGVDAYV
     IDTGANVKHV DFEGRANWGK TIPQGDADED GNGHGTHCSG TIAGKKFGVA KKANVYAVKV
     LRSNGSGTMS DVVKGVEWAA EAHIKKSKKG DKKFKGSVAN MSLGGGSSRT LDLAVNAAVD
     AGIHFAVAAG NDNADACNYS PAAAEKAITV GASTLADERA YFSNYGKCTD IFAPGLNILS
     TWVGSDHATN TISGTSMASP HIAGLLAYYV SLAPAKDSAY AVADVTPKQL KAALISVATE
     GTLTDIPSDT PNLLAWNGGG SANYTKILAD GGYKAHNAET TVEDRIGGII DSAEKAFHKE
     LGAIYSEIKD AVSA
//
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