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Database: UniProt
Entry: W6QCD4_PENRF
LinkDB: W6QCD4_PENRF
Original site: W6QCD4_PENRF 
ID   W6QCD4_PENRF            Unreviewed;       410 AA.
AC   W6QCD4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   08-NOV-2023, entry version 38.
DE   RecName: Full=penicillopepsin {ECO:0000256|ARBA:ARBA00013206};
DE            EC=3.4.23.20 {ECO:0000256|ARBA:ARBA00013206};
GN   ORFNames=PROQFM164_S01g001086 {ECO:0000313|EMBL:CDM27277.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM27277.1};
RN   [1] {ECO:0000313|EMBL:CDM27277.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM27277.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
CC   -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC       proteinaceous substrates. The scissile peptide bond is attacked by a
CC       nucleophilic water molecule activated by two aspartic residues in the
CC       active site. Shows a broad primary substrate specificity. Favors
CC       hydrophobic residues at the P1 and P1' positions, but can also activate
CC       trypsinogen and hydrolyze the B chain of insulin between positions
CC       'Gly-20' and 'Glu-21'. {ECO:0000256|ARBA:ARBA00002983}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity similar to that
CC         of pepsin A, preferring hydrophobic residues at P1 and P1', but also
CC         cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and
CC         activates trypsinogen.; EC=3.4.23.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00000043};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; HG792015; CDM27277.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QCD4; -.
DR   STRING; 1365484.W6QCD4; -.
DR   OMA; WFNRECY; -.
DR   OrthoDB; 4940213at2759; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}.
FT   DOMAIN          38..406
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   410 AA;  44546 MW;  86C966D515E958D6 CRC64;
     MKLPSLVTAS QLTFPLTFQT AFHTTSNTAS LLSAQYGTTL NVDVTFANQT FKLLVDTGSS
     DTYVVRNDFI CINQTTNLEI PQADCQHVSP GYNESDTYRL IPNKIFGIQY GNGIASGVMA
     YEDITLAGIT VPGQAVGIVG HSNPMGDGIN SGVLGLAYPS LTSAHPGDHT DNTTFWFNRE
     CYSPLFNTMY EQGLVSEPYF SIALAHTPRN LSMPTFGGYL TLGDLPPVAY DPKFASVPVE
     ILENIPPSFT SGKRTRSYWA FTVSAVTFGS TTKVDLTTST TSITTNSMEF QVFTDTGNDY
     SYLPAVVADP INALFNPPAI YNETLGVAVV NCNAQPPMFG VQIGDQTFYH DGQDLIYQTG
     DGYCVSSLVA SERVAFEGIM LNILGVPFLK NVVSVYDFGR NELRFAQRSD
//
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