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
//