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Database: UniProt
Entry: A0A0A2I076_PENEN
LinkDB: A0A0A2I076_PENEN
Original site: A0A0A2I076_PENEN 
ID   A0A0A2I076_PENEN        Unreviewed;       399 AA.
AC   A0A0A2I076;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   22-FEB-2023, entry version 41.
DE   RecName: Full=penicillopepsin {ECO:0000256|ARBA:ARBA00013206};
DE            EC=3.4.23.20 {ECO:0000256|ARBA:ARBA00013206};
GN   ORFNames=PEX2_009280 {ECO:0000313|EMBL:KGO51361.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO51361.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO51361.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO51361.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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}.
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:KGO51361.1}.
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DR   EMBL; JQFZ01000288; KGO51361.1; -; Genomic_DNA.
DR   RefSeq; XP_016594314.1; XM_016738205.1.
DR   AlphaFoldDB; A0A0A2I076; -.
DR   STRING; 27334.A0A0A2I076; -.
DR   GeneID; 27673624; -.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   OrthoDB; 615305at2759; -.
DR   PhylomeDB; A0A0A2I076; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..399
FT                   /note="penicillopepsin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009752317"
FT   DOMAIN          86..396
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        117..122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        322..355
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   399 AA;  43487 MW;  77778E19B739A160 CRC64;
     MMKSFTLLTA SALLGSAAAE VHRLKLNKVP LSEQLNTHNI DAHVHNLGQK YMGIRPEKHQ
     DLFHDTSLNP ASGHGVLVDN FLNAQYFSEI TIGTPPQTFK VVLDTGSSNL WVPSSQCSSI
     ACFLHSKYDS SSSSTYQKNG TEFEIRYGSG SLSGFVSRDT LQIGDLKVEG QDFAEATNEP
     GLAFAFGRFD GILGLGYDTI SVNKMVPPFY HMINQKLVDE PVFAFYLGDT NKDGDDSVAT
     FGGIDESHYT GELIKIPLRR KAYWEVELNS IALGNNVAEL DNTGVILDTG TSLIALPSTM
     AELLNKEIGA TKGFTGQYSV ECDKRDSLPD LTFTLGGHKF TIGPFDYILE VQGSCISSFM
     GMDFPEPVGP LAILGDAFLR RWYSVYDVGN NAVGLAKAK
//
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