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Database: UniProt
Entry: B6HU56_PENRW
LinkDB: B6HU56_PENRW
Original site: B6HU56_PENRW 
ID   B6HU56_PENRW            Unreviewed;       505 AA.
AC   B6HU56;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=penicillopepsin {ECO:0000256|ARBA:ARBA00013206};
DE            EC=3.4.23.20 {ECO:0000256|ARBA:ARBA00013206};
GN   ORFNames=Pc22g18210 {ECO:0000313|EMBL:CAP99109.1}, PCH_Pc22g18210
GN   {ECO:0000313|EMBL:CAP99109.1};
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:CAP99109.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP99109.1, 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   -!- 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; AM920437; CAP99109.1; -; Genomic_DNA.
DR   RefSeq; XP_002565726.1; XM_002565680.1.
DR   AlphaFoldDB; B6HU56; -.
DR   STRING; 500485.B6HU56; -.
DR   MEROPS; A01.077; -.
DR   GeneID; 8312838; -.
DR   KEGG; pcs:Pc22g18210; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g18210; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_10_0_1; -.
DR   OMA; AFYPWEL; -.
DR   OrthoDB; 3087283at2759; -.
DR   BioCyc; PCHR:PC22G18210-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
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:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-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};
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:UP000000724};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..505
FT                   /note="penicillopepsin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002843776"
FT   DOMAIN          106..414
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          432..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        137..142
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   505 AA;  54123 MW;  3387F8AC8F771202 CRC64;
     MRLSSCLVFI AGISGVHAFY PWELRMKLST ETTVKRRFVP WTLIGAKSDD STDSTDTSNA
     ANRKPFTLDL KKVPVRRDHV YKIVESHKPS LADSAPLHQD GTDYSYFSPV YVGSQKQEMW
     MAIDTGAPNT WVFDSKCTEP VCIHHHTFDR SASTSFTTDN LAFSLFYGSG KIDGKMGKDT
     LSIAGLEVLQ TFGLANNASE TFESYPFDGI LGLGRSHTSG WNLPSFMDLV AEKKLIKSNL
     VGFSLSRSED NHKDGEINFG DVDTTKFDGT ISYTATNDKN WNIPLDDAYV NGQSCNFSGR
     TATIDTGTTY LLIPPADAKA LFSLVPDSSQ QPDNPNNYLI PCNSTATIEF EFSGVKYNIS
     PKDYVGNPEP EGSDYCISTI VGYASNGADW LVGDVFLKNV YTVFDFDNGQ VGFGALASAS
     ASASALKSNL DPSSTSSSSS SSPPQGNGTF TAPLVTGTAA STADATSSSS PASSAMATVS
     GSSASHLVHG ISWSMLTVMI AAFAV
//
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