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Database: UniProt
Entry: B6HRR4_PENRW
LinkDB: B6HRR4_PENRW
Original site: B6HRR4_PENRW 
ID   B6HRR4_PENRW            Unreviewed;       419 AA.
AC   B6HRR4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Pc22g03580 protein {ECO:0000313|EMBL:CAP97646.1};
GN   ORFNames=Pc22g03580 {ECO:0000313|EMBL:CAP97646.1}, PCH_Pc22g03580
GN   {ECO:0000313|EMBL:CAP97646.1};
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:CAP97646.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP97646.1, 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 A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; AM920437; CAP97646.1; -; Genomic_DNA.
DR   RefSeq; XP_002564399.1; XM_002564353.1.
DR   AlphaFoldDB; B6HRR4; -.
DR   MEROPS; A01.080; -.
DR   GeneID; 8306117; -.
DR   KEGG; pcs:Pc22g03580; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g03580; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_2_1; -.
DR   OMA; WYGGVQS; -.
DR   OrthoDB; 2900143at2759; -.
DR   BioCyc; PCHR:PC22G03580-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN          89..417
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   419 AA;  45349 MW;  A2BD266A707B38CA CRC64;
     MTRIKLIANP HYQKSGTKSY LYAMRKYRFT PTKDGPYFLG TTMVQTGRQF TNKPVGGRAR
     LQQVLQKKDA VSDEVGQVGV HDVQNDSMYL AEIGIGTPAQ TLNLDFDTGS ADLWVWSTEL
     SSKILSANKN HRVFDPTKSS TFEEKDGSTW QIKYGDGSFA SGTVGNDNVT IGGLVVKGQA
     VGIADILSEQ FAQGAGDGLL GLAFSNINTV KPEAVAMPVE NMISQADIPK SAELFTAKLG
     SWRDTDEPDK GESFYTFGYV DQDTVKAAES EIYYTPVDNS QGFWMFDSTS ATVNGKSIAR
     AGNKAIADTG TTLALVDDET CQAVYDAIPG AKYDNASQGW IFPSNTPADK LPVVSFAVGE
     KQFVVQKEDL GFAEAKSGYV YGGIQSRGTM TMDILGDTFL KAIYAVSDML FFGVHSCTN
//
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