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Database: UniProt
Entry: B8P524_POSPM
LinkDB: B8P524_POSPM
Original site: B8P524_POSPM 
ID   B8P524_POSPM            Unreviewed;       413 AA.
AC   B8P524;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-NOV-2023, entry version 65.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EED83975.1};
GN   ORFNames=POSPLDRAFT_96655 {ECO:0000313|EMBL:EED83975.1};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN   [1] {ECO:0000313|EMBL:EED83975.1, ECO:0000313|Proteomes:UP000001743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA   Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA   Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA   Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA   Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA   Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA   Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA   Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA   Brettin T., Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT   placenta supports unique mechanisms of lignocellulose conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; EQ966257; EED83975.1; -; Genomic_DNA.
DR   RefSeq; XP_002470770.1; XM_002470725.1.
DR   AlphaFoldDB; B8P524; -.
DR   MEROPS; A01.019; -.
DR   KEGG; ppl:POSPLDRAFT_96655; -.
DR   HOGENOM; CLU_038846_0_0_1; -.
DR   InParanoid; B8P524; -.
DR   OMA; ANNTEGF; -.
DR   OrthoDB; 1469204at2759; -.
DR   Proteomes; UP000001743; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 2.
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:UP000001743}.
FT   DOMAIN          57..413
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   413 AA;  43727 MW;  96CD56CDFEC0EB98 CRC64;
     MLLRLLSPNL AGAVLISTLF CTAYAGAIVK VPFTSTIMLI SSSGNSNVPT TNAGLKVTVQ
     VQAGNDQTFN DILVDTGSSF LWVGAQEAYA LGPYTQIINE TFDANYGEGG ATGTAYIDRV
     TVGVVTASAA FIGAANNTEG FQIAEPLGGI SQCSPYISSQ LLTYTQTAAR SCRHRQLRSR
     HGPREHELQR RLSGYNTTPT FVQSLAAEGV IPAAMFGVYV SPLSASGEPG STGELTFGGV
     DESKFSAERE PWGDRRDRLA PALRCGQSAL ASRGLYFGWG GEYAINTTLY SLVDTGTYFI
     GIPNDGLFYI LQTTPDAELA SSSLLEGCLT FPANASGTLP PLYVGVGSLN FTITPAEYIV
     PTPLYAALNI TDADTIYTVL CPAGPNQYNL GMSFLEHAYS AFDLIGLAQL ASR
//
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