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
//