ID B8PD81_POSPM Unreviewed; 426 AA.
AC B8PD81;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EED81157.1};
GN ORFNames=POSPLDRAFT_106813 {ECO:0000313|EMBL:EED81157.1};
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:EED81157.1, 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; EQ966320; EED81157.1; -; Genomic_DNA.
DR RefSeq; XP_002473625.1; XM_002473580.1.
DR AlphaFoldDB; B8PD81; -.
DR KEGG; ppl:POSPLDRAFT_106813; -.
DR HOGENOM; CLU_013253_8_2_1; -.
DR InParanoid; B8PD81; -.
DR OrthoDB; 1656645at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 382..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..333
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 426 AA; 46323 MW; 3C23E8D078651C47 CRC64;
MSNGVRIPFR IERIPKGYSS RSIRATRRTV DELAGYDNLN DSRYVGEVLV SGRPFEIILD
TGSHEFWLKT DTTLSNYTNT SITAMIDYGG GTGLGSTVSG FVLLAETQFA NFTIKEQPFI
NVLEPASSFI VPGINGLMGI APLVYIFPCY CWLTVLFGIT TSPNDDTAIN NAFKQANYTA
SNGGNPVENI FAQNPNLTPQ FTMLMTRNDG EVRSSGGVFT MASISPELVE FIYGADAEIT
SNGLAAVVSC ETMLNVSFVI GGVEYPVNPL DSVIPTGHYY NNTVACTGGF QRAQGAPWNE
SMLLLGDTFL RNVYALYNLN LRQSDGNTTL PFVQLLSVTD ANLAASQFPE QNLARLESFA
QAYGYTVPLP PDPLAPILRN SAIIIVMSIV ALILAFIAAF YAVRNARMQS SRGDYVVLSE
EQKGGR
//