ID   B8PD85_POSPM            Unreviewed;      1158 AA.
AC   B8PD85;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EED81176.1};
GN   ORFNames=POSPLDRAFT_106819 {ECO:0000313|EMBL:EED81176.1};
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:EED81176.1, 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; EED81176.1; -; Genomic_DNA.
DR   RefSeq; XP_002473644.1; XM_002473599.1.
DR   AlphaFoldDB; B8PD85; -.
DR   KEGG; ppl:POSPLDRAFT_106819; -.
DR   HOGENOM; CLU_275583_0_0_1; -.
DR   InParanoid; B8PD85; -.
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   CDD; cd05471; pepsin_like; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 4.
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:SF89; SACCHAROPEPSIN; 1.
DR   Pfam; PF00026; Asp; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
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        216..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1109..1129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          271..581
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          737..1059
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        976..1012
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   1158 AA;  126181 MW;  A96EF99AB9166DB5 CRC64;
     MRFAHVGSSR DSLGTRFPAN TDMTLRSRSD PAQTGIDAIS LPIRRMRQTY SVEQQIRRLP
     KRGGPPAAAS RMVVVGRMKA KDEVGDRMSS DRLRFPARAH DALRFDPNGV KLAPDIVSGP
     GPFSHKTYPL FNAQQHFTTV VFQNQRQNHQ ILNELRKPLV VASFAETRSD RMVAALRLGH
     PLAKHRTPPP PACALILEGV DRNGDVRPSS SFSTSLLFAT LTMWGSVSSG LVIFYALVAS
     TSALRVPVRR QSFGRSHSHS MPTRKKHTSN PDLHVLSGYE NILDVILDTG SPDFWISTNV
     TFENAINTSV ISGTNYGTKG GQSRVSGYIL MAEAEFGGFT VHNQTFVDVT NMTTEDGTGL
     LFPGSLSKAK SPYNGSRPVS NIFAQYPYFP PQFTMLFSRY YGNNITSSGG EFTFGDPISG
     YEYIEDAPAM PVIDNSLFEQ YWSIHMDAII INGKRFEAGP TGAKNLTAIL DAGTPTALMD
     SEFVDMLYGA DTPRFQDDTI SYAPCDLEIN MTFVFGDVEM PINPLDLTTP NNVTQNGTVE
     CYGSFERLSG FPPGTLLLGD SFLRHVYTLY NHNPNRNRGN TTRPYVQMIP VSTGAHLAGG
     IAGSAVTSSS SPDFSTLTRN SYIILGLLAG VLVLVLVVLG VSCAGQRSKT GRGYRVVAPM
     DMVGSPSNWA RRALAFRSVF ASTIQFNDME LADRLVLVQR VKTAERTAER YNSRAIHPTK
     RIADEVAGYE NLNDSRYVGE VLVSSRPFEI ILDTGSHEFW LKTDTTLSNY TNTSITAMID
     YGGGTGLGSS VSGFVLLAKT QFANFTIKEQ AFINVLEPAS GLIAPGINGI MGIAPPSNDT
     AINNAFKQAN YTASSGGSPV ESNPNVTPQF TMLMTRNDGE VRSSGGIFTL GDPISEHASV
     TSQPVLPIVN TTLGRYYWTV YLDGIKVNGN WPNGTVFTAV LDSGTPTTFI SPELVEFIYG
     ADAEITSDGL AALVSCETML NVSFVIGGVE YPVNPLDSVI PTGHYYNNTV ACTGAFQRAQ
     GPPWDGNMLL LGDTFLRNVY ALYNLNLRQS DGNTTLPFVQ LLSVTDANLA ASQFPEQNLA
     RLESFAQVYG YTVPLPPDPL APILRNSGII MFMSLVALIL AFIAAFYAIR NARMQSSRDD
     YIVLGEEQKE VRLLFAAD
//