ID B8PDQ8_POSPM Unreviewed; 463 AA.
AC B8PDQ8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EED81000.1};
DE Flags: Fragment;
GN ORFNames=POSPLDRAFT_20586 {ECO:0000313|EMBL:EED81000.1};
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:EED81000.1, 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 NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; EQ966326; EED81000.1; -; Genomic_DNA.
DR RefSeq; XP_002473803.1; XM_002473758.1.
DR AlphaFoldDB; B8PDQ8; -.
DR KEGG; ppl:POSPLDRAFT_20586; -.
DR HOGENOM; CLU_021377_1_2_1; -.
DR InParanoid; B8PDQ8; -.
DR OMA; DHCIFLD; -.
DR OrthoDB; 1434722at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF17; NADH DEHYDROGENASE (EUROFUNG); 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 14..355
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EED81000.1"
FT NON_TER 463
FT /evidence="ECO:0000313|EMBL:EED81000.1"
SQ SEQUENCE 463 AA; 52117 MW; 9FB76BFDF21EB61C CRC64;
RRSFGASAAR REQHLVILGS GWGGYELLRK VDKKRWNVTI VSPNNYFNFT PLLASCAVGT
LEFRSAVEPV RRYTPQVHAY QAWCDSIDFK HKTLTCMPAT PPLPYPSRGG ETPKPDPGTS
ATLQVAPGNR GTQQYELKYD KLVIAVGAYN RTFFIPGVKE HAHFLKDIRD ARAIRARILE
CFEQANQPTI TDDDRRKLLH FCIVGGGPTG VEFAAELHDL LHAEIKQSYP SLARMDKISL
YDVAPRILGI RLHTRSWATK KFTREGINIL TQHHVDRVES GKMYVKEQGE VHFGLLVWST
GLAPNPLVQN LTEAEKDPKT ASILTDEHLN VLMKDTGAPN PDVWAIGDAA IIKGNPLPAT
AQGELPSPAQ YLRKKLNRLV RDRAAPEPFA FHNAGSLAYL GDWQAVYDRS HAESGPKTME
TGRVAWLLWR SAYFTMTLSL KNKILVPTYW FMNWIFGRDL SRF
//
