ID B8MC89_TALSN Unreviewed; 426 AA.
AC B8MC89;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase family protein {ECO:0000313|EMBL:EED18535.1};
GN ORFNames=TSTA_122670 {ECO:0000313|EMBL:EED18535.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED18535.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; EQ962655; EED18535.1; -; Genomic_DNA.
DR RefSeq; XP_002482527.1; XM_002482482.1.
DR AlphaFoldDB; B8MC89; -.
DR STRING; 441959.B8MC89; -.
DR GeneID; 8097732; -.
DR VEuPathDB; FungiDB:TSTA_122670; -.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_8_0_1; -.
DR InParanoid; B8MC89; -.
DR OMA; VDPRSYM; -.
DR OrthoDB; 1585541at2759; -.
DR PhylomeDB; B8MC89; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
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:SF45; NADH DEHYDROGENASE-LIKE PROTEIN RV1812C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..327
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 426 AA; 45352 MW; BDA245D501BDBD0C CRC64;
MLVLVVKFTQ LPPFGIMSFK IVIIGAGFAG VWSALSAKRL IKSTGKENKV EILVISPKPV
LVMRPRLYES KASSLIHPLE TLFKEAGINF CPGVVKTIHT ERRAVEVQCA SGVESTIEYD
RLILAAGSSV IQPQHVGGLR QHTYDIDSLD SAVKLESHLE ALASLPASPS RDTVVVCGAG
FTGIELTAEL PRRLAHIANA RVILVGNTDE VGPSFGSSPR STITQALNDL GVEVKLGAGV
KAVDPEGVTL TSGVRIQTKT TIWTAGVQAT PLTQQVAAPR DALGRLYVDQ YLRVSPVDGV
FATGDAACAL ADGKNQHALM SCQHALQLGR VSGYNAAAEL LGVPLMGYTQ AAYNCCLDLG
AWGALVAAGW DRDIIKMSGD TAKRAKCYIN QKLIYPPDNA HEALASADPV LPDSDQLFEQ
LIHVVD
//
