ID G8BQW7_TETPH Unreviewed; 530 AA.
AC G8BQW7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN Name=TPHA0C04800 {ECO:0000313|EMBL:CCE62629.1};
GN OrderedLocusNames=TPHA_0C04800 {ECO:0000313|EMBL:CCE62629.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62629.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE62629.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE612858; CCE62629.1; -; Genomic_DNA.
DR RefSeq; XP_003685063.1; XM_003685015.1.
DR AlphaFoldDB; G8BQW7; -.
DR STRING; 1071381.G8BQW7; -.
DR GeneID; 11533803; -.
DR KEGG; tpf:TPHA_0C04800; -.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_0_1; -.
DR OMA; WIKLAFF; -.
DR OrthoDB; 1434722at2759; -.
DR Proteomes; UP000005666; Chromosome 3.
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:SF10; ROTENONE-INSENSITIVE NADH-UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 483..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..417
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 530 AA; 59150 MW; 4ABA8EDF9B573005 CRC64;
MLSRVNKTHD VTLWKKLHSL TRKSLSTTTL LRQEAPPSSQ EHLSGTSSFK TVSFLSTDEK
HHKTKKSVVI LGSGWGAISF LKNIDATKYD VSIISPRNYF LFTPLLPSTP AGTVDEKSII
EPVINFASKK KGSITYIEAE AKAINPDRNT VTVDSMTTVA TLKAKDSSSH DSVAGLKRAE
PFEVKYDYLI TAVGAEPNTF GVKGVEEYGH FLKEIPNSLE IRRKFAENIE KANLLPKGDP
ERKRLLSIVV VGGGPTGVET AGELQDYVSQ DLKKFLPSLA EEVQIHLVEA LPVVLNMFEK
KLSSYAQSVL EKTTIKLHLK TAVGKVEKDH LIAKTKKPDG TVEEQKIGYG TLIWATGNKA
RPVVTDLFTK IPEQNQSTRA LNVNQFLQVK GSKNIFAIGD NAFCGLPPTA QVAHQQAEYL
CKNFDKMEKI DGFHNTLLKK TEKFDLPFEE NGFKPFNYIH LGALAYLGSE RAIANITYGK
RSFYTGGGLI TFYVWRILYL SMILSARSRF KVISDWLKLT FFKRDFFKGL
//