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Database: UniProt/TrEMBL
Entry: G8BQW7_TETPH
LinkDB: G8BQW7_TETPH
Original site: G8BQW7_TETPH 
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}.
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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
//
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