ID A0A0J0XLL6_9TREE Unreviewed; 683 AA.
AC A0A0J0XLL6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative 64 kDa mitochondrial NADH dehydrogenase {ECO:0000313|EMBL:KLT41973.1};
GN ORFNames=CC85DRAFT_261019 {ECO:0000313|EMBL:KLT41973.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT41973.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT41973.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT41973.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004137}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; KQ087210; KLT41973.1; -; Genomic_DNA.
DR RefSeq; XP_018278464.1; XM_018420857.1.
DR AlphaFoldDB; A0A0J0XLL6; -.
DR STRING; 879819.A0A0J0XLL6; -.
DR GeneID; 28981460; -.
DR OrthoDB; 1434722at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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:SF50; NADH DEHYDROGENASE (UBIQUINONE)-RELATED; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 490..525
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 531..566
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 683 AA; 76359 MW; 90690556877F99BF CRC64;
MFARSILGAR RLALAAPPRL SAPPGLGLTL TLARGFTTSP PRLTPRIPSR FPPSFFRSHA
FAQSRPTPRR AKWTYARYGL VSPTFAHKHP WLASVLRLFL AVMVGSSVLL LIVLIHDAST
YSQKHIDRVP VNPLALSPRR GGPKNLPIIE VNIDDKESDE KARCEGKPRL IILGGGWGAV
SILKTLPPTA YNVTLIAPDN YFCFTPLLPS ACVGTVEPRS LVEPLRRLVA RVHGHFLQGA
AVDICMSERL LEVEVPTEDG PMRAYVPYDK LVIAVGSRSN DHGVKGLEHC FQLKTIPDAQ
AIRRQIMMNL ETASLPTTTP EQRKHLLSFV VCGGGPTGVE FAAELSDMLN EDVLAYYPKI
LKGDMTVTII QSRDHILNTY SEKISDYAEK HFQREEIDVV TNARVNEVTP KSVRITIKEK
DGSIREAELP ASIVLWSTGI AMQPFTRQMV ELLPNQFHSK AVQVDAYLRV EGAPKGSIYA
IGDAATIHLN MLSDLLLIWE QFDENRDDKL TYDEWALMAE HIKKKYPLTS DYLAQIRDVF
REFDTDGRGH LSLNQVADMF IKMSSKATAL PATAQVASQQ GEYLGHMFGR LARQRKTLQA
NDIDNLDDEA YYHPFKYRNL GTLAYIGNSA AFDIGGYGSA GGLLAMYAWR SVYWSMQVSM
RTRFMLMLDW VKRGLFGRDL SKF
//
