ID A0A168C1B5_CORDF Unreviewed; 692 AA.
AC A0A168C1B5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase, FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:OAA70810.1};
GN ORFNames=LEL_09401 {ECO:0000313|EMBL:OAA70810.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA70810.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA70810.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA70810.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA70810.1}.
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DR EMBL; AZHF01000009; OAA70810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168C1B5; -.
DR STRING; 1081108.A0A168C1B5; -.
DR OrthoDB; 48029at2759; -.
DR Proteomes; UP000076881; 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: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; PF00036; EF-hand_1; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SMART; SM00054; EFh; 1.
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; 1.
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:UP000076881};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 538..573
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 692 AA; 77079 MW; 7FC3D6066DA936B2 CRC64;
MAAPLRPVGS AAVRRLLRPL PRGSSAQPVV QFAPRSRTIA QLHRPTSPTL KAAASQGYCR
AQRPTATTLV HLRALSGKPL PQRQSWTLNF CYRMMAWIGT SIAVGGILVT AFFVYDATTY
KEGADAGDIT VGQLALQPRR GGPKNLPIAD VLIDDNDKNG KSENQDKPKL VILGGGWGGV
ALLKELHADD YHVTVISPTN YFLFTPMLPS ATVGTLESRS LVEPIRRILG RIHGHFIRAS
AEDVCFHEKL VEVSQTDCNG EKVRFYVPYD KLVVAVGSVT NPHGVKGLEN AFFLKDINDA
RMIRNKIIHN LELACLPTTS DIERRRLLSF CISGGGPTGV EFAAELYDLL NEDLTRNFPR
LLRNEISVHL IQSRSHILNT YDEEVSKYAE KRFARDHVDV LTNSRVQEVH PDKIVFSQKQ
ADGTLVTKEL PIGFCLWSTG VSQTEFAQKI AKSLGDFQTN RRALETDTHL RLTGSPLGSV
YAIGDCSTVQ NNVADHIITV LRSIAYKHGK DPENLQLHFS DWRKVATEVR QRFPQAVSHL
RRLDKLFQEF DKDQSGTLDF GELRELLAQI DSKLTSLPAT AQRANQQGVY LGQKLNKMAH
LSRGLEVNDV RDGDLDAAAF KAFEYRHLGS LAYVGNSAVF DLGEGWNFTG GLWAVYAWRS
VYFAQSVSFR TRCLMAMDWA KRGLFGRDLM SF
//
