ID A0A395SSD1_FUSSP Unreviewed; 173 AA.
AC A0A395SSD1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=NADH-ubiquinone oxidoreductase {ECO:0000256|PIRNR:PIRNR017016};
GN ORFNames=FSPOR_838 {ECO:0000313|EMBL:RGP75216.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP75216.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP75216.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP75216.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone.
CC {ECO:0000256|PIRNR:PIRNR017016}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|PIRNR:PIRNR017016}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC {ECO:0000256|ARBA:ARBA00010705, ECO:0000256|PIRNR:PIRNR017016}.
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:RGP75216.1}.
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DR EMBL; PXOF01000016; RGP75216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SSD1; -.
DR STRING; 5514.A0A395SSD1; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR016680; NDUFA8.
DR PANTHER; PTHR13344:SF0; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 8; 1.
DR PANTHER; PTHR13344; NADH-UBIQUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF06747; CHCH; 1.
DR PIRSF; PIRSF017016; NDUA8; 1.
DR PROSITE; PS51808; CHCH; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR017016}; Membrane {ECO:0000256|PIRNR:PIRNR017016};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR017016};
KW Mitochondrion inner membrane {ECO:0000256|PIRNR:PIRNR017016};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Respiratory chain {ECO:0000256|PIRNR:PIRNR017016};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR017016};
KW Ubiquinone {ECO:0000313|EMBL:RGP75216.1}.
FT DOMAIN 91..124
FT /note="CHCH"
FT /evidence="ECO:0000259|Pfam:PF06747"
FT REGION 154..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 173 AA; 19684 MW; 4C39DF9905018804 CRC64;
MSTRRPQFSQ QVLIDTTPLP SDIPAVKEVG ASSAPLLSAS FFIGARCRDY NDDYMQCKND
NPGRGEFECL KEGRRVTRCA SSVIKDINTH CLAEFRKHWE CLDDRNHQLW QCRPAEWKLN
KCVFDNLKLE KKVPDQPTNS TPVHLRPKQI FADVRIGPGD GKPFVPGQED AQQ
//