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Database: UniProt
Entry: A0A0N1HNC5_9EURO
LinkDB: A0A0N1HNC5_9EURO
Original site: A0A0N1HNC5_9EURO 
ID   A0A0N1HNC5_9EURO        Unreviewed;       265 AA.
AC   A0A0N1HNC5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=NADH-ubiquinone oxido 78 kDa subunit, mitochondrial {ECO:0000313|EMBL:KPI36516.1};
GN   ORFNames=AB675_4357 {ECO:0000313|EMBL:KPI36516.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI36516.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI36516.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI36516.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005404}.
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:KPI36516.1}.
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DR   EMBL; LFJN01000030; KPI36516.1; -; Genomic_DNA.
DR   RefSeq; XP_017996479.1; XM_018144489.1.
DR   AlphaFoldDB; A0A0N1HNC5; -.
DR   STRING; 1664694.A0A0N1HNC5; -.
DR   GeneID; 28736369; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000038010; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   Gene3D; 3.40.50.740; -; 1.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR015405; NDUFS1-like_C.
DR   PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF09326; NADH_dhqG_C; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Ubiquinone {ECO:0000313|EMBL:KPI36516.1}.
FT   DOMAIN          1..154
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          185..234
FT                   /note="NADH-ubiquinone oxidoreductase 75 kDa subunit
FT                   mitochondrial-like"
FT                   /evidence="ECO:0000259|Pfam:PF09326"
FT   REGION          235..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  28463 MW;  B90CCB03D9095377 CRC64;
     MIIVGSGVIE HADAKAIYES VGAFVDKNAS VFNTPEWQGY NVLQRAASRA GAYEVGFTVP
     SQKVANTTPK IVWLLGADEI SEADIPSDAF VVYQGHHGDR GAQLADVVLP GCAYTEKSAT
     YVNTEGRAQL TRNAVSIPGA GRTDWKIIRA VSEYLGAPLP YDDVEQLRDR MEEISPALRR
     YDTLEPSALG SLSKVQLVDQ NKGSKASGEK LGLPIKNFYF TDVISRSSPT MARCSAAKET
     GNPNTNFMAP GEIGEQPGQV SYGTA
//
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