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Database: UniProt
Entry: H5WH77_EXODN
LinkDB: H5WH77_EXODN
Original site: H5WH77_EXODN 
ID   H5WH77_EXODN            Unreviewed;       180 AA.
AC   H5WH77;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   22-FEB-2023, entry version 33.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 6 {ECO:0000256|RuleBase:RU004430};
DE            EC=7.1.1.2 {ECO:0000256|RuleBase:RU004430};
GN   ORFNames=HMPREF1120_11013 {ECO:0000313|EMBL:EHY51771.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OG   Mitochondrion {ECO:0000313|EMBL:EHY51771.1}.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY51771.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY51771.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY51771.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000256|RuleBase:RU004430}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU004430};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000256|RuleBase:RU004430}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU004430}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC       {ECO:0000256|RuleBase:RU004430}.
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DR   EMBL; CM001238; EHY51771.1; -; Genomic_DNA.
DR   RefSeq; XP_009161810.1; NW_008751656.1.
DR   AlphaFoldDB; H5WH77; -.
DR   STRING; 858893.H5WH77; -.
DR   GeneID; 20313968; -.
DR   VEuPathDB; FungiDB:HMPREF1120_11013; -.
DR   HOGENOM; CLU_085957_1_0_1; -.
DR   InParanoid; H5WH77; -.
DR   OrthoDB; 2328023at2759; -.
DR   Proteomes; UP000007304; Mitochondrion.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   PANTHER; PTHR33269; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR   PANTHER; PTHR33269:SF17; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU004430};
KW   Membrane {ECO:0000256|RuleBase:RU004430};
KW   Mitochondrion {ECO:0000256|RuleBase:RU004430, ECO:0000313|EMBL:EHY51771.1};
KW   NAD {ECO:0000256|RuleBase:RU004430};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW   Respiratory chain {ECO:0000256|RuleBase:RU004430};
KW   Translocase {ECO:0000256|RuleBase:RU004430};
KW   Transmembrane {ECO:0000256|RuleBase:RU004430};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004430};
KW   Transport {ECO:0000256|RuleBase:RU004430};
KW   Ubiquinone {ECO:0000256|RuleBase:RU004430, ECO:0000313|EMBL:EHY51771.1}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004430"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004430"
FT   TRANSMEM        59..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004430"
FT   TRANSMEM        93..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004430"
FT   TRANSMEM        153..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004430"
SQ   SEQUENCE   180 AA;  20230 MW;  4B4BA7883FBBF729 CRC64;
     MFNGFSVVFL DFFIILSILA GIFTIISKNP IVSVLHLIML FSCISCYLIF LGIKFIGLSY
     LLVYVGAVSI LFLFILMLIN IRVSELISNT NNNIPLAILA ILALFIPYNN LTTDTKTNFY
     PVDIFFVSSN NWDSNLVDIT DITSIGNVMY TNYSIWLLIT SIILLLAMVG SIVITIKQKY
//
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