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Database: UniProt
Entry: F0UWE1_AJEC8
LinkDB: F0UWE1_AJEC8
Original site: F0UWE1_AJEC8 
ID   F0UWE1_AJEC8            Unreviewed;       508 AA.
AC   F0UWE1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404};
DE            EC=7.1.1.2 {ECO:0000256|RuleBase:RU003404};
GN   ORFNames=HCEG_12004 {ECO:0000313|EMBL:EGC40626.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OG   Mitochondrion {ECO:0000313|EMBL:EGC40626.1}.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) 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:RU003404}.
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:RU003404};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC       {ECO:0000256|RuleBase:RU003404}.
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DR   EMBL; DS990652; EGC40626.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UWE1; -.
DR   STRING; 544711.F0UWE1; -.
DR   HOGENOM; CLU_007100_6_0_1; -.
DR   OMA; FWFTRIA; -.
DR   Proteomes; UP000008142; Mitochondrion.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   Pfam; PF00361; Proton_antipo_M; 2.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003404};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003404, ECO:0000313|EMBL:EGC40626.1};
KW   NAD {ECO:0000256|RuleBase:RU003404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003404};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003404}; Transport {ECO:0000256|RuleBase:RU003404};
KW   Ubiquinone {ECO:0000256|RuleBase:RU003404}.
FT   TRANSMEM        29..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        53..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        92..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        116..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        159..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        212..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        253..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        302..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        361..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   TRANSMEM        480..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003404"
FT   DOMAIN          1..30
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          46..158
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          159..266
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   508 AA;  56899 MW;  D087832B2863C551 CRC64;
     MLIPVLIVSS LVHIYSIGYM SHDPHNQRFF SYLSLFTFMM IILVTANNYL LMFLGWEGVG
     VCSYLLINFW FTRIAANQSS ISAFLTNRVG DCFLMIGMFI IIWSFGNINY STIFSLAPYL
     NSNIITLIGI CLLIGAMAKS SQIGLHVWLP QAMEGPTPQL GMMVIAIGLS SYNIALFHLV
     NHAFYKALLF LGAGAIIHSV SDNQDFRKFG GLKAFLPLTY SVMLIASLSL VAIPFMTGFY
     SKDFILESAY GQFYLSSIIV YILASVGAIF TTLYSAKVLY LTFLTNPNGP LITYKKADQG
     DLFINLPLII LAILSIFFGY LTKDLFIGLG TGFFSDNSLF IHPLHESMLD TEFAVITLFK
     LLPFILTISL SFLSLLLSEF FGLFVIKFKY TKLGYNLFGF FNQRFLIELF YNNYITDIVL
     KLGGQTTKII DKGSVELLGP YGLEKSLLVL SNGIGNLSTG IITSYGLYIL IGFFSYISLF
     YFSFIDGNIL LLLLIAIFTI FNKTYNEN
//
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