ID A0A0A0HWQ9_PARBD Unreviewed; 578 AA.
AC A0A0A0HWQ9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial {ECO:0000313|EMBL:KGM91830.1};
GN ORFNames=PADG_12148 {ECO:0000313|EMBL:KGM91830.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:KGM91830.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:KGM91830.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:KGM91830.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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, ECO:0000256|RuleBase:RU004523}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN275964; KGM91830.1; -; Genomic_DNA.
DR RefSeq; XP_010762003.1; XM_010763701.1.
DR AlphaFoldDB; A0A0A0HWQ9; -.
DR STRING; 502780.A0A0A0HWQ9; -.
DR GeneID; 22588045; -.
DR KEGG; pbn:PADG_12148; -.
DR VEuPathDB; FungiDB:PADG_12148; -.
DR eggNOG; KOG2282; Eukaryota.
DR HOGENOM; CLU_000422_11_2_1; -.
DR InParanoid; A0A0A0HWQ9; -.
DR OMA; TMTACNT; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01973; NuoG; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Ubiquinone {ECO:0000313|EMBL:KGM91830.1}.
FT DOMAIN 41..119
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 119..158
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 258..314
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 578 AA; 64141 MW; C91ABE372C1FCEEB CRC64;
MIRPLFLRAA ARARRRVQFG RVGYRCVSGK RGFSSTGERR AEVELTVDGK KVSIEAGSAL
IQACEKAGVT IPRYCYHEKL LIAGNCRMCL VEVERAPKPV ASCAWPVQPG MVVKTNSPIT
HKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMRYGAD RGRFHEIGGK RAVEDKNIGP
LIKTSMNRCI HCTRCVRFAN DIAGAPELGT TGRGNEMQIG TYLEKNLDSE LSGNVIDLCP
VGALTSKPYA FRARPWELQH TESIDVLDAL GSNIRIDARG MEVMRILPRL NDDVNEEWIN
DKTRFACDGL RTQRLTTPLV RRDNKFHPVT WEQALTEIGN VFRTLSLQAN EFKAIAGHLI
EIESLVAMKD LANRLNSDNL ALDQPNGNLP LAHGIDVRSN YLFNSKIYGI EEADAILLVA
TNPRHEAAVL NARIRKQFLR TDLQVALVGE EFDSTFAYNH LGNSLKDLKA ALAGAFGKTL
ASAKRPMIIL GSAAAEHPDA RAIFETGWEE RGGEKWEEWG GVQEGCGGFL FYGCYFEELS
DDGTLLRGQE DGKSRYQLHD RKCGGGTGTY ERCIKRLK
//
