ID C1HB04_PARBA Unreviewed; 229 AA.
AC C1HB04;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=NADH-quinone oxidoreductase subunit I 2 {ECO:0000313|EMBL:EEH37450.1};
GN ORFNames=PAAG_07868 {ECO:0000313|EMBL:EEH37450.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH37450.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH37450.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
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 -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00010277}.
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DR EMBL; KN294018; EEH37450.1; -; Genomic_DNA.
DR RefSeq; XP_002790179.1; XM_002790133.2.
DR AlphaFoldDB; C1HB04; -.
DR STRING; 502779.C1HB04; -.
DR GeneID; 9093459; -.
DR KEGG; pbl:PAAG_07868; -.
DR VEuPathDB; FungiDB:PAAG_07868; -.
DR eggNOG; KOG3256; Eukaryota.
DR HOGENOM; CLU_067218_1_1_1; -.
DR OMA; QFFRAPY; -.
DR OrthoDB; 176717at2759; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
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:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR Gene3D; 3.30.70.3270; -; 1.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR NCBIfam; TIGR01971; NuoI; 1.
DR PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059}.
FT DOMAIN 121..150
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 160..189
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 30..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 25750 MW; EA705C7CBDEA1ED6 CRC64;
MASSKAVSRL IAYRRPALLQ ISPQSSTHLR STPAFSFSTS SPVSATPAGP PRQGFRLPPP
KAWDQGDESA LDKAGKYFLM TEMLRGMYVV LEQFFRPPYT IFYPFEKGPI SPRFRGEHAL
RRYPSGEERC IACKLCEAIC PAQAITIEAE EREDGSRRTT RYDIDMTKCI YCGFCQESCP
VDAIVESPNA EYATETREEL LYNKEKLLAN GDKWEPELAA AARADAPYR
//
