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Database: UniProt
Entry: A0A177DFC8_ALTAL
LinkDB: A0A177DFC8_ALTAL
Original site: A0A177DFC8_ALTAL 
ID   A0A177DFC8_ALTAL        Unreviewed;       747 AA.
AC   A0A177DFC8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=NADH-quinone oxidoreductase {ECO:0000313|EMBL:OAG17529.1};
GN   ORFNames=CC77DRAFT_1052508 {ECO:0000313|EMBL:OAG17529.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG17529.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG17529.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG17529.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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, ECO:0000256|RuleBase:RU004523}.
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DR   EMBL; KV441486; OAG17529.1; -; Genomic_DNA.
DR   RefSeq; XP_018382950.1; XM_018527700.1.
DR   AlphaFoldDB; A0A177DFC8; -.
DR   STRING; 5599.A0A177DFC8; -.
DR   GeneID; 29113294; -.
DR   KEGG; aalt:CC77DRAFT_1052508; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1052508; -.
DR   OMA; QDQAMAY; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
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   CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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   InterPro; IPR015405; NDUFS1-like_C.
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   Pfam; PF09326; NADH_dhqG_C; 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:UP000077248};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          33..111
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          111..150
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          250..306
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   747 AA;  82134 MW;  E9F868C9E144A657 CRC64;
     MLRQQMIRSL KRPAFRAALN GSRALSASAR RPADIELTID GKKVSVEAGS SLIQACDQAG
     VTVPRYCYHE KLMIAGSCRM CLVEVERAPK PVASCAWPVQ PGMVVKTDSP LVHKAREGVM
     EFLLANHPLD CPICDQGGEC DLQDQSMRYG ADRGRFHELE GKRAVEDKNV GPLVKTSMNR
     CIHCTRCVRF SNDIAGAPEF GSFGRGNNLE IGTYLETALD TELSGNVIDL CPVGALTSKP
     YAFKARPWEL YKTESIDVLD GLGSNIRVDS RGIQVMRVLP RLNDDINEEW INDKTRFACD
     ALSTQRLVNP LVRVDEQFQP ATWEQALVEI GNAYKKIAPK GNEFKVVAGH LVETEALVAM
     KDLANKLGSD NLALDQPGGS EPIAHGIDVR SNYAFNSRIY GVEDADYILL IGSNPRWEAA
     VLNARIRKQW LRTDLEIGYV GEDFQSTFEY EKLGNNANDL KSALSGEFGK KLANAKKPMI
     IVGSGVTEHV DAKSIYEQVG SFVEKNKDKF LTEEWNGYNI LQRTASRTGA YEVGFTVPSS
     EVAQTKAKFV WLMGADEINE ADIPKDAFVV YQGHHGDRGA QFADVVLPGA AYTEKSVTYV
     NTEGRVQMTR AAVGLPGASR EDWKIVRAAS EYLGAELPYD DVEQLRDRME EISPALRRYD
     LVESASLPSL SKVQLVDQNQ GAQATGQALK NPIENFFFTD AISRNSPTMA RCSAAKAQNN
     PKTNFMAPGE PYPQVGYGPQ VAAAANV
//
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