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Database: UniProt
Entry: G0R875_HYPJQ
LinkDB: G0R875_HYPJQ
Original site: G0R875_HYPJQ 
ID   G0R875_HYPJQ            Unreviewed;       742 AA.
AC   G0R875;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR52827.1};
GN   ORFNames=TRIREDRAFT_44041 {ECO:0000313|EMBL:EGR52827.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR52827.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR52827.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
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; GL985056; EGR52827.1; -; Genomic_DNA.
DR   RefSeq; XP_006961079.1; XM_006961017.1.
DR   AlphaFoldDB; G0R875; -.
DR   STRING; 431241.G0R875; -.
DR   EnsemblFungi; EGR52827; EGR52827; TRIREDRAFT_44041.
DR   GeneID; 18484955; -.
DR   KEGG; tre:TRIREDRAFT_44041; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_44041; -.
DR   eggNOG; KOG2282; Eukaryota.
DR   HOGENOM; CLU_000422_11_6_1; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000008984; 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:0046872; F:metal ion 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; 3.30.200.210; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT   DOMAIN          32..110
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          110..149
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          249..305
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   742 AA;  81087 MW;  113542D90967D3C1 CRC64;
     MLRQSLARSA WRTGRRAAAV PRAFATTPRR SAEVELTIDG KKVSIEAGSA LIQACEKAGV
     TVPRYCYHEK LMIAGNCRMC LVEVERAPKP VASCAWPVQP GMVVKTNSPL THKAREGVME
     FLLANHPLDC PICDQGGECD LQDQSMRYGA DRGRFHEIGG KRAVEDKNIG PLIKTSMNRC
     IHCTRCVRFA NDIAGAPELG STGRGNDLQI GTYLEKNLDS ELSGNVIDLC PVGALTSKPY
     AFRARPWELK HTESIDVLDG LGSNIRVDSR GLQVMRILPR LNDDVNEEWI NDKTRFACDG
     LSTQRLTVPL IRREGRFENA DWEEALTVIA KAYQQTNPQG NEFKIIAGAL TEVESLVVAK
     DMANKLGSEN LALDTPTGSQ PLAHGIDVRS NYLFNSQIWG IEEADCMLIV GSNPRHEAAV
     LNARIRKQWL RSDLEIGVVG ETWDSTFEFE HLGADHAALK KALAGPFGKK LKAAKKPMII
     VGSGVTDHVD AKAFYETVGT FVEQNAANFR TAEWNGYNVL QREASRAGAF EVGFVTPSAE
     VAQTKPKFVW LLGADEINEA DIPKDAFVVY QGHHGDRGAQ IADVVLPGAA YTEKAGTYIN
     TEGRVQMTRA ATSLPGAART DWKILRAASE FLGAPLPYDD VAAVRDRMVE ISPALAAYDV
     VEPVALKELS KVQLVEQNKG AKASNQPLKK VIENFYFTDA ISRSSPTMAR CSAAKATGDP
     RTNFMAPGME EDRPMGQVAY GA
//
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