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Database: UniProt
Entry: A0A5N7ACJ9_9EURO
LinkDB: A0A5N7ACJ9_9EURO
Original site: A0A5N7ACJ9_9EURO 
ID   A0A5N7ACJ9_9EURO        Unreviewed;       737 AA.
AC   A0A5N7ACJ9;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAE8367445.1};
GN   ORFNames=BDV27DRAFT_123932 {ECO:0000313|EMBL:KAE8367445.1};
OS   Aspergillus caelatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=61420 {ECO:0000313|EMBL:KAE8367445.1, ECO:0000313|Proteomes:UP000326268};
RN   [1] {ECO:0000313|EMBL:KAE8367445.1, ECO:0000313|Proteomes:UP000326268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 763.97 {ECO:0000313|EMBL:KAE8367445.1,
RC   ECO:0000313|Proteomes:UP000326268};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) 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; ML737598; KAE8367445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N7ACJ9; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000326268; 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; 3.30.200.210; -; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000326268};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
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   737 AA;  80746 MW;  3C7087FA15A5C0F5 CRC64;
     MRPQLFRAAA RAVRVPRINN LRSFATTTPR LAEVELTIDG KKVSVEAGSA LIQACEKAGA
     TIPRYCYHEK LMIAGNCRMC LVEVERAPKP VASCAWPVQP GMNVKTNSPL VHKAREGVME
     FLLANHPLDC PICDQGGECD LQDQSMRYGA DRGRFHEVGG KRAVEDKNIG PLVKTSMNRC
     IHCTRCVRFM NDVAGAPELG TAGRGNDMQI GTYLEKNLDS ELSGNVIDLC PVGALTSKPY
     AFRARPWELK HTESIDIHDA LGSNIRIDSR GMEVMRIIPR LNDDINEEWI NDKSRFACDG
     LKTQRLTTPL IRREGKFVPA TWEQALTEIS SARQKLQLKE NEFKAVAGHL VDAESLVAMK
     DLANKLGSDN LALDQPGGSS PIAHGVDVRS SYLFNSKIYG IEEADAILLV ATNPRHEASV
     LNARIRKQYL RSDLEIGLVG ETFESTFDFE HLGSDVSALK TALAGKFGEK LASAKRPMVI
     VGSAAAEHAD AKAIFETVGS FVEKHSSTFN TPEWQGYNVL QRAASRAAAY EIGFTTPSPE
     VAQAKPKMVW LLGADEVGQT EIPNDAFVIY QGHHGDRGAQ LADVVLPGAA FTEKSGTYIN
     TEGRVQVTRA ATSLPGAARD DWKIIRATSE FLDVPLPYDD IEALRDRMEE ISPVMRRYDV
     VEPTSLGSLS KVQLVEQNKG TQPTLAPFKK VIDDFYFTDS ISRSSPTMAR CSAAKATGNP
     ETNFMAAGEM SPQTLYG
//
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