ID A0A319DKR7_9EURO Unreviewed; 922 AA.
AC A0A319DKR7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=electron-transferring-flavoprotein dehydrogenase {ECO:0000256|ARBA:ARBA00012696};
DE EC=1.5.5.1 {ECO:0000256|ARBA:ARBA00012696};
DE AltName: Full=Electron-transferring-flavoprotein dehydrogenase {ECO:0000256|ARBA:ARBA00032754};
GN ORFNames=BO82DRAFT_403728 {ECO:0000313|EMBL:PYH80052.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH80052.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH80052.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH80052.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000256|ARBA:ARBA00002819}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; KZ821713; PYH80052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DKR7; -.
DR STRING; 1448315.A0A319DKR7; -.
DR VEuPathDB; FungiDB:BO82DRAFT_403728; -.
DR OrthoDB; 275372at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 3.30.9.90; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR049398; ETF-QO/FixC_UQ-bd.
DR InterPro; IPR007859; ETF-QO/FixX_C.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10617; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10617:SF107; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF05187; ETF_QO; 1.
DR Pfam; PF21162; ETFQO_UQ-bd; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS50102; RRM; 2.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 598..627
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 633..699
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 723..788
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 19..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 103783 MW; 06C20D0986887833 CRC64;
MASKGAVLPL LRRELRPSSR RLPKAPASLS SLANSARPSN LSLPASYRKV IRPRSLFTPI
QTRAFSQSVT RRLTDAEGNF DPRQLDRESD EVDVCIVGGG PAGLAAAIRL KQLANEAGNE
EFRVILLEKA GELGAHVLSG NVLEPTALNE LLPDWLAEDN PSRFEGATPA KADKMRFLTQ
NSSFPIPAPP QMNNHGNYII SLNELTKWLG ERAEELGVEI YPGFAASEVV YKSDGSVLGV
ATNDLGIGRD GKAKDSFERG MEFHARVTLL AEGCHGSLTK QVAKKFDLRR DSQPQTYGIG
LKEIWEIQPE KFKSGEITHS LGYPLPSDTY GGAWMYHFGD NMVSIGLVVG LDYPNPWLSP
YGEFQKLKHH PLFKEVLEGG KCISYGARAL NEGGFQSIPK CAFPGGALIG DSAGFLNVPK
IKGTHTAMKS AMLAAESTFA ALQGNPDGSV FLFDYEEALR KSSIWKELYE VRNMRPSFST
PLGLYGGILY SGLEAYILKG RTPWTLKHHT TDAAATKLAS QCNKIEYPKP DGVISFDILT
SVSRTGTNHE EDQPVHLQVE DWDKHTDIAW PKYQGVENRF CPAGVYEYVE DSSKQHGVRF
QINAQNCIHC KTCDIKVPTQ DINWQTPQGG EGPNANSVTK QDIEEHFSTH GSGKITEIKL
MNGFGFIEYE DAMDARDVVP AFHGSDFKGE RLTVQFARGP RRKENFPGPM DRPNMPRPRR
TIFRMLLSGL PETSWQDLKD FARQSGLDVV YSETGRELGR GFVEFETAND LKTAVEKLDQ
REFKGSRVTC IADIQSFPPE DRSFRDPYRS RSPRRSFPPM EEYDRRFPAP RGYSPRAHYR
ERSPIPMRRE YYERDGYGRR TPPRPRIEDY PPPRRPYEDP YDVRPPPPPR HYDDPYMQAR
AYPRPRSPPR GEYMPYERRG YW
//
