ID A0A0K3CKC2_RHOTO Unreviewed; 1648 AA.
AC A0A0K3CKC2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=electron-transferring-flavoprotein dehydrogenase {ECO:0000256|ARBA:ARBA00012696};
DE EC=1.5.5.1 {ECO:0000256|ARBA:ARBA00012696};
GN Name=FGENESH: predicted gene_12.135 {ECO:0000313|EMBL:CTR10114.1};
GN ORFNames=BN2166_0059750 {ECO:0000313|EMBL:CTR10114.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR10114.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR10114.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR10114.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CWKI01000012; CTR10114.1; -; Genomic_DNA.
DR STRING; 5286.A0A0K3CKC2; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.30.9.90; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 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 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.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT TRANSMEM 1192..1213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..435
FT /note="ETF-QO/FixC ubiquinone-binding"
FT /evidence="ECO:0000259|Pfam:PF21162"
FT DOMAIN 584..679
FT /note="ETF-QO/FixX C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05187"
FT REGION 681..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1648 AA; 175868 MW; 67BEB476BD3E510F CRC64;
MSERREKGKW GDEGEERRLG GHALQSGHWS HFATSAASLL HIAFCSRVRM LRSTGHAARS
LGSPAPALTR RAAASLPARL PTSSIPLATR SGPSALANRN ASRLALPASL RTFTSTPRAR
QAEPVDQELD FEGVERVQDE VDVCIVGGGP AGLSAAIQLM KMAQEKGEEI RVVVLEKGAE
VGAHILSGAV IEPRALDELI PDWKEKGAPL NQEALSDSMR WLTPTGSFAM PHPPQMSNKG
NYIISLSKLT RWLGEQAEEL GVEIYPGFAG AKILYTEDGT GVRGVQTNDI GLDKNFKPKD
SFEPGMEFLA KVTILAEGCH GSLSKQIQGK FNLREGKDPQ TYGLGVKEVW KVKPEKHEPG
KVQHTLGWPL DNSTYGGTWL YHMEDEMVSL GIVVGLDYKN PYISPYKELQ RLKHHPLFAD
LLEGGECIAY GARALNEGGY QSIPKLTFPG GAMIGDSAGF LNVPKIKGTH TSMKSGMLAA
EAAFNAITSS RASESDSSET ALDVSEYEKL FEESWVAKEL KEVRNLRPSF HTSLGNFGGI
IYSGIDSLLL KGRVPWTFHH PEEDYAATLP ARQFKEIDYP KPDGKLSFDI LESVSRTNTY
HAEDQPVHLH IEPSARAAHV KTNVKQYAGL LGRVCPAAVY EYVDAEGTEE DAEGKRLVIN
SQNCIHCKVR GLSRTCSIKV RPPRSDEASI ADSHSRQRPD PGHPMAGAGR ERRTALRVHV
VVVELAVFAS LDKACSARPE PLSLTSHRLT RVPEAAIATA LLAHASSSSQ QPAGTRTSLA
SLHNTDEPSS HNPPAQHSTF PLRARPSVSL APPQEVRWDR TNFFGKREEE RVGSFEQRGA
TRKQGTSSSL KRKNETFTSS RTPTLAAKDV ANSAALPRFK MMIAVLLAGA HLRIALGRAS
LARILSSSQL ANLAVLSCCL TPCCAVALDH RRALRLFPLP RRSSRTMASS CAVVTGPPTV
TSLVSTTTVL ATQVSTAPDS TLTTSTAVVT SNCLLPTILG QLALCQTTTS FAPLETVVPG
SVVQITSTGQ SLVTVVQTLP GATSTACEAV QTTPPPSSST PASTATTTTP RRTTTTPPPV
LVPSSSATTS SVPSSSAVAP STPTSDSTSS PDPSSSSPSL IDAVSPSSSD TPTPTTPPST
ATEIVAGPRR STSYITSYVT VVDSSGQTLT SASTIPTLLN IPGSNTSRAS PGAIAGGTVG
GIAALALAAF FLWMMRKRGY FRRGDEQIEE DAWDPAGHGD YFAGGGRGGS RRSAAGMAGV
GAGGGRSSPG NSSDEKHDPL SEKDREIDAA TLERHKSWYH RSIASHGDDL DLEEAYGGEM
AQPAAFGYLP TTNEGVGRRA STYAAAPAAP PRRSMSTAMS VASRSSHSHE SYPSRHPSLD
ADRRMSHPTR RPSLDADRRM SLALPMQYSS FQSFVPPTES YVDEPTSYAS RSPPLPQASM
PAIARPKSAS PPTVQHSPYP TVSRQRSLPG LQGHLPIHMR SASLSGRPTL GAIQAGRPST
HSRTVTSDSM STISTPQSHY MPALTSSASE STLVSTIPST PSTSHAHDKS SLLPTPPLPV
LPNIERLKVE HPKRPSMDRN VSSDSIFHPS QWLGARVVNA DDSRSTTTAT DTDTETIASN
VLAGESSDSL AAAAELISRV QVRIDGAR
//
