ID   ETFA_CRYNB              Reviewed;         346 AA.
AC   P0CN61; Q55UP6; Q5KHP5; Q8J0W1; Q8J0X2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Probable electron transfer flavoprotein subunit alpha, mitochondrial;
DE            Short=Alpha-ETF;
DE   Flags: Precursor;
GN   Name=ETF1; OrderedLocusNames=CNBD0620;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC       electron acceptor for several dehydrogenases, including five acyl-CoA
CC       dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers
CC       the electrons to the main mitochondrial respiratory chain via ETF-
CC       ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per dimer. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
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DR   EMBL; AAEY01000019; EAL21366.1; -; Genomic_DNA.
DR   RefSeq; XP_776013.1; XM_770920.1.
DR   AlphaFoldDB; P0CN61; -.
DR   SMR; P0CN61; -.
DR   EnsemblFungi; AAW43187; AAW43187; CND05770.
DR   EnsemblFungi; EAL21366; EAL21366; CNBD0620.
DR   GeneID; 4935451; -.
DR   KEGG; cnb:CNBD0620; -.
DR   VEuPathDB; FungiDB:CNBD0620; -.
DR   HOGENOM; CLU_034178_0_1_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd01715; ETF_alpha; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR001308; ETF_a/FixB.
DR   InterPro; IPR033947; ETF_alpha_N.
DR   InterPro; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; PTHR43153; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Mitochondrion; Transit peptide;
KW   Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..346
FT                   /note="Probable electron transfer flavoprotein subunit
FT                   alpha, mitochondrial"
FT                   /id="PRO_0000410085"
FT   BINDING         285..313
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   346 AA;  36189 MW;  9D37BD3A3E0DB7B5 CRC64;
     MLYRSALRAS RSFTPRLAST NSRLVSSLVF LEHKAGKLNE ASLSAVTAAK TLGNDTHGLL
     VGTKSEIENV LDRTKEIKDL SKIYLATSDT YSHSLAEPLA SLLASIASAK DVSHIFAAHT
     AVGKNIFPRL AGLLDTSLIA DIIALESSGD TFTRPIYAGN AVLTIKSSPK DSVKVVTVRS
     TAFDKAAVAN GSAAVEDVDI ITVDTPTQFV SEELTVSSRP DLASAARVVS GGRALKSKES
     FDTILDPLAD SLGAAVGASR AAVDAGYADN SLQVGQTGKV VAPELYVAIG ISGAIQHLAG
     MKESKMIIAI NKDPDAPIFQ VADVGLVADL FESVPQLVKE IDNVKV