ID   ETFA_CRYNV              Reviewed;         346 AA.
AC   Q8J112;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Probable electron transfer flavoprotein subunit alpha, mitochondrial;
DE            Short=Alpha-ETF;
DE   Flags: Precursor;
GN   Name=ETF1;
OS   Cryptococcus neoformans var. grubii (Filobasidiella neoformans var.
OS   grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=178876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=125.91;
RX   PubMed=15538538; DOI=10.1371/journal.pbio.0020384;
RA   Fraser J.A., Diezmann S., Subaran R.L., Allen A., Lengeler K.B.,
RA   Dietrich F.S., Heitman J.;
RT   "Convergent evolution of chromosomal sex-determining regions in the animal
RT   and fungal kingdoms.";
RL   PLoS Biol. 2:2243-2255(2004).
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; AF542528; AAN75158.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J112; -.
DR   SMR; Q8J112; -.
DR   PRIDE; Q8J112; -.
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_0000008658"
FT   BINDING         285..313
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   346 AA;  35907 MW;  8EF42482E05A1AA5 CRC64;
     MLYRSALRAS CGFTPRLAST RSRLASSLVL LEHKAGRLND ASLSAVTAAK ATGNDTHGIL
     VGSMAEVEGV LKEAKKIKDL SKIYLATSDA YSHSLAEALA PLLASIVPTK DVSHVFAAHT
     AVGKNVFPRL AGMLDSSLVA DIIALDPSRG TFTRPIYAGN AVLTVKSSPK DSVKIVTVRS
     TAFDKAAIAD GSADVEDVEI LAIESPTQFI SEELTVSSRP DLASAARVVS GGRALKSKES
     FDKILDPLAD SLGAAVGASR AAVDAGYADN SLQVGQTGKV VAPELYVAVG ISGAIQHLAG
     MKESKMIVAI NKDPDAPIFQ VADVGLVADL FESVPQLVQE IGSIKA