ID   A0A319DUE1_ASPSB        Unreviewed;       730 AA.
AC   A0A319DUE1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Probable electron transfer flavoprotein subunit alpha, mitochondrial {ECO:0000256|ARBA:ARBA00020656};
GN   ORFNames=BO78DRAFT_464742 {ECO:0000313|EMBL:PYI01286.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI01286.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI01286.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI01286.1,
RC   ECO:0000313|Proteomes:UP000248423};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000256|ARBA:ARBA00025416}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000256|ARBA:ARBA00005817}.
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DR   EMBL; KZ826419; PYI01286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DUE1; -.
DR   STRING; 1448318.A0A319DUE1; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
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   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.30.190.20; -; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 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; IPR023674; Ribosomal_uL1-like.
DR   InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR   PANTHER; PTHR43153:SF1; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF56808; Ribosomal protein L1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423}.
FT   DOMAIN          418..600
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  78213 MW;  051AA8BE16A0AE47 CRC64;
     MVSSTALTTK ATSGSPYQLD KSQVSRASSA LLRHIKTKQD EKEKTATKKT LIGDNDSDDE
     DTPLHNEAVW LVLTTKKHVV DKNRLKPGKI PVPHSLNASP SLSICLITAD PQRSVKNIVA
     DPSFPQHLTS RIDKVIGFSK LKDRYKSFES RRQLLSEHDV FLADDRIIMR LVNTLGKIFY
     KSSKRPIPVR IAEIEKVDGK KVKKDPKSKN KDDDSAFATP AIVAKEIEKA LNCAPVHLAP
     ATTAAIRVGS SKFTAEQLAE NVDAVVNGLT EKYITKGWRN IKAVHIKGAN TMAMPIWLAS
     ELWVEDADVV EEGAEEAKAI EGNKKRKQSG NDEEKLIEEA PKKTKKVKPA ADDEEALSLA
     ARKEKLQKQK AKALEDDTTT GTMLLPQARF SALRAVRAAR TTPSITASTS ALARLLSTLA
     VLEQRDGKLQ SSSLSAIAAA QKLGGPVTAF VAGAGVKATS AAEAAQIKGL DKVIAVENEA
     YEKGLPENYA PLLIENIQKG SYTHIVAGHS AFGKSLLPRV AALLDVQQVS DITGIESEDT
     FVRPIYAGNA ILTVQSTDAI KVLTVRGTSF QGVETSGGSA AIEEGSDPKA ALQTEWVSEE
     LAKSERPDLG TASRVVSGGR GLKNKEEFER LIVPLADTLG AAVGASRAAV DSGFVDNSLQ
     VGQTGKNVAP QLYLCAGISG AIQHLAGMKD SKVIAAINKD PDAPIFQVAD VGLVGDLFEA
     VPELTEKLKQ
//