ID A0A167INW9_CALVF Unreviewed; 310 AA.
AC A0A167INW9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Electron transfer flavo protein beta subunit {ECO:0000313|EMBL:KZO92815.1};
GN ORFNames=CALVIDRAFT_297717 {ECO:0000313|EMBL:KZO92815.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO92815.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO92815.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO92815.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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 beta-subunit/FixA family.
CC {ECO:0000256|ARBA:ARBA00007557}.
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DR EMBL; KV417307; KZO92815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167INW9; -.
DR STRING; 1330018.A0A167INW9; -.
DR OrthoDB; 5476365at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT; 1.
DR PANTHER; PTHR21294:SF8; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT BETA; 1.
DR Pfam; PF01012; ETF; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..269
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
SQ SEQUENCE 310 AA; 33474 MW; C839A4E42811C474 CRC64;
MLPSAREKLV LQGAVSGELG LPAAALPLFS FVAVALFISL YLLTMRPTPR SLLRILVPVK
RCVDYAVKIR VNAQQTGVET NVKHSMNPFD EIAVEEAVRL RERMKDSIKG ITAVTIGPSK
AQETLRTALA MGADDAVHVE VPESANVEPL AVAKLLRAVI EKKGPYELVI LGKQAIDDDA
GQTGQMLAGL MGWGQATFAS KLEVDEAKGS VDVTREVDGG LEQIRVKLPA IITADLRLNE
PRYASLPNIM KAKKKPLEKF KPEDLGVDIT PRLQVLKVTE PPKRVGGQKV ENVDELIAKL
KEAGVLPGAA
//
