GenomeNet

Database: UniProt
Entry: A0A0F4YXV2_TALEM
LinkDB: A0A0F4YXV2_TALEM
Original site: A0A0F4YXV2_TALEM 
ID   A0A0F4YXV2_TALEM        Unreviewed;       349 AA.
AC   A0A0F4YXV2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Probable electron transfer flavoprotein subunit alpha {ECO:0000256|PIRNR:PIRNR000089};
GN   ORFNames=T310_3328 {ECO:0000313|EMBL:KKA22646.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22646.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA22646.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22646.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) 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, ECO:0000256|PIRNR:PIRNR000089}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000089,
CC         ECO:0000256|PIRSR:PIRSR000089-1};
CC       Note=Binds 1 FAD per dimer. {ECO:0000256|PIRNR:PIRNR000089,
CC       ECO:0000256|PIRSR:PIRSR000089-1};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|PIRNR:PIRNR000089}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|PIRNR:PIRNR000089}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000256|ARBA:ARBA00005817, ECO:0000256|PIRNR:PIRNR000089}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKA22646.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LASV01000133; KKA22646.1; -; Genomic_DNA.
DR   RefSeq; XP_013329258.1; XM_013473804.1.
DR   AlphaFoldDB; A0A0F4YXV2; -.
DR   STRING; 1408163.A0A0F4YXV2; -.
DR   GeneID; 25315678; -.
DR   OrthoDB; 5481222at2759; -.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
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; 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; 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   PIRSF; PIRSF000089; Electra_flavoP_a; 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.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000089};
KW   FAD {ECO:0000256|PIRNR:PIRNR000089, ECO:0000256|PIRSR:PIRSR000089-1};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000089};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Transport {ECO:0000256|PIRNR:PIRNR000089}.
FT   DOMAIN          37..219
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   REGION          193..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         239
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         265..266
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         279..283
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         296..303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         317
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   349 AA;  36387 MW;  49F35FFF57C5E30B CRC64;
     MISIARPSVL RAARSQLYPS RAVHETRFSA FARLLSTLAV LEQRNGKLQP SSLSAIAAAQ
     KLGGSITGFV AGSGVKATAA AEAAKIKGLE KVVAVENDAY EKGLPENFAP LLVENIKKGG
     YTHVIAGHSA FGKNLLPRVA ALLDVQQVSD ITAIESEDTF VRPIYAGNAI LTVQSEDPIK
     VITVRGTAFQ GAETEGGSAE IVDGADPQAP SPTEWVSEDL AKSDRPDLAT ASRVVSGGRG
     LKSKEDFDRL IPPLADALGA AIGASRAAVD SGFADNSLQV GQTGKNVAPQ LYLCAGISGA
     IQHLAGMKDS KVIAAINKDP EAPIFQVADV GLVGDLFEKV PELTEKLKK
//
DBGET integrated database retrieval system