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Database: UniProt
Entry: L0ACN9_NATGS
LinkDB: L0ACN9_NATGS
Original site: L0ACN9_NATGS 
ID   L0ACN9_NATGS            Unreviewed;       534 AA.
AC   L0ACN9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:ELY66656.1, ECO:0000313|EMBL:PLK21368.1};
DE   SubName: Full=Electron transfer flavoprotein, alpha subunit {ECO:0000313|EMBL:AFZ71601.1};
GN   OrderedLocusNames=Natgr_0343 {ECO:0000313|EMBL:AFZ71601.1};
GN   ORFNames=C490_12827 {ECO:0000313|EMBL:ELY66656.1}, CYV19_04840
GN   {ECO:0000313|EMBL:PLK21368.1};
OS   Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS   104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronobacterium.
OX   NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ71601.1, ECO:0000313|Proteomes:UP000010468};
RN   [1] {ECO:0000313|EMBL:AFZ71601.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SP2 {ECO:0000313|EMBL:AFZ71601.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000010468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC   {ECO:0000313|Proteomes:UP000010468};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ELY66656.1, ECO:0000313|Proteomes:UP000011613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:ELY66656.1,
RC   ECO:0000313|Proteomes:UP000011613};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4] {ECO:0000313|EMBL:PLK21368.1, ECO:0000313|Proteomes:UP000234484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:PLK21368.1,
RC   ECO:0000313|Proteomes:UP000234484};
RC   TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK21368.1};
RA   Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA   Huang J.;
RT   "The characterization of oligonucleotides binding to NgAgo.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000256|ARBA:ARBA00005817}.
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DR   EMBL; CP003377; AFZ71601.1; -; Genomic_DNA.
DR   EMBL; AOIC01000089; ELY66656.1; -; Genomic_DNA.
DR   EMBL; PKKI01000009; PLK21368.1; -; Genomic_DNA.
DR   RefSeq; WP_005580188.1; NZ_PKKI01000009.1.
DR   AlphaFoldDB; L0ACN9; -.
DR   STRING; 797304.Natgr_0343; -.
DR   GeneID; 14207507; -.
DR   KEGG; nge:Natgr_0343; -.
DR   PATRIC; fig|797304.7.peg.2611; -.
DR   eggNOG; arCOG00448; Archaea.
DR   HOGENOM; CLU_034178_1_1_2; -.
DR   Proteomes; UP000010468; Chromosome.
DR   Proteomes; UP000011613; Unassembled WGS sequence.
DR   Proteomes; UP000234484; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
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   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010468};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          140..363
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..73
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..113
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  59125 MW;  B1085CB59DB9530D CRC64;
     MTIDPDEHTV DELEEELETI DDEDTLQSVM EAEQAGRDRK TAREAIHRRL EAVGAVEGES
     EELEGDTETE GEYEETKETV GEQAEGEEVE EVDADSKDEP ANGEEDEQKA ESEEEDDGLS
     HPTRDKRHVR ALEDGHYEDM WVFCETQGGE LLDISKEMLG KARRLMDDFA EENVVAFLMG
     DDCEGLAEEC IAYGADVAVY HDDERLERFL HKPYTEISAH MARGEGPVES TDWRNYDEPR
     YALFPATNNG RDLSAKVQAE LDSGLASDCS DLFIEANEVS NPVKTGEPGV KKTFEKVLHM
     KRPDFSGFEY STILCLDNPG REFHPQGASV IPGSFDPIEP DYERDGLVVE HEMDLEDDWF
     CVEITESDQL EAGIDLTGHE VIVCLGRGIA DDPTEGMELG LDLVDAFEDA ELGITRGIVT
     SSYQFEGHVE EYSKEERQIG ETGQVVAPDL YVAAGVSGAV QHKVGMDESD TIVAINTDTD
     ARIRDFSDYF LEGDLFEVLP QLSEAIEAGE TELEAIADGS GADADANESD GETR
//
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