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Database: UniProt
Entry: G0WHW8_NAUDC
LinkDB: G0WHW8_NAUDC
Original site: G0WHW8_NAUDC 
ID   G0WHW8_NAUDC            Unreviewed;       436 AA.
AC   G0WHW8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=HTH TFE/IIEalpha-type domain-containing protein {ECO:0000259|PROSITE:PS51344};
GN   Name=NDAI0K01880 {ECO:0000313|EMBL:CCD27379.1};
GN   OrderedLocusNames=NDAI_0K01880 {ECO:0000313|EMBL:CCD27379.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD27379.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD27379.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the TFIIE alpha subunit family.
CC       {ECO:0000256|ARBA:ARBA00008947}.
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DR   EMBL; HE580277; CCD27379.1; -; Genomic_DNA.
DR   RefSeq; XP_003672622.1; XM_003672574.1.
DR   AlphaFoldDB; G0WHW8; -.
DR   STRING; 1071378.G0WHW8; -.
DR   GeneID; 11497745; -.
DR   KEGG; ndi:NDAI_0K01880; -.
DR   eggNOG; KOG2593; Eukaryota.
DR   HOGENOM; CLU_035744_2_0_1; -.
DR   OMA; DAIKWKV; -.
DR   OrthoDB; 7984at2759; -.
DR   Proteomes; UP000000689; Chromosome 11.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039997; TFE.
DR   InterPro; IPR017919; TFIIE/TFIIEa_HTH.
DR   InterPro; IPR002853; TFIIE_asu.
DR   InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13097:SF7; GENERAL TRANSCRIPTION FACTOR IIE, POLYPEPTIDE 1, ALPHA; 1.
DR   PANTHER; PTHR13097; TRANSCRIPTION INITIATION FACTOR IIE, ALPHA SUBUNIT; 1.
DR   Pfam; PF02002; TFIIE_alpha; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          9..99
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51344"
FT   REGION          276..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..396
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  50499 MW;  11873E4C6AF812A3 CRC64;
     MDRNIDEIVK NLLKFVVRGF YGGSYVLVLD AILFHSVLAE DDLKQLLSIN KTELGPLIAR
     LRSDRLISIH KQREYPPNSK SIERVYYYIK FPHAIDAIKW KVHQVVQRLK DDLDKNSAPN
     GYMCPICLTK YTQLEAVQLL NFDRTEFLCS LCDEPLVEDD SGRKNKEKQD KLNRLMDQIQ
     PVIDYLKRID DSRIEENTFE ISLARLIPPQ NQSHAAYTYN PKKGSTMFRP GDAPMANVMG
     TALGNDSSRR AGANSQATLH INITTASDEI AQTKLQERQA EEKRKQNAVP EWHQQSTVGK
     SALGRLDNEE EFDPQTTAQA LQSTESMMNG GNDGYQNHRT LTEQEIEERE SERALNEYYA
     ALARKQAAER KKEEEEEMEE EEEEEMEEKG REEMDQDAID EEAEFEDEFE DVVEEKKENL
     TLQKRRPRRQ LIHRII
//
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