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Database: UniProt
Entry: A0A256ZSL5_9CREN
LinkDB: A0A256ZSL5_9CREN
Original site: A0A256ZSL5_9CREN 
ID   A0A256ZSL5_9CREN        Unreviewed;       173 AA.
AC   A0A256ZSL5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Transcription factor E {ECO:0000256|HAMAP-Rule:MF_01909};
DE            Short=TFE {ECO:0000256|HAMAP-Rule:MF_01909};
DE   AltName: Full=TFIIE subunit alpha homolog {ECO:0000256|HAMAP-Rule:MF_01909};
DE   AltName: Full=Transcription initiation factor TFIIE {ECO:0000256|HAMAP-Rule:MF_01909};
GN   Name=tfe {ECO:0000256|HAMAP-Rule:MF_01909,
GN   ECO:0000313|EMBL:OYT55631.1};
GN   ORFNames=B6U76_05430 {ECO:0000313|EMBL:OYT55631.1};
OS   Desulfurococcales archaeon ex4484_217_2.
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales.
OX   NCBI_TaxID=2012519 {ECO:0000313|EMBL:OYT55631.1, ECO:0000313|Proteomes:UP000216854};
RN   [1] {ECO:0000313|Proteomes:UP000216854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that plays a role in the activation of
CC       archaeal genes transcribed by RNA polymerase. Facilitates transcription
CC       initiation by enhancing TATA-box recognition by TATA-box-binding
CC       protein (Tbp), and transcription factor B (Tfb) and RNA polymerase
CC       recruitment. Not absolutely required for transcription in vitro, but
CC       particularly important in cases where Tbp or Tfb function is not
CC       optimal. It dynamically alters the nucleic acid-binding properties of
CC       RNA polymerases by stabilizing the initiation complex and destabilizing
CC       elongation complexes. Seems to translocate with the RNA polymerase
CC       following initiation and acts by binding to the non template strand of
CC       the transcription bubble in elongation complexes. {ECO:0000256|HAMAP-
CC       Rule:MF_01909}.
CC   -!- SUBUNIT: Monomer. Interaction with RNA polymerase subunits RpoF and
CC       RpoE is necessary for Tfe stimulatory transcription activity. Able to
CC       interact with Tbp and RNA polymerase in the absence of DNA promoter.
CC       Interacts both with the preinitiation and elongation complexes.
CC       {ECO:0000256|HAMAP-Rule:MF_01909}.
CC   -!- DOMAIN: The winged helix domain is involved in binding to DNA in the
CC       preinitiation complex. {ECO:0000256|HAMAP-Rule:MF_01909}.
CC   -!- SIMILARITY: Belongs to the TFE family. {ECO:0000256|HAMAP-
CC       Rule:MF_01909}.
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:OYT55631.1}.
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DR   EMBL; NJEC01000064; OYT55631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256ZSL5; -.
DR   Proteomes; UP000216854; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR   CDD; cd00350; rubredoxin_like; 1.
DR   Gene3D; 2.20.28.30; RNA polymerase ii, chain L; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_01909; TFE_arch; 1.
DR   InterPro; IPR016481; TF_E_archaea.
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; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   NCBIfam; TIGR00373; transcription factor E; 1.
DR   PANTHER; PTHR13097:SF7; GENERAL TRANSCRIPTION FACTOR IIE, POLYPEPTIDE 1, ALPHA; 1.
DR   PANTHER; PTHR13097; TRANSCRIPTION INITIATION FACTOR IIE, ALPHA SUBUNIT; 1.
DR   Pfam; PF08271; TF_Zn_Ribbon; 1.
DR   Pfam; PF02002; TFIIE_alpha; 1.
DR   PIRSF; PIRSF006373; TF_E_archaea; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01909};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01909};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01909}.
FT   DOMAIN          1..87
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51344"
SQ   SEQUENCE   173 AA;  20801 MW;  6EE9C78680823A97 CRC64;
     MRKRNDIVEF VKLMLGEQAA KIFAELYKIG EEVNDEEIAK RLGLKLNEVR RQLYLLSEQG
     LVSYRRTKGK NGEWYTYYWR IEKDRLLGII RSRKMITLNK LRERLRYEET NTFYICPNCG
     IRFTFDEALE NGFRCPRCGT SLEYFDNSKI VEFLRRKIAE LEKIVYSEEK RGK
//
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