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Database: UniProt
Entry: W0I934_9EURY
LinkDB: W0I934_9EURY
Original site: W0I934_9EURY 
ID   W0I934_9EURY            Unreviewed;       171 AA.
AC   W0I934;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
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   ORFNames=TES1_1545 {ECO:0000313|EMBL:AHF80923.1};
OS   Thermococcus paralvinellae.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=582419 {ECO:0000313|EMBL:AHF80923.1, ECO:0000313|Proteomes:UP000019027};
RN   [1] {ECO:0000313|EMBL:AHF80923.1, ECO:0000313|Proteomes:UP000019027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES1 {ECO:0000313|EMBL:AHF80923.1,
RC   ECO:0000313|Proteomes:UP000019027};
RX   PubMed=25082851; DOI=10.1099/ijs.0.066100-0;
RA   Hensley S.A., Jung J.H., Park C.S., Holden J.F.;
RT   "Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov.
RT   of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.";
RL   Int. J. Syst. Evol. Microbiol. 64:3655-3659(2014).
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}.
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DR   EMBL; CP006965; AHF80923.1; -; Genomic_DNA.
DR   RefSeq; WP_042681784.1; NZ_CP006965.1.
DR   AlphaFoldDB; W0I934; -.
DR   STRING; 582419.TES1_1545; -.
DR   GeneID; 24906564; -.
DR   KEGG; ths:TES1_1545; -.
DR   HOGENOM; CLU_100097_0_0_2; -.
DR   OrthoDB; 5935at2157; -.
DR   Proteomes; UP000019027; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; 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   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   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; PF02002; TFIIE_alpha; 1.
DR   PIRSF; PIRSF006373; TF_E_archaea; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 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}; Initiation factor {ECO:0000313|EMBL:AHF80923.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:AHF80923.1};
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          5..88
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51344"
SQ   SEQUENCE   171 AA;  20420 MW;  9EE1E172B0266321 CRC64;
     MPRRKNKELI ELAMDIGGEE AVEIIKALEK KGEATDEELA EMTGIRVNTV RKILYALYDH
     QLAEFRRTRD KETGWYYYYW HLETKRLPEI IRTRKMQELK KLKQMLEEET SEIYYHCGTP
     GHPKLTFDEA LEYEFQCPIC GKMLQQYDNT KIVEELKKRI AQLEKELGIK K
//
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