ID   TFE_PYRAB               Reviewed;         190 AA.
AC   Q9UYS6; G8ZHP0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Transcription factor E {ECO:0000255|HAMAP-Rule:MF_01909};
DE            Short=TFE {ECO:0000255|HAMAP-Rule:MF_01909};
DE   AltName: Full=TFIIE subunit alpha homolog {ECO:0000255|HAMAP-Rule:MF_01909};
DE   AltName: Full=Transcription initiation factor TFIIE {ECO:0000255|HAMAP-Rule:MF_01909};
GN   Name=tfe {ECO:0000255|HAMAP-Rule:MF_01909}; OrderedLocusNames=PYRAB14310;
GN   ORFNames=PAB0950;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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:0000255|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:0000255|HAMAP-Rule:MF_01909}.
CC   -!- DOMAIN: The winged helix domain is involved in binding to DNA in the
CC       preinitiation complex. {ECO:0000255|HAMAP-Rule:MF_01909}.
CC   -!- SIMILARITY: Belongs to the TFE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01909}.
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DR   EMBL; AJ248287; CAB50336.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70877.1; -; Genomic_DNA.
DR   PIR; C75055; C75055.
DR   RefSeq; WP_010868546.1; NC_000868.1.
DR   AlphaFoldDB; Q9UYS6; -.
DR   SMR; Q9UYS6; -.
DR   STRING; 272844.PAB0950; -.
DR   EnsemblBacteria; CAB50336; CAB50336; PAB0950.
DR   GeneID; 1496823; -.
DR   KEGG; pab:PAB0950; -.
DR   PATRIC; fig|272844.11.peg.1522; -.
DR   eggNOG; arCOG04270; Archaea.
DR   HOGENOM; CLU_100097_0_0_2; -.
DR   OMA; DSGWLTY; -.
DR   OrthoDB; 75288at2157; -.
DR   PhylomeDB; Q9UYS6; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 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   PANTHER; PTHR13097; PTHR13097; 1.
DR   Pfam; PF02002; TFIIE_alpha; 1.
DR   PIRSF; PIRSF006373; TF_E_archaea; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   TIGRFAMs; TIGR00373; TIGR00373; 1.
DR   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..190
FT                   /note="Transcription factor E"
FT                   /id="PRO_0000326619"
FT   DOMAIN          4..87
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01909"
FT   REGION          170..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..190
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   190 AA;  22457 MW;  4B29FD8F64EE32AE CRC64;
     MSRKNKALLE IAKDIGGDEA VEIVKALEKK GEATDEELAE ITGIRVNTVR KILYALYDEK
     LADFKRIKDE ETGWYYYYWH LETKRLPEII RARKLRELER LKKMLQEETS EVYYHCGNPE
     HPKLTFDEAF EYGFTCPICG EILQEYDNSA VIEELKKRIE ELEIELGLRP SPKKEKKKTR
     AKAKRKTRKK