TFE_PYRFU
ID TFE_PYRFU Reviewed; 195 AA.
AC Q8U3H5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Transcription factor E;
DE Short=TFE;
DE AltName: Full=TFIIE subunit alpha homolog;
DE AltName: Full=Transcription initiation factor TFIIE;
GN Name=tfe; OrderedLocusNames=PF0491;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP INTERACTION WITH RNA POLYMERASE SUBCOMPLEX E-F.
RX PubMed=17311916; DOI=10.1074/jbc.m611674200;
RA Naji S., Gruenberg S., Thomm M.;
RT "The RPB7 orthologue E' is required for transcriptional activity of a
RT reconstituted archaeal core enzyme at low temperatures and stimulates open
RT complex formation.";
RL J. Biol. Chem. 282:11047-11057(2007).
RN [3]
RP FUNCTION, AND INTERACTION WITH INITIATION COMPLEX AND ELONGATION COMPLEX.
RX PubMed=17921145; DOI=10.1074/jbc.m707371200;
RA Gruenberg S., Bartlett M.S., Naji S., Thomm M.;
RT "Transcription factor E is a part of transcription elongation complexes.";
RL J. Biol. Chem. 282:35482-35490(2007).
RN [4]
RP FUNCTION.
RX PubMed=17965161; DOI=10.1128/jb.01498-07;
RA Micorescu M., Gruenberg S., Franke A., Cramer P., Thomm M., Bartlett M.;
RT "Archaeal transcription: function of an alternative transcription factor B
RT from Pyrococcus furiosus.";
RL J. Bacteriol. 190:157-167(2008).
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.
CC {ECO:0000269|PubMed:17921145, ECO:0000269|PubMed:17965161}.
CC -!- SUBUNIT: Monomer (By similarity). Interaction with RNA polymerase
CC subunits RpoF and RpoE is necessary for Tfe stimulatory transcription
CC activity. Able to interact with RNA polymerase in the absence of Tbp or
CC DNA promoter (By similarity). Interacts both with the preinitiation and
CC elongation complexes. {ECO:0000250, ECO:0000269|PubMed:17311916,
CC ECO:0000269|PubMed:17921145}.
CC -!- DOMAIN: The winged helix domain is involved in binding to DNA in the
CC preinitiation complex.
CC -!- SIMILARITY: Belongs to the TFE family. {ECO:0000305}.
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DR EMBL; AE009950; AAL80615.1; -; Genomic_DNA.
DR RefSeq; WP_011011608.1; NZ_CP023154.1.
DR PDB; 6PLN; X-ray; 2.60 A; A/B=1-195.
DR PDB; 6XJF; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-110.
DR PDBsum; 6PLN; -.
DR PDBsum; 6XJF; -.
DR AlphaFoldDB; Q8U3H5; -.
DR SMR; Q8U3H5; -.
DR STRING; 186497.PF0491; -.
DR EnsemblBacteria; AAL80615; AAL80615; PF0491.
DR GeneID; 41712292; -.
DR KEGG; pfu:PF0491; -.
DR PATRIC; fig|186497.12.peg.514; -.
DR eggNOG; arCOG04270; Archaea.
DR HOGENOM; CLU_100097_0_0_2; -.
DR OMA; DSGWLTY; -.
DR OrthoDB; 75288at2157; -.
DR PhylomeDB; Q8U3H5; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..195
FT /note="Transcription factor E"
FT /id="PRO_0000318947"
FT DOMAIN 6..89
FT /note="HTH TFE/IIEalpha-type"
FT REGION 172..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 6..32
FT /evidence="ECO:0007829|PDB:6PLN"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6PLN"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6PLN"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:6PLN"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:6PLN"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6PLN"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:6PLN"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6XJF"
FT HELIX 88..107
FT /evidence="ECO:0007829|PDB:6PLN"
SQ SEQUENCE 195 AA; 22885 MW; F7507AF9F3353763 CRC64;
MGRDKKNTAL LDIARDIGGD EAVEVVKALE KKGEATDEEL AELTGVRVNT VRKILYALYD
AKLATFRRVR DDETGWYYYY WRIDTKRLPE VIRTRKLQEL EKLKQMLQEE TSETYYHCGT
PGHPKLTFDE AFEYGFQCPI CGEILYEYDN SKIIEELKKR IEELEIELGL RSPPKEEKPK
KATRRKKSRS GKKKK
