ID A0A348B1C0_9CREN Unreviewed; 174 AA.
AC A0A348B1C0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=GCM10007116_06990 {ECO:0000313|EMBL:GGT91863.1},
GN HS1genome_0361 {ECO:0000313|EMBL:BBD71972.1};
OS Sulfodiicoccus acidiphilus.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfodiicoccus.
OX NCBI_TaxID=1670455 {ECO:0000313|EMBL:BBD71972.1, ECO:0000313|Proteomes:UP000276741};
RN [1] {ECO:0000313|Proteomes:UP000276741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-1 {ECO:0000313|Proteomes:UP000276741};
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of Sulfodiicoccus acidiphilus strain HS-1.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBD71972.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HS-1 {ECO:0000313|EMBL:BBD71972.1};
RX PubMed=31331368;
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of the Sulfodiicoccus acidiphilus strain HS-1T,
RT the first crenarchaeon that lacks polB3, isolated from an acidic hot spring
RT in Ohwaku-dani, Hakone, Japan.";
RL BMC Res. Notes 12:444-444(2019).
RN [3] {ECO:0000313|EMBL:GGT91863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGT91863.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [4] {ECO:0000313|EMBL:GGT91863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGT91863.1};
RA Sun Q., Ohkuma M.;
RL Submitted (SEP-2020) 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}.
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DR EMBL; AP018553; BBD71972.1; -; Genomic_DNA.
DR EMBL; BMQS01000005; GGT91863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348B1C0; -.
DR KEGG; sacd:HS1genome_0361; -.
DR Proteomes; UP000276741; Chromosome.
DR Proteomes; UP000616143; 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 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; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51344; HTH_TFE_IIE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01909}; Reference proteome {ECO:0000313|Proteomes:UP000276741};
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 3..87
FT /note="HTH TFE/IIEalpha-type"
FT /evidence="ECO:0000259|PROSITE:PS51344"
FT COILED 144..171
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 174 AA; 20862 MW; C83066C42C9BDADA CRC64;
MEAEELLKEL AVTMLGDEVL PVLEILLKGK SELTDDEIAR MLNVKVNNVR RTLYMLADHG
LVRYKRTRDR ETGWYLYYWR ANTDQVNEIL LNRKREMVQK LKMRLEFETN NTFYICPEDG
SRYIFDEAFE NEFKCPRCGT SLVYYEVERV REVIERKIRQ LEEEINVETK SNFG
//
