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Database: UniProt
Entry: M0CMS3_9EURY
LinkDB: M0CMS3_9EURY
Original site: M0CMS3_9EURY 
ID   M0CMS3_9EURY            Unreviewed;       174 AA.
AC   M0CMS3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=C476_04270 {ECO:0000313|EMBL:ELZ23933.1};
OS   Natrinema limicola JCM 13563.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1230457 {ECO:0000313|EMBL:ELZ23933.1, ECO:0000313|Proteomes:UP000011615};
RN   [1] {ECO:0000313|EMBL:ELZ23933.1, ECO:0000313|Proteomes:UP000011615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13563 {ECO:0000313|EMBL:ELZ23933.1,
RC   ECO:0000313|Proteomes:UP000011615};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(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}.
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:ELZ23933.1}.
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DR   EMBL; AOIT01000021; ELZ23933.1; -; Genomic_DNA.
DR   RefSeq; WP_008010224.1; NZ_AOIT01000021.1.
DR   AlphaFoldDB; M0CMS3; -.
DR   STRING; 1230457.C476_04270; -.
DR   PATRIC; fig|1230457.4.peg.853; -.
DR   eggNOG; arCOG04270; Archaea.
DR   OrthoDB; 5935at2157; -.
DR   Proteomes; UP000011615; 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   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:UP000011615};
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          8..90
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51344"
FT   COILED          93..120
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   174 AA;  20404 MW;  0FDA6E1CFE34D92B CRC64;
     MAFEDLLEDP VIQKYLHELV GPTGMPVAAA PPDGEVTDEE LAEELDLELN DVRRALFILY
     ENDLATYRRL RDEDSGWLTY LWTFEYDNIP ENLEEEMYRL HEALEERQEY ERNHEFYLCE
     ICSIRFEFGE AMDFGFECPE CGSPLESMEN DRLVNAMDDR LDALEDELNI DADA
//
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