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Database: UniProt
Entry: TFE_METJA
LinkDB: TFE_METJA
Original site: TFE_METJA 
ID   TFE_METJA               Reviewed;         173 AA.
AC   Q58187;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   25-OCT-2017, entry version 95.
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=MJ0777;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=15485836; DOI=10.1074/jbc.C400446200;
RA   Ouhammouch M., Werner F., Weinzierl R.O., Geiduschek E.P.;
RT   "A fully recombinant system for activator-dependent archaeal
RT   transcription.";
RL   J. Biol. Chem. 279:51719-51721(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH TBP AND RNA POLYMERASE.
RX   PubMed=16135821; DOI=10.1128/MCB.25.18.8344-8355.2005;
RA   Werner F., Weinzierl R.O.;
RT   "Direct modulation of RNA polymerase core functions by basal
RT   transcription factors.";
RL   Mol. Cell. Biol. 25:8344-8355(2005).
CC   -!- FUNCTION: Transcription factor that plays a role in the activation
CC       of archaeal genes transcribed by RNA polymerase. Facilitates
CC       transcription initiation by enhancing TATA-box recognition by
CC       TATA-box-binding protein (Tbp), and transcription factor B (Tfb)
CC       and RNA polymerase recruitment. Not absolutely required for
CC       transcription in vitro, but particularly important in cases where
CC       Tbp or Tfb function is not optimal. It dynamically alters the
CC       nucleic acid-binding properties of RNA polymerases by stabilizing
CC       the initiation complex and destabilizing elongation complexes.
CC       Seems to translocate with the RNA polymerase following initiation
CC       and acts by binding to the non template strand of the
CC       transcription bubble in elongation complexes.
CC       {ECO:0000269|PubMed:15485836, ECO:0000269|PubMed:16135821}.
CC   -!- SUBUNIT: Monomer (By similarity). Interaction with RNA polymerase
CC       subunits RpoF and RpoE is necessary for Tfe stimulatory
CC       transcription activity. Able to interact with RNA polymerase in
CC       the absence of Tbp or DNA promoter. Interacts both with the
CC       preinitiation and elongation complexes (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The winged helix domain is involved in binding to DNA in
CC       the preinitiation complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TFE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98767.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; L77117; AAB98767.1; ALT_INIT; Genomic_DNA.
DR   ProteinModelPortal; Q58187; -.
DR   SMR; Q58187; -.
DR   STRING; 243232.MJ_0777; -.
DR   EnsemblBacteria; AAB98767; AAB98767; MJ_0777.
DR   KEGG; mja:MJ_0777; -.
DR   eggNOG; arCOG04270; Archaea.
DR   eggNOG; COG1675; LUCA.
DR   InParanoid; Q58187; -.
DR   KO; K03136; -.
DR   OMA; DSGWLTY; -.
DR   OrthoDB; POG093Z0C2C; -.
DR   PhylomeDB; Q58187; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
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; 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   InterPro; IPR013137; Znf_TFIIB.
DR   Pfam; PF08271; TF_Zn_Ribbon; 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   Complete proteome; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    173       Transcription factor E.
FT                                /FTId=PRO_0000107028.
FT   DOMAIN        3     88       HTH TFE/IIEalpha-type.
SQ   SEQUENCE   173 AA;  20667 MW;  F78759126582C7B6 CRC64;
     MLNDPLVQEV LFNIFEGDEK GFEVIDVLLE KGETTEEEIA KELGVKLNVV RKLLYKLYDA
     RLVDYKRWKD EDTNWYSYTW LPTLEKLPYV VKKKINELIK DLEKKLEFEK NNMFFFCPNC
     NVRFTFEEAM DYGFSCPGCG NMLQEFDNSE LIKDLEEQIK FLKEELKNNP FLK
//
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