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TFE_HALSA
ID   TFE_HALSA               Reviewed;         172 AA.
AC   Q9HRC7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 105.
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=VNG_0757G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG19231.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004437; AAG19231.1; ALT_INIT; Genomic_DNA.
DR   PIR; C84233; C84233.
DR   RefSeq; WP_012289219.1; NC_002607.1.
DR   AlphaFoldDB; Q9HRC7; -.
DR   SMR; Q9HRC7; -.
DR   STRING; 64091.VNG_0757G; -.
DR   PaxDb; Q9HRC7; -.
DR   EnsemblBacteria; AAG19231; AAG19231; VNG_0757G.
DR   GeneID; 5952680; -.
DR   GeneID; 62886355; -.
DR   KEGG; hal:VNG_0757G; -.
DR   PATRIC; fig|64091.14.peg.581; -.
DR   HOGENOM; CLU_100097_0_0_2; -.
DR   InParanoid; Q9HRC7; -.
DR   OrthoDB; 75288at2157; -.
DR   PhylomeDB; Q9HRC7; -.
DR   Proteomes; UP000000554; 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:0001113; P:transcription open complex formation at RNA polymerase II promoter; IBA:GO_Central.
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   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..172
FT                   /note="Transcription factor E"
FT                   /id="PRO_0000326591"
FT   DOMAIN          8..90
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01909"
SQ   SEQUENCE   172 AA;  19884 MW;  F95E7BFE4859787E CRC64;
     MAFEDLLDDP VVQKYLHELV GPKGMPVAAA PPDGEVTDEE LAERLGLELN DVRRALFILY
     ENDLATYRRV RDEDSGWLTY LWTFQYENVP GNLREEMDRL LEALVDRREY ELENEFYLCE
     VCSIRFEFGE AMDLGFECPE CGSAVEAMEN TDLVDAMDDR IERLRSELAV EA
 
 
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