1D8K,1D8J


Conserved Protein Domain Family
TFIIE_beta_winged_helix

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cd07977: TFIIE_beta_winged_helix 
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TFIIE_beta_winged_helix domain, located at the central core region of TFIIE beta, with double-stranded DNA binding activity
Transcription Factor IIE (TFIIE) beta winged-helix (or forkhead) domain is located at the central core region of TFIIE beta. The winged-helix is a form of helix-turn-helix (HTH) domain which typically binds DNA with the 3rd helix. The winged-helix domain is distinguished by the presence of a C-terminal beta-strand hairpin unit (the wing) that packs against the cleft of the tri-helical core. Although most winged-helix domains are multi-member families, TFIIE beta winged-helix domain is typically found as a single orthologous group. TFIIE is one of the six eukaryotic general transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF and TFIIH) that are required for transcription initiation of protein-coding genes. TFIIE is a heterotetramer consisting of two copies each of alpha and beta subunits. TFIIE beta contains several functional domains, an N-terminal serine-rich region, a central core domain exhibiting a winged-helix structure capable of binding double-stranded DNA, a leucine repeat, a sigma3 region, and a C-terminal domain containing two basic regions. The assembly of transcription preinitiation complex (PIC) includes the general transcription factors and RNA polymerase II (pol II) initiated by the binding of the TBP subunit of TFIID to the TATA box, followed by either the sequential assembly of other general transcription factors and pol II or a preassembled pol II holoenzyme pathway. TFIIE interacts directly with TFIIF, TFIIB, pol II, and promoter DNA. TFIIE recruits TFIIH and regulates its activities. TFIIE and TFIIH are also important for the transition from initiation to elongation.
Statistics
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PSSM-Id: 153423
View PSSM: cd07977
Aligned: 32 rows
Threshold Bit Score: 61.8717
Threshold Setting Gi: 45185930
Created: 1-Oct-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
1D8K_A         3 SGSSGYKFGVLAKIVNYMKTRHqrgdtHPLTLDEILDETQh-------------LDIGLKQKQWLMTEALvn-------- 61  human
XP_388795     76 TGYGAEVKTQMTFAVEYLKKKG-----DTKTITEIIDHLSl-------------RGYDEEHKRQLAEGLRghprvdwkpd 137 Gibberella zeae...
XP_001905943  79 TGTGDSVISQMAYAVTWLRGKD-----EPQTYHDVLSYLSatgrsdseqeffveQMRRHPQIQWIPDPNLs--------- 144 Podospora anser...
XP_001549685  70 TGYGTEAFTQVTYVIEFLKKKD-----EPKTFQEILEYLSqvh---------veQSKKQLIAQILRRHDRvqwia----d 131 Botryotinia fuc...
P79011        73 SGVGTHYLSQLHYAVEYLKERN-----EPKTAEEIASYLS--------------TPLTPMLLNLLKKNNRi--------- 124 fission yeast
EEH09203      76 TGTGKDIMTQVVFAIDHMKSKD-----YALKFADILSYLSlqqq-------ghdPGYIQALKRILQSHDKvey------- 136 Ajellomyces cap...
NP_983646     89 ALDSTHLSTKMLIATEYIQERA-----EPVPIDQIESYLS--------------LPKDNSVIPMLKGLAKf--------- 140 Ashbya gossypii...
XP_001796962 141 QGTGEHVYTRFTYTVNHLRDKN-----KWLPFDEIMNFLG--------------VKVGDPQREQLRTLFRsesd------ 195 Phaeosphaeria n...
P36145       118 DISKSHDSSKLLWATEYIQKKG-----KPVLVNELLDYLS--------------MKKDDKVIELLKKLDRi--------- 169 baker's yeast
XP_001932717  46 TGTGEHVFTRLTYVNDFLRERKe----KWHTFDDIMEYLN--------------IPPGHIQREQLRALMRadnq------ 101 Pyrenophora tri...
1D8K_A        62 --npKIEVIDGKYAFKPKYNVR 81  human
XP_388795    138 anlsEQTWKTGTYAHRPIIPGV 159 Gibberella zeae PH-1
XP_001905943 145 ----EQTWKTGTYIHRPTIPNV 162 Podospora anserina DSM 980
XP_001549685 132 pklkVQAWDSGTFKHRPIIGVR 153 Botryotinia fuckeliana B05.10
P79011       125 ----YYDERNETFTFKPLHNIR 142 fission yeast
EEH09203     137 --dpSGANGEGTFRFKPPHNIR 156 Ajellomyces capsulatus G186AR
NP_983646    141 ----KFDPKKNTLQYVSIYDVH 158 Ashbya gossypii ATCC 10895
XP_001796962 196 gnriMWNSANDTYRYKPKLDIR 217 Phaeosphaeria nodorum SN15
P36145       170 ----EFDPKKGTFKYLSTYDVH 187 baker's yeast
XP_001932717 102 gnriSWDSHNEKYRYKPKLDIR 123 Pyrenophora tritici-repentis Pt-1C-BFP
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