{PDOC51319}
{PS51319; TFIIS_N}
{BEGIN}
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* TFIIS N-terminal domain profile *
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Transcription factor  IIS  (TFIIS)  is  a transcription elongation factor that
increases the  overall transcription rate of RNA polymerase II by reactivating
transcription elongation complexes that have arrested transcription. The three
structural domains of TFIIS are conserved from yeast to human. The 80 or so N-
terminal residues  form  a  protein  interaction domain containing a conserved
motif, which has been called the LW motif because of the invariant leucine and
tryptophane residues it contains. Although the N-terminal domain is not needed
for transcriptional  activity, a similar sequence has been identified in other
transcription factors  and  proteins  that are predominantly nuclear localized
[1,2]:

 - MED26  (also known as CRSP70 and ARC70), a subunit of the Mediator complex,
   which is required for the activity of the enhancer-binding protein Sp1.
 - Elongin  A, a subunit of a transcription elongation factor previously known
   as SIII.  It  increases  the rate of transcription by suppressing transient
   pausing of the elongation complex.
 - PPP1R10,  a  nuclear  regulatory  subunit of protein phosphatase 1 that was
   previously known as p99, FB19 or PNUTS.
 - PIBP, a small hypothetical protein that could be a phosphoinositide binding
   protein.
 - IWS1,  which  is  thought  to function in both transcription initiation and
   elongation.

The TFIIS  N-terminal  domain is a compact four-helix bundle (see <PDB:1EO0>).
The hydrophobic  core residues of helices 2, 3, and 4 are well conserved among
TFIIS domains, although helix 1 is less conserved [2].

The profile we developed covers the entire TFIIS N-terminal domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2007 / First entry.

[ 1] Booth V., Koth C.M., Edwards A.M., Arrowsmith C.H.
     "Structure of a conserved domain common to the transcription factors
     TFIIS, elongin A, and CRSP70."
     J. Biol. Chem. 275:31266-31268(2000).
     PubMed=10811649; DOI=10.1074/jbc.M002595200
[ 2] Ling Y., Smith A.J., Morgan G.T.
     "A sequence motif conserved in diverse nuclear proteins identifies a
     protein interaction domain utilised for nuclear targeting by human
     TFIIS."
     Nucleic Acids Res. 34:2219-2229(2006).
     PubMed=16648364; DOI=10.1093/nar/gkl239

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