{PDOC51745}
{PS51745; PB1}
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* PB1 domain profile *
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The PB1  (Phox  and  Bem1) domain, comprising about 80 amino acid residues, is
conserved among animals, fungi, amoebas, and plants. It functions as a protein
binding module through PB1-mediated heterodimerization or homo-oligomerization
[1,2,3,4]. The    PB1    domain    is  found  in  several  signaling  proteins
including:

 - Mammalian  MEK5, a MAP kinase kinase implicated in epidermal growth factor-
   induced cell proliferation.
 - Mammalian  Sequestosome-1  (Sqstm1)  or p62/ZIP, a protein linking the zeta
   isoform of protein kinase C to RIP and/or potassium channels.
 - Mammalian  neutrophil  cytosol  factor  4 (NCF-4) or p40(phox), a cytosolic
   factor of the superoxide-generating NADPH oxidase in phagocytes.
 - Mammalian  neutrophil  cytosol  factor  2  (NCF-2) or p67(phox), an oxidase
   activator.
 - Yeast  bud  emergence  protein  1  (Bem1),  necessary for cell polarization
   during vegetative growth.
 - Yeast  cell  division  control  protein  24  (CDC24),  a guanine nucleotide
   exchange factor (GEF) for the small GTPase CDC42.
 - Plant  AUXIN  RESPONSE  FACTOR (ARF) transcription factor family, regulates
   gene expression in response to auxin.
 - Plant  AUXIN/INDOLE 3-ACETIC ACID (Aux/IAA) repressor proteins, repress ARF
   transcription factors    via    direct    interaction   under   low   auxin
   concentrations.

The PB1  domains adopt an ubiquitin-like beta-grasp fold, containing two alpha
helices and a mixed five-stranded beta sheet (see <PDB:1WMH>). The beta-sheet
has a convex surface, and alpha1 fits into the cavity formed by the sheet. PB1
domains may  display an acidic surface (type I), a basic surface (tape II), or
both surfaces  (type  I/II) on opposite faces of the domain structure to allow
for front-to-back orientation of multiple PB1 domains [1,2,3,4].

The profile we developed covers the entire PB1 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2015 / First entry.

[ 1] Sumimoto H., Kamakura S., Ito T.
     "Structure and function of the PB1 domain, a protein interaction
     module conserved  in animals, fungi, amoebas, and plants."
     Sci. STKE 2007:Re6-Re6(2007).
     PubMed=17726178; DOI=10.1126/stke.4012007re6
[ 2] Hirano Y., Yoshinaga S., Takeya R., Suzuki N.N., Horiuchi M.,
     Kohjima M., Sumimoto H., Inagaki F.
     "Structure of a cell polarity regulator, a complex between atypical
     PKC and Par6 PB1 domains."
     J. Biol. Chem. 280:9653-9661(2005).
     PubMed=15590654; DOI=10.1074/jbc.M409823200
[ 3] Terasawa H., Noda Y., Ito T., Hatanaka H., Ichikawa S., Ogura K.,
     Sumimoto H., Inagaki F.
     "Structure and ligand recognition of the PB1 domain: a novel protein
     module binding to the PC motif."
     EMBO J. 20:3947-3956(2001).
     PubMed=11483498; DOI=10.1093/emboj/20.15.3947
[ 4] Korasick D.A., Westfall C.S., Lee S.G., Nanao M.H., Dumas R.,
     Hagen G., Guilfoyle T.J., Jez J.M., Strader L.C.
     "Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the
     control of  auxin response repression."
     Proc. Natl. Acad. Sci. U.S.A. 111:5427-5432(2014).
     PubMed=24706860; DOI=10.1073/pnas.1400074111

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