{PDOC51309}
{PS51309; PABC}
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* Poly(A)-binding protein C-terminal (PABC) domain profile *
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The ~75-residue poly(A)-binding protein C-terminal domain (PABC) is a peptide-
binding domain found in:

 - poly(A)-binding  proteins (PABPs), ubiquitous RNA binding proteins found in
   all eukaryotes.  They  are  implicated  in  stabilizing  mRNA and promoting
   translation. PABPs  are modular proteins consisting of an N-terminal region
   with four  RNA  recognition  motifs  (RRMs)  (see  <PDOC00030>)  and a PABC
   domain.
 - The  HYD  (for  hyperplastic  discs),  EDD or Rat100 family of ubiquitin E3
   protein ligases.   HYD   ubiquitin  ligases  contain  a  HECT  domain  (see
   <PDOC50237>).

The PABC  domain  binds  a  conserved motif of 12-15 amino acids, termed PABP-
interacting motif  (PAM)-2,  with conserved alanine, phenylalanine and proline
residues at position 7, 10 and 12 [1-5].

The PABC   domain   consists   of  five  (see  <PDB:1JH4;  A>)  or  four  (see
<PDB:1IFW; A>)  alpha-helices that form a compact structure with a well packed
hydrophobic core.  Characteristic  to  all PABC domains, the last four helices
fold into  a  right-handed super coil. They encompass the peptide-binding site
and among  PABC domains, sequences conservation is highest among helices 2, 3,
and 5,  which  are  required  for  peptide  recognition  [1-5]. A phylogenetic
analysis of  the  PABC  domain reveals that they can be categorized into three
main classes:  animal, vegetal and a 'divergent' group including Saccharomyces
cerevisiae, Schizosaccharomyces pombe, and the HYD family of ubiquitin ligases
[2,3].

The profile we developed covers the entire PABC domain.

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

[ 1] Kozlov G., Trempe J.-F., Khaleghpour K., Kahvejian A., Ekiel I.,
     Gehring K.
     "Structure and function of the C-terminal PABC domain of human
     poly(A)-binding protein."
     Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001).
     PubMed=11287632; DOI=10.1073/pnas.071024998
[ 2] Kozlov G., Siddiqui N., Coillet-Matillon S., Trempe J.-F., Ekiel I.,
     Sprules T., Gehring K.
     "Solution structure of the orphan PABC domain from Saccharomyces
     cerevisiae poly(A)-binding protein."
     J. Biol. Chem. 277:22822-22828(2002).
     PubMed=11940585; DOI=10.1074/jbc.M201230200
[ 3] Siddiqui N., Kozlov G., D'Orso I., Trempe J.-F., Gehring K.
     "Solution structure of the C-terminal domain from poly(A)-binding
     protein in Trypanosoma cruzi: a vegetal PABC domain."
     Protein Sci. 12:1925-1933(2003).
     PubMed=12930992
[ 4] Kozlov G., De Crescenzo G., Lim N.S., Siddiqui N., Fantus D.,
     Kahvejian A., Trempe J.-F., Elias D., Ekiel I., Sonenberg N.,
     O'Connor-McCourt M., Gehring K.
     "Structural basis of ligand recognition by PABC, a highly specific
     peptide-binding domain found in poly(A)-binding protein and a HECT
     ubiquitin ligase."
     EMBO J. 23:272-281(2004).
     PubMed=14685257; DOI=10.1038/sj.emboj.7600048
[ 5] Siddiqui N., Osborne M.J., Gallie D.R., Gehring K.
     "Solution Structure of the PABC Domain from Wheat Poly (A)-Binding
     Protein: An Insight into RNA Metabolic and Translational Control in
     Plants."
     Biochemistry 46:4221-4231(2007).
     PubMed=17358048; DOI=10.1021/bi061986d

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