{PDOC51483}
{PS51483; B5}
{BEGIN}
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* B5 domain profile *
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Aminoacyl-tRNA synthetases  (aaRSs)  play a crucial role in the translation of
the genetic  code  by  means  of  covalent  attachment of amino acids to their
cognate tRNAs.  Phenylalanine-tRNA synthetase (PheRS) is known to be among the
most complex enzymes of the aaRS family. It is a heterodimeric class II enzyme
of the (AlphaBeta)2 type. The AlphaBeta heterodimer of Thermus thermophilus is
composed of  ten  structural  domains:  two  of them A1-A2 belong to the alpha
subunit and  eight B1-B8 to the beta subunit. The B5 domain is formed by three
alpha-helices and  three  antiparallel  beta-strands  and comprises a surface-
exposed "winged" helix-turn-helix (HTH) motif (see <PDB:1PYS>) [1,2,3]. The B5
domain has been shown to bind DNA [4].

The profile we developed covers the entire B5 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2010 / First entry.

[ 1] Mosyak L., Reshetnikova L., Goldgur Y., Delarue M., Safro M.G.
     "Structure of phenylalanyl-tRNA synthetase from Thermus
     thermophilus."
     Nat. Struct. Biol. 2:537-547(1995).
     PubMed=7664121
[ 2] Rodova M., Ankilova V., Safro M.G.
     "Human phenylalanyl-tRNA synthetase: cloning, characterization of the
     deduced amino acid sequences in terms of the structural domains and
     coordinately regulated expression of the alpha and beta subunits in
     chronic myeloid leukemia cells."
     Biochem. Biophys. Res. Commun. 255:765-773(1999).
     PubMed=10049785; DOI=10.1006/bbrc.1999.0141
[ 3] Moor N., Lavrik O., Favre A., Safro M.
     "Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases
     display conservation of the binding mode of the tRNA(Phe) CCA end."
     Biochemistry 42:10697-10708(2003).
     PubMed=12962494; DOI=10.1021/bi034732q
[ 4] Dou X., Limmer S., Kreutzer R.
     "DNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop
     formation of the double-stranded DNA."
     J. Mol. Biol. 305:451-458(2001).
     PubMed=11152603; DOI=10.1006/jmbi.2000.4312

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