{PDOC51447}
{PS51447; FDX_ACB}
{BEGIN}
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* Ferredoxin-fold anticodon binding (FDX-ACB) domain profile *
**************************************************************

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. Bacterial and mitochondrial PheRSs
share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a
canonical double  split  alpha+beta  motif  having  no insertions. The FDX-ACB
domain displays  a typical RNA recognition fold (RRM) (see <PDOC00030>) formed
by the  four-stranded antiparallel beta sheet, with two helices packed against
it (see <PDB:3CMQ>) [1,2,3,4,5].

The profile we developed covers the entire FDX-ACB domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2009 / 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] Goldgur Y., Mosyak L., Reshetnikova L., Ankilova V., Lavrik O.,
     Khodyreva S., Safro M.
     "The crystal structure of phenylalanyl-tRNA synthetase from thermus
     thermophilus complexed with cognate tRNAPhe."
     Structure 5:59-68(1997).
     PubMed=9016717
[ 3] 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
[ 4] 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
[ 5] Klipcan L., Levin I., Kessler N., Moor N., Finarov I., Safro M.
     "The tRNA-induced conformational activation of human mitochondrial
     phenylalanyl-tRNA synthetase."
     Structure 16:1095-1104(2008).
     PubMed=18611382; DOI=10.1016/j.str.2008.03.020

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{END}