{PDOC50886}
{PS50886; TRBD}
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* tRNA-binding domain profile *
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The tRNA-binding  domain  (TRBD)  [1] is a domain of ~110 amino acids which is
widespread among  all  living  organisms, from eubacteria, archaea or eukarya.
The TRBD  domain,  which  is  also  called Trbp111-like domain or EMAP II-like
domain, is  widely  distributed  among  different  tRNA  synthetases and their
association factors  (such  as  p43,  ARC1,  and Trbp111 isolated from various
species). The  TRBD  domain  has  been shown to possess a general tRNA-binding
capacity with recognition of the L shape of tRNA and it has been proposed that
the TRBD  domain  might  be a non-specific binder of tRNAs acting in cis or in
trans to   enhance  the  catalytic  efficiency  or  substrate  specificity  of
aminoacyl-tRNA synthetases [1,2,3,4].

The resolution  of  the structure of the TRBD domain has shown that part of it
adopts the oligonucleotide/oligosaccharide-binding (OB)-fold (see <PDB:1FL0>).
The OB-fold  of  the  TRBD  domain consists of a five-stranded Greek-key beta-
barrel capped  by  a  short  alpha-helix  located between the third and fourth
strands [3,4,5,6].

Some proteins known to contain a TRBD domain are listed below:

 - Mammalian endothelial-monocyte activating polypeptide II (EMAP-II). EMAP-II
   is an  inflammatory  cytokine  produced  after  apoptotic  cleavage  of the
   multisynthetase complex auxiliary component p43.
 - Yeast  GU4  nucleic-binding protein 1 or ARC1 protein. It binds to tRNA and
   functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.
 - Bacterial  proteins  of the Trb11/CsaA family, which consist only of a TRBD
   domain.

The profile we developed covers the entire TRBD domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2002 / First entry.

[ 1] Kaminska M., Deniziak M., Kerjan P., Barciszewski J., Mirande M.
     "A recurrent general RNA binding domain appended to plant
     methionyl-tRNA synthetase acts as a cis-acting cofactor for
     aminoacylation."
     EMBO J. 19:6908-6917(2000).
     PubMed=11118226; DOI=10.1093/emboj/19.24.6908
[ 2] Galani K., Grosshans H., Deinert K., Hurt E.C., Simos G.
     "The intracellular location of two aminoacyl-tRNA synthetases depends
     on complex formation with Arc1p."
     EMBO J. 20:6889-6898(2001).
     PubMed=11726524; DOI=10.1093/emboj/20.23.6889
[ 3] Kim Y., Shin J., Li R., Cheong C., Kim K., Kim S.
     "A novel anti-tumor cytokine contains an RNA binding motif present in
     aminoacyl-tRNA synthetases."
     J. Biol. Chem. 275:27062-27068(2000).
     PubMed=10852899; DOI=10.1074/jbc.C000216200
[ 4] Crepin T., Schmitt E., Blanquet S., Mechulam Y.
     "Structure and function of the C-terminal domain of methionyl-tRNA
     synthetase."
     Biochemistry 41:13003-13011(2002).
     PubMed=12390027; DOI=10.1021/bi026343m
[ 5] Renault L., Kerjan P., Pasqualato S., Menetrey J., Robinson J.-C.,
     Kawaguchi S., Vassylyev D.G., Yokoyama S., Mirande M., Cherfils J.
     "Structure of the EMAPII domain of human aminoacyl-tRNA synthetase
     complex reveals evolutionary dimer mimicry."
     EMBO J. 20:570-578(2001).
     PubMed=11157763; DOI=10.1093/emboj/20.3.570
[ 6] Kawaguchi S., Mueller J., Linde D., Kuramitsu S., Shibata T., Inoue Y.,
     Vassylyev D.G., Yokoyama S.
     "The crystal structure of the ttCsaA protein: an export-related
     chaperone from Thermus thermophilus."
     EMBO J. 20:562-569(2001).
     PubMed=11157762; DOI=10.1093/emboj/20.3.562

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