{PDOC00614}
{PS00762; WHEP_TRS_1}
{PS51185; WHEP_TRS_2}
{BEGIN}
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* WHEP-TRS domain signature and profile *
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A conserved domain of 46 amino  acids has been shown [1]  to exist in a number
of higher eukaryote aminoacyl-transfer RNA synthetases. This domain is present
one to six times in the following enzymes:

 - Mammalian multifunctional aminoacyl-tRNA synthetase. The domain is  present
   three  times in  a  region  that  separates  the  N-terminal  glutamyl-tRNA
   synthetase domain from the C-terminal prolyl-tRNA synthetase domain.
 - Drosophila multifunctional aminoacyl-tRNA synthetase. The domain is present
   six times in the intercatalytic region.
 - Mammalian tryptophanyl-tRNA synthetase.  The  domain  is  found  at  the N-
   terminal extremity.
 - Mammalian, insect, nematode and plant glycyl-tRNA synthetase. The domain is
   found at the N-terminal extremity [2].
 - Mammalian histidyl-tRNA synthetase.  The domain is found  at the N-terminal
   extremity.

The  structure  of  a  human  WHEP-TRS  domain  has  been  solved  by NMR (see
<PDB:1FYJ>)  [3].  It  consists of two helices arranged in a helix-turn-helix.
This  domain  may  play  a  role  in  the association of tRNA-synthetases into
multienzyme complexes [4].

We  developed a signature pattern based on the first 29 positions of the WHEP-
domain. We also developed a profile that covers the whole WHEP-TRS domain.

-Consensus pattern: [QYR]-[GH]-[DNEAR]-x-[LIV]-[KR]-x(2)-K-x(2)-[KRNG]-[AS]-
                    x(4)-[LIV]-[DENKA]-x(2)-[IV]-x(2)-L-x(3)-K
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for hamster histidyl-tRNA synthetase whose sequence  may be incorrect in that
 region.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2006 / Pattern revised.

[ 1] Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.
     "A component of the multisynthetase complex is a multifunctional
     aminoacyl-tRNA synthetase."
     EMBO J. 10:4267-4277(1991).
     PubMed=1756734
[ 2] Nada S., Chang P.K., Dignam J.D.
     "Primary structure of the gene for glycyl-tRNA synthetase from Bombyx
     mori."
     J. Biol. Chem. 268:7660-7667(1993).
     PubMed=8463296
[ 3] Jeong E.J., Hwang G.S., Kim K.H., Kim M.J., Kim S., Kim K.S.
     "Structural analysis of multifunctional peptide motifs in human
     bifunctional tRNA synthetase: identification of RNA-binding residues
     and functional implications for tandem repeats."
     Biochemistry 39:15775-15782(2000).
     PubMed=11123902; DOI=10.1021/bi001393h
[ 4] Rho S.B., Lee J.S., Jeong E.J., Kim K.S., Kim Y.G., Kim S.
     "A multifunctional repeated motif is present in human bifunctional
     tRNA synthetase."
     J. Biol. Chem. 273:11267-11273(1998).
     PubMed=9556618

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