Protein alignments between regions of the
translated peptide from ATHCOR1 with two conserved domains (A and B)
found in different hydrolases. SHAF, Similar to human-activating factor
acetylhydrolase from C. elegans, U64598; PAF,
platelet-activating factor acetylhydrolase from Cavia
porcellus, JC5021; HDH, haloacetate dehalogenase from
Moraxella sp., A44856; Mtu, unknown Mycobacterium
tuberculosis Z95389; AtsEH, Arabidopsis epoxide hydrolase,
D16628; GlyEH, soybean epoxide hydrolase, D63781; and DLH, dienelactone
hydrolase from Synechocystis sp. dienelactone hydrolase,
D90904. Black boxes indicate conserved amino acids at the minimum of
50%. Gray boxes indicate changes by similar residues. The percentage
of similarity between ATHCOR1 and each of the sequences is presented.
The consensus for the putative ATP-/GTP-binding site described in the
literature (Saraste et al., 1990) is indicated by an asterisk.
Sequences were aligned by the CLUSTAL W program (Thompson et al., 1994)
and shaded by the BOXSHADE program (used at the Bioinformatics Group
WWW site at the Swiss Institute for Experimental Cancer Research,
Lousanne, Switzerland).