HMM Summary Page: TIGR02247

Functionepoxide hydrolase N-terminal domain-like phosphatase
Trusted Cutoff125.40
Domain Trusted Cutoff125.40
Noise Cutoff69.85
Domain Noise Cutoff69.85
Isology Typesubfamily_domain
HMM Length211
AuthorSelengut J
Entry DateJul 28 2004 4:54PM
Last ModifiedFeb 28 2011 3:58PM
CommentThis HMM represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear [1]. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs [2] (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA.
ReferencesRN [1] RL Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1552-7. RT The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. RA Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B, Oesch F, Arand M. RM PMID: 12574508 RN [2] RM PMID: 7966317 RT Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. RA Koonin EV, Tatusov RL. RL J Mol Biol 1994 Nov 18;244(1):125-32