HMM Summary Page: TIGR02252

FunctionHAD hydrolase, REG-2-like, family IA
Trusted Cutoff155.20
Domain Trusted Cutoff155.20
Noise Cutoff120.15
Domain Noise Cutoff120.15
Isology Typesubfamily
HMM Length203
AuthorSelengut J
Entry DateAug 2 2004 9:53AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene [1]. This family is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs [2]. The subfamilies are defined [3] based on the location and the observed or predicted fold of a so-called 'capping domain' [4], or the absence of such a domain. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes.
ReferencesRN [1] RL Curr Biol. 1995 Dec 1;5(12):1424-36. RT Extent and character of circadian gene expression in Drosophila melanogaster: identification of twenty oscillating mRNAs in the fly head. RA Van Gelder RN, Bae H, Palazzolo MJ, Krasnow MA. RM PMID: 8749395 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 RN [2] RM PMID: 11601995 RT MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases. RA Selengut, JD RL Biochemistry 2001 Oct 23;40(42):12704-11 RN [3] RM PMID: 10956028 RT The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification wi thin the HAD enzyme superfamily. RA Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN. RL Biochemistry 2000 Aug 29;39(34):10385-96