HMM Summary Page: TIGR02251

Functiondullard-like phosphatase domain
Trusted Cutoff139.15
Domain Trusted Cutoff139.15
Noise Cutoff101.65
Domain Noise Cutoff101.65
Isology Typesubfamily_domain
HMM Length168
AuthorSelengut J
Entry DateJul 30 2004 4:42PM
Last ModifiedMar 1 2011 11:50AM
CommentThis model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard" [1], and the NLI interacting factor (NIF)-like phosphatases [2]. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs [3] and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3 [4]. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the Pfam model PF03031.
ReferencesRN [1] RL Biochem Biophys Res Commun. 2002 Jul 5;295(1):85-91. RT Molecular cloning and characterization of dullard: a novel gene required for neural development. RA Satow R, Chan TC, Asashima M. RM PMID: 12083771 RN [2] RL Proc Natl Acad Sci U S A. 2004 Apr 6;101(14):4906-11. Epub 2004 Mar 29. RT RBSP3 (HYA22) is a tumor suppressor gene implicated in major epithelial malignancies. RA Kashuba VI, Li J, Wang F, Senchenko VN, Protopopov A, Malyukova A, Kutsenko AS, Kadyrova E, Zabarovska VI, Muravenko OV, Zelenin AV, Kisselev LL, Kuzmin I, Minna JD, Winberg G, Ernberg I, Braga E, Lerman MI, Klein G, Zabarovsky ER. RM PMID: 15051889 RN [3] 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 [4] 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