HMM Summary Page: TIGR02250

FunctionFCP1-like phosphatase, phosphatase domain
Trusted Cutoff135.25
Domain Trusted Cutoff135.25
Noise Cutoff102.30
Domain Noise Cutoff102.30
Isology Typesubfamily_domain
EC Number3.1.3.16
HMM Length156
AuthorSelengut J
Entry DateJul 30 2004 3:16PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model represents the phosphatase domain of the human RNA polymerase II subunit A C-terminal domain phosphatase (FCP1, [1]) and closely related phosphatases from eukaryotes including plants, fungi [2] and slime mold. 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 (hhhhDDppphW). 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 the human NLI interacting factor-like phosphatases, and together both are detected by the Pfam model PF03031.
ReferencesRN [1] RL Biochemistry. 2004 Jun 8;43(22):7111-20. RT An encephalitozoon cuniculi ortholog of the RNA polymerase II carboxyl-terminal domain (CTD) serine phosphatase Fcp1. RA Hausmann S, Schwer B, Shuman S. RM PMID: 15170348 RN [2] RL J Biol Chem. 2004 Mar 19;279(12):10892-900. Epub 2003 Dec 29. RT Schizosaccharomyces pombe carboxyl-terminal domain (CTD) phosphatase Fcp1: distributive mechanism, minimal CTD substrate, and active site mapping. RA Hausmann S, Erdjument-Bromage H, Shuman S. RM PMID: 14701811 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