HMM Summary Page: TIGR02250
Accession | TIGR02250 |
Name | FCP1_euk |
Function | FCP1-like phosphatase, phosphatase domain |
Trusted Cutoff | 135.25 |
Domain Trusted Cutoff | 135.25 |
Noise Cutoff | 102.30 |
Domain Noise Cutoff | 102.30 |
Isology Type | subfamily_domain |
EC Number | 3.1.3.16 |
HMM Length | 156 |
Author | Selengut J |
Entry Date | Jul 30 2004 3:16PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This 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. |
References | RN [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 |