Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6225302    1 RKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALTLIHSRTNCVNILVTTTQLIPALAK 80
Cdd:cd02601 111 RKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLTLALKALDLISSRENCVNVLVTTTQLIPALAK 190

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6225302   81 VLLYGLGVVFPIENIYSATKIGKESCFERIIQRFGRKVV 119
Cdd:cd02601 191 VLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCV 229

protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6225302    1 RKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALTLIHSRTNCVNILVTTTQLIPALAK 80
Cdd:cd02601 111 RKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLTLALKALDLISSRENCVNVLVTTTQLIPALAK 190

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6225302   81 VLLYGLGVVFPIENIYSATKIGKESCFERIIQRFGRKVV 119
Cdd:cd02601 191 VLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCV 229

protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6225302    1 RKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALTLIHSRTNCVNILVTTTQLIPALAK 80
Cdd:cd02601 111 RKLAFRYRRVKENYNTYKNNVGFLLGEAKREAWLQLRTEIEALTDQWLTLALKALDLISSRENCVNVLVTTTQLIPALAK 190

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6225302   81 VLLYGLGVVFPIENIYSATKIGKESCFERIIQRFGRKVV 119
Cdd:cd02601 191 VLLYGLGSVFPIENIYSATKIGKESCFERIQQRFGRKCV 229