The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
about
Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3'-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damageChronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamicsWhat the structure of a calcium pump tells us about its mechanismGenome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomicsBeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphataseStructure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilumEvolution of sucrose synthesisCrystal structures of the novel cytosolic 5'-nucleotidase IIIB explain its preference for m7GMPMolecular basis for the local conformational rearrangement of human phosphoserine phosphataseThe thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activityUncoupling of 3'-phosphatase and 5'-kinase functions in budding yeast. Characterization of Saccharomyces cerevisiae DNA 3'-phosphatase (TPP1).The Saccharomyces cerevisiae PHM8 gene encodes a soluble magnesium-dependent lysophosphatidic acid phosphatase.Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPasesMutations in PMM2 that cause congenital disorders of glycosylation, type Ia (CDG-Ia)Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathwayAn FMN hydrolase is fused to a riboflavin kinase homolog in plantsLEPS2, a phosphorus starvation-induced novel acid phosphatase from tomatoStructural Studies of Medicago truncatula Histidinol Phosphate Phosphatase from Inositol Monophosphatase Superfamily Reveal Details of Penultimate Step of Histidine Biosynthesis in PlantsMutagenic analysis of functional residues in putative substrate-binding site and acidic domains of vacuolar H+-pyrophosphatase.Bovine cytosolic 5'-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate.Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes.'Conserved hypothetical' proteins: prioritization of targets for experimental studyDifferential expression of the LePS2 phosphatase gene family in response to phosphate availability, pathogen infection and during development.Precise amounts of a novel member of a phosphotransferase superfamily are essential for growth and normal morphology in Caulobacter crescentus.Purification, cloning, and expression of an apyrase from the bed bug Cimex lectularius. A new type of nucleotide-binding enzyme.Schizosaccharomyces pombe carboxyl-terminal domain (CTD) phosphatase Fcp1: distributive mechanism, minimal CTD substrate, and active site mapping.Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packagingTracing the origin of functional and conserved domains in the human proteome: implications for protein evolution at the modular level.Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants.Cloning and characterization of an atypical Type IV P-type ATPase that binds to the RING motif of RUSH transcription factors.The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell.Investigation of two evolutionarily unrelated halocarboxylic acid dehalogenase gene familiesCalcium transport across the sarcoplasmic reticulum: structure and function of Ca2+-ATPase and the ryanodine receptor.High residual activity of PMM2 in patients' fibroblasts: possible pitfall in the diagnosis of CDG-Ia (phosphomannomutase deficiency).Modeling a dehalogenase fold into the 8-A density map for Ca(2+)-ATPase defines a new domain structureEscherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase.Probing the mechanism of enzymatic phosphoryl transfer with a chemical trick.Roles of conserved P domain residues and Mg2+ in ATP binding in the ground and Ca2+-activated states of sarcoplasmic reticulum Ca2+-ATPase.Purification, crystallization and preliminary crystallographic analysis of SMU.1108c protein from Streptococcus mutans.Farnesyl phosphatase, a Corpora allata enzyme involved in juvenile hormone biosynthesis in Aedes aegypti.
P2860
Q22003729-87BEEEE6-61D3-4906-B9DC-28D3EB051357Q24319757-A1901108-4766-412D-B49D-9975B8446C92Q24532804-5160FD81-DB8B-4EA9-BFF1-EC8F223D6900Q24548476-C6DA8496-0432-4472-8E2D-2ADBB7E3482BQ24630619-898946F1-7BC1-4CD6-AECD-50B41DAE158EQ24656225-7EBFE919-F207-4D4F-8E8F-122CA3DCB62FQ24678087-A6897F89-1CAF-4A32-992E-AEC48EAD7122Q27316931-5CF2D4D8-7FBC-4E6D-B8DB-1D0BD9C45A45Q27639589-3520C084-D3CE-4D61-ADA4-95DEB98779D8Q27642875-9129DF8F-F358-46C7-931E-2C85D04DCAB8Q27929780-0455DAB4-3C46-44CE-893E-8B61760230A7Q27930790-C4CCEE53-41A7-4AEA-9B57-345EC686D916Q28138155-AB648FCA-A3F7-41B9-A1C0-CAC3F801E4A9Q28142744-DA539CF8-21F3-47DE-8BF5-61A621B5FBA8Q28263057-5895ECFF-A3DD-4584-A0DC-0F00E196E7D0Q28273904-54270237-8496-4E8C-9849-706BFAE3CB6EQ28346656-8923B7AB-7669-419C-8030-8EF4638EB601Q30385824-E53EB590-EF1C-4D42-93C0-B7AFB090080FQ30632669-54F6A1A9-5803-4369-AD3A-F478777D1C4CQ30685039-7638A379-9DA9-4944-B458-7F6CFAD5E9F2Q30779887-E0DD5F2A-8660-4FE3-B377-AE7C81C31A6AQ31120471-E7D2033F-8E25-4503-8E83-92BA5A4DF82DQ31138896-DB1F3665-1851-4CCD-8E6C-E18F0E184076Q31906979-428E28C8-C260-441D-AE16-9D7A4C4D2208Q31980341-7D1DBDB7-D1A0-460C-A11A-346835E613B6Q33196328-CB509C1D-7D6F-40E0-BB9D-F83748C427FDQ33207648-DBA87DDD-7829-46A6-887E-A77878ADD2CBQ33262935-3080F4D0-D670-4DEC-A431-B6C439D3F67DQ33922911-D422A435-89AB-4E0E-933F-65CDBF7DE220Q33923784-506B745B-4904-4B34-9D80-0981220C093CQ33987596-0C0F1C1C-3700-4584-AF1F-046CF6D841FAQ33991789-0A51B7F6-D11E-4C51-A3A4-ED5BD969A07AQ34010108-366F9836-03D5-47AC-999B-28E03BE2BDA9Q34044174-EFCD4111-1EDE-443B-B6CE-164976E53A9BQ34172763-26BDFC36-E65F-4CA4-A463-ABA52B72CB25Q34183951-F194CB45-8100-449F-96DF-7AAD7068EA7EQ34311616-2CB9116F-8359-44AA-907A-CE7B79EBD5CAQ34319472-738409C8-715B-44BF-8402-22B8541C69F5Q34821868-DACFC5F9-758A-47A8-803C-51CD315A985EQ34938188-9C647DC0-6C19-4511-A70A-C81DE079DD44
P2860
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
description
1998 nî lūn-bûn
@nan
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
@ast
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
@en
type
label
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
@ast
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
@en
prefLabel
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
@ast
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
@en
P1476
The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold.
@en
P2093
P304
P356
10.1016/S0968-0004(98)01189-X
P577
1998-04-01T00:00:00Z