| pubmed-article:8819174 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8819174 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:8819174 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
| pubmed-article:8819174 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:8819174 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:8819174 | lifeskim:mentions | umls-concept:C0247248 | lld:lifeskim |
| pubmed-article:8819174 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:8819174 | pubmed:dateCreated | 1997-4-10 | lld:pubmed |
| pubmed-article:8819174 | pubmed:abstractText | A thorough sequence analysis of the various members of the eukaryotic protein serine/threonine phosphatase 2C (PP2C) family revealed the conservation of 11 motifs. These motifs could be identified in numerous other sequences, including fungal adenylate cyclases that are predicted to contain a functionally active PP2C domain, and a family of prokaryotic serine/threonine phosphatases including SpoIIE. Phylogenetic analysis of all the proteins indicates a widespread sequence family for which a considerable number of isoenzymes can be inferred. | lld:pubmed |
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| pubmed-article:8819174 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8819174 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8819174 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8819174 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8819174 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:8819174 | pubmed:author | pubmed-author:SchultzJJ | lld:pubmed |
| pubmed-article:8819174 | pubmed:author | pubmed-author:BorgTT | lld:pubmed |
| pubmed-article:8819174 | pubmed:author | pubmed-author:BrownN PNP | lld:pubmed |
| pubmed-article:8819174 | pubmed:author | pubmed-author:HegyiHH | lld:pubmed |
| pubmed-article:8819174 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8819174 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:8819174 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8819174 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8819174 | pubmed:pagination | 1421-5 | lld:pubmed |
| pubmed-article:8819174 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8819174 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8819174 | pubmed:articleTitle | The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues. | lld:pubmed |
| pubmed-article:8819174 | pubmed:affiliation | European Molecular Biology Laboratory, Heidelberg, Germany. bork@embl-heidelberg.de | lld:pubmed |
| pubmed-article:8819174 | pubmed:publicationType | Journal Article | lld:pubmed |
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