Thaller, M C <br/><br/>
Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily.  [electronic resource] 

 -  Protein science : a publication of the Protein Society  Jul 1998 
 - 1647-52 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0961-8368 
<br/><br/><label>Standard No.: </label>10.1002/pro.5560070722  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acid Phosphatase--chemistry<br/>Amino Acid Sequence<br/>Archaea--enzymology<br/>Aspartic Acid--analysis<br/>Bacteria--enzymology<br/>Conserved Sequence<br/>Databases, Factual<br/>Molecular Sequence Data<br/>Multigene Family<br/>Phosphoric Monoester Hydrolases--chemistry<br/>Plants--enzymology<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid