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A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases

Published online by Cambridge University Press:  01 August 1999

KIRA S. MAKAROVA
Affiliation:
Department of Pathology, F.E. Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814-4799 National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894 Permanent address: Institute of Cytology and Genetics, Russian Academy of Sciences, Novosibirsk 630090, Russia.
L. ARAVIND
Affiliation:
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894 Department of Biology, Texas A&M University, College Station, Texas 77843
EUGENE V. KOONIN
Affiliation:
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894
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Abstract

Computer analysis using profiles generated by the PSI-BLAST program identified a superfamily of proteins homologous to eukaryotic transglutaminases. The members of the new protein superfamily are found in all archaea, show a sporadic distribution among bacteria, and were detected also in eukaryotes, such as two yeast species and the nematode Caenorhabditis elegans. Sequence conservation in this superfamily primarily involves three motifs that center around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa′. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.

Type
FOR THE RECORD
Copyright
© 1999 The Protein Society

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