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A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases
Author(s) -
Makarova Kira S.,
Aravind L.,
Koonin Eugene V.
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.8.1714
Subject(s) - catalytic triad , protein superfamily , biology , proteases , archaea , biochemistry , conserved sequence , peptide sequence , protease , superfamily , caenorhabditis elegans , sequence alignment , cysteine , genetics , bacteria , enzyme , gene
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'.Onthe basis of the experimentally demonstrated activity of the Methano‐bacterium 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.