VapC-like PIN domain of Mycobacterium tuberculosis VapC4, VapC5, and related proteins
This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 toxin of the VapBC toxin/antitoxin (TA) system. This family belongs to the PIN_VapC4-5_FitB-like subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. M. tuberculosis VapC4 interacts with, and cleaves tRNA44Cys-GCA. M. tuberculosis VapC5 has endonucleolytic activity with RNA, this activity is low with dsRNA, and no activity has been demonstrated on dsDNA. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.
Comment:based on homology with related nucleases with structure including VapC toxin from Shigella flexneri 2a virulence plasmid pMYSH6000 and on experimental evidence
Comment:The PIN domain superfamily contains three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues.
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