VapC-like PIN domain of the Pyrobaculum aerophilum Pae0151 and Pae2754 proteins and homologs; Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of the Pyrobaculum aerophilum proteins, Pae0151 and Pae2754, and homologs are included in this subfamily. They are similar to the PIN domains of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607689  13 VVDASAMVDLLARTSDRCSAVRA-RLARTAMHAPAHFDAEVLSALGRMQRAGALTVAYVDAALEELRQVPVTRHGLSSLL 91
Cdd:cd09873   1 VVDASVAVKWLLPEEESEAADRLlERLEEELVAPDLWLYEVANVLRKAVRRGRLTEEEAEEALEDLLDLPIEIDPDPELL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15607689  92 AGAWSRRDTLRLT--DALYVELAETAGLVLLTTDERLARA 129
Cdd:cd09873  81 EEALELARRHGLTayDAAYLALAERLGAPLVTADRKLARA 120

VapC-like PIN domain of the Pyrobaculum aerophilum Pae0151 and Pae2754 proteins and homologs; Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of the Pyrobaculum aerophilum proteins, Pae0151 and Pae2754, and homologs are included in this subfamily. They are similar to the PIN domains of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607689  13 VVDASAMVDLLARTSDRCSAVRA-RLARTAMHAPAHFDAEVLSALGRMQRAGALTVAYVDAALEELRQVPVTRHGLSSLL 91
Cdd:cd09873   1 VVDASVAVKWLLPEEESEAADRLlERLEEELVAPDLWLYEVANVLRKAVRRGRLTEEEAEEALEDLLDLPIEIDPDPELL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15607689  92 AGAWSRRDTLRLT--DALYVELAETAGLVLLTTDERLARA 129
Cdd:cd09873  81 EEALELARRHGLTayDAAYLALAERLGAPLVTADRKLARA 120

VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 and other uncharacterized, annotated PilT protein domain proteins; Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis CDC1551, hypothetical protein MT3492, and similar bacterial and archaeal proteins are included in this subfamily. They are PIN domain homologs of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607689  50 AEVLSALGRMQRAGALTVAYVDAALEELRQ--------VPVTRHGLSslLAGAWSRRDTLRLTDALYVELAETAG-LVLL 120
Cdd:cd09874  40 VEFASALARKVREGELSEEQARAALAAFERdwasllrvVPVTDSLFR--RAAELAERHGLRALDALHLASALRLGaLTFV 117

                        90
                ....*....|
gi 15607689 121 TTDERLARAW 130
Cdd:cd09874 118 TADKRLAEAA 127