PIN domain-containing protein [Treponema denticola]
PIN domain-containing protein( domain architecture ID 10604431)
PIN (PilT N terminus) domain-containing protein may function as a nuclease
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PIN_3 | pfam13470 | PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ... |
3-116 | 3.82e-14 | |||
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases). : Pssm-ID: 463888 Cd Length: 115 Bit Score: 63.90 E-value: 3.82e-14
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Name | Accession | Description | Interval | E-value | |||
PIN_3 | pfam13470 | PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ... |
3-116 | 3.82e-14 | |||
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases). Pssm-ID: 463888 Cd Length: 115 Bit Score: 63.90 E-value: 3.82e-14
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VapC | COG1848 | VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN ... |
3-131 | 8.77e-13 | |||
VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN domain [Defense mechanisms]; Pssm-ID: 441453 Cd Length: 134 Bit Score: 60.77 E-value: 8.77e-13
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PIN_VapC-like | cd18684 | uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN ... |
4-99 | 5.15e-03 | |||
uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain 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. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. 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. Pssm-ID: 350251 Cd Length: 131 Bit Score: 34.90 E-value: 5.15e-03
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Name | Accession | Description | Interval | E-value | |||
PIN_3 | pfam13470 | PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ... |
3-116 | 3.82e-14 | |||
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases). Pssm-ID: 463888 Cd Length: 115 Bit Score: 63.90 E-value: 3.82e-14
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VapC | COG1848 | VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN ... |
3-131 | 8.77e-13 | |||
VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN domain [Defense mechanisms]; Pssm-ID: 441453 Cd Length: 134 Bit Score: 60.77 E-value: 8.77e-13
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PIN_VapC-like | cd18684 | uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN ... |
4-99 | 5.15e-03 | |||
uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain 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. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. 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. Pssm-ID: 350251 Cd Length: 131 Bit Score: 34.90 E-value: 5.15e-03
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PIN_MjVapC2-VapC6_like | cd18677 | VapC-like PIN domain of Methanocaldococcus jannaschii VapC2, and VapC6, and related proteins; ... |
5-122 | 6.87e-03 | |||
VapC-like PIN domain of Methanocaldococcus jannaschii VapC2, and VapC6, and related proteins; This subfamily includes Methanocaldococcus jannaschii VapC2 and VapC6. It belongs to 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. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. 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. Pssm-ID: 350244 Cd Length: 136 Bit Score: 34.48 E-value: 6.87e-03
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Blast search parameters | ||||
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