hypothetical protein [Klebsiella pneumoniae]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| OLD-like_TOPRIM super family | cl13052 | Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the ... |
36-105 | 3.09e-04 | ||
Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain. The nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. The TOPRIM domain has two conserved motifs, one of which centres at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The actual alignment was detected with superfamily member pfam20469: Pssm-ID: 472409 Cd Length: 67 Bit Score: 38.14 E-value: 3.09e-04
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| OLD-like_TOPRIM | pfam20469 | Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the ... |
36-105 | 3.09e-04 | ||
Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain. The nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. The TOPRIM domain has two conserved motifs, one of which centres at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. Pssm-ID: 466618 Cd Length: 67 Bit Score: 38.14 E-value: 3.09e-04
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| OLD-like_TOPRIM | pfam20469 | Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the ... |
36-105 | 3.09e-04 | ||
Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain. The nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. The TOPRIM domain has two conserved motifs, one of which centres at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. Pssm-ID: 466618 Cd Length: 67 Bit Score: 38.14 E-value: 3.09e-04
|
||||||
| Blast search parameters | ||||
|
