MAG: hypothetical protein A2161_13475 [Candidatus Schekmanbacteria bacterium RBG_13_48_7]
Protein Classification
nucleotidyltransferase domain-containing protein( domain architecture ID 34097)
nucleotidyltransferase domain-containing protein, similar to African swine fever virus repair DNA polymerase X
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| NT_Pol-beta-like super family | cl11966 | Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This ... |
197-269 | 2.45e-04 | ||
Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This superfamily includes the NT domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, and Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. The Escherichia coli CCA-adding enzyme belongs to this superfamily but is not included as this enzyme lacks the N-terminal helix conserved in the remainder of the superfamily. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate coordinate two divalent metal cations that are essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism for Rel-Spo enzymes. The actual alignment was detected with superfamily member smart00954: Pssm-ID: 472251 [Multi-domain] Cd Length: 111 Bit Score: 39.86 E-value: 2.45e-04
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| RelA_SpoT | smart00954 | Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ... |
197-269 | 2.45e-04 | ||
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ somewhat. RelA produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species. Pssm-ID: 214934 [Multi-domain] Cd Length: 111 Bit Score: 39.86 E-value: 2.45e-04
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| RelA_SpoT | smart00954 | Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ... |
197-269 | 2.45e-04 | ||
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ somewhat. RelA produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species. Pssm-ID: 214934 [Multi-domain] Cd Length: 111 Bit Score: 39.86 E-value: 2.45e-04
|
||||||
| Blast search parameters | ||||
|
