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9CAUD:A0A076GD02
Contents
Species (Taxon ID) | Sinorhizobium phage phiLM21. (1524882) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | Methyltransferase (ECO:0000313 with EMBL:AII27779.1) | |
External Links | ||
UniProt | A0A076GD02 | |
EMBL | KJ743987 | |
RefSeq | YP_009221498.1 | |
GeneID | 26737522 | |
KEGG | vg:26737522 | |
Proteomes | UP000028671 | |
GO | GO:0008168 | |
InterPro | IPR029063 | |
SUPFAM | SSF53335 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0009007 |
site-specific DNA-methyltransferase (adenine-specific) activity |
ECO:0000314 |
F |
A sequence comparison with two other phages, Rhizobium gallicum (92% identity) and Sinorhizobium medicae (79% identity), showed that ORF27 encodes an N-6 DNA methyltransferase. To prove the ORF27 gene product is a methyltransferase, researchers used ORF27 to methylate phage lambda DNA and assessed whether it could be digested by restriction enzymes (Figure 4). A radioactive methylation assay then showed that the DNA methyltransferase did not methylate other substrates. These findings are consistent with results found from other DNA methyltransferase experiments (Table 3). |
complete | |||||
enables |
GO:0016740 |
transferase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008168 |
methyltransferase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0032259 |
methylation |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Dziewit, L et al. (2014) Molecular characterization of a novel temperate sinorhizobium bacteriophage, ФLM21, encoding DNA methyltransferase with CcrM-like specificity. J. Virol. 88 13111-24 PubMed GONUTS page