C1CVX7
Gene name |
rlmN |
Protein name |
Probable dual-specificity RNA methyltransferase RlmN |
Names |
23S rRNA (adenine(2503)-C(2))-methyltransferase, 23S rRNA m2A2503 methyltransferase, Ribosomal RNA large subunit methyltransferase N, tRNA (adenine(37)-C(2))-methyltransferase, tRNA m2A37 methyltransferase |
Species |
Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115) |
KEGG Pathway |
ddr:Deide_14010 |
EC number |
2.1.1.192: Methyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for C1CVX7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C1CVX7-F1 | Predicted | AlphaFoldDB |
No variants for C1CVX7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C1CVX7 | |||||
No associated diseases with C1CVX7
1 regional properties for C1CVX7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Radical SAM | 89 - 323 | IPR007197 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.1.192 | Methyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| metal ion binding | Binding to a metal ion. |
| rRNA (adenine-C2-)-methyltransferase activity | Catalysis of the reaction: 2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + rRNA containing C2-methyladenine(2503) in 23S rRNA. |
| rRNA binding | Binding to a ribosomal RNA. |
| tRNA (adenine-C2-)-methyltransferase activity | Catalysis of the reaction: 2 S-adenosyl-L-methionine + adenine(37) in tRNA = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + C2-methyladenine(37) in a tRNA. |
| tRNA binding | Binding to a transfer RNA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| rRNA base methylation | The addition of a methyl group to an atom in the nucleoside base portion of a nucleotide residue in an rRNA molecule. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEFLLDLHPD | AYPLEGFRRR | QLLEWVFVQG | VGTFDAMTNL | PAEARAELAR | SYHLNPFREI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ETVRSADGSV | KYLFTLTDGR | QMEAVYMPYL | DRKTICVSTM | VGCPARCAFC | ATGAMGFGRN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LTPGEIVAQV | LAVAGGEGIG | PREIRNLVFM | GMGEAMLNYE | NTMQAARILL | HPQALGMSKR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RVTLSTVGIA | KGIRQLAAED | DLGIKLAISL | HAPDEDTRQR | IIPTGAANSI | AEIMAAARDY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QAVTGRRITL | EYTMLRGIND | HLWQAELLAD | VLQGLVSHVN | LIPMNPWDGS | GFESSTEDQI |
| 310 | 320 | 330 | 340 | ||
| QAFYDTLEAR | GVDVSVRRSR | GKDAGAACGQ | LALKRPGAVT | GAA |