B1M5H7
Gene name |
trmFO |
Protein name |
Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO |
Names |
Folate-dependent tRNA (uracil-5-)-methyltransferase, Folate-dependent tRNA(M-5-U54)-methyltransferase |
Species |
Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1) |
KEGG Pathway |
mrd:Mrad2831_1573 |
EC number |
2.1.1.74: 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 B1M5H7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1M5H7-F1 | Predicted | AlphaFoldDB |
No variants for B1M5H7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1M5H7 | |||||
No associated diseases with B1M5H7
1 regional properties for B1M5H7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | tRNA methyltransferase TRMD/TRM10-type domain | 22 - 215 | IPR016009 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.1.74 | 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity | Catalysis of the transfer of a methyl group from 5,10-methylenetetrahydrofolate to the C5 atom of the uridine residue at position 54 in a tRNA molecule. This occurs in most Gram-positive bacteria and some Gram-negative bacteria. |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity | Catalysis of the reaction: 5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH + H+ = tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD+. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTQIIHIVGG | GLAGSEAAWQ | VAEAGHRAVI | HEMRPVRGTE | AHRTDGLAEL | VCSNSFRSDD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PEGNAVGLLH | QEMRSLGSLI | MRAADTNQVP | AGGALAVDRE | GFSAAVTRAL | EQHPNVTLVR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GEVEGLPPEA | WGPCIVATGP | LTAPALAEGI | RGLTGAESLA | FFDAIAPIVH | RDSIDMDVAW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FQSRYDKPGP | GGTGADYLNC | PMSREQYDTF | VAALVAGEKI | GFKQWEGTPY | FDGCLPVEVM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AERGPETLRH | GPMKPVGLTN | PRDPLVKPCA | IVQLRQDNAL | GTLYNMVGFQ | TKLTYSEQVR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IFRMIPGLER | AEFARLGGLH | RNTYLDSPRL | LDATLRLRAR | PSLRFAGQIT | GCEGYVESAA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VGLMAGRFAV | AEAAGRPLAP | LPQSTALGAL | IAHITGGHLM | ADGEANAPRS | FQPMNVNFGL |
| 430 | 440 | 450 | 460 | 470 | |
| FPPLERAPRN | ETGRRLRGPE | KAALKKRALT | DRARADLALW | LEGARDGAAR | PAAAE |