A8FTT1
Gene name |
mnmC |
Protein name |
tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC |
Names |
tRNA mnm(5)s(2)U biosynthesis bifunctional protein |
Species |
Shewanella sediminis (strain HAW-EB3) |
KEGG Pathway |
sse:Ssed_1643 |
EC number |
2.1.1.61: 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 A8FTT1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A8FTT1-F1 | Predicted | AlphaFoldDB |
No variants for A8FTT1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A8FTT1 | |||||
No associated diseases with A8FTT1
5 regional properties for A8FTT1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | MnmG-related, conserved site | 273 - 287 | IPR020595-1 |
| conserved_site | MnmG-related, conserved site | 368 - 391 | IPR020595-2 |
| domain | tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG, C-terminal | 402 - 616 | IPR026904 |
| domain | MnmG, N-terminal domain | 8 - 398 | IPR040131 |
| domain | tRNA uridine 5-carboxymethylaminomethyl modification enzyme, C-terminal subdomain | 546 - 617 | IPR047001 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.1.61 | 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 |
|---|---|
| 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. |
| oxidoreductase activity, acting on the CH-NH group of donors | Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. |
| tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity | Catalysis of the reaction: S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tRNA wobble base modification | The process in which the nucleotide at position 34 in the anticodon of a tRNA is post-transcriptionally modified. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPNMRHRVNS | LTEEHEENMQ | MSKLTGHLSS | ISTLFPVKND | ASQTLTLGQL | GLGCPCQLVS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LWHYLRKNSP | SRAVNIKIFE | SQFDALADFN | LKLASLTSPD | PRLPRDDEQS | TMVEALLRAD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IVAIEGCQRL | IFDDGRVILD | IYLGDTLSQL | KCILPTSVKG | DMTDNSALIA | HWNITEKVKA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GSLDQAMLWQ | IAKLSRDNAA | LSFTDPESKE | TRQMMALARS | VGLRTLETTV | SETTVPETQQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QTENKNLDTA | SDAIPLQERR | ALRHAQSDKF | QYCPVSAANE | GDEDCDGEIA | IIGGGVASTH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LALSLAQRNK | KVRIFCSDAN | FAQQASGNKQ | GAVYPLLTPD | NGHLSHYFQQ | GYLFTRRRLQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ALVDDKFAVS | YDFCGVLQTG | FDDRSSARLD | KIINGQSWNE | KMAYPIDAAS | ATQIAGIDID |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KAGIYYPLGG | WICPHEFTRA | AFDKAARLSD | VSVEFNADIT | RIEQREGLWY | LYKSVNVQHS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| CTDSHTPDDS | EELEIGPFAN | LVLANGQGLT | QFKQSEKLPA | TGFRGQVSHI | PSRNALTKLS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TVLCSHGYLT | PGNNNFHCTG | ASYVKNPTNL | DYCATEQVEN | LHKIRHSYVD | KPWTEDVDIT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GHSARVGVRM | VTRDHAPMMG | CAPDTDSMLA | QYEQHQHTKE | SIKFWKETPA | PTHKGLFILG |
| 670 | 680 | 690 | 700 | 710 | |
| GLGSRGLTSG | PLAAEALAAQ | LCGEVIPLSM | PMLEMLNPNR | FWMRKLIKGK | AL |