Q166E3
Gene name |
mnmA |
Protein name |
tRNA-specific 2-thiouridylase MnmA |
Names |
|
Species |
Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) |
KEGG Pathway |
rde:RD1_2599 |
EC number |
2.8.1.13: Sulfurtransferases |
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 Q166E3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q166E3-F1 | Predicted | AlphaFoldDB |
No variants for Q166E3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q166E3 | |||||
No associated diseases with Q166E3
2 regional properties for Q166E3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Membrane transport protein MMPL domain | 54 - 382 | IPR004869-1 |
| domain | Membrane transport protein MMPL domain | 602 - 937 | IPR004869-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.8.1.13 | Sulfurtransferases |
| 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 |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| sulfurtransferase activity | Catalysis of the transfer of sulfur atoms from one compound (donor) to another (acceptor). |
| tRNA binding | Binding to a transfer RNA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tRNA modification | The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPLDPSPTLN | SLGFAKPPAE | TRVVVAMSGG | VDSSVVAAML | AEEGYDVVGV | TLQLYDHGAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAKKGACCAG | LDIHDARRVS | EKMGFPHYVL | DYENIFKDAV | IDEFAESYLG | GATPVPCIRC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NERVKFKDLL | ETAKDLDADC | MATGHYIQRK | SGPYGAELHS | AADANRDQSY | FLFSTTPEQL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AFLRFPLGHL | PSKEDTRALA | EKYGLSVANK | PDSQDICFVP | DGDYASVIRK | LRPEAAAPGD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IVDTDGRVLA | RHDGVVNYTI | GQRRGLGIGG | LATPLYVIKL | DAEARQVVVG | PKSMLSTRTV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PVREINWLGD | EPFQSRDAWH | LAVKVRSTRP | PTDAIIRPIS | DTEATVELTS | PEEGISPGQA |
| 370 | |||||
| CVFYDTDSSR | IYGGGWIHKG |