Q5LLM0
Gene name |
miaB |
Protein name |
tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase |
Names |
(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB, tRNA-i(6)A37 methylthiotransferase |
Species |
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) |
KEGG Pathway |
sil:SPOA0002 |
EC number |
2.8.4.3: Transferring alkylthio groups |
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 Q5LLM0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5LLM0-F1 | Predicted | AlphaFoldDB |
No variants for Q5LLM0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5LLM0 | |||||
No associated diseases with Q5LLM0
5 regional properties for Q5LLM0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TRAM domain | 378 - 439 | IPR002792 |
| domain | Elp3/MiaA/NifB-like, radical SAM core domain | 149 - 367 | IPR006638 |
| domain | Radical SAM | 145 - 378 | IPR007197 |
| domain | Methylthiotransferase, N-terminal | 5 - 121 | IPR013848 |
| conserved_site | Methylthiotransferase, conserved site | 153 - 173 | IPR020612 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.8.4.3 | Transferring alkylthio groups |
| 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 |
|---|---|
| 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. |
| methylthiotransferase activity | Catalysis of the addition of a methylthioether group (-SCH3) to a nucleic acid or protein acceptor. |
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 |
| MSDPKKLFIK | TYGCQMNVYD | SERMAEALGG | QGYVETQSAE | DADMILLNTC | HIREKAAEKV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YSELGRFKGL | KAAKPDLKIG | VAGCVAQAEG | EEIMRRQPLV | DLVVGPQSYH | RLPELEAKTR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AGEKALDTDF | PEEDKFEKLK | GRPKAKRGPT | AFLTVQEGCD | KFCAFCVVPY | TRGAEVSRPA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DRILREANEL | VERGVREITL | LGQNVNAYHG | AGPNGDMTLA | GLIWELDKID | GLERIRFTTS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HPNDMADDLI | EAHGTCAKLM | PYLHLPVQAG | SDKILKRMNR | SHTAESYLRL | IERIRAARPD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IVMSGDFIVG | FPEETEADFQ | DTLDLVEQVR | YGYAYSFKYS | TRPGTPAAER | AQVDPAEADD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RLQRLQAVIT | RHQREIQDGM | VGREVSVLFE | KPGRQPGQMV | GKSEYLHAVH | VQDPGLEAGQ |
| 430 | |||||
| IARVRIVASG | ANSLAGELA |