Q58277
Gene name |
MJ0867 |
Protein name |
Probable threonylcarbamoyladenosine tRNA methylthiotransferase |
Names |
tRNA-t(6)A37 methylthiotransferase |
Species |
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
KEGG Pathway |
mja:MJ_0867 |
EC number |
2.8.4.5: 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 Q58277
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q58277-F1 | Predicted | AlphaFoldDB |
No variants for Q58277
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q58277 | |||||
No associated diseases with Q58277
5 regional properties for Q58277
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TRAM domain | 373 - 427 | IPR002792 |
| domain | Elp3/MiaA/NifB-like, radical SAM core domain | 145 - 366 | IPR006638 |
| domain | Radical SAM | 10 - 426 | IPR007197 |
| domain | Methylthiotransferase, N-terminal | 12 - 118 | IPR013848 |
| conserved_site | Methylthiotransferase, conserved site | 149 - 169 | IPR020612 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.8.4.5 | Transferring alkylthio groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 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. |
| N6-threonylcarbomyladenosine methylthiotransferase activity | Catalysis of the methylthiolation (-SCH3 addition) at the C2 of the adenosine ring of N6-threonylcarbomyladenosine (t6A) in tRNA, to form 2-methylthio-N6-threonylcarbamoyladenosine (ms2t6A). |
| tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase | Catalysis of the reaction: N(6)-L-threonylcarbamoyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 2-methylthio-N(6)-L-threonylcarbamoyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tRNA methylthiolation | The addition of a methylthioether group (-SCH3) to a nucleotide in a tRNA molecule. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MWLYYLQVVM | DMRVYVEGYG | CVLNTADTEI | IKNSLKKHGF | EVVNNLEEAD | IAIINTCVVR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LETENRMIYR | INELKNLGKE | VVVAGCLPKA | LKNKVKGFLH | IYPREAHKAG | EILKNYVEKH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YRMPYIEEDI | NKTLYKKLDY | LKPSLITPLP | ICEGCIGNCS | YCIVKIARGG | LISYPREKIV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NKAKELINKG | AKCLLITAQD | TACYGFDIGD | NLANLLNELT | QIKGEFIMRV | GMMHAKNAEL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ILDELIEVYQ | NEKVGKFLHL | PLQSGDDEIL | KRMKRGYTVD | EFKDIVNEFR | RKIKNLCFTT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DIIVGFPGET | EEQFQNTLEV | LRELKPDYIH | GAKYSQRKGT | EAAKMKQIDT | KIRKRRSEIL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DKLRRELSYL | NNKKYIGKAM | KVLVLDEGKG | YTDNFKVVKF | EGGEVGEFRK | VKITDAKTFG |
| LKGELIL |