Q6NS26
Gene name |
cdkal1 |
Protein name |
Threonylcarbamoyladenosine tRNA methylthiotransferase |
Names |
CDK5 regulatory subunit-associated protein 1-like 1, tRNA-t(6)A37 methylthiotransferase |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:432014 |
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 Q6NS26
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6NS26-F1 | Predicted | AlphaFoldDB |
No variants for Q6NS26
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6NS26 | |||||
No associated diseases with Q6NS26
5 regional properties for Q6NS26
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TRAM domain | 427 - 489 | IPR002792 |
| domain | Elp3/MiaA/NifB-like, radical SAM core domain | 199 - 418 | IPR006638 |
| domain | Radical SAM | 59 - 489 | IPR007197 |
| domain | Methylthiotransferase, N-terminal | 60 - 168 | IPR013848 |
| conserved_site | Methylthiotransferase, conserved site | 204 - 224 | 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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
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. |
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 |
| MPAVCESLLD | DIEDMVSATD | PKPHDRQSAR | KNIVPRARKR | NKNNIQEEEP | PADSTIPGTQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KIWIRTWGCS | HNNSDGEYMA | GQLAAYGYSI | TEQPEKADLW | LLNSCTVKSP | AEDHFRNSIK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KAQEANKKVV | VSGCVPQAQP | RQDYMKGLSI | IGVQQIDRVV | EVVEETIKGH | SVRLLGQKKD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NGKRLGGARL | DLPKIRKNPL | IEIISINTGC | LNACTYCKTK | HARGELASYP | VEELVDRATQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SFQEGVCEIW | LTSEDTGAYG | RDIGTDLPTL | LWKLVEVIPE | GAMLRLGMTN | PPYILEHLEE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MAKILNHPRV | YAFLHIPVQS | ASDSVLMDMK | REYCIADFKR | VVDFLKERVP | GITIATDIIC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GFPGETDEDF | KETLKLVEEY | KFPSLFINQF | YPRPGTPAAK | MEQVLAHVKK | RRTKELSQLF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HSYDPYDHKI | GQKQQVLVTE | ESFDSQYYVA | HNRFYEQVLV | PKDPDFMGKM | VEVKIFEAGK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HFMKGQPVQD | SYIYTPSITK | PLAKGEVSGL | TEELKPPNNI | PKSETLLEKH | WERLQVFLFL |
| 550 | |||||
| TALLAAVIAF | VGTKLV |