A0L1C8
Gene name |
rimO |
Protein name |
Ribosomal protein S12 methylthiotransferase RimO |
Names |
S12 MTTase, S12 methylthiotransferase, Ribosomal protein S12 (aspartate-C(3))-methylthiotransferase, Ribosome maturation factor RimO |
Species |
Shewanella sp (strain ANA-3) |
KEGG Pathway |
shn:Shewana3_3627 |
EC number |
2.8.4.4: 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 A0L1C8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A0L1C8-F1 | Predicted | AlphaFoldDB |
No variants for A0L1C8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A0L1C8 | |||||
No associated diseases with A0L1C8
6 regional properties for A0L1C8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TRAM domain | 405 - 471 | IPR002792 |
| domain | Elp3/MiaA/NifB-like, radical SAM core domain | 169 - 394 | IPR006638 |
| domain | Radical SAM | 165 - 402 | IPR007197 |
| domain | Methylthiotransferase, N-terminal | 37 - 147 | IPR013848 |
| conserved_site | Methylthiotransferase, conserved site | 173 - 193 | IPR020612 |
| domain | RimO, TRAM domain | 408 - 470 | IPR041582 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.8.4.4 | 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. |
| protein methylthiotransferase activity | Catalysis of the reaction: 2 S-adenosyl-L-methionine + a |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid | The modification of peptidyl-aspartic acid to form peptidyl-L-beta-methylthioaspartic acid, typical of bacterial ribosomal protein S12. |
| 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 |
| MTVETFNPKQ | TTTLETPAKT | LEAASADLAN | AESATGNRIG | FVSLGCPKNL | VDSERILTQL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RIDGYEVTNS | YDNADLVIVN | TCGFIDAAVE | ESLDAVREAL | EENGKVIVTG | CLGAKENQIR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EVHPDVLEIT | GPHSYEAVLK | HVHKYVPKPE | HNPFTSLIPQ | TGVKLTPKHY | AYLKISEGCD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NRCTFCIIPA | LRGDLDSRPA | GSVLDEAKRL | VESGVQEILV | VSQDTSAYGK | DKGGRTDFWN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GMPVKQDITS | LARQLGKMGA | WVRLHYIYPY | PWVDDLIPLM | AEGLILPYLD | IPMQHASPRI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LKMMKRPGRV | DRQLEAIQRW | REICPDLVIR | STFIVGFPGE | TEEDFEMLLD | FLREARLDRV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GCFKYSEVEG | AVANTIAELI | SEDVKEDRYH | RFMEVQAEIS | AERLARFVGR | TMDILIDDVD |
| 430 | 440 | 450 | 460 | 470 | |
| EEGAIGRSFA | DAPEIDGMVF | INGETELEPG | MLVRAVITHS | DEHDLWAELV | DADAEDDIEA |