A5GQP4
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 |
Synechococcus sp (strain RCC307) |
KEGG Pathway |
syr:SynRCC307_0300 |
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 A5GQP4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5GQP4-F1 | Predicted | AlphaFoldDB |
No variants for A5GQP4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5GQP4 | |||||
No associated diseases with A5GQP4
6 regional properties for A5GQP4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TRAM domain | 405 - 476 | IPR002792 |
| domain | Elp3/MiaA/NifB-like, radical SAM core domain | 177 - 394 | IPR006638 |
| domain | Radical SAM | 173 - 402 | IPR007197 |
| domain | Methylthiotransferase, N-terminal | 38 - 149 | IPR013848 |
| conserved_site | Methylthiotransferase, conserved site | 181 - 201 | IPR020612 |
| domain | RimO, TRAM domain | 408 - 475 | 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 |
| MPAGHGQTAM | TREQQPPRFT | LNCWADAAMA | STATTARPTV | AFAHLGCEKN | RVDTEHMLGL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAQAGYGVSA | DEADAQVVVV | NTCSFIQDAR | AESVRTLVDL | AEQGKQIVIA | GCLAQHFQEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LLESLPEARA | IVGTGDYQHI | VEVLEQVEAG | ERVNRVSQVP | TFVADENLPR | YRTTSEAVAY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKVAEGCDYR | CAFCIIPKLR | GDQRSRPIES | IVAEAQQLAA | QGVKELILIS | QITTNYGLDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YGKPQLAELL | RALGEVEIPW | IRVHYAYPTG | LTPEVLAAYR | EVPNVLPYLD | LPLQHSHPEV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LRAMNRPWQE | GVNGQLLQRI | REQLPDAVLR | TTFIVGYPGE | TEEQFEHLLE | FVQEQRFDHV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GVFCFSPEDG | TPAADLPNAV | PAEVAEARRG | RLMEAQQAIS | AERNGAWVGR | IVDVLVEQEN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PSSGELIGRC | LRFAPDVDGE | VRIRAGSHGA | AASAGTMVPV | RITAADIYDL | EGEVVGAQEM |
| VDAVRHS |