Q5WAE0
Gene name |
tilS |
Protein name |
tRNA(Ile)-lysidine synthase |
Names |
tRNA(Ile)-2-lysyl-cytidine synthase, tRNA(Ile)-lysidine synthetase |
Species |
Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii) |
KEGG Pathway |
bcl:ABC0104 |
EC number |
6.3.4.19: Other carbon--nitrogen ligases |
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 Q5WAE0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5WAE0-F1 | Predicted | AlphaFoldDB |
No variants for Q5WAE0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5WAE0 | |||||
No associated diseases with Q5WAE0
9 regional properties for Q5WAE0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cadherin, Y-type LIR-motif | 843 - 902 | IPR000233 |
| domain | Cadherin-like | 160 - 267 | IPR002126-1 |
| domain | Cadherin-like | 267 - 393 | IPR002126-2 |
| domain | Cadherin-like | 383 - 497 | IPR002126-3 |
| domain | Cadherin-like | 498 - 605 | IPR002126-4 |
| domain | Cadherin-like | 604 - 710 | IPR002126-5 |
| domain | Cadherin prodomain | 31 - 123 | IPR014868 |
| conserved_site | Cadherin conserved site | 370 - 380 | IPR020894-1 |
| conserved_site | Cadherin conserved site | 593 - 603 | IPR020894-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.4.19 | Other carbon--nitrogen ligases |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ligase activity, forming carbon-nitrogen bonds | Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate. |
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 |
| MEARVEQFIE | NNRLFGMETN | VLVAVSGGPD | SMALLAIMAN | LREKWKLNLF | GVHVNHRLRG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EESNKDAELV | QSFSARLGVP | CNVKDVDVAA | FKAEHHVGTQ | QAARALRYQV | FQGEMERVHA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TVLLTAHHGD | DEVETAFMKL | TRGTTPLTKL | GIAATRPFAN | GVLARPLLEE | TKRSIVAYCH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EKAIPYRIDQ | SNFSDAYTRN | RFRMNMAPYL | VEENPHIHKH | IGRFDRWQEE | DNHYLMEQAK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AHLDQILTKK | SEKSIELEIQ | ALCLAPFPLQ | RRMIHLILNY | LHLNVYGVND | MRVFPDAIEQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IQAFLQTSAP | SAQLDLPGRV | QVKRSYGTCL | FTTAPFIETK | AYCHLLSIPG | KVDTPLGVIR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ADTREELLEL | EHTDAVSFQV | SQVAFPLYIR | NRKPGDKLSP | SGMSGSKKVN | RLFIDRKVDR |
| 430 | 440 | 450 | 460 | ||
| AKRDAWPLLV | DANDSILWVP | SLQTSRILTR | SANVQGELLH | VTFSQHKWP |