A9IYI2
Gene name |
tilS |
Protein name |
tRNA(Ile)-lysidine synthase |
Names |
tRNA(Ile)-2-lysyl-cytidine synthase, tRNA(Ile)-lysidine synthetase |
Species |
Bartonella tribocorum (strain CIP 105476 / IBS 506) |
KEGG Pathway |
btr:BT_2359 |
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 A9IYI2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A9IYI2-F1 | Predicted | AlphaFoldDB |
No variants for A9IYI2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A9IYI2 | |||||
No associated diseases with A9IYI2
3 regional properties for A9IYI2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | tRNA(Ile)-lysidine/2-thiocytidine synthase, N-terminal | 21 - 145 | IPR011063-1 |
| domain | tRNA(Ile)-lysidine/2-thiocytidine synthase, N-terminal | 198 - 256 | IPR011063-2 |
| domain | tRNA(Ile)-lysidine synthase, N-terminal | 20 - 258 | IPR012795 |
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 |
| MCVRLARNLF | KTSDFIPCRR | VILAVSGGSD | SLALMFLVKE | YLETLLIPPE | IIAVTVDHQL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RKESAREAEI | VAEICRDHHI | KHITVRWEGK | KPKTHLAFSA | RIARYDLLVQ | EAQKQGASLI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MTGHTLNDQV | ETYQMRCQRL | QKRRGALRDE | VGAMCDGGAA | SGFAGALRDK | AGARRDEDYV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RETRKNIAEK | SYGVLYERGL | SCIPREALLH | RKVRLIRPLL | GVQRQTLRNY | LRLQGKTWID |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DPTNEDRNFE | RVRVRQSLSS | QKLVNIAQKI | NKAAWQRRQQ | AQNIADLILA | LDITVQYGRC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FIVKPAPFLQ | KHSCFPFVVG | LFAVLMGGGF | YLLSNQKLSM | LVQKLCLNSP | EKRRFTCAGC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VIEYNKEGIA | LWRERRNMKE | ALVEPDETLL | WDGRYRITNH | GSEAIKVGVA | NLEQLKSLLQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NSNSNLEKPH | FPSLQSLLML | SNDKGCDIPE | LISQAIIHKN | VIIKRIMAPF | DWLSSREDAA |
| 490 | |||||
| LVNVVEPFFN | LEVKR |