B7ID87
Gene name |
lysS |
Protein name |
Lysine--tRNA ligase |
Names |
Lysyl-tRNA synthetase, LysRS |
Species |
Thermosipho africanus (strain TCF52B) |
KEGG Pathway |
taf:THA_1523 |
EC number |
6.1.1.6: Ligases forming aminoacyl-tRNA and related compounds |
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 B7ID87
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B7ID87-F1 | Predicted | AlphaFoldDB |
No variants for B7ID87
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B7ID87 | |||||
No associated diseases with B7ID87
5 regional properties for B7ID87
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| binding_site | Catalase haem-binding site | 358 - 366 | IPR002226 |
| domain | Catalase immune-responsive domain | 443 - 507 | IPR010582 |
| domain | Catalase core domain | 28 - 416 | IPR011614 |
| active_site | Catalase active site | 64 - 80 | IPR024708 |
| domain | Large catalase, C-terminal domain | 536 - 678 | IPR041399 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.6 | Ligases forming aminoacyl-tRNA and related compounds |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| lysine-tRNA ligase activity | Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| nucleic acid binding | Binding to a nucleic acid. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| lysyl-tRNA aminoacylation | The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLKEFREQRI | NEIKQISAKG | VNPYPYKFEK | THSSQDIKAQ | FENLNPGEVK | EDASVSTAGR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IMSLRHHGKS | AFFHIKDFFG | RIQAYIRQDI | VGKDVYEFFK | EHIAIGDIVG | VKGSVFKSKT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GEVTILVKEI | ELLNKPLRPM | PEKWHGIKDK | EVLYRQRYVD | MIANDETLNR | FRIRFEIIKL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IREFLNSKGF | IEVETPILEY | VTGGASARPF | ITHLNVFDID | MYMRIATELY | LKRFIVGGFE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KVYELGKNFR | NEGLSYKHHP | EFTSIEIYQA | YADYEDMMNL | TEELFVFIVE | KLFGTTKVKY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QDIEIDFSRP | WRRVKMRDFI | KEHLGVDILE | DTEEKMLEVL | KQHDVEVEIK | DKGHLIEKLW |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DLVEDKVVQP | TFLLEHPVEI | SPLAKKHRED | PRVTERFELI | IYGREMANAF | SELNDPVDQY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ERFLRQAKLR | EAGDEEAQMM | DKDFVRALEY | GMPPTGGLGI | GIDRLVMLLT | NSPTIRDVIA |
| 490 | 500 | ||||
| FPLVRPISFE | EEEMNLEGGS | QE |