Q1IJF8
Gene name |
cysS |
Protein name |
Cysteine--tRNA ligase |
Names |
Cysteinyl-tRNA synthetase, CysRS |
Species |
Koribacter versatilis (strain Ellin345) |
KEGG Pathway |
aba:Acid345_3992 |
EC number |
6.1.1.16: 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 Q1IJF8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1IJF8-F1 | Predicted | AlphaFoldDB |
No variants for Q1IJF8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1IJF8 | |||||
No associated diseases with Q1IJF8
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.16 | 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| cysteine-tRNA ligase activity | Catalysis of the reaction: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| cysteinyl-tRNA aminoacylation | The process of coupling cysteine to cysteinyl-tRNA, catalyzed by cysteinyl-tRNA synthetase. A cysteinyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a cysteine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALELFNTLS | GKIETFQPLE | DNEVRMYACG | PTVYDYGHIG | NFRTFIVVDT | LRRFLKQSGY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KLKHVMNVTD | VDDKIIRNAA | RDGKTVQEYT | AKYRKAFLED | CEALNIEHPE | LLVNATDHID |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EMARFIKRME | DLDVAYKTED | GSYYFRIAKF | PEYGKLSKKD | FAGMNDGARV | DVDEYEKDNA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RDFALWKAPK | PGEAKWDTVI | GSGRPGWHIE | CSIMSMKYLG | ESFDIHLGGE | DLVFPHHENE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IAQSESVTHK | KFANFWVHSR | FLLVEGQKMS | KSLGNFFTVR | DLILMGHKPS | SIRFLLMSVP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YRKQLNFTFD | GLKQAAISVD | RLRNFKRRIQ | TEPFAEGTND | KIGLMANETI | TKIKAALDND |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LNTAEALAPI | FDLVRDVNAA | ADAGEVKRGD | VASLLEALQK | FDEIFAVLND | DDSGKVKFAV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DWANQEGKAD | KISAETAEMA | KAAGLSDEKV | EALVAEHSAA | RKAKDFKRSD | AIRAELMESG |
| 490 | |||||
| IILENTKDGV | RWKRK |