Q74MI1
Gene name |
cysS |
Protein name |
Cysteine--tRNA ligase |
Names |
Cysteinyl-tRNA synthetase, CysRS |
Species |
Nanoarchaeum equitans (strain Kin4-M) |
KEGG Pathway |
neq:NEQ055 |
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 Q74MI1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q74MI1-F1 | Predicted | AlphaFoldDB |
No variants for Q74MI1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q74MI1 | |||||
No associated diseases with Q74MI1
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 |
| MLYLYNTLTS | RKEAFIPLEE | PFVKMYTCGV | TPYDKAHVGH | LRTYLVTDLL | RRILRFLGYY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DIAVTNFTDI | DDKIIKKSQE | LNKDWKEIVE | ENIKYVFDVL | KELKVLPFYV | YPRVTYHIDD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IANAVKSLLD | RGYAYKGKYS | IYFDVDKYPY | YGQLSGIKSK | KEWEQEKHLL | EDKKNPYDFA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LWKFKQPGEP | YWNTIVGEGR | PGWHIECSVM | SSKYLGERFD | IHLGGSDLIF | PHHENEIAQS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ETLYNVHPWV | RYWVHIGMVQ | INGEKMSKSL | GNIIEAKEFI | KKYKPEFVRF | FLLSTHYRKP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LDISEENIEQ | AQTIYKKLTD | AYNTAKSIVE | NEVSYRFDKD | VRIILDYYRE | MIKAFLDDMN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TPTAIASLNK | IVSIFNQNPE | YPIAYLTLRA | FEDFNRIMNV | WFEKPIDLDI | INEIIEIRNM |
| 430 | 440 | 450 | |||
| LRREKQYELA | DKIRDILQKK | GIKIKDYKDK | TVWYADI |