Q31C25
Gene name |
proS |
Protein name |
Proline--tRNA ligase |
Names |
Prolyl-tRNA synthetase, ProRS |
Species |
Prochlorococcus marinus (strain MIT 9312) |
KEGG Pathway |
pmi:PMT9312_0509 |
EC number |
6.1.1.15: 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 Q31C25
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q31C25-F1 | Predicted | AlphaFoldDB |
No variants for Q31C25
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q31C25 | |||||
No associated diseases with Q31C25
5 regional properties for Q31C25
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 98 - 483 | IPR002314 |
| domain | Anticodon-binding | 500 - 589 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 34 - 492 | IPR006195 |
| domain | YbaK/aminoacyl-tRNA synthetase-associated domain | 260 - 323 | IPR007214 |
| domain | Proline--tRNA ligase, anticodon binding domain | 497 - 587 | IPR044140 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.15 | 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 |
|---|---|
| aminoacyl-tRNA editing activity | The hydrolysis of an incorrectly aminoacylated tRNA. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| proline-tRNA ligase activity | Catalysis of the reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| prolyl-tRNA aminoacylation | The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-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 |
| MRVTTSFPLG | TLRDTPSEAE | IISHQLLLKA | GYIRRVYSGI | YAYMPIMLKV | IEKISKIIEI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELNSIGCTKL | LLPQLHPANL | WKKSERWEGY | TAGEGIMFNL | KDRQGKEFGL | APTHEEVITS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IASEIINSYK | QLPQCFYQIQ | TKFRDEIRPR | FGLMRSREFI | MKDGYSFHSS | EKDLASFYEK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VGNAYENIFK | SCGLETVGVE | ADSGAIGGAS | SKEFMVTADA | GEDSILFTQS | GSYAANIEKA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VSIPSQPIPL | KNNISGWIET | PEQKTILEVC | KNNNLDPSQI | IKVVVFLAKF | EIKSEVPILA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CIRGDQHINE | VKLFNLINKL | HSSNLLHLQK | IEDIKIIEKN | LVNFPLGFIG | PDLDNETIKA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SSNWDKTWTR | IIDHSASTLS | KFISGANKVN | FHKVFQEFSF | TSKDYLIEDI | RNAKKGDKIK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| INDNEELKEK | KGIEIGHIFQ | LGQKYSEKLN | AKFSDKDGHL | KNLWMGCYGI | GVTRIAQAAI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EQNHDQKGIC | WPIQISPFEV | IIIPTNLKDQ | IQRDLTEQIY | NNFLVNKIDV | LLDDREDRAG |
| 550 | 560 | 570 | 580 | 590 | |
| VKFKDAELIG | IPFQIIIGRD | SINNEVELIC | RTNNTKFKIS | AHKLLETFIS | ESEIMYNKNS |