P38708
Gene name |
YHR020W |
Protein name |
Putative proline--tRNA ligase YHR020W |
Names |
Prolyl-tRNA synthetase, ProRS |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YHR020W |
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 P38708
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P38708-F1 | Predicted | AlphaFoldDB |
2 variants for P38708
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s08-144386 | 133 | N>S | No | SGRP | |
| s08-144664 | 226 | A>T | No | SGRP |
No associated diseases with P38708
5 regional properties for P38708
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 283 - 456 | IPR002314 |
| domain | Anticodon-binding | 475 - 575 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 225 - 468 | IPR006195 |
| domain | Proline-tRNA ligase, class II, C-terminal | 602 - 688 | IPR016061 |
| domain | Prolyl-tRNA synthetase, catalytic domain | 194 - 458 | IPR033721 |
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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| aminoacyl-tRNA synthetase multienzyme complex | A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates. |
| 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 |
| MPVSEAFAKL | CVNEKPPAES | AVAVKSLVFK | PKTPKSATPV | PIVVVALQST | TTPSALIANA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TSSKDPRLAR | DDLVKQAFQS | ESARAFILGD | LANATSNFHL | LIDHELGTVD | GDTILQLNDS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TYMKKSDMMK | FLNNFEDSQK | VVDFSQEVSK | ETATEGKKQQ | KKQQPSKAGT | AAAAAAAALE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DAKLIGITVD | KALDFPGWYQ | QILTKGEMLD | YYDVSGCYIL | RPPSYAIWEN | IQKWFDDKIK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AIGVQNAYFP | MFVSSRVLEK | EKDHVEGFAP | EVAWVTRAGS | SELEEPIAIR | PTSETVMYPY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YAKWVQSYRD | LPLKLNQWNS | VVRWEFKHPQ | PFLRTREFLW | QEGHTAHLTA | KDAEEEVLQI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LDFYAGVYEE | LLAVPVVKGR | KTEKEKFAGG | DFTTTCEGYI | PQTGRGIQGA | TSHHLGQNFS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KMFNLSVENP | LGSDHPKIFA | YQNSWGLSTR | VIGVMVMIHS | DNKGLVIPPR | VSQFQSVVIP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VGITKKTSEE | QRKHIHETAR | SVESRLKKVG | IRAFGDYNDN | YTPGWKFSQY | ELKGIPIRIE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LGPKDIEKNQ | VVVVRRNDSK | KYVVSFDELE | ARIPEILEEM | QGDLFKKAKE | LFDTHRVIVN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EWSGFVPALN | KKNVILAPWC | GVMECEEDIK | ESSAKKDDGE | EFEEDDKAPS | MGAKSLCIPF |
| 670 | 680 | ||||
| DQPVLNEGQK | CIKCERIAVN | YCMFGRSY |