Q59PL9
Gene name |
RPG1A |
Protein name |
Eukaryotic translation initiation factor 3 subunit A |
Names |
eIF3a, Eukaryotic translation initiation factor 3 110 kDa subunit homolog, eIF3 p110, Translation initiation factor eIF3, p110 subunit homolog |
Species |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
KEGG Pathway |
cal:CAALFM_C112770WA |
EC number |
|
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 Q59PL9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q59PL9-F1 | Predicted | AlphaFoldDB |
No variants for Q59PL9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q59PL9 | |||||
No associated diseases with Q59PL9
1 regional properties for Q59PL9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Proteasome component (PCI) domain | 355 - 551 | IPR000717 |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| eukaryotic 43S preinitiation complex | A protein complex composed of the 40S ribosomal subunit plus eIF1A, eIF3, and eIF2-GTP-bound methionyl-initiator methionine tRNA. |
| eukaryotic 48S preinitiation complex | A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA. |
| eukaryotic translation initiation factor 3 complex, eIF3e | An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3e. |
| eukaryotic translation initiation factor 3 complex, eIF3m | An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3m. |
| multi-eIF complex | A multifactor complex composed of multiple translation initiation factors and the initiatior tRNAiMet, which is ready to bind to the small (40S) ribosome to form the 43S preinitiation complex. In S. cerevisiae, this complex is composed of eIF1, eIF2, eIF3, and eIF5. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| mRNA binding | Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns. |
| translation initiation factor activity | Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| formation of cytoplasmic translation initiation complex | Joining of the large subunit, with release of IF2/eIF2 and IF3/eIF3. This leaves the functional ribosome at the AUG, with the methionyl/formyl-methionyl-tRNA positioned at the P site. |
| translation reinitiation | A gene-specific translational control mechanism where the small ribosomal subunit remains attached to the mRNA following termination of translation, then resumes scanning on the same mRNA molecule and initiates again at a downstream start site. Reinitiation depends on de novo recruitment of the ternary complex that is required to recognize the next AUG codon. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAPPHKNHNF | RPENVLKRAE | DLIAVGQKEA | ALDTLYELII | SKRIRYLQVQ | DLEPIASLLI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELAVELRKGK | LAKDALHQYK | KNIQLSENGL | ESVQTIVRKF | IDLAEKKLDA | AQTKADIKID |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EEENAAAAAA | ATSSAGAGGA | GGDAGGAGAG | GDDDLETAQT | PESILLSAVS | NTDSADRTER |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELVTPWLRFL | WEAFRAVLDI | LRNNSKLEIT | YSAIVNQAFK | FCLNFNRKAE | FRRLCELLRT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HMQSVTTQTT | TKTSGHNAID | LSDAETVQRY | LDQRFAQLNI | AVKLELWQES | FRSVDDVHSL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ITASKKAPKP | NMMANYYENL | ARIFAVSDNT | LYHAAAWNKF | FNLYSQSPLA | TDEELKRYAS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VLVLSTLSIP | QRVVQDVDEH | KSKNSKLSSL | LNLTHVPTRE | GLIKSILSRS | ILKYVDEPIQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QLFELLEGGD | FHPLSIKQEI | SQLFQIIESD | KEFKKYIPTL | TEVILIRIFQ | QVSQVYDAVK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LDFLISLGIF | PDLEYSLSEL | QVEDLIVNAV | KDDLVSLTID | HESGVVSFKS | NPFDEIDQEF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ANAGTTTTNT | ITTTTTIGTS | RLQISPAELV | RTQISKLAAT | LSESIYLIDP | NYEARQQQAK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QQALQRCIKD | MVNEQQRIAD | RSKILKDRKV | AAEKRKREEE | ERQARLRQEK | LAMEQKLEQE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RLIAEQERKK | LEKLEKEREL | IKENEKRKIA | EEINAKGIIK | IDLNNLKELD | TTKLQLMQIE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| QLNKDKKELE | TKLQATAKKA | DHLERAYRRY | ELNLLEADLE | IQLDLEKKDY | EFLKQSKINK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| AKKDHDNAIE | LKKRLQRILP | DYSKFKSEID | AKNEVKLKQL | QKEAQIKFEK | AKQERIESVK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| KHRIEELKIR | KERERKAAAE | EAARQAKAAE | MAKLKEELRI | QKEKDEALAR | KRAELEAAAA |
| 910 | 920 | ||||
| AAAAPSSSPP | PKKTMTFAER | MRLKREGKLP |