Q03195
Gene name |
RLI1 (YDR091C) |
Protein name |
Translation initiation factor RLI1 |
Names |
ATP-binding cassette sub-family E member RLI1, RNase L inhibitor |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YDR091C |
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
9 structures for Q03195
No variants for Q03195
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q03195 | |||||
No associated diseases with Q03195
9 regional properties for Q03195
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ABC transporter-like, ATP-binding domain | 70 - 320 | IPR003439-1 |
| domain | ABC transporter-like, ATP-binding domain | 345 - 568 | IPR003439-2 |
| domain | AAA+ ATPase domain | 102 - 298 | IPR003593-1 |
| domain | AAA+ ATPase domain | 377 - 545 | IPR003593-2 |
| domain | RNase L inhibitor RLI-like, possible metal-binding domain | 7 - 37 | IPR007209 |
| conserved_site | ABC transporter-like, conserved site | 468 - 482 | IPR017871 |
| domain | 4Fe-4S ferredoxin-type, iron-sulphur binding domain | 46 - 75 | IPR017896 |
| conserved_site | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site | 55 - 66 | IPR017900 |
| domain | RLI, domain 1 | 78 - 337 | IPR034348 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| iron ion binding | Binding to an iron (Fe) ion. |
| ribosomal small subunit binding | Binding to a small ribosomal subunit. |
| translation initiation factor activity | Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of translation | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
| ribosomal large subunit biogenesis | A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a large ribosomal subunit; includes transport to the sites of protein synthesis. |
| ribosomal subunit export from nucleus | The directed movement of a ribosomal subunit from the nucleus into the cytoplasm. |
| ribosome disassembly | The disaggregation of a ribosome into its constituent components; includes the dissociation of ribosomal subunits. |
| rRNA processing | Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules. |
| translational initiation | The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA. |
| translational termination | The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code). |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSDKNSRIAI | VSADKCKPKK | CRQECKRSCP | VVKTGKLCIE | VTPTSKIAFI | SEILCIGCGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CVKKCPFDAI | QIINLPTNLE | AHVTHRYSAN | SFKLHRLPTP | RPGQVLGLVG | TNGIGKSTAL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KILAGKQKPN | LGRFDDPPEW | QEIIKYFRGS | ELQNYFTKML | EDDIKAIIKP | QYVDNIPRAI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KGPVQKVGEL | LKLRMEKSPE | DVKRYIKILQ | LENVLKRDIE | KLSGGELQRF | AIGMSCVQEA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVYMFDEPSS | YLDVKQRLNA | AQIIRSLLAP | TKYVICVEHD | LSVLDYLSDF | VCIIYGVPSV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YGVVTLPASV | REGINIFLDG | HIPAENLRFR | TEALQFRIAD | ATEDLQNDSA | SRAFSYPSLK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KTQGDFVLNV | EEGEFSDSEI | LVMMGENGTG | KTTLIKLLAG | ALKPDEGQDI | PKLNVSMKPQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KIAPKFPGTV | RQLFFKKIRG | QFLNPQFQTD | VVKPLRIDDI | IDQEVQHLSG | GELQRVAIVL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ALGIPADIYL | IDEPSAYLDS | EQRIICSKVI | RRFILHNKKT | AFIVEHDFIM | ATYLADKVIV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FEGIPSKNAH | ARAPESLLTG | CNRFLKNLNV | TFRRDPNSFR | PRINKLDSQM | DKEQKSSGNY |
| FFLDNTGI |