Q6FRV0
Gene name |
NOG1 (CAGL0H05709g) |
Protein name |
Nucleolar GTP-binding protein 1 |
Names |
|
Species |
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
KEGG Pathway |
cgr:CAGL0H05709g |
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 Q6FRV0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6FRV0-F1 | Predicted | AlphaFoldDB |
No variants for Q6FRV0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6FRV0 | |||||
No associated diseases with Q6FRV0
7 regional properties for Q6FRV0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GTP binding domain | 170 - 190 | IPR006073-1 |
| domain | GTP binding domain | 191 - 209 | IPR006073-2 |
| domain | GTP binding domain | 218 - 233 | IPR006073-3 |
| domain | Nucleolar GTP-binding protein 1, Rossman-fold domain | 234 - 291 | IPR010674 |
| domain | NOG, C-terminal | 396 - 449 | IPR012973 |
| domain | OBG-type guanine nucleotide-binding (G) domain | 168 - 340 | IPR031167 |
| domain | NOG1, N-terminal helical domain | 6 - 164 | IPR041623 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| preribosome, large subunit precursor | A preribosomal complex consisting of 27SA, 27SB, and/or 7S pre-rRNA, 5S rRNA, ribosomal proteins including late-associating large subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic large ribosomal subunit. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP binding | Binding to GTP, guanosine triphosphate. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| assembly of large subunit precursor of preribosome | The aggregation, arrangement and bonding together of a set of components to form the large subunit precursor of the preribosome. |
| 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. |
| rRNA processing | Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQLSWKDIPT | VAPANDMLDI | VLNRTQRKTP | TVIRPGFKIT | RIRAFYMRKV | KFTAEGFEEK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FDDILKGFPN | INDVHPFHRD | LMDTLYEKNH | YKISLAAVSR | AKTLVEQVSR | DYTRLLKFGQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLFQCKQLKR | AALGRMATIV | KKLKDPLVYL | EQVRQHLGRL | PSIDPNTRTL | LICGYPNVGK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SSFLRCITKS | DVEVQPYAFT | TKSLYVGHFD | YKYLRFQAID | TPGILDRPTE | EMNNIEMQSI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YAIAHLRSCV | MYFMDLSEQC | GFSVEAQVKL | FHSIKPLFAN | KSVMVVINKT | DIIRPEDLDE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ERAKLLQTVT | ELPGVEIMSA | SCQLEDNVMN | VRNKACEKLL | ASRIENKLKS | QARITNVLNK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IHVAKPQARD | DVERTPYIPE | EFKKLKKYDP | EDPERRLLAR | DIEAENGGAG | VFNINLKDKY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ILDDDEWKND | IMPEIMDGKN | VYDFLDPDIA | AKLQALEEEE | ERLEKEGFYD | SDEDESYGGF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DQEEIDEIRE | KADWIRNKQK | KMIAEARNKK | SLRNKAMMPR | SKLVKSFGDM | EKHMATLGHD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| MSSLQDKHRA | AAEKSRYVET | GADVVFGQND | SMASGSNGGK | LRQSDRLLDG | VADGSMRSKA |
| 610 | 620 | 630 | 640 | ||
| DRMAKLQRRQ | RNRDARQGEA | DRHATASLPK | HLFSGKRGIG | KSDFR |