Q9UTA4
Gene name |
pop1 (SPAC25B8.16) |
Protein name |
Ribonucleases P/MRP protein subunit pop1 |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC25B8.16 |
EC number |
3.1.26.5: Endoribonucleases producing 5'-phosphomonoesters |
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 Q9UTA4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9UTA4-F1 | Predicted | AlphaFoldDB |
14 variants for Q9UTA4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_4188039_C_T | 165 | R>C | No | Jeffares_SNPs | |
| I_4188120_A_C | 192 | N>H | No | Jeffares_SNPs | |
| I_4188163_C_T | 206 | S>F | No | Jeffares_SNPs | |
| I_4188192_C_T | 216 | R>W | No | Jeffares_SNPs | |
| I_4188257_A_T | 237 | E>D | No | Jeffares_SNPs | |
| I_4188258_G_T | 238 | A>S | No | Jeffares_SNPs | |
| I_4188421_A_G | 292 | Q>R | No | Jeffares_SNPs | |
| I_4188528_G_T | 328 | D>Y | No | Jeffares_SNPs | |
| I_4188732_T_C | 396 | C>R | No | Jeffares_SNPs | |
| I_4188741_A_T | 399 | N>Y | No | Jeffares_SNPs | |
| I_4188773_A_T | 409 | L>F | No | Jeffares_SNPs | |
| I_4189207_G_A | 554 | G>E | No | Jeffares_SNPs | |
| I_4189268_G_A | 574 | M>I | No | Jeffares_SNPs | |
| I_4189294_A_G | 583 | K>R | No | Jeffares_SNPs |
No associated diseases with Q9UTA4
No regional properties for Q9UTA4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9UTA4 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.26.5 | Endoribonucleases producing 5'-phosphomonoesters |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleolar ribonuclease P complex | A ribonuclease P complex located in the nucleolus of a eukaryotic cell, where it catalyzes the 5' endonucleolytic cleavage of precursor tRNAs to yield mature tRNAs. Eukaryotic nucleolar ribonuclease P complexes generally contain a single RNA molecule that is necessary but not sufficient for catalysis, and several protein molecules. |
| 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. |
| 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. |
| ribonuclease MRP complex | A ribonucleoprotein complex that contains an RNA molecule of the snoRNA family, and cleaves the rRNA precursor as part of rRNA transcript processing. It also has other roles: In S. cerevisiae it is involved in cell cycle-regulated degradation of daughter cell-specific mRNAs, while in mammalian cells it also enters the mitochondria and processes RNAs to create RNA primers for DNA replication. |
| ribonuclease P complex | A ribonucleoprotein complex that catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5' end of tRNAs. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ribonuclease P activity | Catalysis of the endonucleolytic cleavage of RNA, removing 5' extra nucleotides from tRNA precursor. |
| tRNA binding | Binding to a transfer RNA. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) | Endonucleolytic cleavage between the SSU-rRNA and the 5.8S rRNA of an rRNA molecule originally produced as a tricistronic rRNA transcript that contained the Small SubUnit (SSU) rRNA, the 5.8S rRNA, and the Large SubUnit (LSU) rRNA, in that order, from 5' to 3' along the primary transcript. |
| endonucleolytic cleavage involved in tRNA processing | Any endonucleolytic RNA phosphodiester bond hydrolysis that is involved in tRNA processing. |
| mRNA cleavage | Any process in which a pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner. |
| RNA phosphodiester bond hydrolysis, endonucleolytic | The chemical reactions and pathways involving the hydrolysis of internal 3',5'-phosphodiester bonds in one or two strands of ribonucleotides. |
| tRNA 5'-leader removal | Generation of the mature 5'-end of the tRNA, usually via an endonucleolytic cleavage by RNase P. |
| tRNA processing | The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKRSTGGTQP | KGLNVKRSKL | ADARFIEVES | PALSNGAVDL | KKFIESRSFE | ITALQDAMKR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SKESSAQRAF | QALPRCLRRR | AASHNIKRIP | KGLRDRALYE | MQLSSSSTLP | IAPSRQRLKR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FIKRLRRKLA | KSGETKAIDS | TGSLVTDNST | DDSRIPSLAA | VKLIRGKFAG | RQLRKVWLPT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HLWVCKRAHM | INAWGYAIPE | KPTEKSYRPT | HRAAFRKDAI | AFDMSYEPLF | CISGPYEALK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EKFGNSFANG | LPPVFLNSSR | SFTSYLVKSD | IHELICPCFL | QWNNPTEDDK | KQIPVKNPTE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CVQLVIRLHP | SAFLQAWNYL | SGIAVLDDRI | AMHDWRLDLA | SFDIHGPDSN | IMLHKVFDDV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ELDEAGKVWQ | SISNYSSACL | PMGASISVKA | LVNTRCDKNL | SEKGEKSLLD | SAENSLPASA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NQYSTHFRYW | ERQEIPSFAV | FENKNRHTHE | KKSSEKEVIP | VYITYRKEWN | GLTVILPWDY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AKFVWRKMMY | QKGIRFGGLE | NLHQIAFEKR | MPFFPIDYPD | TISGQLCEEE | RKKRNEDSWK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RRPPAKRVNY | QKFGDNFSEI | GNPFCCDWVY | LNEMVKASRD | EDKTLQLVRV | QVQLVQRGSL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QDRARIYCLS | DDELSKWKTI | IYKENLTAEN | LLYPKCPNET | AIIGFVTTGN | FNLNAGKPSG |
| 670 | 680 | 690 | |||
| IANVLAKTIK | NEKSGYCIIR | NVGCSVPRLA | QWKFNQSH |