Q922K7
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 Q922K7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q922K7-F1 | Predicted | AlphaFoldDB |
No variants for Q922K7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q922K7 | |||||
No associated diseases with Q922K7
6 regional properties for Q922K7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | SAM-dependent methyltransferase RsmB/NOP2-type | 285 - 572 | IPR001678 |
| domain | Nop2p | 297 - 571 | IPR011023 |
| repeat | P120R repeat | 609 - 630 | IPR012586-1 |
| repeat | P120R repeat | 663 - 685 | IPR012586-2 |
| conserved_site | Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p, conserved site | 439 - 450 | IPR018314 |
| domain | Ribosomal RNA small subunit methyltransferase F, N-terminal | 276 - 359 | IPR031341 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| rRNA (cytosine-C5-)-methyltransferase activity | Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to cytosine to form 5-methylcytosine in small subunit ribosomal RNA. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| blastocyst formation | The initial formation of a blastocyst from a solid ball of cells known as a morula. |
| maturation of LSU-rRNA | Any process involved in the maturation of a precursor Large SubUnit (LSU) ribosomal RNA (rRNA) molecule into a mature LSU-rRNA molecule. |
| positive regulation of cell population proliferation | Any process that activates or increases the rate or extent of cell proliferation. |
| regulation of signal transduction by p53 class mediator | Any process that modulates the frequency, rate or extent of signal transduction by p53 class mediator. |
| ribosomal large subunit assembly | The aggregation, arrangement and bonding together of constituent RNAs and proteins to form the large ribosomal subunit. |
| RNA methylation | Posttranscriptional addition of a methyl group to either a nucleotide or 2'-O ribose in a polyribonucleotide. Usually uses S-adenosylmethionine as a cofactor. |
| rRNA base methylation | The addition of a methyl group to an atom in the nucleoside base portion of a nucleotide residue in an rRNA molecule. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P46087 | NOP2 | Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGRKLDPTKK | EKRGPGRKAR | KQKGAETELV | RFLPAAGDEN | SKRLSSRARK | RAAKRRAGSV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DVPKPNKSPG | IKTLPGELSK | GAVQARGKKR | PAPIQNSDGD | EEEDSGEDDV | VTQGDLWGSE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DSDEDMVDDY | GAASNSEDEE | EKLLPIERAA | LKQKAQDATA | GVLWNEEDTD | EDEDDDGVSP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ESHPRKDDKA | EGDLQINVED | EEAFVLPPAG | ETDQDGQAPD | LQRVHKRIQD | IVGVLRDFGA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QREEGRSRAE | YLSRLQKDLA | TYYSYGDFLL | SKLMELFPLS | ELIEFLEANE | VPRPITLRTN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TLKTRRRDLA | QLLINRGVNL | DPLGKWSKSG | LVVYDSSVPI | GATPEYLAGH | YMLQGASSML |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PVMALAPQEH | ERILDMCCAP | GGKTSYIAQL | MKNTGVILAN | DANADRLKSV | VGNLHRLGVT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NTIISHYDGR | QFPKVVGGFD | RVLLDAPCSG | TGVISKDPAV | KTNKDEKDIQ | RCAHLQKELL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LSAIDSVNAA | SKTGGYLVYC | TCSITVEENE | WVVDYALKKR | NVRLVPTGLD | FGQEGFTRFQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ARRFHPTLRS | TRRFYPHTHN | MDGFFIAKFK | KFSNSIPQPH | AGNSAAATPT | EPDLKDQVTP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KSENGSQPTK | KARGAVKAKQ | QLLRQPHSKK | PFQKLNGIAK | GPGLSTEPSV | PDAQVSTRPS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QSAGNADVNS | KRKRSEKLKQ | RGPKWKPSKE | AAVPKPSAPS | RVEDSGTPVP | TPSEIRAAPR |
| 730 | 740 | 750 | 760 | 770 | 780 |
| PKDCAPSLGK | AKKKQKGKQQ | LAQQPANGAA | PLKEDAVSKG | PSAPFVSPHS | STRPPPAKRR |
| 790 | |||||
| KSMTKGNSQP | LLS |