B4I100
Gene name |
GM12339 |
Protein name |
Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 |
Names |
Histone lysine demethylase NO66 |
Species |
Drosophila sechellia (Fruit fly) |
KEGG Pathway |
|
EC number |
1.14.11.27: With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
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 B4I100
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B4I100-F1 | Predicted | AlphaFoldDB |
No variants for B4I100
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B4I100 | |||||
No associated diseases with B4I100
1 regional properties for B4I100
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | JmjC domain | 307 - 452 | IPR003347 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.11.27 | With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 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. |
| 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-oxoglutarate-dependent dioxygenase activity | Catalysis of the reaction: A + 2-oxoglutarate + O2 = B + succinate + CO2. This is an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from 2-oxoglutarate and one other donor, and one atom of oxygen is incorporated into each donor. |
| histone H3-di/monomethyl-lysine-36 demethylase activity | Catalysis of the removal of a methyl group from a di- or a monomethyl-lysine residue at position 36 of the histone H3 protein. This is a dioxygenase reaction that is dependent on Fe(II) and 2-oxoglutarate. |
| histone H3-methyl-lysine-36 demethylase activity | Catalysis of the removal of a methyl group from a modified lysine residue at position 36 of the histone H3 protein. This is a dioxygenase reaction that is dependent on Fe(II) and 2-oxoglutarate. |
| histone H3-tri/di/monomethyl-lysine-4 demethylase activity | Catalysis of the removal of a methyl group from a tri, a di or a monomethyl-lysine residue at position 4 of the histone H3 protein. This is a dioxygenase reaction that is dependent on Fe(II) and 2-oxoglutarate. |
| iron ion binding | Binding to an iron (Fe) ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| chromatin organization | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. |
| histone H3-K36 demethylation | The modification of histone H3 by the removal of a methyl group from lysine at position 36 of the histone. |
| histone H3-K4 demethylation | The modification of histone H3 by the removal of a methyl group from lysine at position 4 of the histone. |
| negative regulation of DNA-templated transcription | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEKVTNSAAA | KPQGNNKKQE | SAYNGAGKDK | KKPNLDIETT | DSDLLSDMHL | DGTTEQKVGT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LFSKVFEDTD | YGTGPSTSSK | EAAAAKTADH | ERRLQAEADV | NNNDAEKAGQ | LAKESVATQG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ASATERKQAF | SLGLEHTSPI | QVNGAALACP | LVRKSLPPGE | ANSCPPPPKR | DPAAVKSAVK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IIKVKAPEEG | NNNNDEKEMS | TETSEPHKTD | SVEEGRRVVM | WIIFPIKTKF | FFKYFWEQTA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CLVQRTNPKY | FQSLISFKML | DEILIRHNLD | FTVNLDVTTY | KNGKRETLNP | EGRALPPAVW |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GFYSEGCSIR | LLHASAYLTR | LREVCTVLQE | FFHCKVGANM | YLTPPNSQGF | APHYDDIEAF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VIQVEGRKRW | LLYDPPKEAD | HLARISSGNY | NQEQLGKPII | DEVLSAGDVL | YFPRGTVHQA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ITEEQQHSLH | ITLSVYQQQA | YANLLETLMP | MVLKKAVDRS | VALRRGLPLH | TFQILGNAYK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ANDCGSRQLL | VENVQKLVAK | YLMPSEDDID | EAVDQMAKKF | QHEALPPIVL | PSEEVRTVHG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ARSGADDQGN | CVCDYKFNEK | TSVRLLRANI | LRLVTEPDGS | VRIYHHVDNG | LDYCKYEPYF |
| 610 | 620 | 630 | 640 | 650 | |
| MEILPEKAKA | VELLISAYPY | YLTIDQLPLK | SSARKVEVAT | ALWEHGLLMT | EKPFK |