Q2YRB4
Gene name |
pdhS (BAB1_1621) |
Protein name |
Cell-division control histidine kinase PdhS |
Names |
|
Species |
Brucella abortus (strain 2308) |
KEGG Pathway |
bmf:BAB1_1621 |
EC number |
2.7.13.3: Protein-histidine kinases |
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 Q2YRB4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2YRB4-F1 | Predicted | AlphaFoldDB |
No variants for Q2YRB4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2YRB4 | |||||
No associated diseases with Q2YRB4
6 regional properties for Q2YRB4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Biotin/lipoyl attachment | 4 - 78 | IPR000089-1 |
| domain | Biotin/lipoyl attachment | 122 - 196 | IPR000089-2 |
| domain | 2-oxoacid dehydrogenase acyltransferase, catalytic domain | 326 - 552 | IPR001078 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 28 - 57 | IPR003016-1 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 146 - 175 | IPR003016-2 |
| domain | Peripheral subunit-binding domain | 250 - 287 | IPR004167 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.13.3 | Protein-histidine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| phosphorelay sensor kinase activity | Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cell cycle | The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division. |
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| regulation of DNA-templated transcription | Any process that modulates 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 |
| MSGSYPFIDI | AALDSVREGF | ARGDAQLVLA | HDLSTVLWVN | GPGAKLFGYN | RVEDLIEGQL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLPVATRRQI | AAFSSENTSA | PSAVAVRLGG | GLRSELTHLH | VSNIKLPDGV | AALLVATQMP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DNSAEAAISG | LGDDSTHIAL | VDAVGKVVAA | SPRFALLDIS | ASTLEDLIVE | AGDATDRIVK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RRIRTGSHSV | PGAIARLTDT | PALHLLCIVG | DAPAQFQTAA | EAVPLPDNAE | AVLEEILPEQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GDAPAQQAQK | THAEQPRPKT | FAFDHDAPPA | RFIWKVGPDG | TFSEISPNLA | AVVGPNSADI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VGRRFSDVAN | VFGFDTDGSI | AALLLERDTW | SGKRLLWPVE | GTRLRVPVEL | AALPVYSRDR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EFLGFRGFGI | VRPAEAEADP | EEIGLALAGG | IPQNRKPRKE | PAETARMVGE | DDVLALSEEV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ANDDQPAAVL | PKPPLDITPT | PGRRDSDKVI | SLLNSCAQEK | VAADQAKFLK | EKERATRPEG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GLTKTERNAF | REIAERLRKQ | GLANTRAESE | TPVSETSSIE | PVEPTPPVKT | RSEPIQPDET |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALLANLPVPV | IIHSGDAIHY | VNQALLDITG | YESLDDIRSA | GGVDVLFNSE | SDDGETRQSM |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LLRHADGSEE | PVDAHLNAIA | WRGGRALMLS | LMPVTAADLP | APAELPAAND | EEKQALEAHV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EELKTILDTA | TDGVVLIDPE | GRIRSMNHSA | SALFGYERDE | AEGKFFSMLF | AIESQRAAMD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| YLHGLSGNGV | LSVLNDGREV | IGREAKGGFI | PLFMTIGKLP | HTRGFCAVLR | DITQWKRTEE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ELTNARKEAE | RASNQKTEFL | ARISHEIRTP | LNAIIGFSEL | MADEKFGPIG | NDRYRDYLRD |
| 850 | 860 | 870 | 880 | 890 | 900 |
| INRSGNHVLA | LVNDLLDISK | IEAGALDMQF | EAVSLNDAIG | EAIALMQPQA | NRERVIIRSS |
| 910 | 920 | 930 | 940 | 950 | 960 |
| FQSNLPDIVA | DSRSIKQVAL | NLLSNAVRFT | APGGQVIVST | SYELNGDVVM | RVRDTGIGMS |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| KSEVEQALKP | FRQINALERR | KAESAKDWRN | EGTGLGLPLT | KAMVEANRAQ | FAIDSNPGQG |
| 1030 | |||||
| TVVEIVFPPT | RVLAD |