A3QJU3
Gene name |
coq8b (adck4) |
Protein name |
Atypical kinase COQ8B, mitochondrial |
Names |
EC 2.7.-.- , AarF domain-containing protein kinase 4 , Coenzyme Q protein 8B |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
|
EC number |
2.7.-.-: Transferring phosphorus-containing groups |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
268-518 (Activator of bc1 complex, ABC1, kinases, also called aarF domain containing kinase 3) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for A3QJU3
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-A3QJU3-F1 | Predicted | AlphaFoldDB |
No variants for A3QJU3
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for A3QJU3 |
No associated diseases with A3QJU3
14 regional properties for A3QJU3
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Protein kinase domain | 621 - 884 | IPR000719 |
domain | Ephrin receptor ligand binding domain | 20 - 202 | IPR001090 |
domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 622 - 880 | IPR001245 |
conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 178 - 198 | IPR001426-1 |
conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 241 - 261 | IPR001426-2 |
domain | Sterile alpha motif domain | 910 - 977 | IPR001660 |
domain | Fibronectin type III | 324 - 434 | IPR003961-1 |
domain | Fibronectin type III | 435 - 530 | IPR003961-2 |
active_site | Tyrosine-protein kinase, active site | 742 - 754 | IPR008266 |
domain | Tyrosine-protein kinase ephrin type A/B receptor-like | 268 - 302 | IPR011641 |
binding_site | Protein kinase, ATP binding site | 627 - 653 | IPR017441 |
domain | Tyrosine-protein kinase, catalytic domain | 621 - 880 | IPR020635 |
domain | Ephrin receptor, transmembrane domain | 544 - 617 | IPR027936 |
domain | Ephrin type-B receptor 2, ligand binding domain | 19 - 196 | IPR034238 |
Functions
Description | ||
---|---|---|
EC Number | 2.7.-.- | Transferring phosphorus-containing groups |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
3 GO annotations of cellular component
Name | Definition |
---|---|
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
5 GO annotations of biological process
Name | Definition |
---|---|
cerebellar Purkinje cell layer morphogenesis | The process in which the anatomical structure of the cerebellar Purkinje cell layer is generated and organized. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells. |
glomerular basement membrane development | The process whose specific outcome is the progression of the glomerular basement membrane over time, from its formation to the mature structure. The glomerular basement membrane is the basal laminal portion of the glomerulus which performs the actual filtration. |
phosphorylation | The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. |
podocyte development | The process whose specific outcome is the progression of a glomerular visceral epithelial cell over time, from its formation to the mature structure. A glomerular visceral epithelial cell is a specialized epithelial cell that contains 'feet' that interdigitate with the 'feet' of other glomerular epithelial cells. |
ubiquinone biosynthetic process | The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme. |
11 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
P27697 | COQ8 | Atypical kinase COQ8, mitochondrial | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
Q29RI0 | COQ8A | Atypical kinase COQ8A, mitochondrial | Bos taurus (Bovine) | SS |
Q8NI60 | COQ8A | Atypical kinase COQ8A, mitochondrial | Homo sapiens (Human) | EV |
Q96D53 | COQ8B | Atypical kinase COQ8B, mitochondrial | Homo sapiens (Human) | SS |
Q60936 | Coq8a | Atypical kinase COQ8A, mitochondrial | Mus musculus (Mouse) | SS |
Q566J8 | Coq8b | Atypical kinase COQ8B, mitochondrial | Mus musculus (Mouse) | SS |
Q5BJQ0 | Coq8a | Atypical kinase COQ8A, mitochondrial | Rattus norvegicus (Rat) | SS |
Q6AY19 | Coq8b | Atypical kinase COQ8B, mitochondrial | Rattus norvegicus (Rat) | SS |
Q18486 | coq-8 | Atypical kinase coq-8, mitochondrial | Caenorhabditis elegans | SS |
Q9SBB2 | ABC1 | Protein ABC transporter 1, mitochondrial | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q5RGU1 | coq8a | Atypical kinase COQ8A, mitochondrial | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MLLSEVLQVL | RGAGKVGAAF | TSTQGEQLRL | MACNSTFGAG | MKAAAEAVEG | VMGTVMGGGD |
70 | 80 | 90 | 100 | 110 | 120 |
MTSKTDEFAG | IEKWEEMDLD | EAAKWSVASE | MPPDFSSKDG | RGETSETPVG | AATGTIKGAG |
130 | 140 | 150 | 160 | 170 | 180 |
WPAQNTRFLH | VSASQHHFRF | VHDSIVARLS | PEDIQRAREA | KQNIARPVRQ | KLNERAKERK |
190 | 200 | 210 | 220 | 230 | 240 |
VPATRISRLA | NFGGLAVGLG | IGAIAEVAKQ | SFGGKRSEVG | ALLDSPLLSE | ANAERIVNTL |
250 | 260 | 270 | 280 | 290 | 300 |
CKVRGAALKI | GQMLSIQDNS | FINPQLQKIF | ERVRQSADFM | PAWQMHKVLE | EELGSGWREK |
310 | 320 | 330 | 340 | 350 | 360 |
LSSIEEKPFA | AASIGQVHHG | VLPGGKEIAM | KIQYPGVAES | IHSDINNLMS | VLKMSVVLPD |
370 | 380 | 390 | 400 | 410 | 420 |
GLFADSSLEV | LQRELAWECD | YEREAKCAKR | FRNLLKGDPV | FVVPEVFDEL | SARRVITMEL |
430 | 440 | 450 | 460 | 470 | 480 |
VNGVPLDRCV | DLDQETRNEI | CFNILQLCLR | ELFEFRFMQT | DPNWSNFFYN | SEQNKIFLLD |
490 | 500 | 510 | 520 | 530 | 540 |
FGACRDYPEL | FTDHYIEVVH | AASVGDRATV | LKKSKDLKFL | TGFEAKAFED | AHVEAVMILG |
550 | 560 | 570 | 580 | 590 | 600 |
EAFASAEAFD | FGTQSTTQRI | QSLIPVMLRH | RLTPPPEESY | SLHRKMAGSF | LICSKLKARF |
610 | 620 | ||||
SCRNMFLDVY | NAYKRQQQER | RSQV |