| Type |
Details |
Score |
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2102
|
| Description: |
Cysteinyl-tRNA synthetase, class Ia family protein; IPR009080 (Aminoacyl-tRNA synthetase, class 1a, anticodon-binding), IPR024909 (Cysteinyl-tRNA synthetase/mycothiol ligase); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004817 (cysteine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006423 (cysteinyl-tRNA aminoacylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5816
|
| Description: |
protein kinase [Glycine max]; IPR011009 (Protein kinase-like domain), IPR013083 (Zinc finger, RING/FYVE/PHD-type), IPR020683 (Ankyrin repeat-containing domain), IPR027370 (RING-type zinc-finger, LisH dimerisation motif); GO:0004672 (protein kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0008270 (zinc ion binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3606
|
| Description: |
respiratory burst oxidase protein F; IPR000778 (Cytochrome b245, heavy chain), IPR011992 (EF-hand domain pair), IPR013130 (Ferric reductase transmembrane component-like domain), IPR017938 (Riboflavin synthase-like beta-barrel); GO:0004601 (peroxidase activity), GO:0005509 (calcium ion binding), GO:0016020 (membrane), GO:0016491 (oxidoreductase activity), GO:0055114 (oxidation-reduction process) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1689
|
| Description: |
Cysteinyl-tRNA synthetase, class Ia family protein; IPR009080 (Aminoacyl-tRNA synthetase, class 1a, anticodon-binding), IPR024909 (Cysteinyl-tRNA synthetase/mycothiol ligase); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004817 (cysteine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006423 (cysteinyl-tRNA aminoacylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2793
|
| Description: |
protein FAR1-RELATED SEQUENCE 7-like isoform X2 [Glycine max]; IPR003657 (DNA-binding WRKY), IPR004330 (FAR1 DNA binding domain), IPR007527 (Zinc finger, SWIM-type), IPR018289 (MULE transposase domain); GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0008270 (zinc ion binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5742
|
| Description: |
protein kinase [Glycine max]; IPR011009 (Protein kinase-like domain), IPR013083 (Zinc finger, RING/FYVE/PHD-type), IPR020683 (Ankyrin repeat-containing domain), IPR027370 (RING-type zinc-finger, LisH dimerisation motif); GO:0004672 (protein kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0008270 (zinc ion binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2198
|
| Description: |
glutamate--tRNA ligase, chloroplastic/mitochondrial-like [Glycine max]; IPR000924 (Glutamyl/glutaminyl-tRNA synthetase); GO:0000049 (tRNA binding), GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004818 (glutamate-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006424 (glutamyl-tRNA aminoacylation), GO:0043039 (tRNA aminoacylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
6048
|
| Description: |
clathrin heavy chain 1-like [Glycine max]; IPR016341 (Clathrin, heavy chain); GO:0005198 (structural molecule activity), GO:0005488 (binding), GO:0005515 (protein binding), GO:0006886 (intracellular protein transport), GO:0016192 (vesicle-mediated transport), GO:0030130 (clathrin coat of trans-Golgi network vesicle), GO:0030132 (clathrin coat of coated pit) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3392
|
| Description: |
Protein kinase superfamily protein; IPR003591 (Leucine-rich repeat, typical subtype), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2770
|
| Description: |
glycyl-tRNA synthetase / glycine--tRNA ligase; IPR009068 (S15/NS1, RNA-binding), IPR027031 (Glycyl-tRNA synthetase/DNA polymerase subunit gamma-2); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004820 (glycine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006426 (glycyl-tRNA aminoacylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3505
|
| Description: |
Protein kinase superfamily protein; IPR001611 (Leucine-rich repeat), IPR003591 (Leucine-rich repeat, typical subtype), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2146
|
| Description: |
lysine--tRNA ligase-like [Glycine max]; IPR018150 (Aminoacyl-tRNA synthetase, class II (D/K/N)-like); GO:0000166 (nucleotide binding), GO:0003676 (nucleic acid binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004824 (lysine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006430 (lysyl-tRNA aminoacylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2041
|
| Description: |
homeobox-leucine zipper protein HAT4 [Glycine max]; IPR003106 (Leucine zipper, homeobox-associated), IPR006712 (HD-ZIP protein, N-terminal), IPR009057 (Homeodomain-like); GO:0000976 (transcription regulatory region sequence-specific DNA binding), GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5852
|
| Description: |
clathrin heavy chain 2-like [Glycine max]; IPR016341 (Clathrin, heavy chain); GO:0005198 (structural molecule activity), GO:0005488 (binding), GO:0005515 (protein binding), GO:0006886 (intracellular protein transport), GO:0016192 (vesicle-mediated transport), GO:0030130 (clathrin coat of trans-Golgi network vesicle), GO:0030132 (clathrin coat of coated pit) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3608
|
| Description: |
Regulator of chromosome condensation (RCC1) family protein; IPR009091 (Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II), IPR011993 (Pleckstrin homology-like domain), IPR013083 (Zinc finger, RING/FYVE/PHD-type), IPR013591 (Brevis radix (BRX) domain), IPR027988 (Transcription factor BREVIS RADIX, N-terminal domain); GO:0046872 (metal ion binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4368
|
| Description: |
respiratory burst oxidase protein F; IPR000778 (Cytochrome b245, heavy chain), IPR011992 (EF-hand domain pair), IPR013130 (Ferric reductase transmembrane component-like domain), IPR017938 (Riboflavin synthase-like beta-barrel); GO:0004601 (peroxidase activity), GO:0005509 (calcium ion binding), GO:0016020 (membrane), GO:0016491 (oxidoreductase activity), GO:0055114 (oxidation-reduction process) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2427
|
| Description: |
receptor-like protein kinase 4; IPR000858 (S-locus glycoprotein), IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0048544 (recognition of pollen) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1733
|
| Description: |
sucrose transport protein [Glycine max]; IPR005828 (General substrate transporter), IPR005989 (Sucrose/H+ symporter, plant); GO:0005887 (integral component of plasma membrane), GO:0008515 (sucrose transmembrane transporter activity), GO:0015770 (sucrose transport), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2623
|
| Description: |
respiratory burst oxidase protein F; IPR000778 (Cytochrome b245, heavy chain), IPR011992 (EF-hand domain pair), IPR013130 (Ferric reductase transmembrane component-like domain), IPR017938 (Riboflavin synthase-like beta-barrel); GO:0004601 (peroxidase activity), GO:0005509 (calcium ion binding), GO:0016020 (membrane), GO:0016491 (oxidoreductase activity), GO:0055114 (oxidation-reduction process) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3603
|
| Description: |
prolyl-tRNA synthetase family protein; IPR002316 (Proline-tRNA ligase, class IIa), IPR017449 (Prolyl-tRNA synthetase, class II); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004827 (proline-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006433 (prolyl-tRNA aminoacylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2819
|
| Description: |
receptor-like protein kinase 4; IPR001611 (Leucine-rich repeat), IPR003591 (Leucine-rich repeat, typical subtype), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2604
|
| Description: |
receptor-like protein kinase 4; IPR000858 (S-locus glycoprotein), IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0048544 (recognition of pollen) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Diaminopimelate epimerase, DapF |
| Type: |
Family |
| Description: |
Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids - lysine, threonine, methionine and isoleucine - in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential component of bacterial cell wall biosynthesis, and dipicolinic acid, which is involved in sporulation in Gram-positive bacteria. Members of the animal kingdom do not posses this pathway and must therefore acquire these essential amino acids through their diet. Research into improving the metabolic flux through this pathway has the potential to increase the yield of the essential amino acids in important crops, thus improving their nutritional value. Additionally, since the enzymes are not present in animals, inhibitors of them are promising targets for the development of novel antibiotics and herbicides. For more information see [
].Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [
].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [
].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This entry represents diaminopimelate epimerase (
), which catalyses the isomerisation of L,L-dimaminopimelate to meso-DAP in the biosynthetic pathway leading from aspartate to lysine. It is a member of the broader family of PLP-independent amino acid racemases. This enzyme is a monomeric protein of about 30kDa consisting of two domains which are homologus in structure though they share little sequence similarity [
]. Each domain consists of mixed β-sheets which fold into a barrel around the central helix. The active site cleft is formed from both domains and contains two conserved cysteines thought to function as the acid and base in the catalytic reaction []. Other PLP-independent racemases such as glutamate racemase have been shown to share a similar structure and mechanism of catalysis. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
ATP synthase, F0 complex, subunit C, DCCD-binding site |
| Type: |
Binding_site |
| Description: |
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [
,
]. The different types include:F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane []. They are also found in bacteria [].A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [
,
].P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.F-ATPases (also known as ATP synthases, F1F0-ATPase, or H(+)-transporting two-sector ATPase) (
) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), with additional subunits in mitochondria. Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [
]. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.Subunit C (also called subunit 9, or proteolipid) is found in the F0 complex of F-ATPases. Ten C subunits form an oligomeric ring that makes up the F0 rotor. The flux of protons through the ATPase channel drives the rotation of the C subunit ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the C subunit ring of F0. The sequential protonation and deprotonation of Asp61 of subunit C is coupled to the stepwise movement of the rotor [
]. Structurally, subunit c consists of two long terminal hydrophobic regions, which probably span the membrane, and a central hydrophilic region. N,N'-dicyclohexylcarbodiimide (DCCD) can bind covalently to subunit c and thereby abolish the ATPase activity. DCCD binds to a specific glutamate or aspartate residue which is located in the middle of the second hydrophobic region near the C terminus of the protein. This entry represents the site that includes the DCCD-binding residue. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Glucose transporter, type 2 (GLUT2) |
| Type: |
Family |
| Description: |
The ability to transport glucose across the plasma membrane is a feature common to nearly all cells, from simple bacteria through to highly specialised mammalian neurones. Facilitative sugar transport is mediated by members of the GLUT transporter family, which form an aqueous pore across the membrane through which sugars can move in a passive (i.e., energy-independent) manner; in consequence, they can only transport sugars down their concentration gradient. The GLUT family of glycosylated transmembrane proteins are predicted to span the membrane 12 times with both amino- and carboxyl-termini located in the cytosol. On the basis of sequence homology and structural similarity, three subclasses of sugar transporters have been defined: Class I (GLUTs 1-4) are glucose transporters; Class II (GLUTs 5, 7, 9 and 11) are fructose transporters; and Class III (GLUTs 6, 8, 10, 12 and HMIT1) are structurally atypical members of the GLUT family, which are poorly defined at present, indeed GLUT6 may only be a pseudo-gene [
,
,
,
,
].The confirmed isoforms are expressed in a tissue and cell-specific manner, and exhibit distinct kinetic and regulatory properties, presumably reflecting their specific functional roles. They belong to a much larger 'major facilitator superfamily' of 12 TM transporters that are involved in the transport of a variety of hexoses and other carbon compounds, and include: bacterial sugar-proton symporters (H
+/xylose and H
+/arabinose); bacterial transporters of carboxylic acids and antibiotics; and sugar transporters in various yeast, protozoa and higher plants. Nevertheless, amino acid identity within the superfamily may be as low as ~25% [
,
]. Besides the 12 presumed TM domains, the most characteristic structural feature of the superfamily is a five residue motif (RXGRR, where X is any amino acid). In the GLUT transporters, this motif is present in the presumed cytoplasmic loops connecting TM domains 2 with 3, and also 8 with 9. The 12 TM transporter superfamily appears to be structurally unrelated to the Na+-coupled, Na
+/glucose co-transporters (SGLT1-3) found in the intestine and kidney, which are able to transport glucose against its concentration gradient [
].Comparison of the hydropathy profiles for GLUT1-5 reveals that they are virtually superimposable, despite the fact that their primary structures may differ by up to 60%. Of the presumed TM domains, the fourth, fifth and sixth are the most highly conserved, and conserved residues are also found in the short exofacial loops joining the putative TM regions. The presumed cytoplasmic N- and C-termini, and the extracellular loop between the first and second TM domains, show the greatest divergence, both in terms of primary structure and size.GLUT2 is the major glucose transporter isoform expressed in hepatocytes,
insulin-secreting pancreatic beta cells, and absorptive epithelial cellsof the intestinal mucosa and kidney. It functions as a low affinity,
high-turnover transport system; together with the enzyme glucokinase, itis thought to act as a glucose-sensing apparatus that plays a role in blood
glucose homeostasis, by responding to changes in blood glucose concentration(such as might occur following a meal) and altering the rate of glucose
uptake into liver cells, where it can be stored as glycogen. It consists of524 amino acids (human isoform) and is ~55% identical to GLUT1 at the amino
acid level. GLUT2 has received attention as a molecule that could beinvolved in the pathogenesis of diabetes mellitus. Reductions in pancreatic
beta cell GLUT2 levels have been observed in several animal models ofdiabetes, as well as human patients; whether this is causative, or an
epiphenomenon remains to be resolved. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Fructose transporter, type 5 (GLUT5) |
| Type: |
Family |
| Description: |
The ability to transport glucose across the plasma membrane is a feature common to nearly all cells, from simple bacteria through to highly specialised mammalian neurones. Facilitative sugar transport is mediated by members of the GLUT transporter family, which form an aqueous pore across the membrane through which sugars can move in a passive (i.e., energy-independent) manner; in consequence, they can only transport sugars down their concentration gradient. The GLUT family of glycosylated transmembrane proteins are predicted to span the membrane 12 times with both amino- and carboxyl-termini located in the cytosol. On the basis of sequence homology and structural similarity, three subclasses of sugar transporters have been defined: Class I (GLUTs 1-4) are glucose transporters; Class II (GLUTs 5, 7, 9 and 11) are fructose transporters; and Class III (GLUTs 6, 8, 10, 12 and HMIT1) are structurally atypical members of the GLUT family, which are poorly defined at present, indeed GLUT6 may only be a pseudo-gene [,
,
,
,
].The confirmed isoforms are expressed in a tissue and cell-specific manner, and exhibit distinct kinetic and regulatory properties, presumably reflecting their specific functional roles. They belong to a much larger 'major facilitator superfamily' of 12 TM transporters that are involved in the transport of a variety of hexoses and other carbon compounds, and include: bacterial sugar-proton symporters (H
+/xylose and H
+/arabinose); bacterial transporters of carboxylic acids and antibiotics; and sugar transporters in various yeast, protozoa and higher plants. Nevertheless, amino acid identity within the superfamily may be as low as ~25% [
,
]. Besides the 12 presumed TM domains, the most characteristic structural feature of the superfamily is a five residue motif (RXGRR, where X is any amino acid). In the GLUT transporters, this motif is present in the presumed cytoplasmic loops connecting TM domains 2 with 3, and also 8 with 9. The 12 TM transporter superfamily appears to be structurally unrelated to the Na+-coupled, Na
+/glucose co-transporters (SGLT1-3) found in the intestine and kidney, which are able to transport glucose against its concentration gradient [
].Comparison of the hydropathy profiles for GLUT1-5 reveals that they are virtually superimposable, despite the fact that their primary structures may differ by up to 60%. Of the presumed TM domains, the fourth, fifth and sixth are the most highly conserved, and conserved residues are also found in the short exofacial loops joining the putative TM regions. The presumed cytoplasmic N- and C-termini, and the extracellular loop between the first and second TM domains, show the greatest divergence, both in terms of primary structure and size.GLUT5 exhibits the weakest inter-isoform similarity of any of the members
of the GLUT family. This is consistent with its identity as a fructoserather than a glucose transporter [
]. It is expressed abundantly in theupper small intestine, where it is located in the epithelial brush border.
Here it likely forms the principal route for dietary fructose uptake. Itis also found in high levels in the plasma membrane of spermatozoa,
consistent with their ability to utilise the fructose in seminal fluid asan energy source. GLUT5 has also been found in the brain endothelium,
muscle and fat cells, although its function in these locations is unknown.It consists of 501 amino acids (human isoform) and shares ~40% amino acid
identity with the other isoforms. |
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| Protein Domain |
| Name: |
ATP synthase-coupling factor 6 superfamily, mitochondrial |
| Type: |
Homologous_superfamily |
| Description: |
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [
,
]. The different types include:F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [
]. They are also found in bacteria [].A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [
,
].P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.F-ATPases (also known as ATP synthases, F1F0-ATPase, or H(+)-transporting two-sector ATPase) (
) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), with additional subunits in mitochondria. Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis []. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.This entry represents subunit F6 (or coupling factor 6) found in the F0 complex of F-ATPases in mitochondria. The F6 subunit is part of the peripheral stalk that links the F1 and F0 complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, B and D [
]. There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and photosynthetic bacteria. F6 has a flexible structure comprising two helices packed together through a loose hydrophobic core and connected by an unstructured linker and a hairpin topology [
]. |
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| Protein Domain |
| Name: |
Pyridoxal-phosphate binding site |
| Type: |
Binding_site |
| Description: |
Pyridoxal phosphate is the active form of vitamin B6 (pyridoxine or pyridoxal). Pyridoxal 5'-phosphate (PLP) is a versatile catalyst, acting as a coenzyme in a multitude of reactions, including decarboxylation, deamination and transamination [
,
,
]. PLP-dependent enzymes are primarily involved in the biosynthesis of amino acids and amino acid-derived metabolites, but they are also found in the biosynthetic pathways of amino sugars and in the synthesis or catabolism of neurotransmitters; pyridoxal phosphate can also inhibit DNA polymerases and several steroid receptors []. Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy [].PLP enzymes exist in their resting state as a Schiff base, the aldehyde group of PLP forming a linkage with the ε-amino group of an active site lysine residue on the enzyme. The α-amino group of the substrate displaces the lysine ε-amino group, in the process forming a new aldimine with the substrate. This aldimine is the common central intermediate for all PLP-catalysed reactions, enzymatic and non-enzymatic [
].A number of pyridoxal-dependent decarboxylases share regions of sequence similarity, particularly in the vicinity of a conserved lysine residue, which provides the attachment site for the pyridoxal-phosphate (PLP) group [
,
]. Among these enzymes are aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase), which catalyses the decarboxylation of tryptophan to tryptamine []; tyrosine decarboxylase, which converts tyrosine into tyramine; histidine decarboxylase, which catalyses the decarboxylation of histidine to histamine []; L-aspartate decarboxylase, which converts aspartate to beta-alanine []; and phenylacetaldehyde synthase that catalyses the decarboxylation of L-phenylalanine to 2-phenylethylamine []. These enzymes belong to the group II decarboxylases [,
].This signature contains the pyridoxal-phosphate-binding lysine residue. Certain pyridoxal-dependent decarboxylases seem to share regions of sequence similarity [
,
,
,
], especially in the vicinity of the lysine residue which serves as the attachment site for the pyridoxal-phosphate (PLP) group. These enzymes, known collectively as group II decarboxylases, are:Glutamate decarboxylase (
) (GAD), which catalyses the decarboxylation of glutamate into the neurotransmitter GABA (4-aminobutanoate).
Histidine decarboxylase (
) (HDC), which catalyses the decarboxylation of histidine to histamine. There are two completely unrelated types of HDC: those that use PLP as a cofactor (found in Gram-negative bacteria and mammals), and those that contain a covalently bound pyruvoyl residue (found in Gram-positive bacteria).
Aromatic-L-amino-acid decarboxylase (
) (DDC), also known as L-dopa decarboxylase or tryptophan decarboxylase, which catalyses the decarboxylation of tryptophan to tryptamine. It also acts on 5-hydroxy-tryptophan and dihydroxyphenylalanine (L-dopa).
Tyrosine decarboxylase (
) (TyrDC), which converts tyrosine into tyramine, a precursor of isoquinoline alkaloids and various amides.
Cysteine sulphinic acid decarboxylase (
).
L-2,4-diaminobutyrate decarboxylase (
) (DABA decarboxylase).
This entry also includes phenylacetaldehyde synthase and 4-hydroxyphenylacetaldehyde synthase from plants and 3,4-dihydroxyphenylacetaldehyde synthase from insects. Plant aromatic acetaldehyde syntheses (AASs) are effectively indistinguishable from plant aromatic amino acid decarboxylases (AAADs) through primary sequence comparison [
]. Proteins of the AAAD family are grouped together as a result of their high homology, pyridoxal-5'-phosphate (PLP) dependence, and aromatic substrate requirements []. Similarly 3,4-dihydroxylphenylacetaldehyde (DHPAA) from Aedes aegypti (Yellowfever mosquito) is classified into the aromatic amino acid decarboxylase (AAAD) family based on extremely high sequence homology (about 70%) with dopa decarboxylase (Ddc) but has been shown to catalyse the production of 3,4-dihydroxylphenylacetaldehyde (DHPAA) directly from L-dopa []. |
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| Protein Domain |
| Name: |
5-hydroxytryptamine 3 receptor, A subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Serotonin (5-hydroxytryptamine, 5-HT) is widely distributed in both the central and peripheral nervous system, where it acts as a neurotransmitter
and neuromodulator []. It has been implicated in several aspects of brain function, including regulation of affective states, ingestive behavior and addiction. 5-HT can activate a number of different receptor subtypes that produce diverse neuronal responses, principally through activation of G-protein-mediated signalling pathways. Signalling through the 5-HT3 receptor (5-HT3R) differs, since this subtype belongs to the ligand-gated ion channel (LGIC) superfamily, which also includes the inhibitory gamma-aminobutyric acid type A and glycine receptors, and excitatory nicotinic acetylcholine receptors (nAChR) []. 5-HT3 receptor function has been implicated in a variety of neural processes, including pain perception, emesis, anxiety and drug abuse.Like the other members of the LGIC superfamily, the 5HT3R exhibits a high degree of sequence similarity, and therefore putative structural similarity, with nAChRs [
]. Thus, functional 5HT3Rs comprise a pentamer: the ion channel is formed at the centre of a rosette formed between five homologous subunits. Two classes of 5-HT3R subunit are currently known, termed 5-HT3A and 5-HT3B. Whilst homomeric pentamers of 5-HT3A form functional receptors, heteromeric assemblies display channel conductances, cation permeabilities and current-voltage relationships typical of characterised neuronal 5-HT3 channels [].The proposed topology of 5-HT3R subunits comprises four putative transmembrane (TM) domains (designated M1-4); a large extracellular N-terminal region (~200 amino acids); and a variable cytoplasmic loop between M3 and M4. The M2 domains from each subunit are thought to form the channel pore. The agonist binding site is formed by the N terminus, which, on binding, induces a conformational change in the channel pore, a process often referred to as "gating"[
]. Opening of the pore allows cation flux through the neuronal membrane and depolarises the membrane potential. Thus, 5-HT3Rs may be thought of as excitatory receptors [].Cloning of the 5-HT3A subunit from a neuroblastoma expression library was
reported in 1991 []. Whilst recombinant expression of 5-HT3A yieldsfunctional receptors, the channel conductance and permeability to cations
are different from that observed for native receptors []. Alternative exonsplicing gives rise to two isoforms of 5-HT3A, termed 5-HT3AS and 5-HT3AL
for short and long variants, respectively. The 5-HT3RA subunit is widelyexpressed throughout the peripheral and central nervous systems, includingseveral regions of the brain.
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| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, alpha 5 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [
].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Amongst type II members, alpha 5-containing receptors exhibit an altered BZselectivity. Affinity towards the compound zolpidem distinguishes alpha 5
from alpha 2- and alpha 3-containing receptor subtypes []. The alpha 5subunit is expressed primarily in the hippocampus.
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| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, alpha 4 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Alpha 4- and 6-containing receptors are often referred to as `diazepam- insensitive' receptors, since inclusion of such subunits in place of type I and II polypeptides virtually eliminates sensitivity to BZs. The alpha 4 receptor subtype is localised primarily in the thalamus []. |
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| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, alpha 1 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. The alpha 1 subunit is the most widely expressed of the alpha family members
and most commonly found in receptors comprising a gamma 2 and beta subunits.Such subtypes display `classical' BZ affinity and efficacy.
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| Protein Domain |
| Name: |
Phosphotransferase system, EIIB component, type 3 |
| Type: |
Domain |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [
,
] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates and coupled with translocation across the cell membrane, makes the PTS a link between the uptake and metabolism of sugars.The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred via a signal transduction pathway, to enzyme I (EI) which in turn transfers it to a phosphoryl carrier, the histidine protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease, a membrane-bound complex known as enzyme 2 (EII), which transports the sugar to the cell. EII consists of at least three structurally distinct domains IIA, IIB and IIC [
]. These can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII). The first domain (IIA or EIIA) carries the first permease-specific phosphorylation site, a histidine which is phosphorylated by phospho-HPr. The second domain (IIB or EIIB) is phosphorylated by phospho-IIA on a cysteinyl or histidyl residue, depending on the sugar transported. Finally, the phosphoryl group is transferred from the IIB domain to the sugar substrate concomitantly with the sugar uptake processed by the IIC domain. This third domain (IIC or EIIC) forms the translocation channel and the specific substrate-binding site. An additional transmembrane domain IID, homologous to IIC, can be found in some PTSs, e.g. for mannose [
,
,
,
]. According to structural and sequence analyses, the PTS EIIB domain (
) can be divided in five groups [
,
,
]: The PTS EIIB type 1 domain, which is found in the Glucose class of PTS, has an average length of about 80 amino acids. It forms a split alpha/beta sandwich composed of an antiparallel sheet (beta 1 to beta 4) and three alpha helices superimposed onto one side of the sheet. The phosphorylation site (Cys) is located at the end of the first beta strand on a protrusion formed by the edge of beta 1 and the reverse turn between beta 1 and beta 2 [].The PTS EIIB type 2 domain, which is found in the Mannitol and Fructose class of PTS, has an average length of about 100 amino acids. It consists of a four stranded parallel beta sheet flanked by two alpha helices (alpha 1 and 3) on one face and helix alpha 2 on the opposite face, with a characteristic Rossmann fold comprising two right-handed beta-α-β motifs. The phosphorylation site (Cys) is located at the N terminus of the domain, in the first beta strand. The PTS EIIB type 3 domain, which is found in the Lactose class of PTS, has an average length of about 100 amino acids. It is composed of a central four-stranded parallel open twisted beta sheet, which is flanked by three alpha helices on the concave side and two on the convex side of the beta sheet. The phosphorylation site (Cys) is located in the C-terminal end of the first beta strand [
].The PTS EIIB type 4 domain, which is found in the Mannose class of PTS, has an average length of about 160 amino acids. It has a central core of seven parallel beta strands surrounded by a total of six α-helices. Three helices cover the front face, one the back face with the remaining two capping the central beta sheet at the top and bottom. The phosphorylation site (His) is located at the suface exposed loop between strand 1 and helix 1 [
]. The PTS EIIB type 5 domain, which is found in the Sorbitol class of PTS, has an average length of about 190 amino acids. The phosphorylation site (Cys) is located in the N terminus of the domain. The EIIB type 3 domain is often found downstream of the EIIC type 3 domain. |
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|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor epsilon subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. The epsilon subunit was first identified in 1997. Northern blot analysis of several human
brain tissues showed that epsilon transcripts were relatively enriched inamygdala and thalamus, compared to whole brain, and particularly abundant in
the subthalmic nucleus. Heteromeric recombinant receptors containing theepsilon subunit in place of the more usual gamma subunit were found to be insenstitive to the potentiating effects ofanaesthetic agents [
]. |
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•
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•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor delta subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Delta cDNA was first reported in rat, mouse and humans [
]. Delta mRNAwas found to be present in regions of the brain that were low in gamma 2,
and insensitivity towards "classical"BZs was observed in receptors
containing the delta subunit. Furthermore, delta subunits are thought to preferentially pair with the alpha 6 polypeptides over other subtypes, and are often found in place of gamma subunits.
|
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|
| Protein Domain |
| Name: |
5-hydroxytryptamine 3 receptor, B subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Serotonin (5-hydroxytryptamine, 5-HT) is widely distributed in both the central and peripheral nervous system, where it acts as a neurotransmitter
and neuromodulator []. It has been implicated in several aspects of brain function, including regulation of affective states, ingestive behavior and addiction. 5-HT can activate a number of different receptor subtypes that produce diverse neuronal responses, principally through activation of G-protein-mediated signalling pathways. Signalling through the 5-HT3 receptor (5-HT3R) differs, since this subtype belongs to the ligand-gated ion channel (LGIC) superfamily, which also includes the inhibitory gamma-aminobutyric acid type A and glycine receptors, and excitatory nicotinic acetylcholine receptors (nAChR) []. 5-HT3 receptor function has been implicated in a variety of neural processes, including pain perception, emesis, anxiety and drug abuse.Like the other members of the LGIC superfamily, the 5HT3R exhibits a high degree of sequence similarity, and therefore putative structural similarity, with nAChRs [
]. Thus, functional 5HT3Rs comprise a pentamer: the ion channel is formed at the centre of a rosette formed between five homologous subunits. Two classes of 5-HT3R subunit are currently known, termed 5-HT3A and 5-HT3B. Whilst homomeric pentamers of 5-HT3A form functional receptors, heteromeric assemblies display channel conductances, cation permeabilities and current-voltage relationships typical of characterised neuronal 5-HT3 channels [].The proposed topology of 5-HT3R subunits comprises four putative transmembrane (TM) domains (designated M1-4); a large extracellular N-terminal region (~200 amino acids); and a variable cytoplasmic loop between M3 and M4. The M2 domains from each subunit are thought to form the channel pore. The agonist binding site is formed by the N terminus, which, on binding, induces a conformational change in the channel pore, a process often referred to as "gating"[
]. Opening of the pore allows cation flux through the neuronal membrane and depolarises the membrane potential. Thus, 5-HT3Rs may be thought of as excitatory receptors [].Whilst it was initially thought that 5-HT3Rs comprised a homopentamer of
alpha subunits, the channel conductance and permeability to anions wasdifferent in homomeric receptors from that observed in native channels. More
recently, another 5-HT3 receptor subunit, 5-HT3B, was identified and clonedfrom a human brain cDNA library [
]. This subunit was unable to formfunctional channels when expressed alone in oocytes, but produced functional
receptors when injected with 5-HT3A into the same cell. It is thought that5HT3B contributes towards tissue-specific functional changes in
5-HT3-mediated signalling []. |
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|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor theta subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Identification and characterisation of the theta subunit was first reported
in 1999 [
]. Cloning of the full-length cDNA was performed using a humanwhole-brain library, yielding a deduced open reading frame of 627 amino
acids. This polypeptide was found to be most similar to the beta 1 subunitwith regard to sequence identity, and was able to co-assemble with alpha 2,
beta 1 and gamma 1 subunits, yielding heteromeric assemblies with a 4-foldincrease in sensitivity towards GABA. Furthermore, theta mRNA was found
to have a unique spatial distribution, with significant expression withinmonoaminergic neurons of both human and monkey brain.
|
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•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor pi subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. The existence of a pi subunit was first reported in 1997, where it was
detected in a number of human and rat tissues. The subunit shares 30-40%amino acid identity with other members of the GABAA receptor subunit family.
The polypeptide is found in several peripheral tissues, including theuterus, where its function appears to be related to tissue contractility: pi
subunits can co-assemble with other GABAA receptor subunits to formrecombinant receptors with altered sensitivity to pregnenalone [
]. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, alpha subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Alpha subunits
largely determine benzodiazepine binding properties []. Mutagenesis and agonist/antagonist binding studies have suggested a close functional and structural association of alpha-subunits with the agonist/antagonist binding site, and involvement of N-terminal portions of the extracellular domains of all subunits in the gating of the channel []. |
|
•
•
•
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•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, alpha 6 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Alpha 4- and 6-containing receptors are often referred to as `diazepam-
insensitive' receptors, since inclusion of such subunits in place of type Iand II polypeptides virtually eliminates sensitivity to BZs. The alpha 6
subunit is found exclusively in the cerebellar granule cells. It alsoundergoes alternative splicing, generating a non-functional isoform that
lacks 10 residues from the N-terminal domain [Ashcroft, F.M.GABA(A) Receptors. In Ion Channels and Disease. Academic Press 2000, PP.325-336.]. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, alpha 3 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity [
]. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Amongst type II members, alpha 2-containing receptors have a very similar BZaffinity profile to those containing the alpha 3 subunit. Differences in
efficacy can be exploited to differentiate such subtypes: for example, thecompound flunitrazepam has a greater efficacy on the alpha 2 subtype. Alpha
3-containing receptors are less widely distributed and are found primarilyin the cerebellum granule layer [
]. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, alpha 2 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Amongst type II members, alpha 2-containing receptors have a very similar BZaffinity profile to those containing the alpha 3 subunit. Differences in
efficacy can be exploited to differentiate such subtypes: for example, thecompound flunitrazepam has a greater efficacy on the alpha 2 subtype. Alpha
2-containing receptors are widely distributed throughout the CNS and arealso found in some motor neurones and the pancreas [
]. |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3734
|
| Description: |
putative transcription elongation factor SPT5 homolog 1-like isoform X2 [Glycine max]; IPR008991 (Translation protein SH3-like domain), IPR017071 (Transcription elongation factor Spt5); GO:0003735 (structural constituent of ribosome), GO:0005622 (intracellular), GO:0005840 (ribosome), GO:0006357 (regulation of transcription from RNA polymerase II promoter), GO:0006412 (translation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4145
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR010544 (Kinesin-related conserved domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3189
|
| Description: |
protein kinase family protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3319
|
| Description: |
Protein kinase superfamily protein; IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR023413 (Green fluorescent protein-like), IPR025287 (Wall-associated receptor kinase galacturonan-binding domain); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0030247 (polysaccharide binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
7117
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1610
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
6029
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1666
|
| Description: |
Glycine cleavage T-protein family; IPR006222 (Glycine cleavage T-protein, N-terminal), IPR013977 (Glycine cleavage T-protein, C-terminal barrel), IPR017703 (YgfZ/GcvT conserved site), IPR027266 (GTP-binding protein TrmE/Glycine cleavage system T protein, domain 1); GO:0004047 (aminomethyltransferase activity), GO:0005515 (protein binding), GO:0005737 (cytoplasm), GO:0006546 (glycine catabolic process) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4790
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3493
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3396
|
| Description: |
Protein kinase superfamily protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4721
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3914
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR010544 (Kinesin-related conserved domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3551
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1898
|
| Description: |
magnesium transporter 9; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3504
|
| Description: |
disease resistance protein (TIR-NBS-LRR class), putative; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4719
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1963
|
| Description: |
magnesium transporter 6; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2126
|
| Description: |
GTP binding Elongation factor Tu family protein; IPR004541 (Translation elongation factor EFTu/EF1A, bacterial/organelle), IPR005225 (Small GTP-binding protein domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0003746 (translation elongation factor activity), GO:0003924 (GTPase activity), GO:0005525 (GTP binding), GO:0005622 (intracellular), GO:0006414 (translational elongation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2487
|
| Description: |
phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN-like isoform X2 [Glycine max]; IPR000008 (C2 domain), IPR014019 (Phosphatase tensin type); GO:0004725 (protein tyrosine phosphatase activity), GO:0005515 (protein binding), GO:0006470 (protein dephosphorylation), GO:0008138 (protein tyrosine/serine/threonine phosphatase activity), GO:0016311 (dephosphorylation), GO:0016791 (phosphatase activity) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3307
|
| Description: |
kinesin-related protein 11-like isoform X1 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR010994 (RuvA domain 2-like), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3430
|
| Description: |
disease resistance protein (TIR-NBS-LRR class), putative; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2768
|
| Description: |
magnesium (Mg) transporter 10; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1796
|
| Description: |
magnesium transporter 9; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1841
|
| Description: |
GTP binding Elongation factor Tu family protein; IPR004541 (Translation elongation factor EFTu/EF1A, bacterial/organelle), IPR005225 (Small GTP-binding protein domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0003746 (translation elongation factor activity), GO:0003924 (GTPase activity), GO:0005525 (GTP binding), GO:0005622 (intracellular), GO:0006414 (translational elongation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1404
|
| Description: |
magnesium transporter 3; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2107
|
| Description: |
magnesium transporter 2; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
6117
|
| Description: |
dedicator of cytokinesis protein 7-like isoform X1 [Glycine max]; IPR010703 (Dedicator of cytokinesis C-terminal), IPR016024 (Armadillo-type fold), IPR026791 (Dedicator of cytokinesis), IPR027007 (DHR-1 domain), IPR027357 (DHR-2 domain); GO:0005085 (guanyl-nucleotide exchange factor activity), GO:0005488 (binding), GO:0007264 (small GTPase mediated signal transduction) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4640
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
5642
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3126
|
| Description: |
protein kinase family protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1945
|
| Description: |
magnesium transporter 9; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1988
|
| Description: |
receptor-like protein kinase 2; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1323
|
| Description: |
magnesium transporter 4; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2599
|
| Description: |
signal recognition particle subunit SRP72-like [Glycine max]; IPR011990 (Tetratricopeptide-like helical), IPR013699 (Signal recognition particle, SRP72 subunit, RNA-binding), IPR026270 (Signal recognition particle, SRP72 subunit); GO:0005515 (protein binding), GO:0006614 (SRP-dependent cotranslational protein targeting to membrane), GO:0008312 (7S RNA binding), GO:0048500 (signal recognition particle) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
646
|
| Description: |
signal recognition particle 9 kDa protein-like [Glycine max]; IPR008832 (Signal recognition particle, SRP9 subunit), IPR009018 (Signal recognition particle, SRP9/SRP14 subunit); GO:0006614 (SRP-dependent cotranslational protein targeting to membrane), GO:0008312 (7S RNA binding), GO:0045900 (negative regulation of translational elongation), GO:0048500 (signal recognition particle) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3598
|
| Description: |
protein kinase family protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3303
|
| Description: |
Protein kinase superfamily protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3686
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2622
|
| Description: |
receptor-like protein kinase 1; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004713 (protein tyrosine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2778
|
| Description: |
magnesium (Mg) transporter 10; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3336
|
| Description: |
Protein kinase family protein; IPR011009 (Protein kinase-like domain), IPR013032 (EGF-like, conserved site), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR025287 (Wall-associated receptor kinase galacturonan-binding domain); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0030247 (polysaccharide binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2800
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3725
|
| Description: |
receptor-like protein kinase 2; IPR001611 (Leucine-rich repeat), IPR003591 (Leucine-rich repeat, typical subtype), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR025875 (Leucine rich repeat 4); GO:0004672 (protein kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1049
|
| Description: |
lysine--tRNA ligase-like [Glycine max]; IPR004087 (K Homology domain), IPR018150 (Aminoacyl-tRNA synthetase, class II (D/K/N)-like); GO:0000166 (nucleotide binding), GO:0003723 (RNA binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004824 (lysine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006430 (lysyl-tRNA aminoacylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2372
|
| Description: |
receptor-like protein kinase 4; IPR001611 (Leucine-rich repeat), IPR003591 (Leucine-rich repeat, typical subtype), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2239
|
| Description: |
probable 26S proteasome non-ATPase regulatory subunit 3-like [Glycine max]; IPR000717 (Proteasome component (PCI) domain), IPR013143 (PCI/PINT associated module), IPR013586 (26S proteasome regulatory subunit, C-terminal); GO:0000502 (proteasome complex), GO:0005515 (protein binding), GO:0030234 (enzyme regulator activity), GO:0042176 (regulation of protein catabolic process) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5453
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3877
|
| Description: |
kinesin-related protein 11-like isoform X1 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR010544 (Kinesin-related conserved domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1152
|
| Description: |
LOW QUALITY PROTEIN: oxygen-evolving enhancer protein 3, chloroplastic-like [Glycine max]; IPR008797 (Photosystem II PsbQ, oxygen evolving complex), IPR023222 (PsbQ-like domain); GO:0005509 (calcium ion binding), GO:0009523 (photosystem II), GO:0009654 (photosystem II oxygen evolving complex), GO:0015979 (photosynthesis), GO:0019898 (extrinsic component of membrane) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2319
|
| Description: |
ATP binding/protein serine/threonine kinase [Glycine max]; IPR001368 (TNFR/NGFR cysteine-rich region), IPR009091 (Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II), IPR011009 (Protein kinase-like domain); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2793
|
| Description: |
receptor-like protein kinase 2; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
6120
|
| Description: |
dedicator of cytokinesis protein 7-like isoform X1 [Glycine max]; IPR010703 (Dedicator of cytokinesis C-terminal), IPR016024 (Armadillo-type fold), IPR026791 (Dedicator of cytokinesis), IPR027007 (DHR-1 domain), IPR027357 (DHR-2 domain); GO:0005085 (guanyl-nucleotide exchange factor activity), GO:0005488 (binding), GO:0007264 (small GTPase mediated signal transduction) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
687
|
| Description: |
anaphase-promoting complex subunit 4; IPR015943 (WD40/YVTN repeat-like-containing domain), IPR024789 (Anaphase-promoting complex subunit 4), IPR024977 (Anaphase-promoting complex subunit 4, WD40 domain); GO:0005515 (protein binding), GO:0005680 (anaphase-promoting complex), GO:0030071 (regulation of mitotic metaphase/anaphase transition), GO:0031145 (anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5403
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3368
|
| Description: |
Protein kinase superfamily protein; IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR023413 (Green fluorescent protein-like), IPR025287 (Wall-associated receptor kinase galacturonan-binding domain); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0030247 (polysaccharide binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4003
|
| Description: |
putative transcription elongation factor SPT5 homolog 1-like isoform X2 [Glycine max]; IPR008991 (Translation protein SH3-like domain), IPR017071 (Transcription elongation factor Spt5); GO:0003735 (structural constituent of ribosome), GO:0005622 (intracellular), GO:0005840 (ribosome), GO:0006357 (regulation of transcription from RNA polymerase II promoter), GO:0006412 (translation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4993
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
