| Type |
Details |
Score |
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3297
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1236
|
| Description: |
probable tyrosine--tRNA ligase, mitochondrial-like [Glycine max]; IPR002305 (Aminoacyl-tRNA synthetase, class Ic); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004831 (tyrosine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006437 (tyrosyl-tRNA aminoacylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4576
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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: |
2197
|
| Description: |
CBL-interacting serine/threonine-protein kinase 8-like [Glycine max]; IPR011009 (Protein kinase-like domain), IPR015661 (Mitotic checkpoint serine/threonine protein kinase Bub1/Mitotic spindle checkpoint component Mad3); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4695
|
| Description: |
protein timeless homolog [Glycine max]; IPR000394 (RNA polymerase sigma factor 54), IPR006906 (Timeless protein), IPR007725 (Timeless C-terminal); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0003899 (DNA-directed RNA polymerase activity), GO:0016987 (sigma factor activity) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3416
|
| Description: |
receptor-like protein kinase 4; IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR024171 (S-receptor-like serine/threonine-protein kinase); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3340
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4059
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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: |
5148
|
| Description: |
ARF guanine-nucleotide exchange factor GNOM-like isoform X2 [Glycine max]; IPR000904 (Sec7 domain), IPR016024 (Armadillo-type fold), IPR023394 (Sec7 domain, alpha orthogonal bundle); GO:0005086 (ARF guanyl-nucleotide exchange factor activity), GO:0005488 (binding), GO:0032012 (regulation of ARF protein signal transduction) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1942
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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: |
3791
|
| Description: |
ribonuclease E/G-like protein, chloroplastic-like [Glycine max]; IPR012340 (Nucleic acid-binding, OB-fold), IPR013783 (Immunoglobulin-like fold), IPR013784 (Carbohydrate-binding-like fold), IPR019307 (RNA-binding protein AU-1/Ribonuclease E/G); GO:0003723 (RNA binding), GO:0004540 (ribonuclease activity), GO:0006396 (RNA processing), GO:0030246 (carbohydrate binding), GO:2001070 (starch binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
10858
|
| Description: |
BEACH domain-containing protein lvsC-like isoform X5 [Glycine max]; IPR000409 (BEACH domain), IPR008985 (Concanavalin A-like lectin/glucanases superfamily), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR015943 (WD40/YVTN repeat-like-containing domain), IPR016024 (Armadillo-type fold), IPR023362 (PH-BEACH domain); GO:0005488 (binding), GO:0005515 (protein binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3012
|
| Description: |
subtilisin-like protease-like [Glycine max]; IPR015500 (Peptidase S8, subtilisin-related), IPR023827 (Peptidase S8, subtilisin, Asp-active site), IPR023828 (Peptidase S8, subtilisin, Ser-active site); GO:0004252 (serine-type endopeptidase activity), GO:0006508 (proteolysis), GO:0042802 (identical protein binding), GO:0043086 (negative regulation of catalytic activity) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
877
|
| Description: |
psbQ-like protein 2, 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: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2056
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
534
|
| Description: |
threonine--tRNA ligase, mitochondrial-like [Glycine max]; IPR002314 (Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain), IPR011009 (Protein kinase-like domain); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0005524 (ATP binding), GO:0006418 (tRNA aminoacylation for protein translation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2460
|
| Description: |
receptor-like protein kinase 4; IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR024171 (S-receptor-like serine/threonine-protein kinase); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2678
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1971
|
| Description: |
Protein kinase superfamily protein; IPR008985 (Concanavalin A-like lectin/glucanases superfamily), 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:0030246 (carbohydrate binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4748
|
| Description: |
DNA repair protein REV1-like isoform X2 [Glycine max]; IPR012112 (DNA repair protein, Rev1), IPR022880 (DNA polymerase IV); GO:0000287 (magnesium ion binding), GO:0003684 (damaged DNA binding), GO:0003887 (DNA-directed DNA polymerase activity), GO:0006281 (DNA repair), GO:0016779 (nucleotidyltransferase activity) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3798
|
| Description: |
ribonuclease E/G-like protein, chloroplastic-like [Glycine max]; IPR012340 (Nucleic acid-binding, OB-fold), IPR013783 (Immunoglobulin-like fold), IPR013784 (Carbohydrate-binding-like fold), IPR019307 (RNA-binding protein AU-1/Ribonuclease E/G); GO:0003723 (RNA binding), GO:0004540 (ribonuclease activity), GO:0006396 (RNA processing), GO:0030246 (carbohydrate binding), GO:2001070 (starch binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3280
|
| Description: |
receptor-like protein kinase 4; IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR024171 (S-receptor-like serine/threonine-protein kinase); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4600
|
| Description: |
protein kinase family protein; IPR004154 (Anticodon-binding), IPR011009 (Protein kinase-like domain), IPR016135 (Ubiquitin-conjugating enzyme/RWD-like), IPR024435 (Histidyl tRNA synthetase-related domain); 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 arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1974
|
| Description: |
Protein kinase superfamily protein; IPR008985 (Concanavalin A-like lectin/glucanases superfamily), 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:0030246 (carbohydrate binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4628
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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: |
3363
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2651
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2061
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X1 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2145
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2529
|
| Description: |
Homeobox-leucine zipper family protein / lipid-binding START domain-containing protein; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR013978 (MEKHLA), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4713
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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: |
1140
|
| Description: |
receptor-like protein kinase 4; IPR006121 (Heavy metal-associated domain, HMA), IPR011009 (Protein kinase-like domain); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0030001 (metal ion transport), GO:0046872 (metal ion binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1927
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4582
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1053
|
| Description: |
psbQ-like protein 2, 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2166
|
| Description: |
CBL-interacting serine/threonine-protein kinase 8-like [Glycine max]; IPR011009 (Protein kinase-like domain), IPR015661 (Mitotic checkpoint serine/threonine protein kinase Bub1/Mitotic spindle checkpoint component Mad3); 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: |
3799
|
| Description: |
ribonuclease E/G-like protein, chloroplastic-like [Glycine max]; IPR012340 (Nucleic acid-binding, OB-fold), IPR013783 (Immunoglobulin-like fold), IPR013784 (Carbohydrate-binding-like fold), IPR019307 (RNA-binding protein AU-1/Ribonuclease E/G); GO:0003723 (RNA binding), GO:0004540 (ribonuclease activity), GO:0006396 (RNA processing), GO:0030246 (carbohydrate binding), GO:2001070 (starch binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4651
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1196
|
| Description: |
lon protease 2; IPR020568 (Ribosomal protein S5 domain 2-type fold), IPR027065 (Lon protease), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0004176 (ATP-dependent peptidase activity), GO:0004252 (serine-type endopeptidase activity), GO:0005524 (ATP binding), GO:0006508 (proteolysis), GO:0030163 (protein catabolic process) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2226
|
| Description: |
receptor-like protein kinase 4; IPR008985 (Concanavalin A-like lectin/glucanases superfamily), 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:0030246 (carbohydrate binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
708
|
| Description: |
Unknown protein; IPR002541 (Cytochrome c assembly protein), IPR003557 (Cytochrome c-type biogenesis protein CcmC); GO:0006461 (protein complex assembly), GO:0008535 (respiratory chain complex IV assembly), GO:0015232 (heme transporter activity), GO:0015886 (heme transport), GO:0016020 (membrane), GO:0017004 (cytochrome complex assembly) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3986
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4152
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2884
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3037
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X4 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
708
|
| Description: |
Unknown protein; IPR002541 (Cytochrome c assembly protein), IPR003557 (Cytochrome c-type biogenesis protein CcmC); GO:0006461 (protein complex assembly), GO:0008535 (respiratory chain complex IV assembly), GO:0015232 (heme transporter activity), GO:0015886 (heme transport), GO:0016020 (membrane), GO:0017004 (cytochrome complex assembly) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1802
|
| Description: |
coatomer subunit delta [Glycine max]; IPR011012 (Longin-like domain), IPR027059 (Coatomer delta subunit), IPR028565 (Mu homology domain); GO:0005515 (protein binding), GO:0006810 (transport), GO:0006886 (intracellular protein transport), GO:0016192 (vesicle-mediated transport), GO:0030126 (COPI vesicle coat), GO:0030131 (clathrin adaptor complex) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2189
|
| Description: |
coatomer subunit delta [Glycine max]; IPR011012 (Longin-like domain), IPR027059 (Coatomer delta subunit), IPR028565 (Mu homology domain); GO:0005515 (protein binding), GO:0006810 (transport), GO:0006886 (intracellular protein transport), GO:0016192 (vesicle-mediated transport), GO:0030126 (COPI vesicle coat), GO:0030131 (clathrin adaptor complex) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1389
|
| Description: |
Unknown protein; IPR002035 (von Willebrand factor, type A), IPR006896 (Sec23/Sec24, trunk domain), IPR006900 (Sec23/Sec24, helical domain), IPR007123 (Gelsolin domain), IPR012990 (Sec23/Sec24 beta-sandwich); GO:0006886 (intracellular protein transport), GO:0006888 (ER to Golgi vesicle-mediated transport), GO:0030127 (COPII vesicle coat) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4156
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3328
|
| Description: |
subtilisin-like protease-like [Glycine max]; IPR015500 (Peptidase S8, subtilisin-related), IPR023827 (Peptidase S8, subtilisin, Asp-active site), IPR023828 (Peptidase S8, subtilisin, Ser-active site); GO:0004252 (serine-type endopeptidase activity), GO:0006508 (proteolysis), GO:0042802 (identical protein binding), GO:0043086 (negative regulation of catalytic activity) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1650
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X1 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4537
|
| Description: |
uncharacterized protein LOC100818519 isoform X1 [Glycine max]; IPR003591 (Leucine-rich repeat, typical subtype), IPR016024 (Armadillo-type fold), IPR016035 (Acyl transferase/acyl hydrolase/lysophospholipase), IPR025875 (Leucine rich repeat 4); GO:0005488 (binding), GO:0005515 (protein binding), GO:0006629 (lipid metabolic process), GO:0008152 (metabolic process) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4651
|
| Description: |
protein kinase family protein; IPR004154 (Anticodon-binding), IPR011009 (Protein kinase-like domain), IPR016135 (Ubiquitin-conjugating enzyme/RWD-like), IPR024435 (Histidyl tRNA synthetase-related domain); 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4525
|
| Description: |
DNA repair protein REV1-like isoform X2 [Glycine max]; IPR012112 (DNA repair protein, Rev1), IPR022880 (DNA polymerase IV); GO:0000287 (magnesium ion binding), GO:0003684 (damaged DNA binding), GO:0003887 (DNA-directed DNA polymerase activity), GO:0006281 (DNA repair), GO:0016779 (nucleotidyltransferase activity) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2644
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4617
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2463
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4639
|
| Description: |
protein kinase family protein; IPR004154 (Anticodon-binding), IPR011009 (Protein kinase-like domain), IPR016135 (Ubiquitin-conjugating enzyme/RWD-like), IPR024435 (Histidyl tRNA synthetase-related domain); 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: |
416
|
| Description: |
clathrin heavy chain 2-like [Glycine max]; IPR016025 (Clathrin, heavy chain, linker/propeller domain); GO:0005198 (structural molecule activity), 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 echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4466
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
708
|
| Description: |
Unknown protein; IPR002541 (Cytochrome c assembly protein), IPR003557 (Cytochrome c-type biogenesis protein CcmC); GO:0006461 (protein complex assembly), GO:0008535 (respiratory chain complex IV assembly), GO:0015232 (heme transporter activity), GO:0015886 (heme transport), GO:0016020 (membrane), GO:0017004 (cytochrome complex assembly) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3225
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2140
|
| Description: |
Protein kinase superfamily protein; IPR008985 (Concanavalin A-like lectin/glucanases superfamily), 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:0030246 (carbohydrate binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
11504
|
| Description: |
BEACH domain-containing protein lvsC-like isoform X5 [Glycine max]; IPR000409 (BEACH domain), IPR008985 (Concanavalin A-like lectin/glucanases superfamily), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR015943 (WD40/YVTN repeat-like-containing domain), IPR016024 (Armadillo-type fold), IPR023362 (PH-BEACH domain); GO:0005488 (binding), GO:0005515 (protein binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2265
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
858
|
| Description: |
psbQ-like protein 1, 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2980
|
| Description: |
receptor-like protein kinase 4; IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR024171 (S-receptor-like serine/threonine-protein kinase); 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: |
2813
|
| Description: |
zinc finger CCCH domain-containing protein 44-like isoform X1 [Glycine max]; IPR003121 (SWIB/MDM2 domain), IPR003169 (GYF), IPR004343 (Plus-3), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0003677 (DNA binding), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0008270 (zinc ion binding), GO:0016570 (histone modification) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
708
|
| Description: |
Unknown protein; IPR002541 (Cytochrome c assembly protein), IPR003557 (Cytochrome c-type biogenesis protein CcmC); GO:0006461 (protein complex assembly), GO:0008535 (respiratory chain complex IV assembly), GO:0015232 (heme transporter activity), GO:0015886 (heme transport), GO:0016020 (membrane), GO:0017004 (cytochrome complex assembly) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3024
|
| Description: |
uncharacterized protein LOC100808415 isoform X4 [Glycine max]; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR002182 (NB-ARC), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
708
|
| Description: |
Unknown protein; IPR002541 (Cytochrome c assembly protein), IPR003557 (Cytochrome c-type biogenesis protein CcmC); GO:0006461 (protein complex assembly), GO:0008535 (respiratory chain complex IV assembly), GO:0015232 (heme transporter activity), GO:0015886 (heme transport), GO:0016020 (membrane), GO:0017004 (cytochrome complex assembly) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2478
|
| Description: |
receptor-like protein kinase 4; IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR024171 (S-receptor-like serine/threonine-protein kinase); 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: |
855
|
| Description: |
BEST Arabidopsis thaliana protein match is: Galact s in 8 species: Archae - 0; Bacteria - 0; Metazoa - 0; Fungi - 0; Plants - 30; Viruses - 0; Other Eukaryotes - 0 (source: NCBI BLink). |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3530
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2143
|
| Description: |
coatomer subunit delta [Glycine max]; IPR011012 (Longin-like domain), IPR027059 (Coatomer delta subunit), IPR028565 (Mu homology domain); GO:0005515 (protein binding), GO:0006810 (transport), GO:0006886 (intracellular protein transport), GO:0016192 (vesicle-mediated transport), GO:0030126 (COPI vesicle coat), GO:0030131 (clathrin adaptor complex) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2681
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor 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 reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2099
|
| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
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| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2464
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| Description: |
homeobox-leucine zipper protein ANTHOCYANINLESS 2-like isoform X2 [Glycine max]; IPR002913 (START domain), IPR009057 (Homeodomain-like), IPR023393 (START-like domain); GO:0003677 (DNA binding), GO:0003700 (sequence-specific DNA binding transcription factor activity), GO:0005634 (nucleus), GO:0008289 (lipid binding), GO:0043565 (sequence-specific DNA binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
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| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4734
|
| Description: |
ARF guanine-nucleotide exchange factor GNOM-like isoform X2 [Glycine max]; IPR000904 (Sec7 domain), IPR016024 (Armadillo-type fold), IPR023394 (Sec7 domain, alpha orthogonal bundle); GO:0005086 (ARF guanyl-nucleotide exchange factor activity), GO:0005488 (binding), GO:0032012 (regulation of ARF protein signal transduction) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
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| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2912
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| Description: |
subtilisin-like protease-like [Glycine max]; IPR015500 (Peptidase S8, subtilisin-related), IPR023827 (Peptidase S8, subtilisin, Asp-active site), IPR023828 (Peptidase S8, subtilisin, Ser-active site); GO:0004252 (serine-type endopeptidase activity), GO:0006508 (proteolysis), GO:0042802 (identical protein binding), GO:0043086 (negative regulation of catalytic activity) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
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| Protein Domain |
| Name: |
DNA topoisomerase, type IIA, conserved site |
| Type: |
Conserved_site |
| Description: |
DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single- or double-strand breaks, crossing the strands through one another, then resealing the breaks [
]. These enzymes have several functions: to remove DNA supercoils during transcription and DNA replication; for strand breakage during recombination; for chromosome condensation; and to disentangle intertwined DNA during mitosis [,
]. DNA topoisomerases are divided into two classes: type I enzymes (; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (
; topoisomerases II, IV and VI) break double-strand DNA [
].Type II topoisomerases are ATP-dependent enzymes, and can be subdivided according to their structure and reaction mechanisms: type IIA (topoisomerase II or gyrase, and topoisomerase IV) and type IIB (topoisomerase VI). These enzymes are responsible for relaxing supercoiled DNA as well as for introducing both negative and positive supercoils [
].DNA topoisomerase II (
) [
,
,
] is one of the two types of enzyme that catalyze the interconversion of topological DNA isomers. Type II topoisomerases are ATP-dependent and act by passing a DNA segment through a transient double-strand break. Topoisomerase II is found in phages, archaebacteria, prokaryotes, eukaryotes, and in African Swine Fever virus (ASF). Bacteriophage T4 topoisomerase II consists of three subunits (the product of genes 39, 52 and 60). In prokaryotes and in archaebacteria the enzyme, known as DNA gyrase, consists of two subunits (genes GyrA and GyrB). In some bacteria, a second type II topoisomerase has been identified; it is known as topoisomerase IV and is required for chromosome segregation, it also consists of two subunits (genes parC and parE). In eukaryotes, type II topoisomerase is a homodimer. There are many regions of sequence homology between the different subtypes of topoisomerase II. The signature pattern used in this entry is a highly conserved pentapeptide, which is located in GyrB, in ParE, and in protein 39 of phage T4 topoisomerase. |
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| Protein Domain |
| Name: |
Aspartate/homoserine dehydrogenase, NAD-binding |
| Type: |
Domain |
| 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 [
].Homoserine dehydrogenase (
) catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta-semialdehyde into homoserine [
,
]. Homoserine is an intermediate in the biosynthesis of threonine, isoleucine, and methionine. The enzyme can be found in a monofunctional form, in some bacteria and yeast, or a bifunctional form consisting of an N-terminal aspartokinase domain and a C-terminal homoserine dehydrogenase domain, as found in bacteria such as Escherichia coli and in plants. Structural analysis of the yeast monofunctional enzyme () indicates that the enzyme is a dimer composed of three distinct regions; an N-terminal nucleotide-binding domain, a short central dimerisation region, and a C-terminal catalytic domain [
]. The N-terminal domain forms a modified Rossman fold, while the catalytic domain forms a novel α-β mixed sheet.This entry represents the NAD(P)-binding domain of aspartate and homoserine dehydrogenase. Asparate dehydrogenase (
) is strictly specific for L-aspartate as substrate and catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+ [
].Note that the C terminus of the protein contributes a helix to this domain that is not covered by this model. |
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| Protein Domain |
| Name: |
Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain |
| Type: |
Domain |
| Description: |
The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [].Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase;
) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamate-tRNA ligase (Thermus thermophilus) has been solved. The molecule has the form of a bent cylinder and consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I ligases and resembles the corresponding part of Escherichia coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure [
]. |
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| Protein Domain |
| Name: |
Glutamyl/glutaminyl-tRNA synthetase |
| Type: |
Family |
| Description: |
The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [].Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase;
) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamate-tRNA ligase (Thermus thermophilus) has been solved. The molecule has the form of a bent cylinder and consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I ligases and resembles the corresponding part of Escherichia coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure [
]. |
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| Protein Domain |
| Name: |
Glutamine-tRNA synthetase |
| Type: |
Family |
| Description: |
Glutamine-tRNA ligase (
) is a class Ic aminoacyl-tRNA ligase and shows several similarities with glutamine-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer.
Glutamine-tRNA ligase is a relatively rare ligase, found in the cytosolic compartment of eukaryotes, in Escherichia coli and a number of other Gram-negative bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln.The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [
]. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c []. |
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| Protein Domain |
| Name: |
Glutamine-tRNA ligase, alpha-bundle domain superfamily |
| Type: |
Homologous_superfamily |
| Description: |
The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [].Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase;
) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamate-tRNA ligase (Thermus thermophilus) has been solved. The molecule has the form of a bent cylinder and consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I ligases and resembles the corresponding part of Escherichia coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure [
].This superfamily represents the C-terminal end of the Glutamine-tRNA ligase catalytic domain. It forms an α-bundle domain. |
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| Protein Domain |
| Name: |
Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain |
| Type: |
Domain |
| Description: |
The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [
].Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase;
) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamate-tRNA ligase (Thermus thermophilus) has been solved. The molecule has the form of a bent cylinder and consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I ligases and resembles the corresponding part of Escherichia coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure [
]. |
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| Protein Domain |
| Name: |
Peptidase M1, alanyl aminopeptidase |
| Type: |
Family |
| Description: |
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation which is usually zinc, but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys. At least one other residue is required for catalysis, which may play an electrophillic role.
Many metalloproteases contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site []. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [].The M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N,
, after the Escherichia coli enzyme, suggesting a similar activity profile (see
for a description of catalytic activity).
This group of zinc metallopeptidases belong to MEROPS peptidase family M1 (aminopeptidase N, clan MA); the majority are identified as alanyl aminopeptidases (proteobacteria) that are closely related to E. coli PepN and presumed to have a similar (not identical) function. Nearly all are found in proteobacteria, but members are found also in cyanobacteria, plants, and apicomplexan parasites [
,
]. This family differs greatly in sequence from the family of aminopeptidases typified by Streptomyces lividans PepN () and from the membrane bound aminopeptidase N family in animals.
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| Protein Domain |
| Name: |
Phospholipase A2 |
| Type: |
Family |
| Description: |
Phospholipase A2 (
) (PLA2) is a small lipolytic enzyme that releases fatty acids from the second carbon group of glycerol. It is involved in a number of physiologically important cellular processes, such as the liberation of arachidonic acid from membrane phospholipids [
]. It plays a pivotal role in the biosynthesis of prostaglandin and other mediators of inflammation. PLA2 has four to seven disulphide bonds and binds a calcium ion that is essential for activity. Within the active enzyme, the alpha amino group is involved in a conserved hydrogen-bonding network linking the N-terminal region to the active site. The side chains of two conserved residues, His and Asp, participate inthe catalytic network.
Many PLA2's are widely distributed in snakes, lizards, bees and mammals. In mammals, there are at least four forms: pancreatic, membrane-associated as well as two less well characterised forms. The venom of most snakes contains multiple forms of PLA2 [
,
]. Some of them are presynaptic neurotoxins which inhibit neuromuscular transmission by blocking acetylcholine release from the nerve termini.Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.The allergens in this family include allergens with the following designations: Api m 1. |
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| Protein Domain |
| Name: |
DNA topoisomerase I, catalytic core, alpha/beta subdomain |
| Type: |
Homologous_superfamily |
| Description: |
DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single- or double-strand breaks, crossing the strands through one another, then resealing the breaks [
]. These enzymes have several functions: to remove DNA supercoils during transcription and DNA replication; for strand breakage during recombination; for chromosome condensation; and to disentangle intertwined DNA during mitosis [,
]. DNA topoisomerases are divided into two classes: type I enzymes (; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (
; topoisomerases II, IV and VI) break double-strand DNA [
].Type I topoisomerases are ATP-independent enzymes (except for reverse gyrase), and can be subdivided according to their structure and reaction mechanisms: type IA (Topo IA; bacterial and archaeal topoisomerase I, topoisomerase III and reverse gyrase) and type IB (Topo IB; eukaryotic topoisomerase I and topoisomerase V). These enzymes are primarily responsible for relaxing positively and/or negatively supercoiled DNA, except for reverse gyrase, which can introduce positive supercoils into DNA. This function is vital for the processes of replication, transcription, and recombination. Unlike Topo IA enzymes, Topo IB enzymes do not require a single-stranded region of DNA or metal ions for their function. The type IB family of DNA topoisomerases includes eukaryotic nuclear topoisomerase I, topoisomerases of poxviruses, and bacterial versions of Topo IB [
]. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their C-terminal catalytic domain and the overall reaction mechanism with tyrosine recombinases [,
]. The C-terminal catalytic domain in topoisomerases is linked to a divergent N-terminal domain that shows no sequence or structure similarity to the N-terminal domains of tyrosine recombinases [,
].This entry represents the alpha/beta subdomain that comprises part of the catalytic core of eukaryotic and viral topoisomerase I (type IB) enzymes, which occurs near the C-terminal region of the protein. |
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| Protein Domain |
| Name: |
Proline-tRNA ligase, class IIa |
| Type: |
Family |
| Description: |
Proline-tRNA ligase (also known as Prolyl-tRNA synthetase) belongs to class IIa aminoacyl-tRNA synthetases. Prolyl-tRNA synthetase (
) exists in two forms, which are loosely related. The first form is present in the majority of eubacteria species. The second one, present in some eubacteria, is essentially present in archaea and eukaryota. The enzyme from Escherichia coli contains all three of the conserved consensus motifs characteristic of class II aminoacyl-tRNA synthetases [
]. The complex between Thermus thermophilus prolyl-tRNA synthetase (ProRSTT) and its cognate tRNA has been crystallized using two different isoacceptors of tRNA(Pro) [].The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c []. |
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| Protein Domain |
| Name: |
Isoleucine-tRNA ligase, type 2 |
| Type: |
Family |
| Description: |
Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase)(
) is an alpha monomer that belongs to class Ia. The enzyme, isoleucine-tRNA ligase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing"step, the ligase itself rapidly hydrolyses only the valylated products [
,
] as shown from the crystal structures. The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [].In eukaryotes, two forms of isoleucine-tRNA synthetase exist, a cytoplasmic form and a mitochondrial form [
]. Type 2 includes bacterial, archaeal and cytoplasmic (gene iars1) isoleucine-tRNA ligases. |
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| Protein Domain |
| Name: |
Glutamate-tRNA ligase, bacterial/mitochondrial |
| Type: |
Family |
| Description: |
Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase;
) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamate-tRNA ligase (Thermus thermophilus) has been solved. The molecule has the form of a bent cylinder and consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I ligases and resembles the corresponding part of Escherichia coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure [
].This entry contains type 1 glutamate-tRNA ligases, which are found in bacteria and in mitochondria in eukaryotes.The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [
]. |
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| Protein Domain |
| Name: |
Serine-tRNA ligase, type1 |
| Type: |
Family |
| Description: |
Serine-tRNA ligase (
) exists as monomer and belongs to the aminoacyl-tRNA synthetase class IIa [
]. It catalyses the attachment of serine to tRNA (Ser). It is also able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be further converted into selenocysteinyl-tRNA (Sec). There are two distinct types of seryl-tRNA synthetase, as differentiated by primary sequence analysis, three-dimensional structure and substrate recognition mechanism: type 1 (this entry) is found in the majority of organisms (prokaryotes, eukaryotes and archaea), whereas type 2 (
) is confined to some methanogenic archaea [
]. Methanosarcina barkeri possesses two seryl-tRNA synthetases, one of each type [].The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c []. |
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| Protein Domain |
| Name: |
Pyruvate kinase, active site |
| Type: |
Active_site |
| Description: |
Pyruvate kinase (
) (PK) catalyses the final step in glycolysis [
,
], the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP:ADP + phosphoenolpyruvate = ATP + pyruvate The enzyme, which is found in all living organisms, requires both magnesium and potassium ions for its activity. In vertebrates, there are four tissue-specific isozymes: L (liver), R (red cells), M1 (muscle, heart and brain), and M2 (early foetal tissue). In plants, PK exists as cytoplasmic and plastid isozymes, while most bacteria and lower eukaryotes have one form, except in certain bacteria, such as Escherichia coli, that have two isozymes. All isozymes appear to be tetramers of identical subunits of ~500 residues.PK helps control the rate of glycolysis, along with phosphofructokinase (
) and hexokinase (
). PK possesses allosteric sites for numerous effectors, yet the isozymes respond differently, in keeping with their different tissue distributions [
]. The activity of L-type (liver) PK is increased by fructose-1,6-bisphosphate (F1,6BP) and lowered by ATP and alanine (gluconeogenic precursor), therefore when glucose levels are high, glycolysis is promoted, and when levels are low, gluconeogenesis is promoted. L-type PK is also hormonally regulated, being activated by insulin and inhibited by glucagon, which covalently modifies the PK enzyme. M1-type (muscle, brain) PK is inhibited by ATP, but F1,6BP and alanine have no effect, which correlates with the function of muscle and brain, as opposed to the liver.
The structure of several pyruvate kinases from various organisms have been determined [
,
,
]. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a β/α-barrel domain, a β-barrel domain (inserted within the β/α-barrel domain), and a 3-layer α/β/α sandwich domain.This entry represents an active site that includes a lysine residue which seems to be the acid/base catalyst responsible for the interconversion of pyruvate and enolpyruvate, and a glutamic acid residue implicated in the binding of the magnesium ion.
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| Protein Domain |
| Name: |
ATPase, alpha/beta subunit, nucleotide-binding domain, active site |
| Type: |
Active_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.This group of proteins include the alpha and beta subunits found in the F1, V1, and A1 complexes of F-, V- and A-ATPases, respectively (sometimes called the A and B subunits in V- and A-ATPases), as well as Type 3 secretion system ATPase and Flagellum-specific ATP synthase. This entry represents a 10 amino acid signature. The signature pattern contains two conserved serines. The first serine seems to be important for catalysis - in the ATPase alpha-chain at least - as its mutagenesis causes catalytic impairment. |
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| Protein Domain |
| Name: |
DNA polymerase, palm domain superfamily |
| Type: |
Homologous_superfamily |
| Description: |
DNA is the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the life cycle of a cell. This function is performed by DNA- directed DNA-polymerases
) by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA, using a complementary DNA chain as a template. Small RNA molecules are generally used as primers for chain elongation, although terminal proteins may also be used for the de novo synthesis of a DNA chain. Even though there are 2 different methods of priming, these are mediated by 2 very similar polymerases classes, A and B, with similar methods of chain elongation.
A number of DNA polymerases have been grouped under the designation of DNA polymerase family B. Six regions of similarity (numbered from I to VI) are found in all or a subset of the B family polymerases. The most conserved region (I) includes a conserved tetrapeptide with two aspartate residues. Its function is not yet known, however, it has been suggested that it may be involved in binding a magnesium ion. All sequences in the B family contain a characteristic DTDS motif, and possess many functional domains, including a 5'-3' elongation domain, a 3'-5' exonuclease domain [], a DNA binding domain, and binding domains for both dNTP's and pyrophosphate []. The DNA polymerase structure resembles a right hand with fingers, palm, and thumb, with an active site formed by a palm holding the catalytic residues, a thumb that binds the primer:template DNA and fingers interacting with incoming nucleotide, and the N and Exo domains extend from the finger toward the thumb [
,
,
]. This superfamily represents the palm domain of DNA polymerase B composed of 6-stranded β-sheet flanked by two long α-helices from one side and a short helix from the other. |
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| Protein Domain |
| Name: |
Proline-tRNA ligase, class IIa, archaeal-type |
| Type: |
Family |
| Description: |
Proline-tRNA ligase (also known as Prolyl-tRNA synthetase) is a class II tRNA ligase and is recognised by
, which recognises tRNA ligases for Gly, His, Ser, and Pro. The proline-tRNA ligases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi (Lyme desease spirochete). The other family,
, includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis sp. (strain PCC 6308), and one of the two proline-tRNA ligases of Saccharomyces cerevisiae (Baker's yeast).
The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [
,
]. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [,
,
]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c []. |
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| Protein Domain |
| Name: |
Ferrochelatase, active site |
| Type: |
Active_site |
| Description: |
Synonym(s): Protohaem ferro-lyase, Iron chelatase, etc.
Ferrochelatase is the terminal enzyme of the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into the protoporphyrin IX ring yielding protoheme. This enzyme is ubiquitous in nature and widely distributed in bacteria and eukaryotes. Recently, some archaeal members have been identified. The oligomeric state of these enzymes varies depending on the presence of a dimerization motif at the C terminus [
,
,
,
,
,
,
,
,
,
,
,
]. In eukaryotic cells, it binds to the mitochondrial inner membrane with its active site on the matrix side of the membrane.The X-ray structure of
Bacillus subtilisand human ferrochelatase have been solved [
,
].The human enzyme exists as a homodimer. Each
subunit contains one [2Fe-2S]cluster. The monomer is folded into two
similar domains, each with a four-stranded parallelβ-sheet flanked by an α-helix in a beta-α-β motif that is
reminiscent of the fold found in the periplasmic bindingproteins. The topological similarity between the domains suggests that
they have arisen from a gene duplication event. However,significant differences exist between the two domains, including an
N-terminal section (residues 80-130) that forms part of theactive site pocket, and a C-terminal extension (residues 390-423) that
is involved in coordination of the [2Fe-2S]cluster and in
stabilisation of the homodimer. Ferrochelatase seems to have a structurally conserved core region that is common to the enzyme from bacteria, plants and mammals. Porphyrin binds in the identified cleft; this cleft also includes the metal-binding site of the enzyme. It is likely that the structure of the cleft region will have different conformations upon substrate binding and release [
].The signature pattern for this enzyme is based on a conserved region which contains a conserved histidine (H263) that is one of the active site residues. The mutation H263A resulted in total loss of activity in human ferrochelatase activity. Mutants D340E, E343D and H341C result in diminished activity [
]. |
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