9X5G
Cryo-EM structure of quinary complex GA3-MtGID1b-MtDELLA1-SLY1-ASK1
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| A | 0009610 | biological_process | response to symbiotic fungus |
| A | 0009739 | biological_process | response to gibberellin |
| A | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
| A | 0016036 | biological_process | cellular response to phosphate starvation |
| A | 0036377 | biological_process | arbuscular mycorrhizal association |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 2000033 | biological_process | regulation of seed dormancy process |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0010331 | molecular_function | gibberellin binding |
| B | 0010476 | biological_process | gibberellin mediated signaling pathway |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0048530 | biological_process | fruit morphogenesis |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
| C | 0009845 | biological_process | seed germination |
| C | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
| C | 0010162 | biological_process | seed dormancy process |
| C | 0016567 | biological_process | protein ubiquitination |
| C | 0019005 | cellular_component | SCF ubiquitin ligase complex |
| C | 0031146 | biological_process | SCF-dependent proteasomal ubiquitin-dependent protein catabolic process |
| C | 1990756 | molecular_function | ubiquitin-like ligase-substrate adaptor activity |
| D | 0000151 | cellular_component | ubiquitin ligase complex |
| D | 0000226 | biological_process | microtubule cytoskeleton organization |
| D | 0000278 | biological_process | mitotic cell cycle |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005819 | cellular_component | spindle |
| D | 0005829 | cellular_component | cytosol |
| D | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| D | 0007140 | biological_process | male meiotic nuclear division |
| D | 0009524 | cellular_component | phragmoplast |
| D | 0009733 | biological_process | response to auxin |
| D | 0009734 | biological_process | auxin-activated signaling pathway |
| D | 0009753 | biological_process | response to jasmonic acid |
| D | 0009867 | biological_process | jasmonic acid mediated signaling pathway |
| D | 0016567 | biological_process | protein ubiquitination |
| D | 0019005 | cellular_component | SCF ubiquitin ligase complex |
| D | 0031146 | biological_process | SCF-dependent proteasomal ubiquitin-dependent protein catabolic process |
| D | 0045910 | biological_process | negative regulation of DNA recombination |
| D | 0097602 | molecular_function | cullin family protein binding |
Functional Information from PROSITE/UniProt
| site_id | PS01173 |
| Number of Residues | 17 |
| Details | LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. IVfFHGGSFshsSanSA |
| Chain | Residue | Details |
| B | ILE109-ALA125 |
| site_id | PS01174 |
| Number of Residues | 13 |
| Details | LIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. VyMAGDSSGGnIV |
| Chain | Residue | Details |
| B | VAL185-VAL197 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 54 |
| Details | Region: {"description":"Leucine repeat I (LRI)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 37 |
| Details | Region: {"description":"Required for possible homodimerization","evidences":[{"source":"UniProtKB","id":"Q7G7J6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 65 |
| Details | Region: {"description":"VHIID","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Region: {"description":"Leucine repeat II (LRII)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 76 |
| Details | Region: {"description":"SAW","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Motif: {"description":"DELLA motif","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Motif: {"description":"LxCxE motif; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Motif: {"description":"VHIID","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Motif: {"description":"LXXLL motif; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 58 |
| Details | Region: {"description":"Interaction with the F-box domain of F-box proteins","evidences":[{"source":"PubMed","id":"17410169","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
