9O4J
Cryo-EM Structure of the Arabidopsis GA3-GID1A-RGA Complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000976 | molecular_function | transcription cis-regulatory region binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0009409 | biological_process | response to cold |
| A | 0009723 | biological_process | response to ethylene |
| A | 0009737 | biological_process | response to abscisic acid |
| A | 0009739 | biological_process | response to gibberellin |
| A | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
| A | 0009863 | biological_process | salicylic acid mediated signaling pathway |
| A | 0009867 | biological_process | jasmonic acid mediated signaling pathway |
| A | 0009909 | biological_process | regulation of flower development |
| A | 0009938 | biological_process | negative regulation of gibberellic acid mediated signaling pathway |
| A | 0010029 | biological_process | regulation of seed germination |
| A | 0010187 | biological_process | negative regulation of seed germination |
| A | 0010218 | biological_process | response to far red light |
| A | 0010628 | biological_process | positive regulation of gene expression |
| A | 0033206 | biological_process | meiotic cytokinesis |
| A | 0042176 | biological_process | regulation of protein catabolic process |
| A | 0042538 | biological_process | hyperosmotic salinity response |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0080154 | biological_process | regulation of fertilization |
| A | 1900033 | biological_process | negative regulation of trichome patterning |
| A | 1905613 | biological_process | regulation of developmental vegetative growth |
| A | 1905614 | biological_process | negative regulation of developmental vegetative growth |
| A | 1905622 | biological_process | negative regulation of leaf development |
| A | 1990841 | molecular_function | promoter-specific chromatin binding |
| A | 2000033 | biological_process | regulation of seed dormancy process |
| A | 2000377 | biological_process | regulation of reactive oxygen species metabolic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009739 | biological_process | response to gibberellin |
| B | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
| B | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
| B | 0010331 | molecular_function | gibberellin binding |
| B | 0010476 | biological_process | gibberellin mediated signaling pathway |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0048444 | biological_process | floral organ morphogenesis |
| B | 0048530 | biological_process | fruit morphogenesis |
| B | 0071456 | biological_process | cellular response to hypoxia |
| B | 1905516 | biological_process | positive regulation of fertilization |
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. ILfFHGGSFahsSanSA |
| 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. IfLAGDSSGGnIA |
| Chain | Residue | Details |
| B | ILE185-ALA197 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 369 |
| Details | Domain: {"description":"GRAS","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_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 | 87 |
| Details | Region: {"description":"PFYRE","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 76 |
| Details | Region: {"description":"SAW","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Motif: {"description":"DELLA motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Motif: {"description":"LEXLE motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Motif: {"description":"VHYNP motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Motif: {"description":"VHIID","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Motif: {"description":"LXXLL motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Motif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q0ZPV7","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10038","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19037309","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZSI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19037309","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZSH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
