1YYW
Crystal structure of RNase III from Aquifex aeolicus complexed with double stranded RNA at 2.8-Angstrom Resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0003725 | molecular_function | double-stranded RNA binding |
A | 0004518 | molecular_function | nuclease activity |
A | 0004519 | molecular_function | endonuclease activity |
A | 0004525 | molecular_function | ribonuclease III activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006364 | biological_process | rRNA processing |
A | 0006396 | biological_process | RNA processing |
A | 0006397 | biological_process | mRNA processing |
A | 0008033 | biological_process | tRNA processing |
A | 0010468 | biological_process | regulation of gene expression |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0003723 | molecular_function | RNA binding |
B | 0003725 | molecular_function | double-stranded RNA binding |
B | 0004518 | molecular_function | nuclease activity |
B | 0004519 | molecular_function | endonuclease activity |
B | 0004525 | molecular_function | ribonuclease III activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006364 | biological_process | rRNA processing |
B | 0006396 | biological_process | RNA processing |
B | 0006397 | biological_process | mRNA processing |
B | 0008033 | biological_process | tRNA processing |
B | 0010468 | biological_process | regulation of gene expression |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0003723 | molecular_function | RNA binding |
C | 0003725 | molecular_function | double-stranded RNA binding |
C | 0004518 | molecular_function | nuclease activity |
C | 0004519 | molecular_function | endonuclease activity |
C | 0004525 | molecular_function | ribonuclease III activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006364 | biological_process | rRNA processing |
C | 0006396 | biological_process | RNA processing |
C | 0006397 | biological_process | mRNA processing |
C | 0008033 | biological_process | tRNA processing |
C | 0010468 | biological_process | regulation of gene expression |
C | 0016787 | molecular_function | hydrolase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0003723 | molecular_function | RNA binding |
D | 0003725 | molecular_function | double-stranded RNA binding |
D | 0004518 | molecular_function | nuclease activity |
D | 0004519 | molecular_function | endonuclease activity |
D | 0004525 | molecular_function | ribonuclease III activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006364 | biological_process | rRNA processing |
D | 0006396 | biological_process | RNA processing |
D | 0006397 | biological_process | mRNA processing |
D | 0008033 | biological_process | tRNA processing |
D | 0010468 | biological_process | regulation of gene expression |
D | 0016787 | molecular_function | hydrolase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00517 |
Number of Residues | 9 |
Details | RNASE_3_1 Ribonuclease III family signature. ETLEFLGDA |
Chain | Residue | Details |
A | GLU37-ALA45 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 468 |
Details | Domain: {"description":"RNase III"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 272 |
Details | Domain: {"description":"DRBM"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15016361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18047582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11738048","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1JFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RC5","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |