3G8Q
A cytidine deaminase edits C-to-U in transfer RNAs in archaea
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006400 | biological_process | tRNA modification |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016554 | biological_process | cytidine to uridine editing |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006400 | biological_process | tRNA modification |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016554 | biological_process | cytidine to uridine editing |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000049 | molecular_function | tRNA binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006400 | biological_process | tRNA modification |
| C | 0008033 | biological_process | tRNA processing |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016554 | biological_process | cytidine to uridine editing |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000049 | molecular_function | tRNA binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006400 | biological_process | tRNA modification |
| D | 0008033 | biological_process | tRNA processing |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016554 | biological_process | cytidine to uridine editing |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | HIS44 |
| A | GLU46 |
| A | CYS67 |
| A | CYS70 |
| A | HOH326 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS44 |
| B | GLU46 |
| B | CYS67 |
| B | CYS70 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | HIS44 |
| C | CYS67 |
| C | CYS70 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS44 |
| D | CYS67 |
| D | CYS70 |
| D | HOH305 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 302 |
| Chain | Residue |
| D | ASN17 |
| D | GLY113 |
| D | ASP115 |
| D | HOH341 |
| D | HOH342 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA C 302 |
| Chain | Residue |
| C | ASP265 |
| C | ARG270 |
| C | SER272 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 302 |
| Chain | Residue |
| A | LEU123 |
| A | THR125 |
| A | ARG189 |
| A | ARG191 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 303 |
| Chain | Residue |
| A | ASP257 |
| C | ASP173 |
| C | ASP175 |
| C | HOH335 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 302 |
| Chain | Residue |
| B | ASP41 |
| B | ASP173 |
| B | ASP175 |
| B | HOH310 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 303 |
| Chain | Residue |
| C | GLU183 |
| D | GLU176 |
| D | GLU179 |
| D | HOH338 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 304 |
| Chain | Residue |
| C | GLU179 |
| D | GLU179 |
| D | HOH336 |
| D | HOH359 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 404 |
| Details | Domain: {"description":"CMP/dCMP-type deaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 408 |
| Details | Domain: {"description":"THUMP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00529","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19407206","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
