8FAK
DNA replication fork binding triggers structural changes in the PriA DNA helicase that regulate the PriA-PriB replication restart pathway in E. coli
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0006260 | biological_process | DNA replication |
| A | 0006261 | biological_process | DNA-templated DNA replication |
| A | 0006269 | biological_process | DNA replication, synthesis of primer |
| A | 0006270 | biological_process | DNA replication initiation |
| A | 0006276 | biological_process | plasmid maintenance |
| A | 0009314 | biological_process | response to radiation |
| A | 0030894 | cellular_component | replisome |
| A | 0031297 | biological_process | replication fork processing |
| A | 0042802 | molecular_function | identical protein binding |
| A | 1990077 | cellular_component | primosome complex |
| A | 1990099 | cellular_component | pre-primosome complex |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003697 | molecular_function | single-stranded DNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0006260 | biological_process | DNA replication |
| B | 0006261 | biological_process | DNA-templated DNA replication |
| B | 0006269 | biological_process | DNA replication, synthesis of primer |
| B | 0006270 | biological_process | DNA replication initiation |
| B | 0006276 | biological_process | plasmid maintenance |
| B | 0009314 | biological_process | response to radiation |
| B | 0030894 | cellular_component | replisome |
| B | 0031297 | biological_process | replication fork processing |
| B | 0042802 | molecular_function | identical protein binding |
| B | 1990077 | cellular_component | primosome complex |
| B | 1990099 | cellular_component | pre-primosome complex |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0003676 | molecular_function | nucleic acid binding |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003678 | molecular_function | DNA helicase activity |
| H | 0004386 | molecular_function | helicase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006260 | biological_process | DNA replication |
| H | 0006261 | biological_process | DNA-templated DNA replication |
| H | 0006269 | biological_process | DNA replication, synthesis of primer |
| H | 0006270 | biological_process | DNA replication initiation |
| H | 0006276 | biological_process | plasmid maintenance |
| H | 0006302 | biological_process | double-strand break repair |
| H | 0006310 | biological_process | DNA recombination |
| H | 0008270 | molecular_function | zinc ion binding |
| H | 0010332 | biological_process | response to gamma radiation |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0031297 | biological_process | replication fork processing |
| H | 0043138 | molecular_function | 3'-5' DNA helicase activity |
| H | 0046677 | biological_process | response to antibiotic |
| H | 0046872 | molecular_function | metal ion binding |
| H | 1990077 | cellular_component | primosome complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Motif: {"description":"L45 loop","evidences":[{"source":"PubMed","id":"16899446","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 166 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 191 |
| Details | Domain: {"description":"Helicase C-terminal","evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 175 |
| Details | Region: {"description":"Helicase lobe 1","evidences":[{"source":"PubMed","id":"37169801","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 43 |
| Details | Region: {"description":"Helicase lobe 2, N-terminus","evidences":[{"source":"PubMed","id":"37169801","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 54 |
| Details | Region: {"description":"CRR","evidences":[{"source":"PubMed","id":"37169801","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 140 |
| Details | Region: {"description":"Helicase lobe 2, C-terminus","evidences":[{"source":"PubMed","id":"37169801","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 99 |
| Details | Region: {"description":"CTD","evidences":[{"source":"PubMed","id":"24379377","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DEAH box","evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"6DCR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8FAK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
