5A22
Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001172 | biological_process | RNA-templated transcription |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0003968 | molecular_function | RNA-directed RNA polymerase activity |
| A | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| A | 0006397 | biological_process | mRNA processing |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019083 | biological_process | viral transcription |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0032259 | biological_process | methylation |
| A | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| A | 0039689 | biological_process | negative stranded viral RNA replication |
| A | 0044423 | cellular_component | virion component |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106005 | biological_process | RNA 5'-cap (guanine-N7)-methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 3000 |
| Chain | Residue |
| A | CYS1081 |
| A | GLU1108 |
| A | CYS1299 |
| A | CYS1302 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 3001 |
| Chain | Residue |
| A | CYS1120 |
| A | CYS1123 |
| A | HIS1294 |
| A | HIS1296 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 186 |
| Details | Domain: {"description":"RdRp catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00539","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 197 |
| Details | Domain: {"description":"Mononegavirus-type SAM-dependent 2'-O-MTase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00923","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 468 |
| Details | Region: {"description":"Capping domain","evidences":[{"source":"PubMed","id":"26144317","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31914397","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 250 |
| Details | Region: {"description":"PRNTase domain","evidences":[{"source":"PubMed","id":"35108335","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 37 |
| Details | Region: {"description":"priming-capping loop","evidences":[{"source":"PubMed","id":"35108335","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 199 |
| Details | Region: {"description":"Connector domain","evidences":[{"source":"PubMed","id":"26144317","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31914397","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; for GDP polyribonucleotidyltransferase","evidences":[{"source":"PubMed","id":"28053102","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Active site: {"description":"For mRNA (nucleoside-2'-O-)-methyltransferase 2","evidences":[{"source":"PubMed","id":"16227259","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P28887","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26144317","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31914397","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26144317","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 9 |
| Details | Site: {"description":"Interaction with the phosphoprotein","evidences":[{"source":"PubMed","id":"31914397","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for escaping from the 3'-terminal leader promotter followed by the formation of a stable leaderRNA elongation complex","evidences":[{"source":"PubMed","id":"35108335","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
