IED ID | IndEnz0002008907 |
Enzyme Type ID | protease008907 |
Protein Name |
Protein P1-P2 Cleaved into: Serine protease EC 3.4.21.- ; RNA-directed RNA polymerase EC 2.7.7.48 |
Gene Name | ORF1/ORF2 |
Organism | Pea enation mosaic virus-1 (strain WSG) (PEMV-1) |
Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Sobelivirales Solemoviridae Enamovirus Pea enation mosaic virus-1 (PEMV-1) Pea enation mosaic virus-1 (strain WSG) (PEMV-1) |
Enzyme Sequence | MASFLKPVNSQGLWLSLLLAITYLFLLPSAGQSLDPSGIGLAAGCSQSQGGISSFAALPRPCNDSVCTLPDLGWSCQRTAQDTANQQQSPFNHTGHFLTTSGWTWPNWTCSPSQCQLLIHLPTWQIVKQDFLLLLKEWDLLTMCQRCSDLLTKTPGFILRFAGETLILVANLIEFVLVSWSLWLCSVLVYVAQAVPGKFLLYMAAFCTTFWAWPRETASSLIRIVTTPLTLIGFLNKTGIGLISHCLALTWNMFMTWSLLPWVTLMKMMKILITSSRVLTRSGRPKRTSSKSLKHKLKISRAIQKKQGKKTPVEERTIPGVQIKKLREDPPKGVILRCTDQFGDHVGYASAVKLEKGQTGIVLPIHVWTDTVYINGPNGKLKMADFTALYEVTNHDSLIMTSAMAGWGSILGVRPRPLTTIDAVKLKNYSLFTERDGKWYVQAAKCIAPAEGMFRVVSDTRPGDSGLPLFDMKMNVVAVHRGTWPSERFPENRAFAILPVPDLTSSSSPKFTGCETYSEAETAYEMADNFSDGEEILIRTKGQSYRTFIGSNKVALLSIRKLEEELSRGPIGLWADDTEDDESAPRRSGKRIIPVDSGETKSSEDPLPKGRGVSSTPSRSKSRKGKACPSFRNDAGTEESRQPQEEKGQSCQEDSLNSTQEIQGQSTHFVPSSGTGRKSCESSPHRPTTKITSIFEDFYRWKEPREEAPGFNSVGSCPFTVYKCPPKGLSSWGERVARTSAFLQACTEKYSWPETGAEAELSSLRYQAARRQSAQTTAVIPPKDVREDLIKRTTEAYRSTALPAPMWAHNFDESHMRFEFWECVRKLKGQAGSGVPYAAFSGRKTNDKWVFDHESTEDLWETVRDRLFRLLNQDFIDPVQAVKDGLVDPIRLFVKLEPHKMEKIRNKRYRLIASVSIVDQLVARMLFRDQNEEELLQHMAIPSKPGLGFSQDHQVLAFTESVAALAGTSAQDLVDNWSRYLTPTDCSGFDWSVPMWLLEDDLAVRNELTLGLPHGLRKMRETWLKCLGQSVFCLSNGLLLAQTSPGIQKSGSFNTSSTNSRMRYMLALYAGASWAVTMGDDALESVGSDLSQYARLGIKCERAEEFDFCSHLFRAPDVVIPKNLEKMVYGLLSGTSPESPLLADRFSWLSALQSILEEMRHMPQDFVNMLIEHLGVGDLVE |
Enzyme Length | 1181 |
Uniprot Accession Number | P29154 |
Absorption | |
Active Site | ACT_SITE 366; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216; ACT_SITE 396; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216; ACT_SITE 465; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; |
DNA Binding | |
EC Number | 3.4.21.-; 2.7.7.48 |
Enzyme Function | FUNCTION: RNA-dependent RNA polymerase that plays an essential role in virus replication. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (3); Compositional bias (2); Domain (2); Natural variant (9); Region (1); Sequence caution (1); Signal peptide (1); Transmembrane (4) |
Keywords | Hydrolase;Membrane;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA suppression of termination;RNA-directed RNA polymerase;Reference proteome;Ribosomal frameshifting;Serine protease;Signal;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: [Protein P1-P2]: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The protease probably cleaves itself and releases the RdRp (Potential). Cleavages have been shown in the P1 protein, but since the N-terminus containing the serine protease is shared between P1 and P1-P2, cleavages should also occur within the P1-P2 protein (By similarity). {ECO:0000250, ECO:0000305}. |
Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 131,890 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:21248 |
Cross Reference Brenda |