| IED ID | IndEnz0002001913 |
| Enzyme Type ID | protease001913 |
| Protein Name |
Non-structural polyprotein p200 p200 Cleaved into: Protease/methyltransferase p150 p150 EC 3.4.22.- ; RNA-directed RNA polymerase p90 p90 EC 2.7.7.48 EC 3.6.1.15 EC 3.6.4.13 |
| Gene Name | |
| Organism | Rubella virus (strain RA27/3 vaccine) (RUBV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Hepelivirales Matonaviridae Rubivirus Rubivirus rubellae Rubella virus (RUBV) Rubella virus (strain RA27/3 vaccine) (RUBV) |
| Enzyme Sequence | MERLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVSAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHWIEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHGGRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRPCTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAEVGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNARLAGIMKSAKRCAADSLSVAGWLDTIWGAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEIAATWIVHAASADRHCACAPRCDVPRERPSAPAGPPDDEALIPPWLFAEHRALRCREWDFEVLRARADTAAAPAPLAPRPARYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARAWAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPGQSAATSSPPGDPPPPRCARRSQRHSDARGTPPPAPARDPPPPAPSPPAPPRAGDPVPPTSAGPADRARDAELEVAYEPSGPPTSTKADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVATPGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWARVACPLLGAGVYGWSAAESLRAALAATRTEPAERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELCRYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGVPQVRCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPRCAYGRALSEARTHKDFAALSQRWSASHADASSDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGGGPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTTRILAAFTREDLYVCPTNALLHEIQAKLRARDIEIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVICVGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVRRLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAELKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKNHTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAARELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKIIMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLRELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKHVSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVRELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD |
| Enzyme Length | 2116 |
| Uniprot Accession Number | O40955 |
| Absorption | |
| Active Site | ACT_SITE 1152; /note=For cysteine protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01237; ACT_SITE 1273; /note=For cysteine protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01237 |
| 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:0000250|UniProtKB:Q86500, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:Q86500}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q86500}; |
| DNA Binding | |
| EC Number | 3.4.22.-; 2.7.7.48; 3.6.1.15; 3.6.4.13 |
| Enzyme Function | FUNCTION: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}.; FUNCTION: [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA-directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}.; FUNCTION: [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 1352..1359; /note=NTP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00990 |
| Features | Active site (2); Chain (3); Compositional bias (1); Domain (6); Metal binding (4); Motif (4); Nucleotide binding (1); Region (6); Site (1) |
| Keywords | ATP-binding;Calcium;Helicase;Host cytoplasm;Host membrane;Hydrolase;Membrane;Metal-binding;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Thiol protease;Transferase;Viral RNA replication;Zinc |
| Interact With | Q07021; Q9MZE0 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}.; SUBCELLULAR LOCATION: [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Non-structural polyprotein p200]: Specific enzymatic cleavage by its own cysteine protease yield mature proteins p150 and p90. {ECO:0000250|UniProtKB:Q86500}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 727..732; /note=PxxPxR; class II SH3-binding; /evidence=ECO:0000250|UniProtKB:Q86500; MOTIF 747..752; /note=PxxPxR; class II SH3-binding; /evidence=ECO:0000250|UniProtKB:Q86500; MOTIF 761..766; /note=PxxPxR; class II SH3-binding; /evidence=ECO:0000250|UniProtKB:Q86500; MOTIF 1902..1906; /note=Human RB1 binding; /evidence=ECO:0000250|UniProtKB:Q86500 |
| Gene Encoded By | |
| Mass | 230,322 |
| Kinetics | |
| Metal Binding | METAL 1175; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01237; METAL 1178; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01237; METAL 1227; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01237; METAL 1273; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01237 |
| Rhea ID | RHEA:21248; RHEA:23680; RHEA:13065 |
| Cross Reference Brenda |