| IED ID | IndEnz0002010395 |
| Enzyme Type ID | protease010395 |
| Protein Name |
Non-structural polyprotein Cleaved into: Helicase EC 3.6.4.13 ; 3C-like protease 3CL-PRO EC 3.4.22.- ; RNA-directed RNA polymerase EC 2.7.7.48 |
| Gene Name | |
| Organism | Ectropis obliqua picorna-like virus (EoPV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Iflaviridae Iflavirus Ectropis obliqua virus Ectropis obliqua picorna-like virus (EoPV) |
| Enzyme Sequence | MMTTQTNQLFNRSLNDELGNRTDTITLHPWNVSEYVTSTGLAEAEFEACTGKDLEIQKYLVTVSEECPCGHPTTFSEIDMSRGMVMASSDNIYSDDIVTLVPTENGYEDSDPCFCENQKEDCDNCMYLQILRMAPGKWNMTYGLRHNHQAQLTYYLTEERGFTCEGYTLEADTSDSEGFGDTADYTLYCIQYSGKYKQRRQWHVLLDDESCGFCKYRVTTGLIVPEVPRHWTNELGRRQNLLVPKVLGQYVDFIEAKSPLRLDWLSMSKLVSGKCSLPNFYVNLTTLRTFQVAGGKFLPYLYNGSAANNDLKLPIQVTAQGDEDTPAGELSIEQDTHENTTLAESTDASTAYVATEEFSMMPWITDGPHTYPDLTERWTKAFQFQWTTSQAQGEIIQRFDLPIEAIQNFINSPNALPWRQHAFYKSDIELKVQVNSQPGQSGYLILGAMYEASEGTAIGNRVDHAANIVAMPHMRISAGSSNSGDMVIPFIRHFPVGCILNNAFDVPQYFVTLFVAPLLQLRTGADGPQVVDVTIMIRFPNCEFYGQRTTEQIVTAQGWAPDLTQDGDVESNPGPFLSGLLGTVAAVGKTVAGAGSSIGSIATGVSGVANGIGSIGSAAGKVIGGVESLLRPLFPKKDMDRPQNIIEPTNFYLQQNTSLSLATGTNNVKLLQLQAENSVSHPPGFVPVDDQFNNRFILSVFGLSDYFQWFSGSASGTLLYSFDVTPLKSFTRGIPLQPEFYLTPMAALSGQYGGYHGDMEMRLTFAVSKFHSGRVFIVYSPDVVPTFDNIGAYYNVLLDVQDQSVYTFKIPYQVPTPYAPIFESLQGDTGTFLTPAVSAGNVRCMAYGFVSIFVENQLRVMQTAAPTIDVLVELRGADNFHLVLPAGGKFRSLSTITTTEAPVVTAMGDERREPHTVNPPPRRIMPVWAAQLNESYDCRDVVKRYHDWFDIVSPAVVAGRGFTDMYMNVTVFHVPVPAFDAAPIQNVQFTDMLVGSSILNKSMVLARERINLATNNTISIRVPWTNYASMISNSINPASGRSNTMAPYSNGRVVVYIEYLSSYTTTLGAFRVVWDVTAGSASTRPDTYTPDMLTLLHDGFRFAKGDFNYQMDFTPVPSGANTAIRMRCFRAYGDGGNLYVFQGFPKMLGTYTPRQAISGVTPTRGGLQRQNIIGGGQRDLTQDGDIESNPGPTQSKPTGAQPPPDDILTDEDREGLEGGSIRISFFEKLGDYCKRALGWSGERIVEFIRELRSIKKHVGSIPGMTRISELITTIKELSVVTNGLNRMSAAVEELNEQIKKTREKVETFVGGVGGKLNSLDTGDLVSNGIEYVAYILNIYNSKSVGMTLINVAALLSKMGLGRYLVNDLVDRLGTFAKGEDTEEIEREYTSLIITGVLGAFGLGTMNVEKEGFVKPFLSNVKDFFRNGFAVKKFLDSHFKCINDICGWVRSKIFGKVDKGGLTVDLLVWCERVQVLAEVYNYDTILNDPEFAETLLSLQDEAFEFDRLFIASRIRPPNQYSMYRTKLQRAIDLLGQQGTMQKSKPVPFCLWVYGHSGCGKSHVCDNVLTEIGSALGINTANPIYTRSPDVEFWNGYTGQKLISWQDFAKITTGETYRKQVSELSSLIEPTPFNPPFAALEDKRKIADAWAVYVSSNKAFPEVQNMGMEDSALFYRRRHALVKMRINPEIIQEYARREPPISLEDKYKGQTVYYPSNIPSEDFATRGPYFHVQFAFHVTSLSTAEPTEWLGYDGFIAEVTRRAIDHRQREVDACIQRRGIYSKLRRSAPTGVEFREEVRTLKEELDRLTQERVAEAHGSDNAVKNLATTMDYEKRATFEETEALGSVILQYRLDPNCDCTNQAIMKAATSNEPRKICEVSFCEKCEPVNQRKKNVYKAMSEQLEGVAVSNPFGGIAMIERGDSARIPRAGRQYTPLDYARQATIGTLKWIQGKGLPAGYAYWSEIMPVCCHKKEILELAYFENVGDNIELVLDLSSMKARHGVSFPLFHKLEWFDLRKLDAWATTGFKVILPVVCEQSKFNWNNCIEVKPGERGRIPITPKWAPELIGRVTLEEFKRSWSCDAVQKPSVSYYKIEKDLIRFLVSGTYVQIEGVENMTAGLNHLMSLHTKDTVAFCNSFFYWKSGGKLRAAKFYPFVNGMLKDMSFIFSNIMIAVGAVMLAYKVYRLIRNSSECVEAQAKDYDQKTEAPKIPKVNFVQSTPVVVAAKGDEELSIIHNSLCQLRKGSMRLLGVRLCSNFVLAPQHLAWVPGEFGISLHSSGAWSTELIFEATSVKYSCVKGFDYAVYRFVTLPAGRNIVNYFTTRAQGATLKSEATLMTLSGASLQLRPVRISQYTGALTYDNASFPGTGTSMIGWQYWLGAQSVRCGSLIMSNNLLCGFHVAQNLKTGDAYAVSICKEMLVEALRILGATPFDMKMKRTTPITTVGEPKMQPPETAVVIPLGKAIEPVRYSGKSNLEKSIMHGELAEPFRIPAAQSATAKGECIGYDIVMKGCEKQFKPPKPIDPEEVEKIGDYLIERLVPQSIPLIPTISEPLSLGEAIAGIDGIPLMCGMKLNTSIGWPLCNEYPKGTKKSNIIRVDREEGEVHVDVVAFDDYAKANTLRKQAILPPTTFMDFPKDELLKPGKDTRLINGAPLHHTLDMRRYLMEFFAAITTINNKIAVGIDVHSGDWALIHGGADDVVDEDYSGFGPGFHSQWLTVVCPIAVAWCKHHKKVDKEYEDVVNCLIMELQNAYHVAGDLVYQVLCGSPSGAFATDRINSLANLCYHCLCHLRKYGTLTGFWSHYTLVYGDDTRRRETAYTGDEFQECMASVGIVVNRDKSGVTSFLKRQFIPIDHRDVRVMLAPLPRPIVEDILNWVRKPYASKLSALEETVGSYLSEIFHHGQDEFNNSRSKIQAILARHGSHPELPTFDDLFRQKYLSNGVWPVLMPLANALGPIPAAESEPTHKVTSGQVVCVPHEAGECCAITLGG |
| Enzyme Length | 2987 |
| Uniprot Accession Number | Q6UP17 |
| Absorption | |
| Active Site | ACT_SITE 2261; /note="For picornain 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:22534091"; ACT_SITE 2299; /note="For picornain 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:22534091"; ACT_SITE 2383; /note="For picornain 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:22534091" |
| 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, ECO:0000269|PubMed:20423615}; 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:0000269|PubMed:23449794}; |
| DNA Binding | |
| EC Number | 3.6.4.13; 3.4.22.-; 2.7.7.48 |
| Enzyme Function | FUNCTION: [Helicase]: Displays RNA helix destabilizing and strand annealing acceleration activity. This activity is necessary at several points during genome replication, for example to separate duplexes that form after genome replication. {ECO:0000305|PubMed:23449794}.; FUNCTION: [3C-like protease]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. {ECO:0000269|PubMed:22534091}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates genomic and antigenomic RNA. {ECO:0000269|PubMed:20423615}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:22534091}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 for 3C-like protease. {ECO:0000269|PubMed:22534091}; |
| Pathway | |
| nucleotide Binding | NP_BIND 1553..1560; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (3); Chain (4); Coiled coil (2); Compositional bias (1); Domain (2); Mutagenesis (3); Nucleotide binding (1); Region (1); Site (2) |
| Keywords | ATP-binding;Coiled coil;Direct protein sequencing;Helicase;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Thiol protease;Transferase;Viral RNA replication |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: [Non-structural polyprotein]: Specific enzymatic cleavages in vivo by the viral 3C-like protease yield three mature proteins. {ECO:0000269|PubMed:22534091}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 332,444 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21248; RHEA:13065 |
| Cross Reference Brenda |