| IED ID | IndEnz0002006358 |
| Enzyme Type ID | protease006358 |
| Protein Name |
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 ; Capsid protein VP1 |
| Gene Name | |
| Organism | Solenopsis invicta virus 3 (SINV-3) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Solinviviridae Invictavirus Solenopsis invicta virus 3 (SINV-3) |
| Enzyme Sequence | MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFLGIPNYKFAKNQKLVNTISKSLDACAKFIRDCPKDKQTEIFPLQGLHTATVKRRNEILTNVMPKFARQEPFVVLFQGPGGIGKTHLVQQLATKCVNSFYQDHEDDYIEISPDDKYWPPLSGQRVAFFDEAGNLNDLTEDLLFRNIKSICSPAYFNCAAADIEHKISPCPFELVFATVNTDLDTLQSKISSTFGQASVFPIWRRCIVVECSWNEKELGPFNYKNPSGHRSDYSHITMNYMSYDDKTQKLALEKEINFDTLFDMIRLRFRKKQQEHDTKISILNNEIQRQSNSKQHFSVCLYGEPGQGKTYNLNKLITTFANATNLKIGSEEKPSIHIFDDYIKDENDENCSKFMDIYNNKLPNNSVIFSATNVYPKTHFFPTFFLTNLIYAFIQPFKQVGLYRRLGFDGYTDIPNSSVNAPIFVQNFKFYERKQHICYFLSLEFLKNIICYIFFFLYFPLKFIKKIDLIEIKDVNKYVYDRYINFLSLSKQIEIVEYPPNLENVEFDFRFNMNKFHRVSFNNPFELDKYIHFNKNSYENLLHFDWKMYLSPRVKHRLALSYEKFFITISEVNKEIIIEELKRYVLLFKQFNIDPNMEINLGEYGSFYYINGKIHLMTINIESNVSEIPVFTDGDYVYISEHKIPVIDLFDNININSKYNLSFDQSIALNSFKTGDSFYSNAKVRKSLSKFVLLNYQTKFKLYLKEAKDKVKNFIETPIGHLLSILLTIFVICYASFKIYSKFSNFFSKDQAIEDQRKGEKKIKKITNYDSDGVQPQRKGEKKIKKVTNYDSDGVQPQSNVKVEEEIKLVFDPTGQKLLFGNDFTSELETLVELEKDDEEFTKSKIDNKSMAGLRREVRRRRYARSKKAQIEKQEVLTLPDVNGFEGGKPYFQIAEEKARKNLCQIYMIANNENCIASKFSDHIVCYGLFVFKKRLASVGHIVEALKCAPGYNLYAGCDQFNGKLYKMNLVRNYRKRELSVWDVDCPNDFVDLTSFFIPKEELYDAENCNTVLGRFGMNKREVYLYGNCEFIQEFFKVDNKGAQEFGYIDWATVDITLTTGGDCGLPYYICERKKFHNKIMGLHFAGNNVNHKTIGMSALIYKEDLVVWKGAERQSKCKFCDVKDIIIAQPDIPKEKYKGYNHEIVWNSLHESSPTTLNEELEHYLNIFPKFTGTIIKHSGDKFYGSVKHSHTQFISKFKTELTVTNGWKLSTAGDCQFESNHISPNTEVMYRVVDVQFNSIFKAFKSQPYIKNFRLIANVYEKDGKQRVTILTIIPVSDFNVKQQTVRQALVPLHLNEDEEVYVTEDVSDIFKTAIKRKQRGILPDVPYETVENETVEILGITHRNMTPEPAQMYKPTPFYKLALKFNLDHKLPVNFNMKDCPQEQKDMMVLDRLGQPNPRITQSLKWAHKDYSPDYELRKYVKEQYMCNIMEYYAGCNLLTEEQILKGYGPNHRLYGALGGMEIDSSIGWTMKELYRVTKKSDVINLDSNGNYSFLNNEAAQYTQELLKISMEQAHNGQRYYTAFNELMKMEKLKPSKNFIPRTFTAQDLNGVLMERWILGEFTARALAWDENCAVGCNPYATFHKFATKFFKFKNFFSCDYKNFDRTIPKCVFEDFRDMLIQANPHMKNEIYACFQTIIDRIQVSGNSILLVHGGMPSGCVPTAPLNSKVNDIMIYTAYVNILRRADRGDITSYRYYRDLVCRLFYGDDVIIAVDDSIADIFNCQTLSEEMKILFGMNMTDGSKSDIIPKFETIETLSFISRFFRPLKHQENFIVGALKKISIQTHFYYATDDTPEHFGQVFKTIQEEAALWEEEYFNKIQSYIQEIIRKFPEISKFFNFESYKSIQKRYIMNGWNEFVKLEKLDLNLNKKKSSKVTGIHSKQYSKFLKFLSRIENEKAALEGNFNKESVNTWYFKMSKAMHLNEIFQKGLISKPLAEFYFNEGQKMWDCNITFRRSKDDLPFTFSGSGTTKACAREQAAEEALVLFSQEDEIVRQINDIQSDCKFCKKMIRYKKLLSGVSIQRQMNVSKITENHVPSAGMMATDPSVAPDSGIATNTQTPSISRVLNPIARALDNPAGTGAPFDKHTYVYNVFTRWPEMSTVVNKSLAAGAEVFKISLDPNKLPKRILQYIQFHKTIIPQIEVQILIGGAAGTVGWLKVGWVPDASTAKKYSLDDLQLVASETINLNSTITMSMIINDSRRNGMFRLTKSDPEPWPGIVCLVEHPITNVQRNDDVNYPVIVSVRLGPDCQLMQPYNDLN |
| Enzyme Length | 2580 |
| Uniprot Accession Number | C1JCT1 |
| Absorption | |
| Active Site | ACT_SITE 1258; /note="For 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000305|PubMed:19403154"; ACT_SITE 1295; /note="For 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000305|PubMed:19403154"; ACT_SITE 1381; /note="For 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000305|PubMed:19403154" |
| 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}; 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:Q6UP17}; |
| DNA Binding | |
| EC Number | 3.6.4.13; 3.4.22.-; 2.7.7.48 |
| Enzyme Function | FUNCTION: [Capsid protein VP1]: Assembles with VP1-FSD and VP2 to form an icosahedral capsid. VP1 is about 5 time more abundant than VP1-FSD in the virion. {ECO:0000269|PubMed:24686475}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates genomic and antigenomic RNA. {ECO:0000250|UniProtKB:Q6UP17, ECO:0000255|PROSITE-ProRule:PRU00539}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 396..403; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (3); Chain (5); Domain (3); Modified residue (1); Nucleotide binding (1); Site (2) |
| Keywords | ATP-binding;Acetylation;Helicase;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Reference proteome;Ribosomal frameshifting;Thiol protease;Transferase;Viral RNA replication;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000269|PubMed:24686475}. |
| Modified Residue | MOD_RES 2346; /note=N-acetylmethionine; by host; /evidence=ECO:0000269|PubMed:24686475 |
| Post Translational Modification | PTM: [Capsid protein VP1]: N-acetylated. {ECO:0000269|PubMed:24686475}.; PTM: [Polyprotein]: Proteolytic cleavages of the polyprotein yield mature proteins. {ECO:0000305|PubMed:24686475}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 299,117 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21248; RHEA:13065 |
| Cross Reference Brenda | 2.7.7.48; |