Detail Information for IndEnz0002000920
IED ID IndEnz0002000920
Enzyme Type ID protease000920
Protein Name Polyprotein-FSD
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-FSD; Capsid protein VP2
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 MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFLGIPNYKFAKNQKLVNTISKSLDACAKFIRDCPKDKQTEIFPLQGLHTATVKRRNEILTNVMPKFARQEPFVVLFQGPGGIGKTHLVQQLATKCVNSFYQDHEDDYIEISPDDKYWPPLSGQRVAFFDEAGNLNDLTEDLLFRNIKSICSPAYFNCAAADIEHKISPCPFELVFATVNTDLDTLQSKISSTFGQASVFPIWRRCIVVECSWNEKELGPFNYKNPSGHRSDYSHITMNYMSYDDKTQKLALEKEINFDTLFDMIRLRFRKKQQEHDTKISILNNEIQRQSNSKQHFSVCLYGEPGQGKTYNLNKLITTFANATNLKIGSEEKPSIHIFDDYIKDENDENCSKFMDIYNNKLPNNSVIFSATNVYPKTHFFPTFFLTNLIYAFIQPFKQVGLYRRLGFDGYTDIPNSSVNAPIFVQNFKFYERKQHICYFLSLEFLKNIICYIFFFLYFPLKFIKKIDLIEIKDVNKYVYDRYINFLSLSKQIEIVEYPPNLENVEFDFRFNMNKFHRVSFNNPFELDKYIHFNKNSYENLLHFDWKMYLSPRVKHRLALSYEKFFITISEVNKEIIIEELKRYVLLFKQFNIDPNMEINLGEYGSFYYINGKIHLMTINIESNVSEIPVFTDGDYVYISEHKIPVIDLFDNININSKYNLSFDQSIALNSFKTGDSFYSNAKVRKSLSKFVLLNYQTKFKLYLKEAKDKVKNFIETPIGHLLSILLTIFVICYASFKIYSKFSNFFSKDQAIEDQRKGEKKIKKITNYDSDGVQPQRKGEKKIKKVTNYDSDGVQPQSNVKVEEEIKLVFDPTGQKLLFGNDFTSELETLVELEKDDEEFTKSKIDNKSMAGLRREVRRRRYARSKKAQIEKQEVLTLPDVNGFEGGKPYFQIAEEKARKNLCQIYMIANNENCIASKFSDHIVCYGLFVFKKRLASVGHIVEALKCAPGYNLYAGCDQFNGKLYKMNLVRNYRKRELSVWDVDCPNDFVDLTSFFIPKEELYDAENCNTVLGRFGMNKREVYLYGNCEFIQEFFKVDNKGAQEFGYIDWATVDITLTTGGDCGLPYYICERKKFHNKIMGLHFAGNNVNHKTIGMSALIYKEDLVVWKGAERQSKCKFCDVKDIIIAQPDIPKEKYKGYNHEIVWNSLHESSPTTLNEELEHYLNIFPKFTGTIIKHSGDKFYGSVKHSHTQFISKFKTELTVTNGWKLSTAGDCQFESNHISPNTEVMYRVVDVQFNSIFKAFKSQPYIKNFRLIANVYEKDGKQRVTILTIIPVSDFNVKQQTVRQALVPLHLNEDEEVYVTEDVSDIFKTAIKRKQRGILPDVPYETVENETVEILGITHRNMTPEPAQMYKPTPFYKLALKFNLDHKLPVNFNMKDCPQEQKDMMVLDRLGQPNPRITQSLKWAHKDYSPDYELRKYVKEQYMCNIMEYYAGCNLLTEEQILKGYGPNHRLYGALGGMEIDSSIGWTMKELYRVTKKSDVINLDSNGNYSFLNNEAAQYTQELLKISMEQAHNGQRYYTAFNELMKMEKLKPSKNFIPRTFTAQDLNGVLMERWILGEFTARALAWDENCAVGCNPYATFHKFATKFFKFKNFFSCDYKNFDRTIPKCVFEDFRDMLIQANPHMKNEIYACFQTIIDRIQVSGNSILLVHGGMPSGCVPTAPLNSKVNDIMIYTAYVNILRRADRGDITSYRYYRDLVCRLFYGDDVIIAVDDSIADIFNCQTLSEEMKILFGMNMTDGSKSDIIPKFETIETLSFISRFFRPLKHQENFIVGALKKISIQTHFYYATDDTPEHFGQVFKTIQEEAALWEEEYFNKIQSYIQEIIRKFPEISKFFNFESYKSIQKRYIMNGWNEFVKLEKLDLNLNKKKSSKVTGIHSKQYSKFLKFLSRIENEKAALEGNFNKESVNTWYFKMSKAMHLNEIFQKGLISKPLAEFYFNEGQKMWDCNITFRRSKDDLPFTFSGSGTTKACAREQAAEEALVLFSQEDEIVRQINDIQSDCKFCKKMIRYKKLLSGVSIQRQMNVSKITENHVPSAGMMATDPSVAPDSGIATNTQTPSISRVLNPIARALDNPAGTGAPFDKHTYVYNVFTRWPEMSTVVNKSLAAGAEVFKISLDPNKLPKRILQYIQFHKTIIPQIEVQILIGGAAGTVGWLKVGWVPDASTAKKYSLDDLQLVASETINLNSTITMSMIINDSRRNGMFRLTKSDPEPWPGIVCLVEHPITNVQRNDDVNYPVIVSVRLGPDCQLMQPYNDLNLSGGTDPDPDPEPDPDPEPGPDPEPGVDELDLSKYIPNQLIDLLICNSYVPNNVSVDFLSTYPNLNFSIHNITDVVVSSKPYTLALFETESQINSASVWRGDLTQLSVFIQYKFYTRVEAYNKVTTVHTDKWTPNFDGTVYKPVDVKIEHAYGTYELTTMWLTSYGLVMEWSLDESRVFYGTYKTDSNGRRWLIDGNTPIARSDHCFIVSSPDLLSDDKAYYNNPIGAKQGGKLVDGAQIYRIFKTESGGYRSDPFVPETYWPSETPYNADWSGVKMPYQIRKVIQTGNNLAGKHLDGDLKMCAMIRQGSSSTQSTDNYFYPIYVHNFSALLKQMNLILKERKTKYIKFDLQVGGKPFAQMGFGDGAFIGRTTMFRQIRAAITNVILLKNIVGVDDLSGLQALPTSGFADWVVKAQSTNSKFLNDFYNDKISIERQASLGIAAAIGAGQGLFGGLSAQWQWQQQADWSRQMQRERLDMMEKLANINNQARLNQLTQSGAQQRITQQAAYQQQMNALGAGSVSAQNGMYTPSNYTPLPSYKSNTTNYYNNSVYHTDNNITNNPSNTSLTNNINNFNPELFQQQRERMPTPSEAYDNSKGFVPQPGTSKSIATENINPNYKDEEHIYEPIEQQNHEYADIDYNAMNISRENKNSSNFGNVGILDHQYADIDYDAMKIARDQQNSSKFGNVGVLNHQYAELDFSKNNTRKNSQILDNSLYSKTQPSSKMIDNSLYGINPNKMVENQNYEPASMERKNSIYSSNLNSSNNLKFNNIPNFKGPTNLNISGAKPAGFGSGIIQPAINKYTDFSKPN
Enzyme Length 3390
Uniprot Accession Number C1JCT2
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: [Capsid protein VP1-FSD]: Assembles with VP1 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: [Capsid protein VP2]: Assembles with VP1 and VP1-FSD to form an icosahedral capsid. {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 (6); Compositional bias (1); Domain (3); Modified residue (1); Nucleotide binding (1); Region (2); 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-FSD]: Virion {ECO:0000269|PubMed:24686475}.; SUBCELLULAR LOCATION: [Capsid protein VP2]: 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-FSD]: N-acetylated. {ECO:0000269|PubMed:24686475}.; PTM: [Polyprotein-FSD]: 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 390,107
Kinetics
Metal Binding
Rhea ID RHEA:21248; RHEA:13065
Cross Reference Brenda