Detail Information for IndEnz0002011491
IED ID IndEnz0002011491
Enzyme Type ID protease011491
Protein Name Replicase polyprotein
EC 2.7.7.48
EC 3.4.22.-
Gene Name ORF1
Organism Acute bee paralysis virus (strain Rothamsted) (ABPV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Dicistroviridae Aparavirus Acute bee paralysis virus Acute bee paralysis virus (strain Rothamsted) (ABPV)
Enzyme Sequence MNFTKQPASLKYLSSMKLITSQDQDFFNFGEVSREFILEQAYVNGYDFHMLHQDMNCIGFVLSIFDEDARDEYEYKDLNCEYHENLFDAVVDSEFDKIWPHLVLKYITYYPCSLNWRGMPTIPIVYVSKHFWYELYRTGFLNKLYHCGSWTDILLLLSGDVETNPGPVETYKDLCRRKNIRKRKSRIREEIKMQQHIDKIIGQENEEYKIINVNMQGIFSFNEEKEIIKSTAWKFNSTLDKTNSIIDNLIPQLEETLAGFRKTYSKCESKIFGTISVVDVCVDLISALLQVSFAKPAMKIASLAVEVFRLIKKYVSNININIDKIKELLSYGKVALNNNNPIIHVTMQSNSPILEVLLQPNIIVSAIFIALSVVFHKKFTYKKLGIEAMIKRLGDLGRAAKGCSDLNVVLNQAITNHMLEHFGKNVLGLKQEDELKVLVEGYRNWCDEVRDLVGHKINSDGELDSKSIVENIMKDVYEIQRIENMYKKGLEISRNIAELKLPTKLTISFNTHMRYLTEVFKSVDTSGAFGNKPRTQPIVIWLFGESGRGKSGMTWPLAIDLNNSLLDNVDEMRNFSKNIYMRNVEQEFWDNYQGQNIVCXDDFGQMRDSSSNPNPEFMELIRTANIAPYPLHMAHLEDKRKTKFTSKVIIMTSNVFEQDVNSLTFPDAFRRRVDLCAEVKNKDEFTKMCWSKSAGKMVQRLDKGKVKKITGDIHSTVPYIVDLIDPESGEVYKTGLEYEEFLDMCLEKTSQCRDDSAKLNDFLMDYAEKRANRSREIDEVCARTMDEAFVDAYDDVIDVNMQIETVDEMELIEPNKLREMIEQCSNKIVYTYEGIAVKITSLAFKLATLNYEEQWEQIKEMKYYVKVSSGVNYLKRVLSQGMKVCEEWMKEMINYVKEHPWMTVSLILGTLIGILTVVGFWKWLCSGDKKKNPIKRHFINTGNVLILPDRELNTFWKNQESLDLRDMYINRVEEHIISLLKLQHKVVLVPKVTKYILTTVENHAKISDKIILITRNRYLNYQGKFVELICGEINQFFIDPETLDTNVEAFASADLKTFVQRKPIVIEGPEFVEAQTSGDQITLRKQTQKVIEAFASSDAITMARKTPKFVESDDVVEVSMQMWKDQVAQKLITNRVLTNLYKICLVKENGDMVPLLNGLFVRSNIMLAPGHLVGFLSDSDTIEIRNLFDVVFRVPWKDVKKVDVVNAFGESKEAVLLCFPKFVCQHTDLVKHFQDSESMSKFKRCEVTLPVLRYSDKMNRFLATLIECDKVEAYDRPYTLNDSSKGQYILRQGLEYTMPTTNGDCGAPLVINETQVIRKIAGIHVAGDARGKAYAESISQKDLIRAFSKIDVSMQIQLDLDQTLNFNQQQXIIPPNAEFGPEDLDFCDLPSLKMIPVGRLSEPLFEPGKTDIRPSLVYGKISEIKTKPAILRNVIVDGKIVNIKHKNLKKCAMDTPYVSKEMTEEAFQLVKSVWLKGMRNELKKVLTYEEAICGNDSSEFISAINRSSSPGFPWIRDRIKGTKGKQGWFGAEGEYILDEDVFEAVKTRIQNAKNGVRTPVMWVDTLKDERRPIEKVDQLKTRVFSNGPMDFSITFRMYYLGFIAHLMENRITNEVSIGTNVYSQDWNKTVRKLKTMGPKVIAGDFSTFDGSLNVCIMEKFADLANEFYDDGSENALIRHVLLMDVYNSTHICGDSVYMMTHSQPSGNPATTPLNCFINSMGLRMVFELCSKKYSALNGTKCYVMKDFSKHVSIVSYGDDNVINFSDEVSEWFNMETITEAFEKLGFTYTDELKGKNGEVPKWRTIEDVQYLKRKFRYDSKRKVWEAPLCMDTILEMPNWCRGSLDIQEGTKVNCENAIMELSMHEEYVFDKWSKVISKAYQKATGDCLDISTYNGYAQERFLNYYL
Enzyme Length 1906
Uniprot Accession Number Q9DSN9
Absorption
Active Site ACT_SITE 1171; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1213; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1305; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222
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 2.7.7.48; 3.4.22.-
Enzyme Function FUNCTION: Replicase polyprotein contains helicase, VPg, protease and RNA-directed RNA polymerase functions.; FUNCTION: RNA-directed RNA polymerase replicates genomic and antigenomic RNA and transcribes the vial genome.; FUNCTION: The protease generates mature viral proteins from the precursor polyprotein.; FUNCTION: VPg is covalently linked to the 5'-end of genomic RNA.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 544..551; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551
Features Active site (3); Chain (1); Domain (3); Nucleotide binding (1); Region (1)
Keywords ATP-binding;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Reference proteome;Thiol protease;Transferase;Viral RNA replication
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Specific enzymatic cleavages in vivo by the viral protease yield a variety of precursors and mature proteins. {ECO:0000305}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 219,430
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda