Detail Information for IndEnz0002001226
IED ID IndEnz0002001226
Enzyme Type ID protease001226
Protein Name RNA replication polyprotein
223 kDa protein
ORF1 protein

Cleaved into: Helicase
EC 3.6.4.13

Includes: Viral methyltransferase
EC 2.1.1.-
; Putative Fe
2+
2-oxoglutarate dioxygenase
EC 1.14.11.-
; Protease
EC 3.4.22.-
; RNA-directed RNA polymerase
EC 2.7.7.48
Gene Name ORF1
Organism Blueberry scorch virus (BBScV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Tymovirales Betaflexiviridae Quinvirinae Carlavirus Blueberry scorch virus (BBScV)
Enzyme Sequence MALTYRSPVEEVLTLFEPTAQSLIASAAVSAFQRHEKDNFEWFRYSVPAFAKEHLSKAGIYLSPYAGFPHSHPVCKTLENYILYVVVPSIVNSTFFFVGIKDFKINFLKSRFDKLNMISALNRYVSSADKIRYGNDFVIRAGVEHRALKRHRGLVDSPTLKALMPNVKSGSKLFLHDELHYWSKEELIGFLEICEPEVLLGTVIYPPELLIGSDCSLNPWCYEYEVKKKKLLFYPDGVRSEGYEQPLSGGYLLQTSRIKLPNAGIYCVDLLCSRFAHHLFSITRGDLITPDNRSFGPFEAVHSGALAGISRGKPNFYPVSQHTILRVYRYLRSLKKPDKQSAMAKFSQIVHEPCGRAVKFMEEFSDLIINTGTLRTVINPEQVKLFFGNLGRCMPPCFASKLKGTRTVCLDEFISMLRPLSVDVTLETISMHSMTMVVTTWSQEAEEGVDLPKIFEEKWEGKQSLDRTEAPYLGLAPFVDYKIQWRLQFNIPKFLNQLAELFVNSCSVNGGVRSMSIPAYLRRLATCRSCVGRAMLCCLTEVDIASLRVVVRNRYPYTEDFYRCRRRWFLRIGAQRRPSFYIEDAKHLERLGQFEEEQFQRPMSRRSLYTLASVSMNGTDDPFCSDCFYDPVPVARAKIVPTPTVIVERALEPLAIDTGTTSDAPCDAPGATCLRGAQAVVCACGLSMAVSAVPYAELKMDFYPDALKGRDAAWYSKEDREYKYNGGSHLCRGWPKWLQLWMQANGVDETYDCMLAQRYGAQGKIGFHADNEEIFMRGAPVHTVSMDGNADFGTECAAGRQYTTLRGNVQFTMPSGFQETHKHAVRNTTAGRVSYTFRRLAKKDESRVIEEVVEVETKDMGFSSSLFGVQIIVDEPCDGVEETFNVQCVPGDGNCFWHSLGSFTGLTVECMKAGIKNFACGPEGAEKLSRQLEPNVWAEDEALCAACAHLGVDLVIFDEDQGFKMLYRYPGNKREALLRLKGSHFEPLEPKEMCVVKAIAQAVKRSPMDVLRVALKKMGEDFKEQICRGKGVMLDVFMVLAKIFDVSACVLQGTEQIMINPKGRIKGLFRMTTDHLSYDGVPDKVKHSEVNVYKHDVALQIEDLIELRELSSLVEYTPSFSRAKLLADCLHDGSTGVMCSELYNDKGHLCPEGRETTRVTIGVLLGTFGCGKSRLFKEILFKLCGKSVCYISPRKALCDSFDDEIRKARGNMGERGIKHYKSLTFEKAILQASKLHKGSLVIIDEIQLYPPGYLDLLLLLAGPTMKYFALGDPCQSDYDSEKDRTILGSVRSDVFELLDGIEYKFNILSRRFQSSLFRGRLPCLMYEEDLEAGAPLRLIDGLESIDTSAAYSRCCLVSSFEEKKIVNAYFGERTKCLTFGESTGMTFDVGCVLITSISAHTSEQRWITALSRFRKDIVFVNAASVAWDTLQSVYANRWLGRFLNRSARQEDLRRMLPGTPLFVEGFQKNLLGADEGKRECKLEGDPWLKTMVDLLQVEDMEDIEIAKEVLQDEWCKTHLPQCELESVRARWVHKILAKEFREKRMGCLVSEQFTDQHSKQMGKHLTNSAERFETIYPRHRAADTVTFIMAVRKRLSFSCPIKESAKLNQALPYGPFLLKEFLKRVPLKPMHDRKMMEQAKFDFEEKKTSKSAATIENHSNRSCRDWLIDVGLVFSKSQLCTKFDNRFRDAKRAQTIVCFQHAVLCRFAPYMRYIEKKLNEVLPSKYYIHSGKGLEELNRWVIEGRFEGVCTESDYEAFDASQDHYIVAFEICLMRYLGLPNDLIEDYKFIKTHLGSKLGNFAIMRFSGEASTFLFNTMANMLFTFLQYDLKGNERICFAGDDMCANGRLHVSSKHKNFMSKLKLKAKVSNTMNPTFCGWNLSSDGIFKKPQLVLERLCIAKETNNLANCIDNYAIEVSFAYLMGERAKQRMDEEEVEAFYNCVRIIVKSKHLLKSDVATIYQTARVD
Enzyme Length 1967
Uniprot Accession Number Q65652
Absorption
Active Site ACT_SITE 994; /evidence=ECO:0000269|PubMed:7871721; ACT_SITE 1075; /evidence=ECO:0000269|PubMed:7871721
Activity Regulation
Binding Site BINDING 832; /note=2-oxoglutarate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805
Calcium Binding
catalytic Activity 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:0000305}; 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 3.6.4.13; 2.1.1.-; 1.14.11.-; 3.4.22.-; 2.7.7.48
Enzyme Function FUNCTION: [RNA replication polyprotein]: RNA-directed RNA polymerase involved in viral RNA replication. {ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000305}.; FUNCTION: Protease: Thiol protease that cleaves the polyprotein. {ECO:0000269|PubMed:7871721}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 1166..1173; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00990
Features Active site (2); Binding site (1); Chain (2); Domain (7); Metal binding (3); Nucleotide binding (1); Site (1)
Keywords ATP-binding;Dioxygenase;Helicase;Hydrolase;Iron;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Oxidoreductase;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 by the viral protease yield mature proteins. {ECO:0000269|PubMed:7871721}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 223,431
Kinetics
Metal Binding METAL 768; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805; METAL 770; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805; METAL 823; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805
Rhea ID RHEA:13065; RHEA:21248
Cross Reference Brenda