Detail Information for IndEnz0002013799
IED ID IndEnz0002013799
Enzyme Type ID protease013799
Protein Name RNA replication polyprotein
ORF1 protein

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
; Helicase
EC 3.6.4.13
Gene Name ORF1
Organism Citrus leaf blotch virus (isolate Nagami kumquat/France/SRA-153/1984) (CLBV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Tymovirales Betaflexiviridae Trivirinae Citrivirus Citrus leaf blotch virus Citrus leaf blotch virus (isolate Nagami kumquat/France/SRA-153/1984) (CLBV)
Enzyme Sequence MALMSNKTAIESILGNFEKKHVDAIYNAAAQTILSHSEFRNKHFAYSLNSYQKKIASKVGIELYPNGYLPHSHPLSKIFENHLLFDVLPGVVNTSRLVMCSIKESKVLVFKGIRDKSRRQVSDLNALNSLNNSHTSFINRLVASKDVSRYTEEADAFFQSKKGSPELFSRNFIKSLENKEAVFFHDEVHHWTKAQMFSFLKSTKVKRFIFTVVYPPEILKKFANSQNPKVYDFKVDKGRLFFFPDGVKTEAYEQKLNMEWLFSASHLRSGDCVWTVTRHKSIYAHHLFEISIGELVTDSKLFFSDYNSIDMSKIFLDRFRSYEVFPISIEHLYKVYSYLLCLKKPDLESGLAKLRQIIGDDVEIKEFLFFEQFCKRLIERQTSWGLFGHSFFEKLTDMALSSLPNSIARIFPQWKKKNTFEFLFSLGTLVVDVERKVCFEHVLEEWGFEVVITDENAYLDPLSIFAINENFNEDRVDDGYLERIRLPFWNLNDYDLKRKRVNAYNILSYRFEEERKIESAQKGPNKMLQIEWYGIKEFKVDPFISNSITEFTLLEALLGKRIDPKKYSYSKQACTLSNYLTFLCAEGLDGFNLEEHLERRLKAAGHDVSDDEEEELTSAEQAGPIKILADPLGFMKECLEEIPIETEPSLEERGQFSTDYHSEKFEINYNDIFNPHNCMNTHGDEIPTPSDGNCFFSAFTETFEVERPDTLRSDFSDWLMEFNGGSYASLAEMIRPNGVFMEAELIYLFCVFRGVTLIIHDRTHEKENVYAVHRGFEEGHMVHRGNHFVGIETYNISTLTSDPLLGDIPCGFSEEITKFHFRPDHFNCAQFRGRKAAFITKVDADYGHNGMVYPHNSWVPSLEEIIQICGQGDDFNCALINFYEANSSLGFHRDNERVYNDDPILTVCTFGEGRFTIEFKDQVTSFLMTAGSFFLMPKGFQKKARHSVSNEMSRVSITFRKHVRRLNGSPIAIREENYKNTCLINAFSKAMKRSKQAIIAKLKTVNSPFWSRYLSEGNGGSIEDCQSACEALDVTVDLNVNGKCVVLGKGALRISMALRNNHFSVINAAQLMERTFVSHLLEKGNVNVLEGFDAMLSGDVGAAGVNKIQFAANFEFARILANSFLNMTTGICLGKALDNGEKYFLHILKDRVKQIGIDVTMVCGFAGSGKSRKLQSWLHSRKKGNFCVVSPRTNLAADWAFKLELEPNEQRKVSTFEKFIKTDKSKLDLIVIDELTLFPNGYLDLLVYELADVNRHCQIILLFDPLQARYHNKMDESILTFEHDVDRLIGGQNIEYIYSTHRMSRYFNRFFDVPCFNQADRTEEQRLWIFDDVYSIPSICSDRQEPCDVLLVESDLEKKAFSPIINVMTFGESQGLTFNHVCILLSESSAASNEFRWMVALTRARTRFSLCSTFLGGIEEFKVKRKESLITSILQGEKITFNRLNLMLKCNLIRREKENGCRDEVDREERLEGDPFLKPFIFLGQRVEKDEDEVEEVKIREPTCQTHLYITEPNFGLCYNFDFIREKEQREYREDMLVTNQFCDSYDKVHINGKRETPGPLRFKAIYPKHSADDDMTFWMAVRKRLVFREEEENYQRLSRAHLVGGLLYTNFKKKMGLEFTFDQGLLEESINAFEKKKLEKSCGTIKSHSIRSDIDWALNDVFLFMKSQLCTKYEKQFVDAKAGQTLACFQHLILVQFAPWCRYLETQIRNQLPEEIYIHSNKNFDDLNAWVKKFFQRDICVESDYEAFDASQDEYILSFEIHLMKDAHFPQKIIDAYIDLKCKLGCKLGHFSIMRFTGEFCTFLFNTLANMAFTMCRYEWRRGQPIAFAGDDMCALNNLAVCHDFDDLFELISLKAKVERTETPMFCGWRLTPYGIVKEPELVYNRFQVAIEEGKVLECLENYAIEVSYAYSLSERLYEVLKSERQVQYHQAVVRFIVTHIDKLKTKVRDLFLEQSSDEDI
Enzyme Length 1962
Uniprot Accession Number Q91QZ3
Absorption
Active Site ACT_SITE 982; /evidence=ECO:0000250|UniProtKB:Q65652; ACT_SITE 1062; /evidence=ECO:0000250|UniProtKB:Q65652
Activity Regulation
Binding Site BINDING 954; /note=2-oxoglutarate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805
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;
DNA Binding
EC Number 2.1.1.-; 1.14.11.-; 3.4.22.-; 2.7.7.48; 3.6.4.13
Enzyme Function FUNCTION: RNA replication polyprotein: RNA-directed RNA polymerase involved in viral RNA replication. {ECO:0000250|UniProtKB:Q65652}.; FUNCTION: Protease: Thiol protease that cleaves the polyprotein. {ECO:0000250|UniProtKB:Q65652}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 1164..1171; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00990
Features Active site (2); Binding site (1); Chain (1); Domain (7); Metal binding (3); Nucleotide binding (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:0000250|UniProtKB:Q65652}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 227,379
Kinetics
Metal Binding METAL 892; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805; METAL 894; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805; METAL 946; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805
Rhea ID RHEA:21248; RHEA:13065
Cross Reference Brenda