| IED ID | IndEnz0002011913 |
| Enzyme Type ID | protease011913 |
| Protein Name |
Genome polyprotein Cleaved into: Core protein; Envelope glycoprotein E1; Envelope glycoprotein E2 NS1 ; p13; p6; Viroporin p7; Protease NS2 EC 3.4.22.- Non-structural protein 2 NS2 ; Serine protease/helicase NS3 EC 3.4.21.98 EC 3.6.1.15 EC 3.6.4.13 Hepacivirin NS3 helicase NS3 protease NS3P ; Non-structural protein 4A NS4A ; Non-structural protein 4B NS4B ; Non-structural protein 5A NS5A ; RNA-directed RNA polymerase EC 2.7.7.48 NS5B |
| Gene Name | |
| Organism | Hepatitis GB virus B (GBV-B) (GB virus B) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Flasuviricetes Amarillovirales Flaviviridae Hepacivirus Hepacivirus B Hepatitis GB virus B (GBV-B) (GB virus B) |
| Enzyme Sequence | MPVISTQTSPVPAPRTRKNKQTQASYPVSIKTSVERGQRAKRKVQRDARPRNYKIAGIHDGLQTLAQAALPAHGWGRQDPRHKSRNLGILLDYPLGWIGDVTTHTPLVGPLVAGAVVRPVCQIVRLLEDGVNWATGWFGVHLFVVCLLSLACPCSGARVTDPDTNTTILTNCCQRNQVIYCSPSTCLHEPGCVICADECWVPANPYISHPSNWTGTDSFLADHIDFVMGALVTCDALDIGELCGACVLVGDWLVRHWLIHIDLNETGTCYLEVPTGIDPGFLGFIGWMAGKVEAVIFLTKLASQVPYAIATMFSSVHYLAVGALIYYASRGKWYQLLLALMLYIEATSGNPIRVPTGCSIAEFCSPLMIPCPCHSYLSENVSEVICYSPKWTRPVTLEYNNSISWYPYTIPGARGCMVKFKNNTWGCCRIRNVPSYCTMGTDAVWNDTRNTYEACGVTPWLTTAWHNGSALKLAILQYPGSKEMFKPHNWMSGHLYFEGSDTPIVYFYDPVNSTLLPPERWARLPGTPPVVRGSWLQVPQGFYSDVKDLATGLITKDKAWKNYQVLYSATGALSLTGVTTKAVVLILLGLCGSKYLILAYLCYLSLCFGRASGYPLRPVLPSQSYLQAGWDVLSKAQVAPFALIFFICCYLRCRLRYAALLGFVPMAAGLPLTFFVAAAAAQPDYDWWVRLLVAGLVLWAGRDRGPRIALLVGPWPLVALLTLLHLATPASAFDTEIIGGLTIPPVVALVVMSRFGFFAHLLPRCALVNSYLWQRWENWFWNVTLRPERFLLVLVCFPGATYDTLVTFCVCHVALLCLTSSAASFFGTDSRVRAHRMLVRLGKCHAWYSHYVLKFFLLVFGENGVFFYKHLHGDVLPNDFASKLPLQEPFFPFEGKARVYRNEGRRLACGDTVDGLPVVARLGDLVFAGLAMPPDGWAITAPFTLQCLSERGTLSAMAVVMTGIDPRTWTGTIFRLGSLATSYMGFVCDNVLYTAHHGSKGRRLAHPTGSIHPITVDAANDQDIYQPPCGAGSLTRCSCGETKGYLVTRLGSLVEVNKSDDPYWCVCGALPMAVAKGSSGAPILCSSGHVIGMFTAARNSGGSVSQIRVRPLVCAGYHPQYTAHATLDTKPTVPNEYSVQILIAPTGSGKSTKLPLSYMQEKYEVLVLNPSVATTASMPKYMHATYGVNPNCYFNGKCTNTGASLTYSTYGMYLTGACSRNYDVIICDECHATDATTVLGIGKVLTEAPSKNVRLVVLATATPPGVIPTPHANITEIQLTDEGTIPFHGKKIKEENLKKGRHLIFEATKKHCDELANELARKGITAVSYYRGCDISKIPEGDCVVVATDALCTGYTGDFDSVYDCSLMVEGTCHVDLDPTFTMGVRVCGVSAIVKGQRRGRTGRGRAGIYYYVDGSCTPSGMVPECNIVEAFDAAKAWYGLSSTEAQTILDTYRTQPGLPAIGANLDEWADLFSMVNPEPSFVNTAKRTADNYVLLTAAQLQLCHQYGYAAPNDAPRWQGARLGKKPCGVLWRLDGADACPGPEPSEVTRYQMCFTEVNTSGTAALAVGVGVAMAYLAIDTFGATCVRRCWSITSVPTGATVAPVVDEEEIVEECASFIPLEAMVAAIDKLKSTITTTSPFTLETALEKLNTFLGPHAATILAIIEYCCGLVTLPDNPFASCVFAFIAGITTPLPHKIKMFLSLFGGAIASKLTDARGALAFMMAGAAGTALGTWTSVGFVFDMLGGYAAASSTACLTFKCLMGEWPTMDQLAGLVYSAFNPAAGVVGVLSACAMFALTTAGPDHWPNRLLTMLARSNTVCNEYFIATRDIRRKILGILEASTPWSVISACIRWLHTPTEDDCGLIAWGLEIWQYVCNFFVICFNVLKAGVQSMVNIPGCPFYSCQKGYKGPWIGSGMLQARCPCGAELIFSVENGFAKLYKGPRTCSNYWRGAVPVNARLCGSARPDPTDWTSLVVNYGVRDYCKYEKLGDHIFVTAVSSPNVCFTQVPPTLRAAVAVDGVQVQCYLGEPKTPWTTSACCYGPDGKGKTVKLPFRVDGHTPGVRMQLNLRDALETNDCNSINNTPSDEAAVSALVFKQELRRTNQLLEAISAGVDTTKLPAPSIEEVVVRKRQFRARTGSLTLPPPPRSVPGVSCPESLQRSDPLEGPSNLPSSPPVLQLAMPMPLLGAGECNPFTAIGCAMTETGGGPDDLPSYPPKKEVSEWSDGSWSTTTTASSYVTGPPYPKIRGKDSTQSAPAKRPTKKKLGKSEFSCSMSYTWTDVISFKTASKVLSATRAITSGFLKQRSLVYVTEPRDAELRKQKVTINRQPLFPPSYHKQVRLAKEKASKVVGVMWDYDEVAAHTPSKSAKSHITGLRGTDVRSGAARKAVLDLQKCVEAGEIPSHYRQTVIVPKEEVFVKTPQKPTKKPPRLISYPHLEMRCVEKMYYGQVAPDVVKAVMGDAYGFVDPRTRVKRLLSMWSPDAVGATCDTVCFDSTITPEDIMVETDIYSAAKLSDQHRAGIHTIARQLYAGGPMIAYDGREIGYRRCRSSGVYTTSSSNSLTCWLKVNAAAEQAGMKNPRFLICGDDCTVIWKSAGADADKQAMRVFASWMKVMGAPQDCVPQPKYSLEELTSCSSNVTSGITKSGKPYYFLTRDPRIPLGRCSAEGLGYNPSAAWIGYLIHHYPCLWVSRVLAVHFMEQMLFEDKLPETVTFDWYGKNYTVPVEDLPSIIAGVHGIEAFSVVRYTNAEILRVSQSLTDMTMPPLRAWRKKARAVLASAKRRGGAHAKLARFLLWHATSRPLPDLDKTSVARYTTFNYCDVYSPEGDVFVTPQRRLQKFLVKYLAVIVFALGLIAVGLAIS |
| Enzyme Length | 2864 |
| Uniprot Accession Number | Q69422 |
| Absorption | |
| Active Site | ACT_SITE 870; /note=For protease NS2 activity; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU01030; ACT_SITE 888; /note=For protease NS2 activity; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU01030; ACT_SITE 909; /note=For protease NS2 activity; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU01030; ACT_SITE 997; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01166; ACT_SITE 1021; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01166; ACT_SITE 1079; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01166 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000269|PubMed:10497107}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: 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:0000269|PubMed:10497107}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: 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 | 3.4.22.-; 3.4.21.98; 3.6.1.15; 3.6.4.13; 2.7.7.48 |
| Enzyme Function | FUNCTION: [Core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Probably affects various cell signaling pathways, host immunity and lipid metabolism (Probable). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}.; FUNCTION: [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). {ECO:0000250|UniProtKB:P27958}.; FUNCTION: [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). {ECO:0000250|UniProtKB:P27958}.; FUNCTION: [p13]: May function as a multimeric ion channel protein (viroporin). {ECO:0000269|PubMed:16492760}.; FUNCTION: [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}.; FUNCTION: [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (PubMed:10497107). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (PubMed:17093192). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:10497107, ECO:0000269|PubMed:17093192}.; FUNCTION: [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). {ECO:0000250|UniProtKB:P27958}.; FUNCTION: [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly. {ECO:0000250|UniProtKB:Q99IB8}.; FUNCTION: [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable from 6 to 8.5. {ECO:0000269|PubMed:10497107}; |
| Pathway | |
| nucleotide Binding | NP_BIND 1144..1151; /note=ATP; /evidence=ECO:0000305 |
| Features | Active site (6); Chain (13); Compositional bias (2); Domain (5); Glycosylation (15); Helix (3); Lipidation (1); Metal binding (13); Motif (1); Mutagenesis (4); Natural variant (30); Nucleotide binding (1); Region (3); Site (10); Transmembrane (16); Turn (1) |
| Keywords | 3D-structure;ATP-binding;Activation of host autophagy by virus;Apoptosis;Capsid protein;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;Helicase;Host cytoplasm;Host endoplasmic reticulum;Host lipid droplet;Host membrane;Host mitochondrion;Host nucleus;Host-virus interaction;Hydrolase;Inhibition of host MAVS by virus;Inhibition of host RLR pathway by virus;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Interferon antiviral system evasion;Ion channel;Ion transport;Lipoprotein;Magnesium;Manganese;Membrane;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Oncogene;Palmitate;Phosphoprotein;Protease;RNA-binding;RNA-directed RNA polymerase;Ribonucleoprotein;SH3-binding;Serine protease;Thiol protease;Transcription;Transcription regulation;Transferase;Transmembrane;Transmembrane helix;Transport;Viral RNA replication;Viral attachment to host cell;Viral envelope protein;Viral immunoevasion;Viral ion channel;Viral nucleoprotein;Viral penetration into host cytoplasm;Virion;Virus entry into host cell;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}.; SUBCELLULAR LOCATION: [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}.; SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}.; SUBCELLULAR LOCATION: [p13]: Host endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}.; SUBCELLULAR LOCATION: [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N-terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}.; SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity). P13 may be further cleaved into p6 and p7 if the internal cleavage site is used (PubMed:15060070, PubMed:16492760). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:15060070, ECO:0000269|PubMed:16492760}.; PTM: [Envelope glycoprotein E1]: Highly N-glycosylated. {ECO:0000250|UniProtKB:P27958}.; PTM: [Envelope glycoprotein E2]: Highly N-glycosylated. {ECO:0000250|UniProtKB:P27958}.; PTM: [Non-structural protein 4B]: Palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions. {ECO:0000250|UniProtKB:P27958}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (3) |
| Cross Reference PDB | 2LZP; 2LZQ; 2MKB; |
| Mapped Pubmed ID | 16882659; 18632962; 20701941; 24741107; |
| Motif | MOTIF 1228..1231; /note=DECH box; /evidence=ECO:0000250|UniProtKB:Q99IB8 |
| Gene Encoded By | |
| Mass | 312,705 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.64 mM for ATP for NS3 NTPase; KM=1.41 mM for CTP for NS3 NTPase; KM=1.12 mM for UTP for NS3 NTPase; KM=1.87 mM for dATP for NS3 NTPase; KM=1.22 mM for dCTP for NS3 NTPase; KM=0.65 mM for dTTP for NS3 NTPase; |
| Metal Binding | METAL 1037; /note=Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01166; METAL 1039; /note=Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01166; METAL 1085; /note=Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01166; METAL 1089; /note=Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01166; METAL 1151; /note=Magnesium 1; catalytic; for NS3 helicase activity; /evidence=ECO:0000250|UniProtKB:Q9WMX2; METAL 1229; /note=Magnesium 1; catalytic; for NS3 helicase activity; /evidence=ECO:0000250|UniProtKB:Q9WMX2; METAL 1905; /note=Zinc 2; structural; /evidence=ECO:0000250|UniProtKB:Q9WMX2; METAL 1923; /note=Zinc 2; structural; /evidence=ECO:0000250|UniProtKB:Q9WMX2; METAL 1925; /note=Zinc 2; structural; /evidence=ECO:0000250|UniProtKB:Q9WMX2; METAL 1947; /note=Zinc 2; structural; /evidence=ECO:0000250|UniProtKB:Q9WMX2; METAL 2491; /note=Magnesium 2; catalytic; for RNA-directed RNA polymerase activity; /evidence=ECO:0000250|UniProtKB:P26663; METAL 2589; /note=Magnesium 2; catalytic; for RNA-directed RNA polymerase activity; /evidence=ECO:0000250|UniProtKB:P26663; METAL 2590; /note=Magnesium 2; catalytic; for RNA-directed RNA polymerase activity; /evidence=ECO:0000250|UniProtKB:P26663 |
| Rhea ID | RHEA:23680; RHEA:13065; RHEA:21248 |
| Cross Reference Brenda |