Detail Information for IndEnz0002000957
IED ID IndEnz0002000957
Enzyme Type ID protease000957
Protein Name Genome polyprotein
Cleaved into: Nuclear inclusion protein A
NI-A
NIA
EC 3.4.22.44
49 kDa proteinase
49 kDa-Pro
; Nuclear inclusion protein B
NI-B
NIB
EC 2.7.7.48
RNA-directed RNA polymerase
; Capsid protein
CP
Coat protein

Fragment
Gene Name
Organism Watermelon mosaic virus II (isolate USA)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Watermelon mosaic virus Watermelon mosaic virus II (isolate USA)
Enzyme Sequence LSVTRKQCLELGMVLSLSPMGTYLEGTMGCLQLKHGHGGFVIHNTTQLRIHFIQGKDAILIRMPKIFLRLQSATSLDNQNVRNEFAWLEQTFKRRAYGQQSQSSSIILPEGKGSFWIHWITTQDGFCGLPLVSVNDGHVVGIHGLTSNDSEKNFFVPFTDGFEKEYLDNADNLSWDKHWFWEPSKIAWGPLNLVEEQPKEEFKISKLVSDLFGNTVAVQSRKERWVLDAMEGNLVACGQADSALVTKHVVKGKCPYFAQYLSLHDGAXQFFEPLMGAYQPSRLNKDAFKKDFFKYNKPVVLNEVDFNAFEKAVEGVITMMVDFEFAECLFVTDPDEIYGSLNMKAAVGAQYKGKKQDYFSGMDSFDKERLLYLSCERLFNGEKGIWNGSLKAELRPIEKVQANKTRTFTAAPLDTLLGAKVCVDDFNNQFYSFNLKCPWTVGMTKFYGGWDKLMRSLPDGWTYCHADGSQFDSSLTPLLLNAVLSIRCCFMEDWWVGREMLENLYAEIVYTPILAPDGTIFKKFRGNNSGQPSTVVDNTLMVVIAMYYSCCKQGWSEEDIERRLVFFANGDDIILAVKDEDVWLYDTLSASFAELGLNYNFDERTKKREELWFMSHQAMLVDGIYIPKLEPERIVSILEWDRSKELMHRTEAICAAMIEAWGYTELLQEIRKFYLWLLSKDEFKELAASGKAPYIAETALRKLYTDVNTQPSELQRYLEVLDFNHIDGCCESVSLQSGKETVENLDAGKESKKDASDKGNKPQNSQVGQGSKEPTKTGTVSKDVNVGSKGKEVPRLQKITKKMNLPTVGGKIILSLDHLLEYKPSQVDLFNTRATKTQFESWYSAVKVEYDLNDEQMGVIMNGFMVWCIDNGTSPDVNGVWVMMDGEEQVEYPLKPIVENAKPTLRQIMHHFSDAAEAYIEMRNSESPYMPRYGLLRNLRDRELARYAFDFYEVTSKTPNRAREAIAQMKAAALAGVNSRLFGLDGNISTNSENTGRHTARDVNQNMHTLLGMGPPQ
Enzyme Length 1017
Uniprot Accession Number P18478
Absorption
Active Site ACT_SITE 57; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766; ACT_SITE 127; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.; EC=3.4.22.44; 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 3.4.22.44; 2.7.7.48
Enzyme Function FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.; FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and proteolytic activities.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (4); Compositional bias (2); Domain (2); Non-terminal residue (1); Region (1); Site (2)
Keywords Capsid protein;Genetically modified food;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Thiol protease;Transferase;Viral RNA replication;Virion
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
Modified Residue
Post Translational Modification PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 115,489
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda