Detail Information for IndEnz0002009676
IED ID IndEnz0002009676
Enzyme Type ID protease009676
Protein Name Polyprotein P3
Includes: Putative movement protein
MP
; Capsid protein
Coat protein
CP
; Protease
PR
EC 3.4.23.-
; Reverse transcriptase
RT
EC 2.7.7.49
; Ribonuclease H
EC 3.1.26.4
Gene Name
Organism Commelina yellow mottle virus (CoYMV)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Caulimoviridae Badnavirus Commelina yellow mottle virus (CoYMV)
Enzyme Sequence MATRRLPAVTQTDGSRTATESGVPEYEDQIRSYRNDQRRRHIWAGRGRRLLSIMPGVSSSERTLEMQMNPEVQLQRSMNHRAEAVPAEVLYRTFHGSVNHRVYSHRSEERMMVVNGSQVDRSFIQESSFEVLSRTGIEFIHIGVMLVRIQILHRKFAGTMALIVFRDTRWSDDRAVLAAMEIDLSEGNQIVYVLPDIMMTIKSFYRHIQICVMTKGYDGWQGEDNLLITRGLTGRLSNTSNVGFAYDVKAMVEHLQSNGVKAIKGEKWDAKRFHNGQWNIEPSKVVVPMQPTEMKAVSNYDGTTSLRFSNYAAASTSKPPQYNEKDEEINEDEQEINHSLNLILNDEESTDEDEEYYQYQRYAWSQVGDSTFYYDTDGVWEEIDRCNDLPEYVPSETSTPTIDESEAIIDEFLEHAYEQRCDSDESLQSGDPRKYEYPTPQSSPEHLDNESRSRSSSASSTSMQDDVEEIVRLMKEMRMKKQKKKKAQQALSSQAQEEPIIEENIEENKQAQEEPTQEEIPTHKENQPEEIQNEEIHVFEEEPAFKHLAAQLSELVNMAESSGQSGVGFQPPVNAQPDVNMEGPAGYAPATSQATWSNGVNIPVKSANFRWKGPVGNFQLPSAQGKDGAMLVFGMNYSPEVFDRWASITRNYISSFNFNDGGDKIAWMEDLLGETERKIFVSWRMRFKDEYQNLAKIANQDGGTQAILSQIRRIFLGEDPVLGQNTVQNIAFRKLKQLVCPNYQSIRRYLMDYLTLAAETGLMWSETEGPAISEELFTKMPAAIGERVAQAYKIMDPTSAVNLPSRVYFTINYLTEQCKEASYMRSLKALDFCRDFPIEGYYGRSGEKKKYTARKATKYTGKAHDNHIRVTKAKYQRKCKCYICGQEGHYANQCRNKHKDQQRVAILQSLDLKENEEVVSADDKEEEDDEIFSVLGEEDYQEETIMVLEEDDIQQIIKEFSKFGDLSRRNVGPNFPGPAEVQMGVLKPKSSWRRPIQATLEEINCHHNWTAISTGQLACRSCKQFLAGVQCHHCHAVYCFMCAEAYHDVQAEKILSKDYSFSARGKKGKAVIIEEDEIEGEFLISQLQQENQRLQKQVERLQEELMKLHREKDEALKHSEKASRVFSTIQESDEAELNLIKEELRQFKEETRMAIAQLKEAIIVQEEDTIEERCAMILEEKHTENIYSATAKAEYNGLYNVKVGIKPDNMEPYYINAIVDTGATACLIQISAIPENYYEDAKVTVNFRSVLGIGTSTQMIKAGRILIGEQYFRMPVTYVMNMGLSPGIQMIIGCSFIRSLEGGLRIEKDIITFYKLVTSIETSRTTQVANSIEELELSEDEYLNIAASVETPSFLDQEFARKNKDLLKEMKEMKYIGENPMEFWKNNKIKCKLNIINPDIKIMGRPIKHVTPGDEEAMTRQINLLLQMKVIRPSESKHRSTAFIVRSGTEIDPITGKEKKGKERMVFNYKLLNENTESDQYSLPGINTIISKVGRSKIYSKFDLKSGFWQVAMEEESVPWTAFLAGNKLYEWLVMPFGLKNAPAIFQRKMDNVFKGTEKFIAVYIDDILVFSETAEQHSQHLYTMLQLCKENGLILSPTKMKIGTPEIDFLGASLGCTKIKLQPHIISKICDFSDEKLATPEGMRSWLGILSYARNYIQDIGKLVQPLRQKMAPTGDKRMNPETWKMVRQIKEKVKNLPDLQLPPKDSFIIIETDGCMTGWGAVCKWKMSKHDPRSTERICAYASGSFNPIKSTIDAEIQAAIHGLDKFKIYYLDKKELIIRSDCEAIIKFYNKTNENKPSRVRWLTFSDFLTGLGITVTFEHIDGKHNGLADALSRMINFIVEKNDESPYRFTSSVEDALKVCNDDHGRNLISAVINDIITVLRR
Enzyme Length 1886
Uniprot Accession Number P19199
Absorption
Active Site ACT_SITE 1220; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
DNA Binding
EC Number 3.4.23.-; 2.7.7.49; 3.1.26.4
Enzyme Function FUNCTION: Capsid protein self assembles to form a bacilliform capsid about 90-900 nm in length. The capsid encapsulates the genomic dsDNA. Following virus entry into host cell, provides nuclear import of the viral genome. Virus particles do not enter the nucleus, but are targeted to the nuclear membrane through the interaction with host importins (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Compositional bias (2); Domain (3); Metal binding (5); Region (3); Zinc finger (1)
Keywords Aspartyl protease;Endonuclease;Hydrolase;Magnesium;Metal-binding;Nuclease;Nucleotidyltransferase;Protease;RNA-directed DNA polymerase;Reference proteome;Transferase;Transport;Viral movement protein;Viral penetration into host nucleus;Virus entry into host cell;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Polyprotein P3 is presumably proteolytically cleaved into several chains by viral protease. {ECO:0000305}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 215,662
Kinetics
Metal Binding METAL 1715; /note=Magnesium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1715; /note=Magnesium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1758; /note=Magnesium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1784; /note=Magnesium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1833; /note=Magnesium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408
Rhea ID RHEA:22508
Cross Reference Brenda