Detail Information for IndEnz0002011230
IED ID IndEnz0002011230
Enzyme Type ID protease011230
Protein Name Polyprotein P3
P194 protein

Cleaved into: Putative movement protein
MP
; Capsid protein
Coat protein
CP
; Protease
PR
EC 3.4.23.-
; Reverse transcriptase/Ribonuclease H
RT
EC 2.7.7.49
EC 3.1.26.4
p55
Gene Name
Organism Rice tungro bacilliform virus (isolate Philippines) (RTBV)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Caulimoviridae Tungrovirus Rice tungro bacilliform virus Rice tungro bacilliform virus (isolate Philippines) (RTBV)
Enzyme Sequence MSLRPFTGTSRTITQDSTSESNIKKGKNSTKRELIEEVDVNQEVENFDWKKLSGIKPNKLYEKNWQEKVKLKQQSIVSAYKEEAISVTHNAYTTTLFPQEVIKNVKNQGKLYYHIGMMAIGVKGLHRRKIGTKVMIMFYDDSFGKAREASIGSIEMDMNAGCGVFYSCPDFAKYIKDLSHLKIGIQTLGYENYEGKNLSVAIKTIGRLTTNIQSKYKINVKDIVEQISSQGIIMVAPMEIDSSHLDGNEWDLSKFLNHENTSRVPTKALIYQNLQGGESLRFSNYKQTRMHDPTENNSDEDEDLKILGEQLNIKMARFYTMQTPEEELREVIQQLEREKQAMIAKLEAKMKESSKMAIVEDNFNPNNEYLEDTYSEYEDLEFEKLGLTGWEDLDQDSIETEEITEWENPNQVLHREIRAYKSVSEQIEDIFGELLKEHGNYDMALKNLEEKYDLDKIEKAKSIEEIAKSSTSSEIRPTKRPKEEQTAYEDDMRDDWKRKELTVNPIEASKDRNFERIGSSYKKNFYPSRSEILNLDNVPPQFYYDQLVTWEGIVKNEWEARKKDGMDMWSWMDGRITGLVLYLVQDWISKNQAAYNDIKSRGDRPENFVKMVKDRFLIEDPTDERRTALQRLAQRELEALNCEDPTKIQPFMAEYLKKASEAKKGFDVVYVERLFDRLPEAVGKVVKADFVKDGNSYEAGIGIAVSYISTWMRAKCIKETEAKTQKKASLAFCRSIYTIGDYKKRKILKRVTNYNKNRRKNYVRRPSIKKKCRCYICQDENHLANRCPRRYTNQARASLIDGLDEDIVSIASDDEDIENFLEIIELDEFIAHSSQEHEHTWEIGGKKDKVCEICSYFTDYNKTVSCKTCETQYCKTCSDQLALEVTEVKKPTKEETMIDDLKLNVKNLEFRVTILEHKVEMQNLQDKFETMQIRNKSEITEIPTTSLAMRANESNYIKTSINKTAGCYVETKISFNNENRIITALIDSGSTHNIICPTLIPASWINNTHREIIMFAVDNSKYNLNQELIDDIKLQFQEVDETFGIKYKLGQTYVAPKPTKTFIIGHRFLTNENGSVTIHKDYITIQKTTGIYPTARHELKSEFARKHGGRPPLFSNIPETYNKIPHLHSYQPQPILGYKNEIGNQSLITMVKELEALGFIGDDITKNRTTWVCDFKIINPDINITCATIPYTPADKEVFEKQIKELLDNKLIKKADPTCRHRTAAFIVRNHSEEVAQKPRIVYNYKRLNDNMHTDPFNIPHKISMINLIQKANIFSKFDLKAGFHHMKLKDDFKDWTTFTCSEGLYTWNVCPFGIANAPCAFQRFMQESFGDLKFALLYIDDILIASNNEKEHIEHLKIFFNRVKEVGCVLSKKKSKMFLKEVEYLGVEIKEGKISLQPHIVDKIKKFDKNKLNTLKGLQAYLGLLNYARGYIKDLSKLVGPLYKKTGKNGQRIFNKEDWNIIFKIEREVSKIKPLERPKETDYIIIETDASEEGWGAVLVCKPDKYSGKDTEKIAGYASGNFGEKKTWTSLDYEIEAINEALNKFQIYLDKDFTIRTDCEAIVKGIKTEDYKKRSKTRWIKLRDNLLKDGYKPTFEHIKGNKNFLPNFLSREGDFILKCLQNPDSTESYSIDSSESIPLYIDSKESHSIESDDSIPLYRDKLLPLVERLKEKSA
Enzyme Length 1675
Uniprot Accession Number P27502
Absorption
Active Site ACT_SITE 987; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01160
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; 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 130 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, ECO:0000269|PubMed:15914861}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (4); Compositional bias (2); Domain (2); Motif (2); Propeptide (3); Region (2); Sequence conflict (3); Zinc finger (1)
Keywords Aspartyl protease;Capsid protein;Direct protein sequencing;Endonuclease;Host nucleus;Host-virus interaction;Hydrolase;Metal-binding;Nuclease;Nucleotidyltransferase;Protease;RNA-directed DNA polymerase;Reference proteome;Transferase;Transport;Viral movement protein;Viral penetration into host nucleus;Virion;Virus entry into host cell;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Capsid protein]: Virion. Host nucleus.
Modified Residue
Post Translational Modification PTM: Polyprotein P3 is proteolytically cleaved into several chains by viral protease. {ECO:0000269|PubMed:15831103}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 479..499; /note=Bipartite nuclear localization signal 1; /evidence=ECO:0000255; MOTIF 744..760; /note=Bipartite nuclear localization signal 2; /evidence=ECO:0000255
Gene Encoded By
Mass 194,082
Kinetics
Metal Binding
Rhea ID RHEA:22508
Cross Reference Brenda