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 |