Detail Information for IndEnz0002012221
IED ID IndEnz0002012221
Enzyme Type ID protease012221
Protein Name Protein P1-P2
Cleaved into: Serine protease
EC 3.4.21.-
; RNA-directed RNA polymerase
EC 2.7.7.48
69.6 kDa protein
Gene Name ORF1/ORF2
Organism Potato leafroll virus (strain Potato/Scotland/strain 1/1984) (PLrV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Sobelivirales Solemoviridae Polerovirus Potato leafroll virus (PLrV) Potato leafroll virus (strain Potato/Scotland/strain 1/1984) (PLrV)
Enzyme Sequence MNRFTAYAALFFMFSLCSTAKEAGFLHPAFNFRGTSTMSASSGDYSAAPTPLYKSWALPSSLNLTTQPPPPLTDRSYYELVQALTSKMRLDCQTVGDMTWRHLSEMLFASWNSVKEVSLKAASVTLWAIINIWFGLYWTLARLITLFLWTFSIEALCLILLGCITSLIYKGALSLSEHLPVFLFMSPLKIIWRAAFSKRNYKNERAVEGYKGFSVPQKPPKSAVIELQHENGSHLGYANCIRLYSGENALVTAEHCLEGAFATSLKTGNRIPMSTFFPIFKSARNDISILVGPPNWEGLLSVKGAHFITADKIGKGPASFYTLEKGEWMCHSATIDGAHHQFVSVLCNTGPGYSGTGFWSSKNLLGVLKGFPLEEECNYNVMSVIPSIPGITSPNYVFESTAVKGRVFSDEAVKELEREASEAVKKLARFKSLTDKNWADDYDSDEDYGLEREAATNAPAEKTAQTNSAEKTAPSTSAEKTALTNKPFKWASGTVRQNKRQLRHPRRRYKRTTNGQNGRTDHHSYGGENQSLGDRGEDSEQGVSESPAEAQTKEARKAWREEQAKQFTSYFNAIYKWGAQEGGCPPGFRKCGHIPRYYHPRTRGETQWGQKLCQVHPELADKTAGFGWPKAGSEAELQSLNLQAARWLQRAESATIPGAEARKRVIEKTVEAYRNCVTNAPLCSLKSKLDWAGFQQDIREAVQSLELDAGVGIPYIAYGLPAHRGWVEDHKLLPVLTQLTFDRLQKMSEASFEDMSAEELVQEGLCDPIRLFVKGEPHKQSKLDEGRYRLIMSVSLVDQLVARVLFQNQNKREISLWRSVPSKPGFGLSTDTQTAEFLECLQKVSGAPSVEELCANHKEYTRPTDCSGFDWSVAYWMLEDDMEVRNRLTFNNTQLTKRLRAAWLKCIGNSVLCLSDGTLLAQTVPGVQKSGSYNTSSSNSRIRVMAAYHCGADWAMAMGDDALEAPNSDLEEYKTLGFKVEVGRELEFCSHIFRNPTLAVPVNTNKMLYKLIHGYNPECGNPEVIQNYLAAVFSVLQELRHDRELVAKLHQWLVPSATTKEH
Enzyme Length 1062
Uniprot Accession Number P17520
Absorption
Active Site ACT_SITE 255; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216; ACT_SITE 286; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216; ACT_SITE 354; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity 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 3.4.21.-; 2.7.7.48
Enzyme Function FUNCTION: Precursor from which the RNA-dependent RNA polymerase (RdRp) is probably released. RNA-dependent RNA polymerase plays an essential role in virus replication (Potential). {ECO:0000305}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (3); Compositional bias (2); Domain (2); Region (1); Sequence caution (1); Signal peptide (1); Site (2); Transmembrane (3)
Keywords Hydrolase;Membrane;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Reference proteome;Ribosomal frameshifting;Serine protease;Signal;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Protein P1-P2]: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification PTM: Specific enzymatic cleavages in vivo yield mature proteins. The protease probably cleaves itself and releases the RdRp (Potential). Cleavages have been shown in the P1 protein, but since the N-terminus containing the serine protease is shared between P1 and P1-P2, cleavages should also occur within the P1-P2 protein. {ECO:0000305}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 118,730
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda