Detail Information for IndEnz0002013759
IED ID IndEnz0002013759
Enzyme Type ID protease013759
Protein Name P3N-PIPO polyprotein
Cleaved into: P1 proteinase
EC 3.4.-.-
N-terminal protein
; Helper component proteinase
HC-pro
EC 3.4.22.45
; Movement protein P3N-PIPO
Pretty interesting potyviridae ORF
PIPO
Gene Name
Organism Plum pox potyvirus (isolate NAT) (PPV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Plum pox virus Plum pox potyvirus (isolate NAT) (PPV)
Enzyme Sequence MSTIVFGSFTCHLDAAIHQDNADRLAKAWTRPENRQVSNAHLLCRRAAESLINTYESATASAWKGLEEKLQPMFAKREFSKTVTKRKGLRCFKESSEKFIEKKLRKQYQEERERLQFLNGPDAIVNQISVDKCEASVRVPSPHIIEKPSFVTPSMKKKVVFKKVRMSEASLQLFMRRVAANAKANGQKVEIIGRKRVVGNYTTKSRLTYFRTHVRHLDGSKPRYDLVLDEATKKILQLFANTSGFHHVHKKGEVTPGMSGFVVNPMNLSDPMQVYDTDLFIVRGKHNSILVDSRCKVSKKQSNEIIHYSDPGKQFSDGFTNSFMQCKLRETDHQCTSDLDVKECGYVAALVCQAIIPCGKITCLQCAQKYSYMSQQEIRDRFSTVIEQHEKTVMDNYPQFSHVLAFLKRYRELMRVENQNYEAFKDITHMIGERKEAPFSHLNKINELIIKGGMMSAQDYIEASDHLRELARYQKNRTENIRSGSIKAFRNKISSKAHVNMQLMCDNQLDTNGNFVWGQREYHAKRFFRNYFDVIDVSEGYRRHIVRENPRGIRKLAIGNLVMSTNLAALRKQLLGEECIHFEVSKECTSKRGENFVYQCCCVTHEDGTPLESEIISPTKNHLVVGNSGDSKYVDLPTAKGGAMFIAKAGYCYINIFLAMLININEDEAKSFTKTVRDTLVPKLGTWPSMMDLATACHFLAVLYPETRNAELPRILVDHEAKIFHVVDSFGSLSTGMHVLKANTINQLISFASDTLDSNMKTYLVGGLEVDKCDEFKNVKLLIRSIYKPQIMEQVLKEEPYLLLMSVLSPGVLMALFNSGSLEKATQYWITRSHSLAAITSMLSALAAKVSLASTLNAQMSVIDEHAAVLYDSVFVGTQPYASYMMAVKTLERMKARTESDHTLNDLGFSVLRQATPHLVEKKLSPGIGASLERVKLVGKILCNLGIAAMAKTYTKTFHPKRRRRFRRQVRHLRSVITWQPVQTPERRSPMEKRRCGLLYIPVDGEAILQSHRNLTKFSS
Enzyme Length 1020
Uniprot Accession Number P0CK02
Absorption
Active Site ACT_SITE 216; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 225; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 259; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 652; /note=For helper component proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01080; ACT_SITE 725; /note=For helper component proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01080
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.; EC=3.4.22.45;
DNA Binding
EC Number 3.4.-.-; 3.4.22.45
Enzyme Function FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity). {ECO:0000250}.; FUNCTION: [Movement protein P3N-PIPO]: Allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (5); Chain (4); Domain (2); Motif (2); Sequence uncertainty (1); Site (2)
Keywords Host cell junction;Host-virus interaction;Hydrolase;Protease;Ribosomal frameshifting;Serine protease;Suppressor of RNA silencing;Transport;Viral movement protein
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Host cell junction, host plasmodesma {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 360..363; /note=Involved in interaction with stylet and aphid transmission; /evidence=ECO:0000250; MOTIF 618..620; /note=Involved in virions binding and aphid transmission; /evidence=ECO:0000250
Gene Encoded By
Mass 116,033
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda