ID   MVP_PRSVH               Reviewed;        1228 AA.
AC   P0CJ98;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=P3N-PIPO polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.-;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
DE   Contains:
DE     RecName: Full=Movement protein P3N-PIPO;
DE     AltName: Full=Pretty interesting potyviridae ORF;
DE              Short=PIPO;
OS   Papaya ringspot virus (strain P / mutant HA).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=31731;
OH   NCBI_TaxID=3649; Carica papaya (Papaya).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   AGRICOLA=IND20450567;
RA   Wang C.H., Bau H.J., Yeh S.D.;
RT   "Comparison of the nuclear inclusion b protein and coat protein genes of
RT   five papaya ringspot virus strains distinct in geographic origin and
RT   pathogenicity.";
RL   Phytopathology 84:1205-1210(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1402799; DOI=10.1099/0022-1317-73-10-2531;
RA   Yeh S.D., Jan F.J., Chiang C.H., Doong T.J., Chen M.C., Chung P.H.,
RA   Bau H.J.;
RT   "Complete nucleotide sequence and genetic organization of papaya ringspot
RT   virus RNA.";
RL   J. Gen. Virol. 73:2531-2541(1992).
CC   -!- FUNCTION: [Helper component proteinase]: Required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC       dipeptide at its own C-terminus. Interacts with virions and aphid
CC       stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC       known as post-transcriptional gene silencing (PTGS), a mechanism of
CC       plant viral defense that limits the accumulation of viral RNAs. May
CC       have RNA-binding activity (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Movement protein P3N-PIPO]: Allows efficient cell to cell
CC       propagation, by bypassing the host cell wall barrier. Transports viral
CC       genome to neighboring plant cells directly through plasmosdesmata,
CC       without any budding (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC         the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC         potyviral polyprotein.; EC=3.4.22.45;
CC   -!- SUBUNIT: Interacts (via PIPO domain) with host PCaP1 protein; this
CC       interaction may help to anchor the movement complex to the plasma
CC       membrane from which the complex could move to the plasmodesmata.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ98-1; Sequence=Displayed;
CC       Name=Genome polyprotein;
CC         IsoId=Q01901-1; Sequence=External;
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved in
CC       interaction with stylets. The central part is involved in interaction
CC       with virions and the C-terminus is involved in cell-to cell movement of
CC       the virus (By similarity). {ECO:0000250}.
CC   -!- PTM: Potyviral RNA is expressed as two polyproteins which undergo post-
CC       translational proteolytic processing. Genome polyprotein is processed
CC       by NIa-pro, P1 and HC-pro proteinases resulting in the production of at
CC       least ten individual proteins. P3N-PIPO is cleaved by P1 and HC-pro
CC       proteinases resulting in the production of three individual proteins.
CC       The P1 proteinase and the HC-pro cleave only their respective C-termini
CC       autocatalytically (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform P3N-PIPO polyprotein]: Produced by -1 ribosomal
CC       frameshifting in P3 ORF.
CC   -!- SIMILARITY: Belongs to the potyviridae P3N-PIPO polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; X67673; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; S46722; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0CJ98; -.
DR   Proteomes; UP000006688; Genome.
DR   Proteomes; UP000007380; Genome.
DR   GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.150; -; 1.
DR   InterPro; IPR022199; DUF3725.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   Pfam; PF12523; DUF3725; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF13608; Potyvirid-P3; 1.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
PE   3: Inferred from homology;
KW   Host cell junction; Host-virus interaction; Hydrolase; Protease;
KW   Ribosomal frameshifting; Serine protease; Suppressor of RNA silencing;
KW   Transport; Viral movement protein.
FT   CHAIN           1..1228
FT                   /note="P3N-PIPO polyprotein"
FT                   /id="PRO_0000420060"
FT   CHAIN           1..547
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000420061"
FT   CHAIN           548..1004
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000420062"
FT   CHAIN           1005..1228
FT                   /note="Movement protein P3N-PIPO"
FT                   /id="PRO_0000408542"
FT   DOMAIN          408..547
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          882..1004
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   MOTIF           598..601
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           856..858
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        456
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        465
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        499
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        890
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        963
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            547..548
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            1004..1005
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   UNSURE          1155..1161
SQ   SEQUENCE   1228 AA;  140607 MW;  AC25362634FE64A4 CRC64;
     MSSLYTLRAA AQYDRRLESK KGSGWVEHKL ERKGERGNTH YCSEFDISKG AKILQLVQIG
     NTEVGRTFLE GNRFVRANIF EIIRKTMVGR LGYDFESELW VCRNCDKTSE KYFKKCDCGE
     TYYYSERNLM RTMNDLMYQF DMTPSEINSV DLEYLANAVD YAEQLVKRSQ VPEPVELAMM
     EPIVASGEGI LMVSEPEVMP VTTKVEEAWT IQIGEIPVPL VVIKETPVIS GVEGTLNSTG
     FSLEADITKL VEKEILQEEV KEAVHLALEV GNEIAEKKPE LKLIPYWSAS LELHKRIRKH
     KEHAKIAAIQ VQKEREKDQK VFSALELRLN LKSRRRNQAV VCDKRGTLKW ETQRGHKKSK
     LMQQASDFVV TQIHCDFGCK TQYSEPHIPG IKQSTSKKIC KPRKHSRIVG NSKINYIMKN
     LCDTIIERGI PVELVTKRCK RRILQKEGRS YVQLRHMNGI RARQDVSSSP DMELLFTQFC
     KFLVGHKPLK SKNLTFGSSG LIFKPKFADN VGRYFGDYFV VRGRLGGKLF DGRSKLARSV
     YAKMDQYNDV AEKFWLGFNR AFLRHRKPTD HTCTSDMDVT MCGEVAALAT IILFPCHKIT
     CNTCMSKVKG RVIDEVGEDL NCELERLRET LSAYGGSFGH VSTLLDQLNR VLNARNMNDG
     AFKEIAKKID EKKESPWTHM TTINNTLYKG SLATGYEFER ASNSLREIVR WHLKRTESIK
     AGSVESFRNK RSGKAHFNPA LTCDNQLDKN GNFLWGERQY HAKRFFANYF EKIDHSKGYE
     YYSQRQNPNG IRKIAIGNLV FSTNLERFRQ QMVEHHIDQG PITRECIALR NNNYVHVCSC
     VTLDDGTPAT SELKTPTKNH IVLGNSGDPK YVDLPTLESD SMYIAKKGYC YMNIFLAMLI
     NIPENEAKDF TKRVRDLVGS KLGEWPTMLD VATCANQLVV FHPDAANAEL PQILVDHRQK
     TMHVIDSFGS VDSGYHILKA NTVNQLIQFA RDPLDSEMKH YIVGGEFDPT TNCLHQLIRV
     IYKPHELRSL LRNEPYLIVI ALMSPSVLLT LFNSGAVEHA LNYWIKRDQD VVEVIVLVEQ
     LCRKVTLART ILEQFNEIRQ NARDLHELMD RNNKPWISYD RSLELLSVYA NSQLTDEGLL
     KQGFSTLDPR LREAVEKNLR HSFAGRMACV KFVSKVALKV LCVQITTVFF RVFKAKRARR
     FKNCIRLLTE ILCTRGRKSV PTASQGWG