MVP_BCMNN
ID MVP_BCMNN Reviewed; 999 AA.
AC P0CJ94;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 30.
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 Bean common mosaic necrosis virus (strain NL-3) (BCMNV) (Bean common mosaic
OS virus serotype A (strain NL-3)).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=500578;
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Michigan;
RX PubMed=8607279; DOI=10.1016/s0168-1702(95)00072-0;
RA Fang G.W., Allison R.F., Zambolim E.M., Maxwell D.P., Gilbertson R.L.;
RT "The complete nucleotide sequence and genome organization of bean common
RT mosaic virus (NL3 strain).";
RL Virus Res. 39:13-23(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Infectious clone Calhoun;
RA Calhoun C.L., Allison R.F.;
RT "Construction of a BCMNV-full length infectious clone.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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=P0CJ94-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=Q65399-1; 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; U19287; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY282577; -; NOT_ANNOTATED_CDS; mRNA.
DR SMR; P0CJ94; -.
DR PRIDE; P0CJ94; -.
DR Proteomes; UP000007452; 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; 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; 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 2: Evidence at transcript level;
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..999
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420045"
FT CHAIN 1..317
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420046"
FT CHAIN 318..774
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420047"
FT CHAIN 775..999
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408537"
FT DOMAIN 176..317
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 652..774
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 370..373
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 626..628
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 239
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 271
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 660
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 733
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 317..318
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 774..775
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 925..931
SQ SEQUENCE 999 AA; 114541 MW; 5F615939214614E7 CRC64;
MATIMFGSIA AEIPVIKEAI MIAMPKSKHT LHVVQVEAKH MATEIRSERG KLYVAKRFAD
NAIKAYDSQL KAFDELLKKN SDLQKRLFIG QNSPIKQKKG GACFVRSLSF KQAEERHAKY
LKLQEEEHQF LSGAYGDKAY VGSVQGTLDR KVAEKVSFKS PYYKRTCKAV RQVKVLKKAV
GSGKVLDQVL EIVAETGVPV TFVGKGANKT LRAQYVRRYG LVIPKIFLCH ESGRKVHREM
SYWHHKETLQ YLCKHGKYGA LNENALCKGD SGLLFDQRTA FVKRVTYLPH FIVRGRQEGQ
LVCATEYLDN VYTIEHYTHK PEEQFFKGWK QVFDKMAPHT FEHDCTIDYN NEQCGELAAT
ICQTLFPVRK LSCNKCRHRI KDLSWEEFKQ FILAHLGCCA KLWEEQKNLP GLEKIHSFVV
QATSENMIFE TSMEIVRLTQ NYTSTHMLQI QDINKALMKG SSATQEDLKK ASEQLLAMTR
WWKNHMTLTN EDALKTFRNK RSSKALINPS LLCDNQLDRN GNFVWGERGR HSKRFFENFF
EEVVPSEGYK KYVIRNNPNG FRKLAIDSLI VPMDLARARI ALQGESIKRE DLTLACVSKQ
DGNFVYPCCC VTQDDGRPFY SELKSPTKRH LVVGTSGDPK YIDLPATDSD RMYIAKEGYC
YLNIFLAMLV NVNEDEAKDF TKMVRDVVVP KLGTWPSMMD VATAVYIMTV FHPETRSAEL
PRILVDHASQ TMHVIDSFGS LSVGYHVLKA GTVNQLIQFA SNDLEGEMKH YRVGGDAEQR
MRCERALISS IFKPKKMMQI LENDPYTLVL GLVSPTVLIH MFRMKHFEKG VELWINKDQS
VVKIFLLLEH LTRKIAMNDV LLEQLEMISQ QAGRLHEIIC DCPKNIHSYR AVKDFLEVKM
EAALTNKELA NNGFFDINES LGHVSEKNLC KSLREGMARA KLVGKIFCNM AIEKVLKGYG
RAFDKESCRR QKRIFKKICE CVLHECPNTP RKCTYYNFK
