MVP_BYMV
ID MVP_BYMV Reviewed; 975 AA.
AC P0CJ95;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 29.
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 yellow mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12197;
OH NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH NCBI_TaxID=4627; Canna.
OH NCBI_TaxID=3828; Crotalaria.
OH NCBI_TaxID=52517; Eustoma.
OH NCBI_TaxID=58987; Freesia.
OH NCBI_TaxID=49747; Gladiolus.
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3873; Lupinus luteus (European yellow lupine).
OH NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH NCBI_TaxID=3469; Papaver somniferum (Opium poppy).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=35938; Robinia pseudoacacia (Black locust).
OH NCBI_TaxID=74517; Trifolium hybridum (Alsike clover).
OH NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
OH NCBI_TaxID=57577; Trifolium pratense (Red clover).
OH NCBI_TaxID=3899; Trifolium repens (Creeping white clover).
OH NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
OH NCBI_TaxID=97047; Trifolium vesiculosum.
OH NCBI_TaxID=78534; Trigonella foenum-graecum (Fenugreek).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
OH NCBI_TaxID=3908; Vicia sativa (Spring vetch) (Tare).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate GDD;
RX PubMed=14648299; DOI=10.1007/s00705-003-0185-7;
RA Hammond J., Hammond R.W.;
RT "The complete nucleotide sequence of isolate BYMV-GDD of Bean yellow mosaic
RT virus, and comparison to other potyviruses.";
RL Arch. Virol. 148:2461-2470(2003).
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=P0CJ95-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P17765-1; 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; AY192568; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CJ95; -.
DR Proteomes; UP000007620; 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 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..975
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420048"
FT CHAIN 1..284
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420049"
FT CHAIN 285..741
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420050"
FT CHAIN 742..975
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408538"
FT DOMAIN 139..284
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 619..741
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 335..338
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 593..595
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 192
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 201
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 232
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 627
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 700
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 284..285
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 741..742
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 895..901
SQ SEQUENCE 975 AA; 111115 MW; 39880EB0E1A5494E CRC64;
MTTINIGTIP VVINQNADTQ MGEGTKNIFP IVKDFVDPFA DLEMRCAERV KRMGELCFSK
KGRYITMIPK PDYIKAREKE QREEELNFQN SEHVLNSLDT TCTPEHHSSR NNGMQVSFKT
QHYKRTFRKP RIQAKKRDLK GQHTIHYVAK ELLSIVKKRD MVLEVVDKRK HANFATFRRY
GKTYGMHITL NHMVRKRRRV DVTLNKLMTE IAMHCAIPFE CLNTLTLRKG HSGLVLQTET
VPNVHKIKSK ITIVRGVVNE GNIPVLIDAR KKLSGRDMST IREFSAGDLF WKGYNQTFID
NRPTDLNHQC TSDLNVTQCG SVMALLTLAL FPCGRITCKK CVENFLNQNN KERFNNASVF
INQVIQLLEK GFSEFKHSKE ILLMFKERLQ MENPATDQCM EIAKATAALP EAPFSHIKEI
NNVLLKYGSL SNEEVGGASK HLLEVVRYIR NRTDSIQRND LSKFRNKISS KTHINLDLMC
DNQLDKNANF VWGQRAYHAK RFLSNYFNEI NPSEGYDKFI FRKLPNGARE LAIGRLIMPT
NFEAFREQMK GKMIDNGPIG KDCVSRMRGS FCYPCCCTTD DVGTAVISDF KMPTKYHLVL
GGNDLAKYIK LPTDTTGNMY IAKDGFCHIN IFFAMLVNVS EEKSKDFTKM VRDQIMPKLG
EWPTMMDVAT ACWQLTVWFP DTLSAELPRI LVDHKLGIMH VLDSYGSISA GYHVLKANIV
SQLIKFASDD LESELKYYRV GGDCNFGSRV RIDTKFLLKS IYRPDLLERI IEHEPFVLVL
AMQSPAVLLA LFNSASLEKA VQYWMHREMQ VSHIMTLLAV LASNVSASKL LTTQFEIIEA
SAPQILAEMD KVHLPMHSIH SANVFLMNMS ESRETDKTID ELGFYSFKKS SRILMEKNLN
GGFGGAMARI RIVGTVVFNK AVVASASKIF KLCNPTRRAR YKRQVHNLTQ VIRGSDKTTV
TCSEGSGCPF CRKED
