MVP_PEMVM
ID MVP_PEMVM Reviewed; 1008 AA.
AC P0CK00;
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 Peanut mottle virus (strain M).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=103926;
OH NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH NCBI_TaxID=108216; Arachis pintoi.
OH NCBI_TaxID=53851; Cassia.
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=35627; Stylosanthes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Flasinski S., Gonzales R.A., Cassidy B.G.;
RT "The complete nucleotide sequence of peanut mottle virus (M strain) genomic
RT RNA.";
RL Submitted (SEP-1997) 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=P0CK00-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=O56075-1; 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; AF023848; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK00; -.
DR Proteomes; UP000000471; 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..1008
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420066"
FT CHAIN 1..322
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420067"
FT CHAIN 323..779
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420068"
FT CHAIN 780..1008
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408544"
FT DOMAIN 180..322
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 657..779
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 374..377
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 631..633
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 233
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 242
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 275
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 665
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 738
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 322..323
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 779..780
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 932..938
SQ SEQUENCE 1008 AA; 114275 MW; 56EAFBB0F6AE302A CRC64;
MASITFGNAC TVVFGQVRKE EVTAGPVAVN LNEGTRMVVV PTAAQMATPT PSVSIKIINR
WSNKAVSSYE RQVEDVFANF FAKKERSDEL LTRYYGKVVQ KGNKLMVKRA PLHVARVLEK
QRLQDIEDEK AFLQYRDAGV HVAGSVKFTD TRSRGQTVSF RTEHYKPTGK IVQKKKAQKQ
RANADVDHLI DEVMKICSAD CKQVEFISMG KRRLTAKFKL FGKSVIPCIH LAHEQGRRLR
RELDPRIHEQ VIAHLVTGRK VRELIKDDMV TYGWSGAILN KNLFKRTPFR WDEVVIRGRL
YGKLVDARSK LSECSKDKIH QYSSFEAQFW KGWKNKFDTL HPHNKDHICE PTINNEKCGE
IVATIFQAIH PVIKVSCSTC RERLTKASNE ELNEYLATNL ACHKATFDDM RQQHATVNTV
LNKIEQTSLA NPNLKDSMEI VRLLQNLNQT QARQLMKVNN TLLKGNVATS EEFSDATTQL
LEVTRWYAKH LSLVDEGSIS SFRNKATSKS LINPSLLCDN QLDRNGNFVW GERGRHSKRF
FENFFEEVVP GGGYKKYQIR NSPNCTRKLA IGNLIVPMSL ERARNALIGE SVERLPVTEA
CVSRVNGAFM HVASCVTSDN GSAHFSPLYS PTKRHLVVGT TGDSKYIDLP ATESDKMYVA
KEGYCYINIF LAMLVNVNED SAKDFTKMIR DTIVPMLGTW PSMMDVATAC YILTVFHPET
KSAELPRILV DHTNKTMHVI DSFGSISTGY HILKAGTVSQ LIHFASNELV SEMKHYVVGG
EAPHARRMRM EKALIQGIFK PKQLVYLIEE DPYILMMSLV SPTLLINLFN VGGLEVAMKH
WIKKEMNIGL IFSMLSSLAQ KVSRADLVNE QITMIDANAA QFIETLAGID VENPMRNELV
SALTMMLARS DVDSTLNKTG FTGFSDTLLE MREKNYWRRA QQGMVRAKLV GKIFFNHFLE
ASAKAYYGTF AKHKATRYRR QVCNLMYLVT WKDQGPIQWS KKCNIRSV
