MVP_ZYMVS
ID MVP_ZYMVS Reviewed; 997 AA.
AC P0CK15;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 28.
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 Zucchini yellow mosaic virus (strain Singapore) (ZYMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=117130;
OH NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Lee K.C., Wong S.M.;
RL Submitted (MAY-2001) 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=P0CK15-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=O36979-1; 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; AF014811; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK15; -.
DR Proteomes; UP000008612; 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: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; Suppressor of RNA silencing; Transport;
KW Viral movement protein.
FT CHAIN 1..997
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420107"
FT CHAIN 1..313
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420108"
FT CHAIN 314..769
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420109"
FT CHAIN 770..997
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408558"
FT DOMAIN 173..313
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 647..769
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 365..368
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 621..623
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 235
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 267
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 655
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 728
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 313..314
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255"
FT SITE 769..770
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 997 AA; 114071 MW; 2148A75F5992158B CRC64;
MAAIMIGSIS VPIIGSAQCA TAPIGNRVNI VAPGHMAICK PQMRSHAYYK HASQKLSEQS
SRGIEVLNSF FNNDPEDAFR LTRNGMSKVK KGPNGRIILR KPKARHVFER INLEKSEKEQ
KGKFFNGEYD TTVTSIKGVT TSKENDLGAF SLRSPFYKRT CKKEKRRITR ENIVCVDDVN
NLCERILKIT RDKNIPVEII GKRRNHHTLT FKKFKGSFVG KVSLAPERSQ MKHVEMSYGQ
FDYILQAICR ITSTKHVRDE DIKPGCSGWV FSTDHALTQK YSRLPYLVIR GRDDDGIVNA
LEPVLFYSDV EHYSFQNEVQ FFNGWRKMFD KLKPHSDHTC KVDHNNEECG EMAAVLSQAI
FPVLKLSCQV CREKLSRVSF EEFKDFLSRN FMTHESEWST LRDGVHCDNV LKLIKGAVQT
TQNLKLSSDI MKLVQNHTST HMKQIQDINK ALMKGSLVTQ DELDLALKQL LEMTQWFKNH
MHLTGEEALK TFRNKRSNKA MINPSLLCDN QLDKNGNFIW GERGYHSKRL FKNFFEEVIP
SEGYTKYIVR NFPNGTRKLA IGSLIVPLNL DRARTALLGE SIEKEPLTSA CISQQNENYI
HSCCCVTMDD GTPMYSELKS PTKRHLVIGA SGDPKYIDLP ASEAERMYIA KEGYCYLNIF
LAMLVNVNEN EAKDFTKMIR DVLIPMLGQW PSLMDVATAA YILGVFHPET RCAELPRILV
DHATQTMHVI DSYGSLTVGY HVLKAGTVNH LIQFASNDLQ SEMKHYRVGG TPTQRIRLEE
QLIKGIFKPK IMMQLLHDDP YILLLGMISP TILVHMYRMR HFERGIEIWI KRDHEIGKIF
VILEQLTRKV ALAEILVDQL DLISEASPHL LEIMNGCQDN QRAYAPALDL LTIQVEREFS
NKELKTNGYP DLHQTLHDMR EKNVCEAVTQ FMARAKLAGK ILCNRAIEAI LDFYGKKFDP
ASKRKKARIF ATICSRVLYH DPSTCEEHSR CRRAQTK
