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MVP_PPVSK
ID   MVP_PPVSK               Reviewed;        1026 AA.
AC   P0CK04;
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   Plum pox potyvirus (strain SK 68) (PPV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=103927;
OH   NCBI_TaxID=36596; Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OH   NCBI_TaxID=36595; Prunus cerasifera (cherry plum).
OH   NCBI_TaxID=3758; Prunus domestica (Garden plum).
OH   NCBI_TaxID=105665; Prunus glandulosa.
OH   NCBI_TaxID=3760; Prunus persica (Peach) (Amygdalus persica).
OH   NCBI_TaxID=88123; Prunus salicina.
OH   NCBI_TaxID=114937; Prunus spinosa (Blackthorn) (Prunus domestica var. spinosa).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8122394; DOI=10.1007/bf01703390;
RA   Palkovics L., Burgyan J., Balazs E.;
RT   "Comparative sequence analysis of four complete primary structures of plum
RT   pox virus strains.";
RL   Virus Genes 7:339-347(1993).
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=P0CK04-1; Sequence=Displayed;
CC       Name=Genome polyprotein;
CC         IsoId=Q84934-1; 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; M92280; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0CK04; -.
DR   Proteomes; UP000007637; 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..1026
FT                   /note="P3N-PIPO polyprotein"
FT                   /id="PRO_0000420078"
FT   CHAIN           1..308
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420079"
FT   CHAIN           309..766
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420080"
FT   CHAIN           767..1026
FT                   /note="Movement protein P3N-PIPO"
FT                   /id="PRO_0000408548"
FT   DOMAIN          165..308
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          644..766
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   MOTIF           360..363
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           618..620
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        216
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        225
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        259
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        652
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        725
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            308..309
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            766..767
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   UNSURE          920..926
SQ   SEQUENCE   1026 AA;  116782 MW;  8D1339961875CF72 CRC64;
     MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
     SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLKKQYKE ERERFQFLNG
     PDAIVNQISV DKCEASVWVP FPHIIEKPSF TTPSMKKKVV FTKVRMSEAS LQLFMRRVAA
     NAKANGQKVE IIGRKRVVGH YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
     NTSGFHHVHK KGEITPGMSG FVVNPMNLSD PMHVYDTDLF IVRGKHNSIL VDSRCKVSKE
     QSNEIVHYSD PGKQFWDGFT NSFMQCKLRE TDHQCTSDLD VKECGYVAAL VCQAIIPCGK
     ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTVMDNYPQF SHVLAFLKRY RELMRVENQN
     YEAFKDITHM IGERKEAPFS HLNKINELII KGGMMSAQDY IEASDHLREL ARYQKNRTEN
     IRSGSIKAFR NKISSKAHVN MQLMCDNQLD TNGNFVWGQR EYHAKRFFRN YFDVIDVSEG
     YRRHIVRENP RGIRKLAIGN LVMSTNLAAL RKQLLGEECI HFEVSKECTS KRGENFVYQC
     CCVTHEDGTP LESEIISPTK NHLVVGNSGD SKYVDLPTAK GGAMFIAKAG YCYINIFLAM
     LININEDEAK SFTKTVRDTI VPKLGTWPSM MDLATACHFL AVLYPETRNA ELPRILVDHE
     AKIFHVVDSF GSLSTGMHVL KANTINQLIS FASDTLDSSM KTYLVGGLEV DKCDEFKNVK
     LLIRSIYKPQ IMEQVLKEEP YLLLMSVLSP GVLMALFNSG SLEKATQYWI ARSHSLAAIT
     AMLSALAAKV SLASTLNAQM SVIDEHAAVL CDSVFVGTKP YASYMMAVKT LERMKARTES
     DHTLNDLGFS VLRQATPHLV EKKLSPGVGA GLERIKLVGK VLCNLGIAAV AKTYTKTFHP
     ERRSRFRRQV RHLRSVITWQ PIQTPERRSS AEKRRRCLLH TPVDGKAILQ SYRNFHKFSS
     KHSEDV
 
 
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