GenomeNet

Database: UniProt
Entry: P17767
LinkDB: P17767
Original site: P17767 
ID   POLG_PPVRA              Reviewed;        3140 AA.
AC   P17767;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   18-SEP-2019, entry version 151.
DE   RecName: Full=Genome 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=Protein P3;
DE   Contains:
DE     RecName: Full=6 kDa protein 1;
DE              Short=6K1;
DE   Contains:
DE     RecName: Full=Cytoplasmic inclusion protein;
DE              Short=CI;
DE              EC=3.6.4.-;
DE   Contains:
DE     RecName: Full=6 kDa protein 2;
DE              Short=6K2;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein A;
DE              Short=NI-a;
DE              Short=NIa;
DE              EC=3.4.22.44;
DE     AltName: Full=49 kDa proteinase;
DE              Short=49 kDa-Pro;
DE     AltName: Full=NIa-pro;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-b;
DE              Short=NIb;
DE              EC=2.7.7.48;
DE     AltName: Full=RNA-directed RNA polymerase;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
OS   Plum pox potyvirus (strain Rankovic) (PPV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12214;
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.
RX   PubMed=2773595; DOI=10.1016/0168-1702(89)90013-0;
RA   Lain S., Riechmann J.L., Garcia J.A.;
RT   "The complete nucleotide sequence of plum pox potyvirus RNA.";
RL   Virus Res. 13:157-172(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1778-2342.
RX   PubMed=2658302; DOI=10.1016/0042-6822(89)90426-1;
RA   Garcia J.A., Riechmann J.L., Lain S.;
RT   "Proteolytic activity of the plum pox potyvirus NIa-like protein in
RT   Escherichia coli.";
RL   Virology 170:362-369(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2263-3140.
RA   Lain S., Riechmann J.L., Mendez E., Garcia J.A.;
RT   "Nucleotide sequence of the 3' terminal region of plum pox potyvirus
RT   RNA.";
RL   Virus Res. 10:325-342(1988).
RN   [4]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
CC   -!- FUNCTION: Capsid protein: involved in aphid transmission, cell-to-
CC       cell and systemis movement, encapsidation of the viral RNA and in
CC       the regulation of viral RNA amplification.
CC   -!- FUNCTION: Nuclear inclusion protein B: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC   -!- FUNCTION: Helper component proteinase: required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a
CC       Gly-Gly dipeptide at its own C-terminus. Interacts with virions
CC       and aphid stylets. Acts as a suppressor of RNA-mediated gene
CC       silencing, also known as post-transcriptional gene silencing
CC       (PTGS), a mechanism of plant viral defense that limits the
CC       accumulation of viral RNAs. May have RNA-binding activity (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Cytoplasmic inclusion protein: has helicase activity. It
CC       may be involved in replication (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus
CC       replication. {ECO:0000250}.
CC   -!- FUNCTION: Nuclear inclusion protein A: has RNA-binding and
CC       proteolytic activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that
CC         vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-
CC         Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The
CC         natural substrate is the viral polyprotein, but other proteins
CC         and oligopeptides containing the appropriate consensus sequence
CC         are also cleaved.; EC=3.4.22.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus,
CC         commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
CC         processing of the potyviral polyprotein.; EC=3.4.22.45;
CC   -!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000305}.
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved
CC       in interaction with stylets. The central part is involved in
CC       interaction with virions and the C-terminus is involved in cell-to
CC       cell movement of the virus.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently
CC       attached to the 5'-end of the genomic RNA. This uridylylated form
CC       acts as a nucleotide-peptide primer for the polymerase (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Genome polyprotein of potyviruses undergoes post-
CC       translational proteolytic processing by the main proteinase NIa-
CC       pro resulting in the production of at least ten individual
CC       proteins. The P1 proteinase and the HC-pro cleave only their
CC       respective C-termini autocatalytically. 6K1 is essential for
CC       proper proteolytic separation of P3 from CI (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; M21847; AAA85458.1; -; Genomic_RNA.
DR   EMBL; M26965; AAA47085.1; -; mRNA.
DR   PIR; A60009; GNVSRA.
DR   PRIDE; P17767; -.
DR   ABCD; P17767; -.
DR   Proteomes; UP000006686; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.90.70.150; -; 1.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF13608; Potyvirid-P3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Capsid protein; Complete proteome;
KW   Covalent protein-RNA linkage; Helical capsid protein; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Protease; RNA-directed RNA polymerase; Serine protease;
KW   Suppressor of RNA silencing; Thiol protease; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN         1   3140       Genome polyprotein.
FT                                /FTId=PRO_0000420008.
FT   CHAIN         1    308       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040341.
FT   CHAIN       309    766       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040342.
FT   CHAIN       767   1116       Protein P3. {ECO:0000250}.
FT                                /FTId=PRO_0000040343.
FT   CHAIN      1117   1168       6 kDa protein 1. {ECO:0000250}.
FT                                /FTId=PRO_0000040344.
FT   CHAIN      1169   1803       Cytoplasmic inclusion protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040345.
FT   CHAIN      1804   1856       6 kDa protein 2. {ECO:0000250}.
FT                                /FTId=PRO_0000040346.
FT   CHAIN      1857   2049       Viral genome-linked protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040347.
FT   CHAIN      2050   2292       Nuclear inclusion protein A.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040348.
FT   CHAIN      2293   2810       Nuclear inclusion protein B.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040349.
FT   CHAIN      2811   3140       Capsid protein. {ECO:0000250}.
FT                                /FTId=PRO_0000040350.
FT   DOMAIN      165    308       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      644    766       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1240   1392       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1411   1570       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2050   2268       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2534   2658       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1253   1260       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       360    363       Involved in interaction with stylet and
FT                                aphid transmission. {ECO:0000250}.
FT   MOTIF       618    620       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1342   1345       DECH box.
FT   MOTIF      1897   1904       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    216    216       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    225    225       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    259    259       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    652    652       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    725    725       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2095   2095       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2130   2130       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2200   2200       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   SITE        308    309       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        766    767       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1116   1117       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1168   1169       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1803   1804       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1856   1857       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2049   2050       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2292   2293       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2810   2811       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    1919   1919       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   3140 AA;  355581 MW;  5F3DBB07982CF3F5 CRC64;
     MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
     SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLRKQYQE ERERFQFLNG
     PDAIVNQISV DKCEASVRVP FPHIIEKPSF ATPSMKKKVV FTKVRMSEAS LQLFMRRVAA
     NAKANGQKVE IIGRKRVVGN YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
     NTSGFHHVHK KGEVTPGMSG FVVNPMNLSD PMQVYDTDLF IVRGKHNSIL VDSRCKVSKE
     QSNEIIHYSD 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 SFTKTVRDTL VPKLGTWPSM MDLATACHFL AILYPETRNA ELPRILVDHE
     AKIFHVVDSF GSLSTGMHVL KANTINQLIS FASDTLDSNM KTYLVGGLEV DKCDEFKNVK
     LLIRSIYKPQ IMEQVLKEEP YLLLMSVLSP GVLMALFNSG SLEKATQYWI TRSHSLAAIT
     SMLSSLAAKV SLASTLNAQM SVIDEHAAVL CDSVFVGTKP YASYMMAVKT LERMKARTES
     DHTLNDLGFS VIRQATPHLV EKSYLQELEQ AWKELSWSEK FSAILESQRW RKHIPKPFIP
     KDGADLGGRY DISVRSLLGN QYKRLRDVVR RKRDDVVCYT HQSMGKLFCK AIGISTSFLP
     STLKMFDMLI VFSLLLSIGA TCNSMINEHK HLKQLAADRE DKKRFKRLQV LHTRLSEKVG
     CTPTADEFLE YVGGENPDLL KHAEDLIGDG QVVVHQSKRD SQANLERVVA FVALVMMLFD
     SERSDGVYKI LNKLKGIMGS VDQAVQHQSL DDIEDILDEK KLTVDFVLQS NEVAPTVPFD
     STFEKWWTNQ LETGNVIPHY RTEGHFLEFT RENAAHIANE VMHGSHQDIL IRGAVGSGKS
     TGLPFHLSKK GHVLLIEPTR PLAENVCKQL RGQPFNVNPT LRMRGMSTFG STPITVMTSG
     YALHFLANNP TYLDNYKCII FDECHVHDAS AMAFRCLLSE YSYPGKILKV SATPPGHEVD
     FKTQKEVKVI VEESLSFQQF VSNLGTGCNS DILKHGVNVL VYVASYNEVD TLSKLLTDRS
     FKVSKVDGRT MKIGNVEIPT SGTQAKPHFV VATNIIENGV TLDIDVVVDF GLKVVPVLDI
     DNRLVRYTKK SISYGERIQR LGRVGRNKPG AALRIGFTEK GLTQIPPIIA TEAAFLCFTY
     GLPVMTNGVS TSLLAMCTVK QARTMQQFEL SPFYTVALVR FDGTMHQEIF RLLKSYRLRD
     SEVILNKLAI PNSNVCGWMS VRDYKRQGCN LDLDENIRVP FYVKDIPETL HERIWQVVET
     HKSDAGFGRI CSSSACKIAY TLQTDIHSIP RTIKIIDALL EQERTKQAHF RAMTSQSCSS
     SNFSLSSITS AIRSKYAKDH TEENIGVLQT AKSQLLEFKN LNIDPSYPEL VRNFGALECV
     HHQTKEGVSK ALQLKGHWNK RLITRDATLM LGVLGGGAWM IFSYLRDSFK EEVVHQGFNR
     RQRQKLKFRQ ARDNRMAREV YGDDSTMADY FGSAYSKKGK SKGKTRGMGT KTRKFVNMYG
     YDPTDYNFVR FVDPLTGHTL DENPLMDINL VQEHFSQIRN DYIGDDKITM QHIMSNPGIV
     AYYIKDATQK ALKVDLTPHN PLRVCDKTAT IAGFPEREFE LRQTGHPVFV EPNAIPKINE
     EGDEEVDHES KSLFRGLRDY NPIASSICQL NNSSGARQSV MFGLGFGGLI VTNQHLFKRN
     DGELTIRSHH GEFVVKDTKT LKLLPCKGRD IVIIRLPKDF PPFPKRLQFR TPTTEDRVCL
     IGSNFQTKSI SSTMSETSAT YPVDNSHFWK HWISTKDGHC GLPIVSTRDG SILGLHSLAN
     STNTQNFYAA FPDNFETTYL SNQDNDNWIK QWRYNPDEVC WGSLQLKRDI PQSPFTICKL
     LTDLDGEFVY TQSKTTHWLR DRLEGNLKAV GACPGQLVTK HVVKGKCTLF ETYLLTHPEE
     HEFFRPLMGA YQKSALNKDA YVKDLMKYSK PIVVGAVDCD QFERAVDVVI SMLISKGFEE
     CNYVTDPDDI FSALNMKAAV GALYSGKKRD YFKNVSDQDK ESFVRASCKR LFMGKKGVWN
     GSLKAELRPK EKVEANKTRS FTAAPIDTLL GGKVCVDDFN NQFYSLNLHC PWSVGMTKFR
     GGWDKLLRAL PEGWIYCDAD GSQFDSSLSP YLINAVLNIR LAFMEEWDIG EQMLSNLYTE
     IVYTPIATPD GTIVKKFKGN NSGQPSTVVD NTLMVILAMT YSLLKLGYHP DTHDCICRYF
     VNGDDLVLAV HPAYESIYDE LQEHFSQLGL NYTFATKTEN KEELWFMSHK GVLYDDMYIP
     KLEPERIVSI LEWDRSNEPI HRLEAICASM VEAWGYKELL REIRKFYSWV LEQAPYNALS
     KDGKAPYIAE TALKKLYTDT EASETEIERY LEAFYDDFND DGESNVVVHQ ADEREDEEEV
     DAGKPSVVTA PAATSPILQP PPVIQPAPRT TASMLNPIFT PATTQPATKP VSQVSQPQLQ
     TFGTYGNEDA SPSNSNALVN TNRDRDVDAG SVGTFTVPRL KAMTSKLSLP KVKGKAIMNL
     NHLAHYSPAQ VDLSNTRAPQ SCFQTWYEGV KRDYDVTDDE MSIILNGLMV WCIENGTSPN
     INGMWVMMDG ETQVEYPIKP LLDHAKPTFR QIMAHFSNVA EAYIEKRNYE KAYMPRYGIQ
     RNLTDYSLAR YAFDFYEMTS TTPVRAREAH IQMKAAALRN VQNRLFGLDG NVGTQEEDTE
     RHTAGDVNRN MHNLLGVRGV
//
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