ID L8E9I6_9POTV Unreviewed; 3140 AA.
AC L8E9I6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Plum pox virus strain Marcus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus; Plum pox virus.
OX NCBI_TaxID=587197 {ECO:0000313|EMBL:CCQ48556.1};
RN [1] {ECO:0000313|EMBL:CCQ48556.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Marcus {ECO:0000313|EMBL:CCQ48556.1};
RA Subr Z.W., Kamencayova M., Nagyova A., Predajna L., Glasa M.;
RT "Molecular analysis of plum pox virus host-atypical isolates.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: An RNA-dependent RNA polymerase that plays an essential role
CC in the virus replication. {ECO:0000256|ARBA:ARBA00029404}.
CC -!- FUNCTION: Has RNA-binding and proteolytic activities.
CC {ECO:0000256|ARBA:ARBA00029399}.
CC -!- FUNCTION: Has helicase activity. It may be involved in replication.
CC {ECO:0000256|ARBA:ARBA00029422}.
CC -!- FUNCTION: Indispensable for virus replication.
CC {ECO:0000256|ARBA:ARBA00034080}.
CC -!- FUNCTION: Involved in aphid transmission, cell-to-cell and systemis
CC movement, encapsidation of the viral RNA and in the regulation of viral
CC RNA amplification. {ECO:0000256|ARBA:ARBA00029405}.
CC -!- FUNCTION: Mediates the cap-independent, EIF4E-dependent translation of
CC viral genomic RNAs (By similarity). Binds to the cap-binding site of
CC host EIF4E and thus interferes with the host EIF4E-dependent mRNA
CC export and translation (By similarity). VPg-RNA directly binds EIF4E
CC and is a template for transcription (By similarity). Also forms
CC trimeric complexes with EIF4E-EIF4G, which are templates for
CC translation. {ECO:0000256|ARBA:ARBA00037225}.
CC -!- FUNCTION: Required for aphid transmission and also has proteolytic
CC activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus.
CC Interacts with virions and aphid stylets. Acts as a suppressor of RNA-
CC mediated gene silencing, also known as post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs. May have RNA-binding activity.
CC {ECO:0000256|ARBA:ARBA00029420}.
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 Evidence={ECO:0000256|ARBA:ARBA00001848};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000256|ARBA:ARBA00000785};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Host cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00034108}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000256|ARBA:ARBA00006064, ECO:0000256|RuleBase:RU003351}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF585103; CCQ48556.1; -; Genomic_RNA.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.90.70.150; Helper component proteinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR039560; Potyvirid-P3.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR PANTHER; PTHR43519; ATP-DEPENDENT RNA HELICASE HRPB; 1.
DR PANTHER; PTHR43519:SF1; ATP-DEPENDENT RNA HELICASE HRPB; 1.
DR Pfam; PF00270; 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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Helical capsid protein {ECO:0000256|ARBA:ARBA00022497};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022463};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022463};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Suppressor of RNA silencing {ECO:0000256|ARBA:ARBA00022463};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00022463};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT DOMAIN 165..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 644..766
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1240..1392
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1411..1570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2050..2268
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2534..2658
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2876..2905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2887..2902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 725
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3140 AA; 355556 MW; 324A9A1BD492B77B CRC64;
MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLKKQYKE ERERFQFLNG
PDAIVNQISV DKCEASVWVP FPHIIEKPSF TTPSMKKKAV FAKVRMSEAS LQLFMRRVAA
NAKANGQKVE IIGRKRVVGH YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
NTSGFHHVHK KGEITPGMSG FVVNPMNLSD PMQVYDTDLF IVRGKHNSIL VDSRCKVSKE
QSSEIVHYSD 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
CCVTHEDGAP LESEIISPTK NHLVVGNSGD SKYVDLPTAK GGAMFIAKAG YCYINIFLAM
LININEDEAK SFTKTVRDII VPKLGTWPSM MDLATACHFL AVLYPETRNA ELPRILVDHE
AKIFHVVDSF GSLSTGMHVL KANTVNQLIS FASDTLDSSM KTYLVGGLEV DKCDEFKNVK
LLIRSIYKPQ IMEQVLKEEP YLLLMSVLSP GVLMALFNSG SLEKATQYWI TRSHSLAAIT
SMLSALAAKV SLASTLNAQM SVIDEHAAVL CDSVFDGTKP YASYMMAVKT LERMKARTES
DHTLNDLGFS VLRQATPHLV EKSYLQELEQ AWRELSWSER FSAILESQRW RKHIPKPFIP
KDAADLGGRY DISVRSLLGS QYKRLKDVVR RKRDDVVCYT HQSMGKLFCK AIGISTSFLP
STLKMFDMLI IFGLLLSIGA TCNSMINEHK HLKQVAADRE DKKRFKRLQV LYTRLLEKIG
CTPTADEFLE YVQGENPDLL KYAEDLIGDG QVVVHQSKRD SQASLERVVA FVALVMMLFD
SERSDGVYKI LNKLKGVMGS IDQTVHHQSL DDVEDMLDEK KLTVDFVLQS NEVAPTVPFD
STFEKWWTNQ LETGNVIPHY RTEGHFLEFT RENAAHIANE VMHGSHQDIL IRGAVGSGKS
TGVPFHLSKK GHVLLIEPTR PLAENVCKQL RGQPFNVNPT LRMRGMSTFG STPITIMTSG
YALHFLANNP TYLDNYKCII FDECHVHDAS AMAFRCLLSE YSYPGKILKV SATPPGHEVD
FKTQKEVKVI VEEALSFQQF VSNLGTGCNS DILKHGVNVL VYVASYNEVD TLSKLLTDRS
FKVSKVDGRT MKVGNVEIPT SGTQAKPHFV VATNIIENGV TLDIDVVVDF GLKVVPVLDI
DNRLVRYMKK SISYGERIQR LGRVGRNKPG AALRIGFTEK GLTQIPPIIA TEAAFLCFTY
GLPVMTNGVS TSLLAMCTVK QARTMQQFEL SPFYTVALVR FDGTMHQEIF RLLKSYRLRD
SEVILNKLAI PNSNVCGWMS VRDYKRQGCN LDLDENIRVP FYVKDIPETL HDKVWQAVEA
HKSDAGFGRI CSSSACKIAY TLQTDIHSIP RTVKIIDALL EQERTKQAHF RAMTSQSCSS
SNFSLSSITS AIRSKYAKDH TEENIGVLQM AKSQLLEFKN LNIDPSYPEL VRNFGALECV
HHQTKEGISK TLQLKGHWTK RLITRDATLM LGVLGGGAWM IFTYLKDSFQ EEVVHQGFNR
RQRQKLKFRQ ARDNRMPREG YGDDSTMEDY FGSAYSKKGK SKGKTRGMGT KTRKFVNMYG
YDPTDYNFVR FVDPLTGHTL DENPLMDINL VQEHFSQIRN DYIGDDKITM QHIMSNPGIV
AYYIKDATQK ALKVDLTPHN PLRVCDKTAT IAGFPEREFE LRQTGHPTLV EPNAIPKINE
EGEEEVGHES KSLFRGLRDY NPIASSICRL NNSSGTRQSE MFGLGFGGLI VTNQHLFKRN
DGELTIRSHH GEFVVKDTKT LKLLPCKGRD IVIIRLPKDF PPFPKRLQFR TPTTEDRVCL
IGSNFQTKSI SSTMSETSAT YPVDNSHFWK HWISTKDGHC GLPIVSTRDG SILGLHSLAN
STNTQNFYAA FPDNFETIYL SNQDNDNWIK QWRYNPDEVC WGSLQLKRDI PQSPFTVCKL
LTDLDGEFVY NQSQTTHWLR DKLEGNLKAV GACPGQLVTK HVVKGKCTLF ETYLLTHPEE
HEFFRPLMGA YQKSALNKDA YVKDLMKYSK PIVVGAVDCE QFERAVDVVI SMLISKGFEE
CNYVTDPDDI FSALNMKAAV GALYSGKKRD YFKDASEQDK EDFIKASCKR LFMGKKGVWN
GSLKAELRPK EKVEANKTRS FTAAPIDTLL GGKVCVDDFN NQFYSLNLHC PWSVGMTKFR
GGWDKLLRAL PDGWIYCDAD GSQFDSSLSP YLINAVLNIR LAFMEEWDIG EQMLSNLYTE
IVYTPIATPD GTIVKKFKGN NSGQPSTVVD NTLMVILAMT YSLLKLGYHP DTHECICRYF
VNGDDLVLAV HPAYESMYDE LQEHFSQLGL NYTFTTKTEN KEELWFMSHR GVLFEDMYIP
KLEPERIVSI LEWDRSNEPI HRLEAICASM VEAWGYKELL REIRKFYSWV LEQAPYNALS
KDGKAPYIAE TALKKLYTDS EASETEIERY LEAFYNDVDD SLDSNIVIHQ ADEREDDEEV
DAGRPTVVTA PAATVATTQP APVIQPAPQT TAPMFNPIFT PATTQPAVRP VPPISGTKPR
SFGVYGNEDA SPSTSNTLAN TGRDRDVDAG SIGTFAVPRL KTMTSKLSLP KVKGKAIMNL
NHLAHYSPAQ VDLSNTRAPQ SCFQTWYEGV KRDYDVTDEE MSIILNGLMV WCIENGTSPN
INGMWVMMDG ETQVEYPIKP LLDHAKPTFR QIMAHFSNVA EAYIEKRNYE KAYMPRYGIQ
RNLTDYSLAR YAFDFYEMTS TTPVRAREAH IQMKAAALRN VQNRLFGLDG NVGTQEEDTE
RHTAGDVNRN MHNLLGVRGV
//
