ID F2YI27_9POTV Unreviewed; 3215 AA.
AC F2YI27;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Watermelon mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=146500 {ECO:0000313|EMBL:ADZ76016.1};
RN [1] {ECO:0000313|EMBL:ADZ76016.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cg09-640 {ECO:0000313|EMBL:ADZ76016.1};
RX PubMed=21471312; DOI=10.1099/vir.0.031401-0;
RA Desbiez C., Joannon B., Wipf-Scheibel C., Chandeysson C., Lecoq H.;
RT "Recombination in natural populations of watermelon mosaic virus: new
RT agronomic threat or damp squib?";
RL J. Gen. Virol. 92:1939-1948(2011).
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 -!- SUBUNIT: Interacts with host eIF4E protein (via cap-binding region);
CC this interaction mediates the translation of the VPg-viral RNA
CC conjugates (By similarity). Part of a complex that comprises VPg, RNA,
CC host EIF4E and EIF4G; this interaction mediates the translation of the
CC VPg-viral RNA conjugates. {ECO:0000256|ARBA:ARBA00044023}.
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}.
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DR EMBL; JF273467; ADZ76016.1; -; 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:0008236; F:serine-type peptidase 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; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 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 nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
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 Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
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 298..439
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 774..896
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1367..1519
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1538..1697
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2173..2391
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2657..2781
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2936..2989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2937..2957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2958..2982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 782
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 855
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3215 AA; 366356 MW; 3DC9F78E1911D845 CRC64;
MATIMFGDFA VQLKHSTVIE KRKRVVETTK LVQEVHMDTV YEQVMESITV GCTERCAGLS
AYTKSSLRRA IKEGDLSASG GCNYCGLRAL VGEGRERVIS VPRTVAQQKE VVVTKEVPHI
YEEEYEVEVP HPTSEMVLPT GGNVCGTAVQ TKVAKNIVTK EMMAKSEPSL KQVSRSLVLA
GRKEIGNYDL AIKKMDEAMK HDPALQRRLF IQQQSTIKQL PKGAVQFRLC SYEQAKKRAE
LEHKRKQEEE DFLNGKYEQQ AYIGTTAVNT MKSTGGSMSF RTIHWRSTPK QNKTKRVKKQ
CDKPIHVLEG VLSLAAKSGK PVEFITKRKR KNFKVNYVRK YGAVIPKFTL PHEEGKYVHQ
ELQYANICEF LPYICMFAKY KAVRADDLTH GDSGLLFDER SSITSEHTTL PYFVVRGRKN
GKLVSAFGEF KEIGDIQHYS HIPEVQFFLG WKKVFDKMQP RIDAHECTID FTNEQCGELA
AAISQSIFPV KKLSCKHCRR HIKDLSWEEY KQFLLTHMGC SETTWADVRK VEGVEHVKKL
IERSTAENLS LQTSMEIVRL TQNYKSTHML QIQDINKALM KGSSVTQDEL EQASKQLLAM
TQWWKNHMTL TDEDALKVFR NKRSSKALLN PSLLCDNQLD KNGNFIWGER GKHSKRFFAN
YFEEVIPSEG YNKYVIRKNP NGQRELAIGS LIVPLDFERA RMALQGKSIA REPITMACIS
RQDGNFVYPC CCVTHDDGKA FYSELKSPTK RHLVIGTSGD PKYIDLPATE TDRMYIAKEG
YCYLNIFLAM LVNVNEDEAK DFTKMVRDVI VPKLGQWPTM FDVATAVYML TVFHPETRNA
ELPRILVDHA CQTMHVIDSF GSLTVGYHVL KAGTVNQLIQ FASNDLHREM KFYRVGGVAQ
QRMKCETALI TSIFKPKRMI QILEEDPYIL LMGLISPSIL IHMYRMRHFE KGIEMWINKE
HSVAKIFIIM EQLTKKIAAN DLLLEQLDII AGTSHKLMDV LEDCPQSAHS YKTVKDLLAM
YIERKASNNQ LVENGFVDMN DQLYVMHEKI YVDRLKQEWR ALSWLEKSSI TWQLKRFTPH
TEQCLTKRVV EESSAYSRNF VSACFMNAQS HLKNVRNTFF RKCDQAWTAS VRGFVRFIIS
TLHKCYSDIV YLVNICLIFS LLIQMASVLQ GIVSTAKKDK AFVHMYKRNE DEQAVVHLYE
MCEKIGNKHP SVEEFLSHVK KVRPELLPVA KSMTGQSEDV SAQAKTATQL QLEKIVAFMA
LLTMCIDNER SDAVFKILSK LKTFFGTMGE EVKVQSLDEI QNIDEDKKLT IDFDLETSKE
PSSVSFDVKF EDWWHRQLQQ NRVIPHYRST GEFLEFSRET AAKIANLIAT SSHTEFLIRG
AVGSGKSTGL PHHLSKKGKV LLLEPTRPLA ENVSKQLGLE PFYHNVTLRM RGLSKFGSSN
IVVMTSGFAF HYYVNNPHQL SDFDFIIIDE CHVQDSHTIA FNCALKEFEF SGKLLKVSAT
PPGRECEFTT QHPVKLKIED HLSFQNFVQA QGTGSNADML QHGNNLLVYV ASYNEVDQLS
RLLTEKHYKV TKVDGRTMQM GNVEITTTGT EGKPHFIVAT NIIENGVTLD IDCVIDFGLK
VVAVLDTDNR CVRYNKQSVS YGERIQRLGR VGRHKPGFAL RVGHTEKGIE EVPEFIATEA
AFLSFAYGLP VTTQSVSTNI LSRCTVKQAR VALNFELTPF FTINFIKYDG GMHPEIHRLL
KPYKLRESEM MLHKLAIPHQ FVGQWISVKE YDRQGIHLNC PETVKVPFYV NGIPDKLYES
LWETVCNYKC DAGFGSIRSV NASKISYTLS TDPTAIPRTL AILDHLLSEE MTKKSHFDTI
GSSVTGYSFS LAGIADGFRK RYLRDYTQQN IAILQQAKAQ LLEFDCTKVD INNLQSVEGI
GILNAVQLQS KHEVSKFLQL KGKWDGKKFM NDAIVAIFAL IGGGWMLWDY FTRMIREPVT
TQGKKRQIQK LKFRDAFERK VGREVYADDY TMEHTFGEAY TKKGKQKGST KTKGMGRKSR
NFIHMYGVEP ENYSMIRFVD PLTGHTMDES TRVDIRLVQQ EFGEIREEMI GADELDPQRV
YHSPGIQAYF MGKNAEEALK VDLTPHVPTL LCQNSNAISG FPEREGELRQ TGLPQIVSKA
DVPRAKERVE VESKSVYKGL RDYSGISTLI CQLTNSSDGH KETMFGVGYG SFIITNGHLF
RRNNGMLTVK TWHGEFVIHN TTQLRIHFIQ GKDAILIRMP KDFPPFAKRN FFRQPKREER
VCMVGTNFQE KSLRATVSES SIILPEGKGS FWIHWITTQD GFCGLPLVSV NDGHVVGIHG
LTSNDSEKNF FVPFTDGFEK EYLDNADNLS WDKHWFWEPS KIAWGSLNLV EEQPKEEFKI
SKLVSDLFGN TVAVQSRKER WVLDAMEGNL VACGQADSAL VTKHVVKGKC PYFAQYLTLH
NEAKQFFEPL MGAYQPSRLN KDAFKKDFFK YNKPVVLNEV DFNAFEKAVE GVITMMVDFE
FAECLFVTDP DEIYGSLNMK AAVGAQYKGK KQDYFSGMDS FDKERLLYLS CERLFNGEKG
IWNGSLKAEL RPIEKVQANK TRTFTAAPID TLLGAKVCVD DFNNQFYSFN LKCPWTVGMT
KFYGGWDKLM RSLPDGWTYC HADGSQFDSS LTPLLLNAVL SIRCCFMEDW WVGKEMLENL
YAEIVYTPIL APDGTIFKKF RGNNSGQPST VVDNTLMVVI AMYYSCCKQG WSEEDIERRL
VFFANGDDII LAVRDEDVWL YDTLSASFAE LGLNYNFDER TKKREELWFM SHQAMLVDGI
YIPKLEPERI VSILEWDRSK EIMHRTEAIC AAMIEAWGYT ELLQEIRKFY LWLLSKDEFK
ELAASGKAPY IAETALRKLY TDINTQPSEL QRYLEVLDFN HTDGCCESVS LQSGKEKETV
ENLDAGKDSK KDTSGKGDKP QNLQTGQGSK EPTKTGTVSK DVNVGSKGKE VPRLPKITKK
MNLPTVGGKI ILSLDHLLEY KPNQVDLFNT RATKTQFESW YSAVKIEYDL NDEQMGVIMN
GFMVWCIDNG TSPDVNGVWV MMDGEEQVEY PLKPIVENAK PTLRQIMHHF SDAAEAYIEM
RNSESPYMPR YGLLRNLRDR ELARYAFDFY EVTSKTPNRA REAITQMKAA ALAGINSRLF
GLDGNISTNS ENTERHTARD VNQNMHTLLG MGPPQ
//
