ID I3RGV5_9POTV Unreviewed; 3080 AA.
AC I3RGV5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Zucchini yellow mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12232 {ECO:0000313|EMBL:AFK23495.1};
RN [1] {ECO:0000313|EMBL:AFK23495.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3rd {ECO:0000313|EMBL:AFK23495.1};
RX PubMed=22592263; DOI=10.1099/vir.0.042622-0;
RA Simmons H.E., Dunham J.P., Stack J.C., Dickins B.J., Pagan I., Holmes E.C.,
RA Stephenson A.G.;
RT "Deep sequencing reveals persistence of intra- and inter-host genetic
RT diversity in natural and greenhouse populations of zucchini yellow mosaic
RT virus.";
RL J. Gen. Virol. 93:1831-1840(2012).
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; JN192426; AFK23495.1; -; 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:0042025; C:host cell nucleus; 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 170..310
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 1236..1388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1407..1566
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2042..2260
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2526..2650
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2802..2835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2812..2829
FT /note="Basic and acidic 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 3080 AA; 350646 MW; 43D509E1ECB2658C CRC64;
MASIMIGSIS VPIAKTEQCA NTQVSNRVNI VAPGHMATCP LPLKTHMYYR HESKKLMQSN
KSIDILNNFF STDEMKFRLT RNEMSKVKKG PSGRIVLRKP SKQRVFARIE QDEAARKEEA
VFLEGNYDNS IINLARVLPP EVTHNVDVSL RSPFYKRTYK KERKKVAQKQ IVQTPLNSLC
TRVLKIARNK NIPVEMIGNK KARHTLTFKK FRGYFVGKVS VAHEEGRMRH TEMSYEQFKW
ILKAICQVTH TERIREEDIK PGCSGWVLGT NHTLTKRYSR LPHLVIRGRD DDGIVNALEQ
VLFYSDVDHY SSQPEVQFFQ GWRRMFDKFR PSPDHVCKVD HNNEECGELA AIFCQALFPV
VKLSCQTCRE KLSRVSFEEF KDSLNANFII HKDEWGSFKE GSQYDNIFKL IKVATQATQN
LKLSSEVMKL VQNHTSTHMK QIQDINKALM KGSLVTQDEL DLALKQLLEM TQWFKNHMHL
TGEEALKMFR NKRSSKAMIN PSLLCDNQLD KNGNFVWGER GXHSRRLFKN FFEEVIPSEG
YTKYVVRNFP NGTRKLAIGS LIVPLNLDRA RTALLGESIE KKPLTSACVS QQNGNYIHSC
CCVTMDDGTP MYSELKSPTK RHLVIGASGD PKYIDLPASE AERMYIAKEG YCYLNIFLAM
LVNVNENEAK DFTKMIRDVL IPMLGQXPSL XDXAXXXYIL GVFHPETRCA ELPRILVDXA
TQTXHVIDSY GXLTVGYHVL XAXTVNHLIQ FASNDLQSEM KHYRVXXXPT QRXKLEEQLX
XXIFKPKXXX QLLXXXPYIL LXXXISPTIL VHMYRMRHFE RGIEIWIKRD HEIGKIFVIL
EQLTRKVALA EVLVDQFNLI SEASXHLLEI MRGCQDXXXA YVPALDLLTI XXXREFSNKE
LXTNXYXDLQ QTLFDMXEKX YXKXLHNSWQ ELSXLEXSXX TVXLKXXXIF TXRNLTQRXK
EGKXXSSLQF VHXXFITTRV HXKSIRDASV XXXXXXXVXT XXFXXXCGXX IXAXCYXDXI
YLVNVCLVFS LVLQMSNTVR SXIAATXEEK ERAMANKADE NERXLMHMYH IFSKKQDDAP
IYNDFLEHVR NVRPDLEETL LYMAGAEVVS TXAKSAXXVQ FEKIIAVLAL LTMCFDAXRS
DAIFKIXTXL KTVFSTVGGT VXXQGLEDIX SLEDDKRLTI DFDINXXXXH SSTTFXXXXX
XWWXRQLXXN RTVXHYRTTG KFLEFTRNTA AFVANEIASS SEGEFLVRGA VGSGKSTSLP
AHXXKKGKVX XXEPTRPLAE NVSRQLAGDP FFQNVXLRMR GLSCFGSSNI TVMTSGFAFH
YYVNNPHQLM EFDFVIIDEC HVTDSATIAF NCALKEYNFA GKLIKVSATP PGRECDFDTQ
FAVKVKTEDH LSFHAFVGAQ KTGSNADMVQ HGNNILVYVA SYNEVDMLSK LLTERQFSVT
KVDGRTMQLG KTTIETHGTS QKPHFIVATN IIENGVTLDV ECVVDFGLKV VAELDSENRC
VRYNKKSVSY GERIQRLGRV GRSKPGTALR IGHTEKGIET IPEFIATEAA ALSFAYGLPV
TTHGVSTNIL GKCTVKQMRC ALNFELTPFF TTHLIRHDGS MHPLIHEELK QFKLRDSEMV
LNKVALPHQF VSQWMDQGEY ERIGVHVQCH ESTRIPFYTN GIPDKVYERI WKCIQENKND
AVFGKLSSAC STKVSYTLST DPAALPRTIA IIDHLLAEEM MKRNHFDTIS SAVTGYSFSL
AGIADSFRKR YMRDYTAHNI AILQQARAQL LEFNSKNVNI NNLSDLEGIG VIKSVVLQSK
QEVSSFLGLR GKWDGRKFAN DVILAIMTLL GGGWFMWEYF TKKINEPVRV ESKKRRTQKL
KFRDAYDRKV GREIFGDDDT IGRTFGEAYT KRGKVKGNNN TKGMGRKTRN FVHLYGVEPE
NYSFIRFVDP LTGHTXDEST HTDISLVQEE FGSIREKFLE NDLISRQSII NKPGIQAYFM
GKGTEEALKV DLTPHVPLLL CRNTNAIAGY PERENELRQT GTPVKVSFKD VPEKNEHVEL
ESKSIYKGVR DYNGISTIVC QLTNDSDGLK ETMYGIGYGP IIITNGHLFR KNNGTLLVRS
WHGEFIVKNT TTLKVHFIEG KDVVLVRMPK DFPPFKSNAS FRAPKREERA CLVGTNFQEK
SLRSTVSESS MTIPEGTGSY WIHWISTNEG DCGLPMVSTT DGKIIGVHGL ASTVSSKNYF
VPFTDDFIAT HLSKLDDLTW TQHWLWQPSK IAWGTLNLVD EQPGPEFCIS NLVKDLFTSG
VETQSKRERW VYESCEGNLR AVGTAQSALV TKHVVKGKCP FFEEYLQTHA EASAYFRPLM
GEYQPSKLNK EAFKKDFFKY NKPVTVNQLD HDKFLEAVDG VIRMMCDFEF NECRFITDPE
EIYNSLNMKA AIGAQYRGKK KEYFEGLDDF DRERLLFQSC ERLFNGYKGL WNGSLKAELR
PLEKVRANKT RTFTAAPIDT LLGAKVCVDD FNNEFYRKNL KCPWTVGMTK FYGGWDKLMR
SLPDGWLYCH ADGSQFDSSL TPALLNAVLI IRSFYMEDWW VGQEMLENLY AEIVYTPILA
PDGTIFKKFR GNNSGQPSTV VDNTLMVVIS IYYACMKFGW NCEEIENRLI FFANGDDLIL
AVKDEDSGXL DNMSSSFCEL GLNYDFSERT HKREDLWFMS HQAMLVDGMY IPKLEKERIV
SILEWDRSKE IMHRTEAICA AMIEAWGHTE LLQEIRKFYL WFVEKEEVRE LAALGKAPYI
AETALRKLYT DKGADKSELA RYLQALHQDI LFEQGDTVML QSGTQPTVSD AGATKKDKED
DKGKNKDVTG SGSGERTVAA VTKDKDVNAG SHGKIVPRLS KITKKMSLPR VKGNVILDID
HLLEYKPDQI ELYNTRASHQ QFASWFNQVK TEYDLNEQQM GVVMNGFMVW CIENGTSPDI
NGVWXMMDGN EQVEYPLKPI VENAKPTLRQ IMHHFSDAAE AYIEMRNAEA PYMPRYGLLR
NLRDRSLARY AFDFYEVNSK TPERAREAVA QMKAAALSNV SSRLFGLDGN VATTSEDTER
HTARDVNRNM HTLLGVNTMQ
//
