ID A9EEY5_9POTV Unreviewed; 3080 AA.
AC A9EEY5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
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:BAF93929.1};
RN [1] {ECO:0000313|EMBL:BAF93929.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RDA {ECO:0000313|EMBL:BAF93929.1};
RA Choi S., Sohn S., Park J., Kim K., Lee S., Ryu K., Choi J.;
RT "Molecular characterization of papaya ringspot virus in Korea.";
RL Submitted (NOV-2007) 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 -!- 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; AB369279; BAF93929.1; -; Genomic_RNA.
DR MEROPS; C06.001; -.
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; 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 2809..2843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2812..2827
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; 350745 MW; 13E494561020047A CRC64;
MASIMIGSVS VPIAKPAQCA NTQASSRVSI VAPGHMATYP PPLKTHMYYR HESKKLMQSN
KSIDILNNFF STDEMKFRLT RNEMSKVKKG PSGRIVLRKP SKQRVFARIE QDEAARKEEA
VFLEGNYDDS ITTLESVLPS EVTRDVDVSL RSPFYKRTCK KERKRVAQKQ IVQAPLNSLC
TRILKIARNK NIPVEIIGNK KAKHTLTFKR FRGHFVGKVS VAHEEGRMRH TEMSYEQFKW
ILKAICQVTH TERIREEDIK PGCSGWVLGT NHALTKRYSR LPHLVIRGRD DDGIVNALEP
VLFYSEVDHY SSQPEVQFFQ GWRRMFDKFR PSPDHVCKVD HNNEECGELA AIFCQALFPV
VKLSCQTCRE KLSRVSFEEF KDSLNANFII HKDEWDSFKE GSHYDNIFKL IKVATQATQN
LKLSSEVMKL VQNHTSTHMK QIQDVNKALM KGSLVTQDEL DLALKQLLEM TQWFKNHMHL
TGEEALKTFR NKRSSKAMIN PSLLCDNQLD KNGNFVWGER GYHSKRLFKN FFEEVIPSEG
YTKYVVRNFP NGTRKLAIGS LIVPLNLDRA RTALLGESIE KKPLTSACVS QQNGNYIHSC
CCVTMDDGTP MYSELKSPTK RHLVIGASGD PKYIDLPASE AERMYIAKEG YCYLNIFLAM
LVNVNESEAK DFTKMIRDVL IPMLGQWPSL MDVATAAYIL GVFHPETRCA ELPRILVDHA
TQTMHVIDLY GSLTVGYHVL KAGTVNHLIQ FASNDLQSEM KHYRVGGTPT QRIKLEEQLI
KGIFKPKLMM QLLHDDPYIL LLGMISPTIL VHMYRMRHFE RGIEIWIKRD HEIGKIFVIL
DQLTRKVALA EILVDQLDLI SEASPHLLEI MKGCQDNQRA YVPALDLLTI QVEREFSNKE
LKTNGYPDLQ QTLFDMREKI YAKQLHNSWQ ELSLLEKSCV TVRLKRFSVF TERNLIQRAK
EGKRTSSLQF VHECFITTRV HAKSIRDASV RKLNEALVGT CKFFFSCGFK IFARCYSDII
YLVNVCLVFS LVLQMSNTVR NMIAAIREEK ERAMANKADE NERTLMHMYH IFSKKQDDAP
IYNDFLEHVR NVRPDLEETL LYMAGAEVVA TQAKSAVQVQ FEKIIAVLAL LTMCFDAERS
DAIFKILTKL KTVFGTVGET VRLQGLEDIE SLEDDKRLTI DFDINTNEAQ SSTTFDVHFD
DWWNRQLQQN RTVPHYRTTG KFLEFTRNTA AFVANEIASS SEGEFLVRGA VGSGKSTSLP
AHLAKKGKVL LLEPTRPLAE NVSRQLAGDP FFQNVTLRMR GLNCFGSSNI TVMTSGFAFH
YYVNNPHQLM EFDFIIIDEC HVTDSATIAF NCALKEYNFA GKLIKVSATP PGRECDFDTQ
FAVKVKTEDY LSFQAFVGAQ KTGSNADMVQ HGNNILVYVA SYNEVDMLSK LLTERQFSVT
KVDGRTMQLG RTTIETHGTS QKPHFIVATN IIENGVTLDV ECVVDFGLKV VAELDSENRC
VRYNKKSVSY GERIQRLGRV GRSKPGTALR IGHTEKGIEN IPEFIATEAA ALSFAYGLPV
TTHGVSTNIL GKCTVKQMRC ALNFELTPFF TTHLIRHDGS MHPLIHEELK QFKLRDSEMV
LNKVALPHQF VSQWMDQSEY ERIGVHVQCH ESTRIPFYTN GVPDKVYEKI WKCIQEHKND
ADFGKLSSAC STKVSYTLST DPAALPRTIA IIDHLLAEEM MKRNHFDTIS SAVTGYSFSL
AGIADSFRKR YMRDHTAHNI AILQQARAQL LEFNSKNVNI NNLSDLEGIG VIKSVVLQSK
QEVSNFLGLR GKWDGRKFSN DVILAIMTLL GGGWFMWEYF TKKINEPVRV ESKKRRSQKL
KFRDAYDRKV GREIFGDDGT IGRTFGEAYT KRGKVKGNNS TKGMGRKTRN FVHLYGVEPE
NYSFIRFVDP LTGHTLDEST HTDIALVQEE FGSIREKFLE DDLISRQSII NKPGIQAYFM
GKGTEEALKV DLTPHVPLLL CRNTNAIAGY PERENELRQT GTPVKVSFKD VPEKNEHVEL
ESKSIYKGMR DYNGISTIVC QLTNDSDGLK ETMYGIGYGP IIITNGHLFR KNNGTLLVKS
WHGEFTVKNT TTLKVHFIEG KDVVLVRMPK DFPPFKSNAF FRAPKREERA CLVGTNFQEK
SLRSTVSESS MTIPEGTGSY WIHWISTNEG DCGLPMVSTT DGKIIGVHGL ASTVSSKNYF
VPFTDDFIAT HLSKLDDLTW TQHWLWQPSK IAWGTLNLVD EQPGPEFRIS NLVKDLFTSG
VETQSKRERW VYESCEGNLR VVGTAQSALV TKHVVKGKCP FFEEYLQTHA EASAYFRPLM
GEYQPSKLNK EAFKKDFFKY NKPVTVNQLD HDKFLEAVDG VIRMMCDFEF NECRFITDPE
EIYNSLNMKA AIGAQYRGKK KEYFEGLDDF DRERLLFQSC ERLFNGYKGL WNGSLKAELR
PLEKVRANKT RTFTAAPIDT LLGAKVCVDD FNNEFYSKNL KCPWTVGMTK FYGGWDKLMR
SLPDGWLYCH ADGSQFDSSL TPALLNAVLI IRSFYMEDWW VGQEMLENLY AEIVYTPILA
PDGTIFKKFR GNNSGQPSTV VDNTLMVVIS IYYACMKFGW NHEDIENKLV FFANGDDLIL
AVKDEDSGLL DNMSSSFCEL GLNYDFSERT HKREDLWFMS HQAMLVDGMY IPKLEKERIV
SILEWDRSKE IMHRTEAICA AMIEAWGHTE LLQEIRKFYL WFVEKEEVRE LAAIGKAPYI
AETALRKLYT DKGAETSELA RYLQALHQDI FFEQGDTVML QSGTQQTVAD AGATKKDKED
DKAKNKDATS SSSGNKTVAA VTKDKDVNAG SHGKIVPRLA KITKKMSLPT VKGNVILDID
HLLNYKPDQI ELYNTRASHQ QFASWFNQVK TEYDLNDQQM GVVMNGFMVW CIENGTSPDI
NGVWVMMDGD EQVEYPLKPI VENAKPTLRQ IMHHFSDAAE AYIEMRNAEA PYMPRYGLLR
NLRDRSLARY AFDFYEVNSK TPERAREAVA QMKAAALSNV SSRLFGLDGN VATTSEDTER
HTARDVNRNM HTLLGVNTMQ
//
