ID A0A067XIY5_9POTV Unreviewed; 3219 AA. AC A0A067XIY5; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 25-MAY-2022, entry version 43. 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:AGE83528.1}; RN [1] {ECO:0000313|EMBL:AGE83528.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WMV-ShanXi {ECO:0000313|EMBL:AGE83528.1}; RA Lei Z., Hao X., Wu Y.; RT "Complete genomic sequence analyses of Watermelon mosaic virus isolates RT from China."; RL Submitted (MAY-2012) 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: Both 6K peptides are indispensable for virus replication. CC {ECO:0000256|ARBA:ARBA00002011}. 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: 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: Recruits the host translation initiation complex for viral CC genome translation by binding to host plant eIF4E/eIF(iso)4E and CC eIF4G/eIF(iso)4G proteins. {ECO:0000256|ARBA:ARBA00029412}. 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: Host nucleus {ECO:0000256|ARBA:ARBA00004147}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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; JX079685; AGE83528.1; -; Genomic_RNA. DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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-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; 2.40.10.10; -; 2. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR Gene3D; 3.90.70.150; -; 1. 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 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; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF56672; SSF56672; 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:ARBA00022806}; 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 nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; 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 Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Suppressor of RNA silencing {ECO:0000256|ARBA:ARBA00022463}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}; KW Virion {ECO:0000256|ARBA:ARBA00022844}. FT DOMAIN 302..443 FT /note="Peptidase S30" FT /evidence="ECO:0000259|PROSITE:PS51871" FT DOMAIN 778..900 FT /note="Peptidase C6" FT /evidence="ECO:0000259|PROSITE:PS51744" FT DOMAIN 1371..1523 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1542..1701 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2177..2395 FT /note="Peptidase C4" FT /evidence="ECO:0000259|PROSITE:PS51436" FT DOMAIN 2661..2785 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 2940..2989 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2941..2961 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2962..2984 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 786 FT /note="For helper component proteinase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080" FT ACT_SITE 859 FT /note="For helper component proteinase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080" SQ SEQUENCE 3219 AA; 366473 MW; AC736E183203B6FB CRC64; MATIMFGDFT VQLKHSTVTE KRKRVIETTK LEQEVRMETV CETVMESITV GCTARCAGLS AYTKSSLKRA IKEGDLSASG GCNYCGLRAL VGEGRERVIS VPRVVTQQKE IIVTKEVPHI YEEEYEVEVP YLATEPVLPM VSTFPGSDVY KTTVQAKALN NIVTKDMMAK SEPSMKQVSR SLVLAGRKEI GSYDVAIKRM DEAMQHDSAL QRKLLIQQYS TIKQLPKGAV QLSLCSYEQA KKRAESARKR KQEEDFLNGK YEQQAYIGTA ATNTTKTIGG SVGFRTIHWK PTPKQNKIKR AKKRCVKLTH VLEEILSLSA KTGKPIEFIT KRARKNFKVN YVRKHGAVIP KFTLPHEEGK YVYQELQYAN ICEFLPYICM FAKYKVISAD DLTYGDSGLL FDERSSITTE HTTLPYFVVR GRENGRLVSA FEEFREIGDI QHYSHTPEVQ FFLGWKKVFD KMQPRVDAHE CTVDFTNEQC GELAAAISQS IFPVKKLSCK HCRRHIKDLS WEEYKQFLLT HMGCSEATWK DVRKAEGMEH VKKLIERSTA ENLSLQTSME IVRLTQNYKS THMLQIQDIN KALMKGSSVT QDELEQASKQ LLAMTQWWKN HMTLTDEDAL KVFRNKRSSK ALLNPSLLCD NQLDKNGNFV WGERGKHSKR FFANYFEEVI PSEGYSKYVI RKNPNGQREL AIGSLIVPLD FERARMALQG KSIAREPITM ACISRQDGNF VYPCCCVTHD DGKAFYSELK SPTKRHLVIG TSGDPKYIDL PATETDRMYI AKEGYCYLNI FLAMLVNVNE DEAKDFTKMV RDVIVPKLGQ WPTMFDVATA VYMLTVFHPE TRNAELPRIL VDHACQTMHV IDPFGSLTVG YHVLKVGTVN QLIQFASNDL HSEMKFYRVG GEAQQRMKCE TALIKSIFKP KRMIQILEDD PYILLMGLIS PSILIHMYRM KHFEKGIELW ISKEHSVAKI FIIMEQLTRK IAANDLLLEQ LDIIAGTSQE LMDVLEDCPQ SAHSYKTAKD LLAIYIERRA SNNQLIENGF VDINDQLYIT HEKIYVDRLK QEWHALSWLE KSSITWQLKR FTPHTEQCLT KKVVEESSAY SRNFVSACFM NAQSHLKNVR NTFFRKCDQA WTASVRAFVR FIIATPHKCY SDIVYLVNIC LIFSLLVQVA SVLQGIVSAA KRDKAFVHMH KRIEDEQAVV HLYEMCEKME NKHPSVDEFL NHVKKVRPEL FPVAKSMAGQ SEDVSAQAKT ATQLQLEKIV AFMALLTMCI DNERSDAVFK ILSKLKTFFG TMGEEVKVQS LDEIQNIDED KKLTIDFDLE TSKEPSSVSF DVKFEDWWHR QLQQNRVVPH YRSTGEFLEF SRETAAKTAN LIATSSHTEF LIRGAVGSGK STGLPHHLSK KGKVLLLEPT RPLAENVSKQ LSLEPFYHNV TLRMRGLSKF GSSNIVVMTS GFAFHYYVNN PQQLSDFDFI IIDECHVQDS NTIAFNCALK EFEFSGKLLK VSATPPGREC EFTTQHPVKL KIEDHLSFQS FVQAQGTGSN ADMLQHGSNL LVYVASYNEV DQLSRLLTEK HYKVTKVDGR TMQMGNVEIT TTGTEGKPHF IVATNIIENG VTLDIDCVID FGLKVVAVLD TDNRCVRYNK QSVSYGERIQ RLGRVGRHKP GFALRVGHTE KGIEEVPEFI ATEAAFLSFA YGLPVTTQSV STNILSRCTV KQARVALNFE LTPFFTTNFI KYDGGMHPEI HRLLKPYKLR ESEMMLHKLA IPHQFVGQWL SVKEYDRQGI HLNCPETVKV PFYVNGIPDK LYESLWETVC NYKCDAGFGS IRSVNASKIS YTLSTDPTAI PRTLAILDHL LSEEMTKKSH FDTIGSSVTG YSFSLAGIAD GFRKRYLRDY TQQNIAILQQ AKAQLLEFDC TKVDINNLQS VEGIGILNAV QLQSKHEVSK FLQLKGKWDG KKFMNDAIVA IFALIGGGWM LWDYFTRMIR EPVTTQGKKR QMQKLKFRDA FDRKVGREVY ADDYTMEHTF GEAYTKKGKQ KGSTKTKGMG RKSRNFIHMY GVEPENYSMI RFVDPLTGHT MDESTRVDIR LVQQEFGEIR EEMIGADELD PQRVYHNPGI QAYFIGKNAE EALKVDLTPH VPTLLCQNSN AIAGFPEREG ELRQTGLPQI VPKADVPRAK ERVEVESKSV YKGLRDYSGI STLICQLTNS SDGHKETMFG VGYGSFIITN GHLFRRNNGM LTVKTWHGEF VIHNTTQLRI HFIQGKDAIL IRMPKDFPPF AKRNFFRQPK REERVCMVGT NFQEKSLRAT VSESSIILPE GKGSFWIHWI TTQDGFCGLP LVSVNDGYIV GIHGLTSNDS EKNFFVPFTD GFETEYLNNA DNLSWDKHWF WEPSKIAWGS LNLVDEQPKE EFKISKLVSD LFGNTVAVQS RKERWVLDAM EGNLVACGQA DSALVTKHVV KGKCPYFAQY LTLHNEAKQF FEPLMGAYQP SRLNKDAFKK DFFKYNKPVV LNEVDFNAFE KAVEGVITMM VDFEFAECLF VTDPDEIYGS LNMKAAVGAQ YKGKKQDYFS GMDSFDKERL LYLSCERLFN GEKGIWNGSL KAELRPIEKV QANKTRTFTA APIDTLLGAK VCVDDFNNQF YSFNLKCPWT VGMTKFYGGW DKLMRSLPDG WTYCHADGSQ FDSSLTPLLL NAVLSIRCCF MEDWWVGKEM LENLYAEIVY TPILAPDGTI FKKFRGNNSG QPSTVVDNTL MVVIAMYYSC CKQGWSEEDI ERRLVFFANG DDIILAVRDE DVWLYDTLSA SFAELGLNYN FDERTKKREE LWFMSHQAML VDGIYIPKLE PERIVSILEW DRSKEIMHRT EAICAAMIEA WGYTELLQEI RKFYLWLLSK DEFKELAASG KAPYIAETAL KKLYTDVNTQ PSELQRYLEV LDFNHTDGCC ESVSLQSGKE KETVENLDAG KDSKKDTSGK GDKPQNLQTG QGSKEPTKAG TVSKDVNVGS KGKEVPRLQK ITKKMNLPTV GGKIILSLDH LLEYKPNQVD LFNTRATKTQ FESWYSAVKV EYDLNDEQMG VIMNGFMVWC IDNGTSPDVN GVWVMMDGEE QVEYPLKPIV ENAKPTLRQI MHHFSDAAEA YIEMRNSESP YMPRYGLLRN LRDRELARYA FDFYEVTSKT PNRAREAIAQ MKAAALAGIN SRLFGLDGNI STNSENTERH TARDVNQNMH TLLGMGPPQ //