ID A0A067XIY5_9POTV Unreviewed; 3219 AA. AC A0A067XIY5; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 11-DEC-2019, entry version 31. DE SubName: Full=Polyprotein {ECO:0000313|EMBL:AGE83528.1}; OS Watermelon mosaic virus. OC Viruses; Riboviria; 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: Helper component proteinase: required for aphid transmission CC and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at CC its own C-terminus. Interacts with virions and aphid stylets. Acts as a CC suppressor of RNA-mediated gene silencing, also known as post- CC transcriptional gene silencing (PTGS), a mechanism of plant viral CC defense that limits the accumulation of viral RNAs. May have RNA- CC binding activity. {ECO:0000256|SAAS:SAAS00890155}. 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|SAAS:SAAS01116832}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.48; Evidence={ECO:0000256|SAAS:SAAS01198479}; CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family. CC {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:0019028; C:viral capsid; IEA:UniProtKB-KW. 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:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase 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:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR Gene3D; 3.90.70.150; -; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. 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; IPR001592; Poty_coat. DR InterPro; IPR001730; Potyv_NIa-pro_dom. DR InterPro; IPR039560; Potyvirid-P3. DR InterPro; IPR013648; PP_Potyviridae. 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 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; PS50507; RDRP_SSRNA_POS; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS01198603}; KW Capsid protein {ECO:0000256|SAAS:SAAS01208933}; KW Helicase {ECO:0000256|SAAS:SAAS01199809}; KW Hydrolase {ECO:0000256|SAAS:SAAS01198589}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS01198580}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01198562}; KW Protease {ECO:0000256|SAAS:SAAS00272399}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS01198530}; KW Suppressor of RNA silencing {ECO:0000256|SAAS:SAAS00890154}; KW Transferase {ECO:0000256|SAAS:SAAS01198537}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS01198628}; KW Virion {ECO:0000256|SAAS:SAAS01208933}. 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="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2962..2984 FT /note="Polar" 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 //