ID A0A067XIY5_9POTV Unreviewed; 3219 AA. AC A0A067XIY5; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 24-JUN-2015, entry version 7. DE SubName: Full=Polyprotein {ECO:0000313|EMBL:AGE83528.1}; DE Flags: Precursor; OS Watermelon mosaic virus. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC 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 RT isolates from China."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Helper component proteinase: required for aphid CC transmission and also has proteolytic activity. Only cleaves a CC Gly-Gly dipeptide at its own C-terminus. Interacts with virions CC and aphid stylets. Acts as a suppressor of RNA-mediated gene CC silencing, also known as post-transcriptional gene silencing CC (PTGS), a mechanism of plant viral defense that limits the CC accumulation of viral RNAs. May have RNA-binding activity (By CC similarity). {ECO:0000256|SAAS:SAAS00208798}. CC -!- CATALYTIC ACTIVITY: Hydrolyzes a Gly-|-Gly bond at its own C- CC terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the CC processing of the potyviral polyprotein. CC {ECO:0000256|SAAS:SAAS00118595}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|SAAS:SAAS00153520}. CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family. CC {ECO:0000256|RuleBase:RU003351}. CC -!- SIMILARITY: Contains RdRp catalytic domain. CC {ECO:0000256|SAAS:SAAS00153546}. CC -!- SIMILARITY: Contains helicase ATP-binding domain. CC {ECO:0000256|SAAS:SAAS00252625}. CC -!- SIMILARITY: Contains helicase C-terminal domain. CC {ECO:0000256|SAAS:SAAS00251432}. CC -!- SIMILARITY: Contains peptidase C6 domain. CC {ECO:0000256|SAAS:SAAS00191835}. 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 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; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR001456; HC-pro. 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; IPR001592; Poty_coat. DR InterPro; IPR001730; Potyv_NIa-pro_dom. DR InterPro; IPR013648; PP_Potyviridae. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009003; Trypsin-like_Pept_dom. 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; 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; 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|RuleBase:RU000452, KW ECO:0000256|SAAS:SAAS00180352}; KW Helicase {ECO:0000256|RuleBase:RU000452, KW ECO:0000256|SAAS:SAAS00261943}; KW Hydrolase {ECO:0000256|RuleBase:RU000452, KW ECO:0000256|SAAS:SAAS00180363}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00075875}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00153703}; KW Protease {ECO:0000256|SAAS:SAAS00118600}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00153521}; KW Suppressor of RNA silencing {ECO:0000256|SAAS:SAAS00118628}; KW Transferase {ECO:0000256|SAAS:SAAS00153681}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00250960}. FT CHAIN 1 443 P1 protein. {ECO:0000313|EMBL: FT AGE83528.1}. FT /FTId=PRO_5001237111. FT CHAIN 444 900 helper component-protease. FT {ECO:0000313|EMBL:AGE83528.1}. FT /FTId=PRO_5001237120. FT CHAIN 901 1247 P3 protein. {ECO:0000313|EMBL: FT AGE83528.1}. FT /FTId=PRO_5001237118. FT CHAIN 1248 1299 6K1 protein. {ECO:0000313|EMBL: FT AGE83528.1}. FT /FTId=PRO_5001237117. FT CHAIN 1300 1933 cylindrical inclusion protein. FT {ECO:0000313|EMBL:AGE83528.1}. FT /FTId=PRO_5001237112. FT CHAIN 1934 1986 6K2 protein. {ECO:0000313|EMBL: FT AGE83528.1}. FT /FTId=PRO_5001237116. FT CHAIN 1987 2176 NIa-VPg. {ECO:0000313|EMBL:AGE83528.1}. FT /FTId=PRO_5001237114. FT CHAIN 2177 2419 protease. {ECO:0000313|EMBL:AGE83528.1}. FT /FTId=PRO_5001237119. FT CHAIN 2420 2936 NIb. {ECO:0000313|EMBL:AGE83528.1}. FT /FTId=PRO_5001237115. FT CHAIN 2937 3219 coat protein. {ECO:0000313|EMBL: FT AGE83528.1}. FT /FTId=PRO_5001237113. 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 //