ID A0A097BVS2_9POTV Unreviewed; 3222 AA. AC A0A097BVS2; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 18-JAN-2017, entry version 13. DE SubName: Full=Polyprotein {ECO:0000313|EMBL:AIS72951.1}; OS Bean common mosaic virus. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Potyviridae; Potyvirus. OX NCBI_TaxID=12196 {ECO:0000313|EMBL:AIS72951.1}; RN [1] {ECO:0000313|EMBL:AIS72951.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DXH015 {ECO:0000313|EMBL:AIS72951.1}; RX PubMed=25107622; DOI=10.1016/j.virusres.2014.07.029; RA Zhou G.C., Wu X.Y., Zhang Y.M., Wu P., Wu X.Z., Liu L.W., Wang Q., RA Hang Y.Y., Yang J.Y., Shao Z.Q., Wang B., Chen J.Q.; RT "A genomic survey of thirty soybean-infecting bean common mosaic virus RT (BCMV) isolates from China pointed BCMV as a potential threat to RT soybean production."; RL Virus Res. 191:125-133(2014). RN [2] {ECO:0000313|EMBL:AIS72951.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DXH015 {ECO:0000313|EMBL:AIS72951.1}; RA Zhou G.-C., Shao Z.-Q., Wu X.-Y., Zhang Y.-M., Wu P., Wu X.-Z., RA Hang Y.-Y., Yang J.-Y., Wang Q., Wang B., Chen J.-Q.; RL Submitted (MAY-2014) 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. CC {ECO:0000256|SAAS:SAAS00534160}. 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:SAAS00494791}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|SAAS:SAAS00510455}. CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family. CC {ECO:0000256|RuleBase:RU003351}. CC -!- SIMILARITY: Contains 1 peptidase C6 domain. {ECO:0000256|PROSITE- CC ProRule:PRU01080}. 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; KJ807805; AIS72951.1; -; Genomic_RNA. DR GO; GO:0019028; C:viral capsid; IEA:InterPro. 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; IPR031159; HC_PRO_CPD_dom. 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; 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; 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:SAAS00510945}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Helicase {ECO:0000256|SAAS:SAAS00481789}; KW Hydrolase {ECO:0000256|SAAS:SAAS00510997}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00510884}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510590}; KW Protease {ECO:0000256|SAAS:SAAS00494788}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600}; KW Suppressor of RNA silencing {ECO:0000256|SAAS:SAAS00494786}; KW Transferase {ECO:0000256|SAAS:SAAS00510371}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00664279}. FT DOMAIN 778 900 Peptidase C6. {ECO:0000259|PROSITE: FT PS51744}. FT DOMAIN 1371 1523 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1542 1701 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 2177 2395 Peptidase C4. {ECO:0000259|PROSITE: FT PS51436}. FT DOMAIN 2660 2784 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50507}. FT COILED 193 220 {ECO:0000256|SAM:Coils}. FT ACT_SITE 786 786 For helper component proteinase activity. FT {ECO:0000256|PROSITE-ProRule:PRU01080}. FT ACT_SITE 859 859 For helper component proteinase activity. FT {ECO:0000256|PROSITE-ProRule:PRU01080}. SQ SEQUENCE 3222 AA; 366335 MW; 13C6ADE86FCCAF7E CRC64; MATIMFGDFT VQLKHNTRTE KRKRVVETTR LEKEVRMETV HVQVMESITV GCSARCAGLS AYTKSSLKRA IKEGDLSASG GCHYCGLRAL VGEGRERVIS VPQLVAQQKE VVVTKEVPHF YEEEYEVEVP CTTTELLPSV MVINPATNVC ETAVQTQVAH NIVTKDMMAT SEPSLKQISR AFVVAGKQAV NSYDLAIKKM DEAMQQNSEL QRKLLVQQQS TIKQRPKGAV QLRLCSYDQA KKRADLVRKR QEEEEAFLQG RYQQQEYIGR VLDPMNIQRG ESVGFRSPYW HRSFKQSVNT PPKKKVRSAT RVLREILSVV RDRDMTVEFI GHRTKRLEAR YVRRGNLVIP KVTLPHEGGK YKKTELDINI YSQCLAALCE HGIYRSLSDE EIKPGDSGLV FDKRSPFVFD HTQQTFMIIR GRLDEKLVNA LDEQQDIHSI HHYSQNPEMQ FFTGWRDKFN KLVPHTQQHE CSVDYDNAQC GQFAAIMSQM LYPVRKLSCT RCRQHIQTLS WEEYKQFVAA NISCHKTILD ESKDIIGLDI VHKLINKATS ENLNLTASME IAKLTHNNKC TAMLQIQDIN KALMKGSSVT QEELDLALSQ LLKMTQWWKN HRSLAESDPL KTFRNKRSSK ALLNPSLLCD NQLDKNGNFI WGERGYHSKR FFSNFFDEVI PSEGYGKYRI RKNPNGQREL AIGSLIVPLS LERARTALQG KSVETVPLTM ACVARQNGNF VYPCCCVTLD DGTPMYSELK SPTKRHLVVG TSGDPKYIDL PQNDEDRMYI AKEGYCYLNI FLAMLVNVNE REAKDFTKMV RDVIIPMLGT WPTMHDLATA VYILTVFHPE TRNAELPRIL VDHASQTMHV IDSFGSLTTG YHVLKAGTIN QLINFAATDL DGEMKHYRVG GDAQQRMRCE TALITSIFKP KRMIKILESD PYILLMGLVS PSLLIHLYRM RHLEKAIEVW IQRDQSVSRI FVLLEQLTKK VAVCEVLKDQ LDTINNAAGH LLDILKDCPK TMHSYVPAND LLTLYLERQT ANSQLLTNGF TDINDLLYVE MEKIYISRLK QEWHALSLLE KSSVTWHLKQ FSVAMEKDLI KRVTEGRGGF SVSSVSECFT TAKSHLRSKK DLILRACENF GRSLVRKCVN MLFSIVKKCY SDIIYLVNVI IIFSLLVQMI STMHSMITVA QQNKAFVKQA ERESKEKSVL HTYDMCCKAA GEPPTRDEFL EHLEKIRPEL VPTAKEMMAM TNNVSVQAKN ATQLQFEKIV AFMALLTMII DTERSDAIFK ILNKLKTVFH TMGENVQMQS LDEILSVDEE KKLTIDFDME SSKEATSTSF DVKFGDWWNR QLQQNRVVPH YRNCGKFMEF TRETAAKVAN EISISTETEF LVRGAVGSGK STGLPHHLAK KGKVLLCEPT RPLAENVSKQ LSKDPFYQNV TLRMRGMSKF GSSNITVMTS GFAFHYYVNN PQQLSDFDFI IFDECHVMDT SAIAFNCALK EFEFAGKLLK VSATPPGREC EFTTQHPVKL KVEEQLSFTN FVQAQGTGSN ADMIQHGSNL LVYVASYNEV DQMSKLLIEK NFKVTKVDGR TMQMGNVEIN TMGSEGKPHF VVATNIIENG VTLDVDCVID FGLKVVATLD SDSRCVRYVK KPVSYGERIQ RLGRVGRHKP GFALRIGYTE KGVEEITEFI ATEAAFLSFA YGLPVTTQSV TTNMLSQCTV KQAKSALNFE LTPLFTTHFV KYDGTMHPEV HRILKAFKLR ESEMVLNKLA IPHQYTGQWL SVAEYERMGI HIQCTGKTRI PFYVNGIPDK IFEMLWDTVC KYKSDAGFGK LTSVNATKVS YTLSTDPNAL PRTIAIIDHL ISEEMMKKSH FDTMSSAITG HSFSLNGIAE AIRKRYLKDH TQQNIVILQQ AKAQLLEFSN TKVDINDLST LGDLGVLNTV RLQGKEEVVK FLGLKGKWDG KKFMNDAILA VFTLIGGGWM MWEYFSKKMK EGVTTQGKKR MLQKLKFRDA FDRKVGREVY ADDYTMEHTF GEAYTKKGKQ KGSTKTKGMG RKTRNFIHMY GVEPENYSMI RFVDPLTGAT LDENPRVDIR LVQEEFGEVR MQKINDGELD SAAVASRPGI QAYFIGKNAE EALKVDLTPH RPTLLCMNSN AISGFPEREN ELRQTGLPVH IKRSDVPEPN EEVAVESKSI YKGLRDYNGI SSLVCLLTNI SDGHSETIFG IGYGSYIITN GHLFKRNNGV LNIRTWHGEF EIKNTTQIKI HFIEGKDAIL IRMPKDFPPF AKKSLFRPPI KEERVCMVGT NFQEKSLRAT VSESSMVLPE GVGSFWIHWI TTQDGYCGLP LVSVNDGLIV GFHGLTSNDS NKNFFVPFCE DFENKYLKSA ESLSWDKHWF WQPDKIAWGS LNLVSDQPKE EFKVSKLISD LFGGTVATQS KQQWVLESVE GNLKACARAD SALVTKHVVK GKCPYFEQYL RERDEAAAFF KPLMGAYQPS RLNKEAFKKD FFKYNKVVTL NEVCYEAFEA AFNGVVMMMI EHGFSECSYV TDPDEIYSSL NLKAAVGAQY KGKKQDYLCD MDEFDKERLL YMSCERLFYG KKGLWNGSLK AELRPLEKVE ANKTRTFTAA PMDTLLGAKV CVDDFNNQFY SLNLECPWTV GMTKFYGGWD TLMRKLPDGW VYCHADGSQF DSSLTPLLLN SVLGIRRFFM EDWWVGEEML ENLYAEIVYT PILAPDGTVF KKFRGNNSGQ PSTVVDNTLM VVMSVYYSCH KVGWSDDDIQ ERLVFFANGD DIILSMQETD LWVLDTFASS FRELGLNYNF DERTRKREDL WFMSHCAIEV DGIYIPKLEP ERVVSILEWD RSKEMMHRTE AICAAMIEAW GYPELLQEIR KFYLWLLERD ELREIAASGG APYIAESALK TLYTNKRTRI EELAKYLAVL DFEYEVGCGE SVHLQSGGNP TPPPVVDAGE GINKDKKEKS NKGKGPESSE GSGNNNRGTE NQSMRDKDVN AGSKGKVVPR LQRITKRMNL PMVRGNVILN LDHLLDYKPE QTDLFNTRAT KMQFEMWYNA VKGEYEIDDE QMSIVMNGFM VWCIDNGTSP DVNGTWVMMD GEEQVEYPLK PMVENAKPTL RQIMHHFSDA AEAYIEMRNS ERPYMPRYGL LRNLRDKNLA RYAFDFYEVT SKTSDRAREA VAQMKAAALS NVNSKLFGLD GNVATTSENT ERHTARDVNQ NMHTLLGMGS PQ //