ID A0A097BVS2_9POTV Unreviewed; 3222 AA. AC A0A097BVS2; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 25-MAY-2022, entry version 42. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS Bean common mosaic virus. OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes; OC Patatavirales; 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 soybean RT 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., Hang Y.-Y., RA Yang J.-Y., Wang Q., Wang B., Chen J.-Q.; RL Submitted (MAY-2014) 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; KJ807805; AIS72951.1; -; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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 303..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 2660..2784 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 2933..2998 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 193..220 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 2950..2965 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2966..2980 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 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 //