ID A0A7S7PNC7_PVMA Unreviewed; 3059 AA. AC A0A7S7PNC7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 24-JAN-2024, entry version 12. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; GN Name=PVAgp1 {ECO:0000313|EMBL:QOZ05775.1}; OS Potato virus A (PVA). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes; OC Patatavirales; Potyviridae; Potyvirus. OX NCBI_TaxID=12215 {ECO:0000313|EMBL:QOZ05775.1}; OH NCBI_TaxID=45843; Solanum betaceum (Tamarillo) (Cyphomandra betacea). OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade). OH NCBI_TaxID=4113; Solanum tuberosum (Potato). RN [1] {ECO:0000313|EMBL:QOZ05775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5998981 {ECO:0000313|EMBL:QOZ05775.1}; RX PubMed=33174824; RA Fuentes S., Gibbs A., Adams I., Wilson C.R., Botermans M., Fox A., RA Kreuze J., Boonham N., Kehoe M., Jones R.; RT "Potato virus A isolates from three continents: their biological RT properties, phylogenetics and prehistory."; RL Phytopathology 0:0-0(2020). 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: Indispensable for virus replication. CC {ECO:0000256|ARBA:ARBA00034080}. 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: Mediates the cap-independent, EIF4E-dependent translation of CC viral genomic RNAs (By similarity). Binds to the cap-binding site of CC host EIF4E and thus interferes with the host EIF4E-dependent mRNA CC export and translation (By similarity). VPg-RNA directly binds EIF4E CC and is a template for transcription (By similarity). Also forms CC trimeric complexes with EIF4E-EIF4G, which are templates for CC translation. {ECO:0000256|ARBA:ARBA00037225}. 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: Cytoplasmic vesicle CC {ECO:0000256|ARBA:ARBA00004541}. Host cytoplasmic vesicle CC {ECO:0000256|ARBA:ARBA00034108}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. Vesicle CC {ECO:0000256|ARBA:ARBA00004373}. 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; MT521082; QOZ05775.1; -; Genomic_RNA. DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW. DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell. 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-dependent 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:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 3.90.70.150; Helper component proteinase; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. 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 PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1. DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1. 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; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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:ARBA00022840}; 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 cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488}; 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 RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; 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 154..298 FT /note="Peptidase S30" FT /evidence="ECO:0000259|PROSITE:PS51871" FT DOMAIN 633..755 FT /note="Peptidase C6" FT /evidence="ECO:0000259|PROSITE:PS51744" FT DOMAIN 1226..1378 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1397..1556 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2032..2250 FT /note="Peptidase C4" FT /evidence="ECO:0000259|PROSITE:PS51436" FT DOMAIN 2516..2640 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 2797..2816 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2801..2816 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 641 FT /note="For helper component proteinase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080" FT ACT_SITE 714 FT /note="For helper component proteinase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080" SQ SEQUENCE 3059 AA; 346058 MW; 32CC4295E742C51C CRC64; MATQAIMVGE FKILEVNCKP HAPVAAIHVP TQAPKTNDIQ WADLEFTLAK SLQRQAHGVV KVDKHGTARI KRASKHHMSC LEQQMADEVA EREAFMAAPT QLVTSIIFAG TTPPSMMETE TIVKKIHTVG KHAKVMRKRS YITPXTDKSL RNHGVXPYSV QQLCRTLGNL SKRTGISLEV VGKTSKATKL RFTKTSFGYM ARVQLKHHDG RMHRRDLVVD TSTTTIMQTL FLKTARTNAN LDVLTHGSSG LVFWNYLVTG QRMRTRDNFI IVRGRCNGIL VDARAKLSES TMLSTHHYST GDVFWRGFNR TFLENKPINL DHVCSSDFSV EECGSIAALI CQSLLPCGKI TCRACAAKNL NMDEDTFKEF QTQRAREISA VIISKYPNFA CVSQFIDRYF SHQRVLNPNV NAYREILKIV GGFTQSPYTH IQELNEILVL GGRATPEQLS SASAHLLEIT RFVRNRTDNI KKGSLALFRN KISAKAHVNT ALMCDNQLDR NGNLIWGERG YHAKRFFSNY FDIITPGGGY KQYIERRVPN GIRKLAIGNL IVTTNLEALR EQLEGESIEK KAVTKACVSM SDNNYKYPCC CVTLDDGTPL YSTFIMPTKN HLVIGNSGDP KFLDLPTDIS TQMYIAKSGY CYINIFLAML VNVDESDAKD FTKKVRDIIV PDLGEWPTLI DVATSCSLLS AFYPATSAAE LPRILVDHDL KTMHVIDSYG SLNTGYHVLK ANTVRQLIQF ASNSLDSEMK HYRVGGTPNS QINGYATIKM LAKAVYRPKL MKEIIHEQPY MLVMSLMSPG ILIALANSGA LEMGIHHWIR EGDSLVKMAH MLRTVAQNVS VARATWVQQE IISDSAQQML ETILNGTIPN VSYFQAIQYL TMLAASKEVD AEVRVTGYYT FKLQTSELLE KTYLSLLEDS WQELSYFGRF QAIRHSRRYC TAGTIVVKPE RHVDLGGIYA TSYQFALAKQ MEYSKKAVCQ AVNGLQARFN NITSQIYCKI LNWPKRLFPD LVKFINTMLA ITVALQLYIA FATILRHHQQ CKQDSLELEY CKKERQLITL YDFFIAKQPY ATEEEFMAHV DEQNPDLSNF AREYCAEVVL FQAKASEQVN FERIIAFISL VLMMFDCERS DCVYRSLTKL KSLMSTVENT VQFQSLDDIG PTLEEKNMTI DFDLDTDTIV GKSIIGHTFK EWWDVQLNTN RIVPHYRTEG HFMEFTRANA PTIAHQISHD LHTDIMLRGA VGSGKSTGLP YHLSKKGTVL LLEPTRPLAE NVTKQLKSDP FHVSPTLRMR GMAVFGSTPI HVMTTGFALH YLANNLKMLS TYDFIIIDEF HVHDSNAIAL RNLLHEHNYQ GKLIKVSATP PGREVEFSTQ YPVEIRVEDQ VSFQDFVKAQ GNGSNLDLTS KCDNLLVYVA SYNEVDQLSK LLLERHFLVT KVDGRSMKLG QVEIITKGSA NKKHFIVATN IIENGVTLDI DAVIDFGMKV VPFLDSDNRM ISYNKVSISY GERIQRLGRV GRNKAGVALR IGHTEKGISD VPVVIATQAA FLCFVYGLPI STQSVTTQVL SNVTLKQART MVQFELPIFY MAHLVRYDGT MHPAIHNELK KYKLRDSEIQ LSKLAIPSKC VPIWMTGKAY RLLTHNSQIP DDVRVPFLTK EIPDKLHENV WAIVEKFKCD AGIGRMTSAQ ASKVAYTLET DIHSIQRTIL IIDQLLEREM QKQSHFEMVT NQSCSSGMLS LQTMMNAIQS RYAKNHTAGN IEILQRAKAQ LLEFSNLSGD ISTESALREF GYLEAVQFQS GTQMSNFLGL EGHWKKSLIT KDLLIVGGVC VGAAWMIGEY FFKKSKEVVA FQGYNKRQRQ KLKFARARDE KMGHYVEAPD STLEHYFGSA YTKKGKTKGK THGMGKKNHR FVNMYGFDPS DYTFIRYVDP LTGYTLDESP YTDIRLIQSQ FSDIREQQLL NDELERNMVY HKPGVQGYLV KDKTSQILKI DLTPHIPLKV CDATNNIAGH PDREGELRQT GKGQLLDYAE LPQKKELVEF ESTSMFRGVR DYNPISSVIC QLENESEGRT TQLFGLGFGP FIITNQHLFV RNNGSLTVRS QMGVFKVNST VTLQMRPVEG RDVLIIKMPK DFPPFPQRLK FRQPTHSEKV CLILTNFQQK SSSSMVSETS HIIPKENTYF WKHWISTKEG HCGSPIVSTT DGAILGIHSL SNMTNTSNYF ACFPKGFTET YLATESVHEW VKGWKFNASN VCWGSFHLQD SKPTKEFKTV KLVTDLLGEA VYTQGCDSKW LFNAAHTNIQ AVAQLESNLV TKHTVKGKCK LFETYLNVDK AAHDFFSKYM GFYKPSKLNR EAYTQDLMKY SKVIQVGEVD CEVFESALTG LLHNLGRWGF TTACYTTDED SIYAALNMKA AVGALYRGKK RDYFDAMSPS EKEHLLFLSC KRLYFGQLGV WNGSLKAELR PKEKVDLNKT RTFTAAPIET LLGGKVCVDD FNNMFYSLHL KAPWSVGMTK FYGTWNQLMC KLPDDWVYCD ADGSQFDSSI SPYMINAVLR IRLHFMEDWD IGSQMLQNLY TEIVYTPIST PDGTVVKKFK GNNSGQPSTV VDNTLLVVLA MHYALLKSGV PLEEQDSVCV YCVNGDDLLI AIRPDMEHKL DGFQALFSEL GLNYEFNSRS KDKKDLWFMS HKAIQCGEIL IPKLEEERIV SILEWDRSHE PIHRLEAICA SMVESWGYPE LTHEIRRFYA WVLEQSPYNA LATTGLAPYI AESALKTLYT NVHPTSTELE KYSIQFDEQM DEEDDMVYFQ AGTLDAGETP AQKSEGKKKE GEGNSGKAVA VKDKDVDLGT AGTHSVPRLK SMTSKLTLPM LKGKSVVNLD HLLSYKPKQV DLSNARATHE QFQNWYDGVM ASYELEESSM EIILNGFMVW CIENGTSPDI NGVWTMMDNE EQVSYPLKPM LDHAKPSLRQ IMRHFSALAE AYIEMRSREK PYMPRYGLQR NLRDQSLARY AFDFYEITAT TPVRAKEAHL QMKAAALKNS NTNMFGLDGN VTTSEEDTER HTATDVNRNM HHLLGVKGV //