ID   A0A7S7PNC7_PVMA         Unreviewed;      3059 AA.
AC   A0A7S7PNC7;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   19-JAN-2022, entry version 3.
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: Both 6K peptides are indispensable for virus replication.
CC       {ECO:0000256|ARBA:ARBA00002011}.
CC   -!- FUNCTION: an RNA-dependent RNA polymerase that plays an essential role
CC       in the virus replication. {ECO:0000256|ARBA:ARBA00003643}.
CC   -!- FUNCTION: has RNA-binding and proteolytic activities.
CC       {ECO:0000256|ARBA:ARBA00002112}.
CC   -!- FUNCTION: has helicase activity. It may be involved in replication.
CC       {ECO:0000256|ARBA:ARBA00025234}.
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:ARBA00002176}.
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:ARBA00025057}.
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: Virion {ECO:0000256|ARBA:ARBA00004328}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00006064, ECO:0000256|RuleBase:RU003351}.
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DR   EMBL; MT521082; QOZ05775.1; -; 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   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   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          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   COILED          556..576
FT                   /evidence="ECO:0000256|SAM:Coils"
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
//