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}.
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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: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
//