ID   POLG_ASGVK              Reviewed;        2105 AA.
AC   Q6PLS1; Q6PLS0;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Genome polyprotein;
DE   AltName: Full=241 kDa polyprotein;
DE   AltName: Full=ORF1 polyprotein;
DE   Contains:
DE     RecName: Full=Putative RNA-directed RNA polymerase/helicase;
DE              EC=2.7.7.48;
DE              EC=3.6.4.13;
DE   Contains:
DE     RecName: Full=Coat protein;
OS   Apple stem grooving virus (strain Korea) (ASGV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Betaflexiviridae; Trivirinae; Capillovirus.
OX   NCBI_TaxID=273525;
OH   NCBI_TaxID=3752; Malus sylvestris.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15528995;
RA   Shim H., Min Y., Hong S., Kwon M., Kim D., Kim H., Choi Y., Lee S.,
RA   Yang J.;
RT   "Nucleotide sequences of a Korean isolate of apple stem grooving virus
RT   associated with black necrotic leaf spot disease on pear (Pyrus
RT   pyrifolia).";
RL   Mol. Cells 18:192-199(2004).
CC   -!- FUNCTION: [Putative RNA-directed RNA polymerase/helicase]: Replicates
CC       genomic RNA, and might as well transcribe a subgenomic RNA coding for
CC       coat protein. {ECO:0000250}.
CC   -!- FUNCTION: Coat protein: encapsidates the viral genome. Forms particles
CC       of very flexuous filaments, 619 nm long and 12 nm in width, with
CC       obvious cross-banding, helical symmetry and a pitch of c. 3.8 nm.
CC       Synthesis remains unclear: either by cleavage of the ORF1 polyprotein,
CC       or by translation of a subgenomic RNA (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: [Coat protein]: Virion {ECO:0000305}.
CC   -!- DOMAIN: The V-region of the ORF1-encoded protein between the polymerase
CC       and the CP, that encodes ORF2 in another frame does not have any
CC       functional motifs found in other known plant virus genomes. This region
CC       shows high variability among isolates and sequence variants.
CC   -!- PTM: The N-terminus of the coat protein is blocked. {ECO:0000250}.
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DR   EMBL; AY596172; AAT01925.1; -; Genomic_RNA.
DR   EMBL; AY596172; AAT01926.1; -; Genomic_RNA.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR008879; Coat_protein_tricho/vitivirus.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR008745; DUF1717.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF05414; DUF1717; 1.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF05892; Tricho_coat; 1.
DR   Pfam; PF01443; Viral_helicase1; 2.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Helicase; Hydrolase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1868
FT                   /note="Putative RNA-directed RNA polymerase/helicase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000249220"
FT   CHAIN           1869..2105
FT                   /note="Coat protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000249221"
FT   DOMAIN          63..250
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          753..929
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          930..1067
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1358..1466
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          552..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1585..1868
FT                   /note="V-region"
FT                   /evidence="ECO:0000250"
FT   REGION          1832..1862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1960..1980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1963..1980
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         781..788
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   2105 AA;  241989 MW;  7D2675EB6E5AD591 CRC64;
     MAFTYRNPLE IAINKLPSKQ TDQLLSLTTD EIEKTLEVTN RFFSFSITPE DQELLTKHGL
     TLAPIGFKAH SHPVSKMIEN HLLYICVPSL LSSFKSVAFF SLRESKANSF LKMHSAFSHG
     KIKSMGMYNA IIDGKDKYRY GDVSFTSFRE RVIGLRDQCL TRNKFPKIIF MHDELHFLSP
     FDIAYLFETI PEIDRVIATT VFPIELLFGD KVSKEPRVYT YKVHGSSFSF YPDGVASECY
     EQNLANSKWP FTCNGIQWAN RRVRVTKLQS LFAHHVFSFD RGRACNDFNH FNKPGCLLSE
     EMRLLTKRFD KAVINRSTVS SLSTYMACLK TANAASAVAK LRQLEKRDLY PDELNFVYSF
     GEHFKNFGMR DDFDVSVLQW VKDKFCQVMP HFISASFFEP TEFHLNMRKL LNDLATKGIE
     VPLPTIVLDK VNFIETRFHA RMFEVASAIG VNLDLLGKRF DFENESEEYF SENGYLFMPS
     KHNTDRNWIL NSCPVRVDYS KLVRARRFRL KRDFVEEILK KRPPRTQLFL EFNKDFGGPV
     SFEKEEVEKK GEAATRVEDK APHEPSCSNL STEDGQGFEG SLPLDLISCF EQEEIRLPKR
     KRKNDCVFKA IAAHLGIETQ DLLNFLVNED ISDELLDCIE EDKGLSHEMI EEVLVTKGLS
     MVYTSDFKEM AVLNRKYGVN GKMYCTIKGN HCELSSKECF IRLLKEGGNA QMSNENLNAD
     SMFDLGKFVH NKERAVKLAK SMARGTTGLL NSFDPNFCKE VVGLSELFPD NFSSVVGLRL
     GFAGSGKTHK VLQWINYTPN VKRMFISPRR MLAEEVEGRL KGTACQVHTW ETALRKIDGT
     FMEVFVDEIG LYPPGYLTLL QMCAFRRTVK GQSERFLKSK LAELSKTCLS LRCFGDPLQM
     RYYSAEDTNL LDKTHELDLM IKTIKHKYLL QGYRFGEWFQ SLINMPTRID SSEISIKFFA
     DMSSVKSEDY GLVLVARRED IGVFAGRIPV ATVSESQGMT IDKRVLICLD QNLFAGGANA
     AIVAITRSRV GFDFVLKGNT LKEIQRMSQK TIWQFILEKK RIPMERIVNM NPGASFYESP
     LDVGNSSIQD KASHDVFIMP FINLAEEEVD PEEICGDVIK PVEWFKCHVP VFDTDPMLAE
     IFDKVAAKEK REFQSILGMS NQFLDMEKNG CKIDILPFAR QNVFPHHQAS DDVTFWAGVQ
     KRIRKSNWRR EKTKFEEFEI QGRELLSEFL SMLPCEFKVN IKDIEEGEKS FLEKRKLKSE
     KMWANHSERS DIDWKLDHVF LFMKSQYCTK EGKMFTEAKA GQTLACFQHI VLFRFGPMLR
     AIESAFLRSC GDSYYIHSGK NFFCLDSFVT KNAEVFDGFS IESDYTAFDS SQDHVILAFE
     MALLQYLGVS KEFQLDYLRL KLTLGCRLGS LAIMRFTGEF CTFLFNTFAN MLFTQLKYKI
     DPRKHRILFA GDDMCSLSSL KRRRGERATR LMKSFSLTAV EEVRKFPMFC GWYLSPYGII
     KSPKLLWARI KMMSERQLLK ECVDNYLFEA IFAYRLGERL YTILKEEDFE YHYLVIRFFV
     KNSKLLTGLS KSLIFEIGEG IGSEWQLSMS TTSSKRLNQQ ISRLMPSRHL NFIKMQPFSS
     QMFSIASNDL NQMSKCLKVR VMDSCCPTSS CLMTQKLTPL ERRATSTNTY IMELFLLASK
     QCCPTSGEWK GGSLYMTVPV WTQKEVIYVP TYSDLSLTAV TLDSDQNIAY LQLMLIWQKG
     SGSEWILTVH NTNRTQSCLL LTLELHTGVS TQLDSWKPKQ VIQDGLHRQS AAVKHLNTMK
     RSRWRSWITN HRCFWRKVHR MCILKKECSE GTRSGGRALS LPKGGQTQGQ KKREDLGPSQ
     RGLKDLGKMS LEDVLQLARR HRVGVYLWKT QIDPGKEILT VPPPESFKEG ESFEGRELYL
     LLCNHYCKYL FGNIAVFGSS DKTQFPAVGF DTPPVHYNLT TTPKEGETEE QKKAREGSSG
     EKSKIWRIDL SNVVPELKTF AATSRQNSLN ECTFRKLCEP FADLAREFLH ERWSKGLATN
     IYKKWPKAFE KSPWVAFDFA TGLKMNKLTP DEKQVIDRMT KRLFRTEGQK GVFEAGSESN
     LELEG