ID   POLG_ASGVP              Reviewed;        2105 AA.
AC   P36309;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 111.
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 P-209) (ASGV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Betaflexiviridae; Trivirinae; Capillovirus.
OX   NCBI_TaxID=36402;
OH   NCBI_TaxID=3752; Malus sylvestris.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1413530; DOI=10.1016/0042-6822(92)90170-t;
RA   Yoshikawa N., Sasaki E., Kato M., Takahashi T.;
RT   "The nucleotide sequence of apple stem grooving capillovirus genome.";
RL   Virology 191:98-105(1992).
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.
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.
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.
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DR   EMBL; D14995; BAA03639.1; -; Genomic_RNA.
DR   PIR; A44059; A44059.
DR   RefSeq; NP_044335.1; NC_001749.2.
DR   PRIDE; P36309; -.
DR   GeneID; 1494893; -.
DR   KEGG; vg:1494893; -.
DR   Proteomes; UP000000396; Genome.
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   Gene3D; 3.40.50.300; -; 1.
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; IPR027417; P-loop_NTPase.
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   4: Predicted;
KW   ATP-binding; Capsid protein; Helicase; Hydrolase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1868
FT                   /note="Putative RNA-directed RNA polymerase/helicase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040221"
FT   CHAIN           1869..2105
FT                   /note="Coat protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040222"
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          529..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1585..1868
FT                   /note="V-region"
FT   REGION          1960..1979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1963..1979
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;  241242 MW;  331291A5FA137131 CRC64;
     MAFTYRNPLE IAINKLPSKQ SDQLLSLTTD EIEKTLEVTN RFFSFSITPE DQELLTKHGL
     TLAPIGFKSH SHPISKMIEN HLLYICVPSL LSSFKSVAFF SLRENKVDSF LKMHSVFSHG
     KIKSLGMYNA IIDGKDKYRY GDVEFSSFRD RVIGLRDQCL TRNKFPKVLF LHDELHFLSP
     FDMAFLFETI PEIDRVVATT VFPIELLFGD KVSKEPRVYT YKVHGSSFSF YPDGVASECY
     EQNLANSKWP FTCSGIQWAN RKIRVTKLQS LFAHHVFSFD RGRACNEFNH FDKPSCLLAE
     EMRLLTKRFD KAVINRSTVS SLSTYMACLK TANAASAVAK LRQLEKRDLY PDELNFVYSF
     GEHFKNFGMR DDFDVSVLQW VKDKFCQVMP HFIAASFFEP TEFHLNMRKL LNDLATKGIE
     VPLSVIILDK VNFIETRFHA RMFDIAQAIG VNLDLLGKRF DYEAESEEYF SENGYIFMPS
     KSNPERNWIL NSGSLKIDYS RLVRARRFRL RRDFLDPISK GKSPRKQLFL ESTGNIKSNP
     NAEKNSESGE IKIEGSAEND QPHEVSHTSM ETEDGQGFEG SIPVDLINCF EPEEIKLPKR
     RRKNDCVFKA ISAHLGIDSQ DLLNFLVNED ISDELLDCIE EDKGLSHEMI EEVLITKGLS
     MVYTSDFKEM AVLNRKYGVN GKMYCTIKGN HCELSSKECF IRLLKEGGEA QMSNENLNAD
     SLFDLGRFVH NRDRAVKLAK SMARGTTGLL NEFDLEFCKN MVTLSELFPE NFSSVVGLRL
     GFAGSGKTHK VLQWINYTPS VKRMFISPRR MLADEVEPQL KGTACQVHTW ETALKKIDGT
     FMEVFVDEIG LYPPGYLTLL QMCAFRKIVK GQSENFLKGK LLELSKTCLN IRCFGDPLQL
     RYYSAEDTNL LDKTHDIDLM IKTIKHKYLF QGYRFGQWFQ ELVNMPTRVD ESKFSRKFFA
     DISSVKTEDY GLILVAKRED KGVFAGRVPV ATVSESQGMT ISKRVLICLD QNLFAGGANA
     AIVAITRSKV GFDFILKGNS LKEVQRMAQK TIWQFIIEGK SIPMERIVNM NPGASFYESP
     LDVGNSSIQD KASNDLFIMP FINLAEEEVD PEEVVGDVIQ PVEWFKCHVP VFDTDPTLAE
     IFDKVAAKEK REFQSVLGLS NQFLDMEKNG CKIDILPFAR QNVFPHHQAS DDVTFWAGVQ
     KRIRKSNWRR EKSKFEEFES QGKELLQEFI SMLPFEFKVN IKEIEDGEKS FLEKRKLKSE
     KMWANHSERS DIDWKLDHAF LFMKSQYCTK EGKMFTEAKA GQTLACFQHI VLFRFGPMLR
     AIESAFLRSC GDSYYIHSGK NFFCLDSFVT KNASVFDGFS IESDYTAFDS SQDHVILAFE
     MALLQYLGVS KEFQLDYLRL KLTLGCRLGS LAIMRFTGEF CTFLFNTFAN MLFTQLKYKI
     DPRRHRILFA GDDMCSLSSL KRRRGERATR LMKSFSLTAV EEVRKFPMFC GWYLSPYGII
     KSPKLLWARI KMMSERQLLK ECVDNYLFEA IFAYRLGERL YTILKEEDFE YHYLVIRFFV
     RNSKLLTGLS KSLIFEIGEG IGSKWLSSTS TASSRRSNLQ TSKLMLSRPQ SFTRMQPFSN
     QTCLIASKGL NQTSRFPLDL VTASSCLISN CLMTPKLIQS GRKATSTNTY TMESSWLGSK
     QCCQTLEAWK GESLYMMEPA WIRKEATFAR IFSSLSLTVA TLVSGQSTVC LPQTQIWPKG
     LDFVWTLIVH NMNRTLSCLL LTLELHTDAS TLQGFWKPKL AIQDGLHRQS AAVKHLNSMR
     KSRWPSWIAD PRCFWKKVHQ TCTLKRDCSE VTRLEGHAQF PLKGGQTQGC KKREDLGPSR
     LELKDLEKMS LEDVLQQARR HRVGVYLWKT HIDPAKELLT VPPPEGFKEG ESFEGKELYL
     LLCNHYCKYL FGNIAVFGSS DKTQFPAVGF DTPPVHYNLT TTPKEGETDE GRKARAGSSG
     EKTKIWRIDL SNVVPELKTF AATSRQNSLN ECTFRKLCEP FADLAREFLH ERWSKGLATN
     IYKKWPKAFE KSPWVAFDFA TGLKMNRLTP DEKQVIDRMT KRLFRTEGQK GVFEAGSESN
     LELEG