RDRP_ASPVP
ID RDRP_ASPVP Reviewed; 2183 AA.
AC Q64962;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RNA replication polyprotein {ECO:0000250|UniProtKB:Q65652};
DE AltName: Full=ORF1 protein {ECO:0000250|UniProtKB:Q65652};
DE Includes:
DE RecName: Full=Viral methyltransferase {ECO:0000255};
DE EC=2.1.1.- {ECO:0000305};
DE Includes:
DE RecName: Full=Putative Fe(2+) 2-oxoglutarate dioxygenase {ECO:0000255};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE Includes:
DE RecName: Full=Protease {ECO:0000250|UniProtKB:Q65652};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q65652};
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE Contains:
DE RecName: Full=Helicase {ECO:0000250|UniProtKB:Q65652};
DE EC=3.6.4.13 {ECO:0000305};
GN ORFNames=ORF1 {ECO:0000250|UniProtKB:Q65652};
OS Apple stem pitting virus (isolate PA66) (ASPV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Betaflexiviridae; Quinvirinae; Foveavirus.
OX NCBI_TaxID=651356;
OH NCBI_TaxID=23159; Crataegus (hawthorn).
OH NCBI_TaxID=106566; Malus sieboldii.
OH NCBI_TaxID=3752; Malus sylvestris.
OH NCBI_TaxID=23211; Pyrus communis (Pear) (Pyrus domestica).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8021584; DOI=10.1099/0022-1317-75-7-1535;
RA Jelkmann W.;
RT "Nucleotide sequences of apple stem pitting virus and of the coat protein
RT gene of a similar virus from pear associated with vein yellows disease and
RT their relationship with potex- and carlaviruses.";
RL J. Gen. Virol. 75:1535-1542(1994).
CC -!- FUNCTION: [RNA replication polyprotein]: RNA-directed RNA polymerase
CC involved in viral RNA replication. {ECO:0000250|UniProtKB:Q65652}.
CC -!- FUNCTION: Protease: Thiol protease that cleaves the polyprotein.
CC {ECO:0000250|UniProtKB:Q65652}.
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 Evidence={ECO:0000305};
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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. {ECO:0000250|UniProtKB:Q65652}.
CC -!- SIMILARITY: Belongs to the potexviruses/carlaviruses RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; D21829; BAA04853.1; -; Genomic_RNA.
DR RefSeq; NP_604464.1; NC_003462.2.
DR MEROPS; C23.001; -.
DR PRIDE; Q64962; -.
DR GeneID; 935270; -.
DR KEGG; vg:935270; -.
DR Proteomes; UP000000678; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006508; P:proteolysis; 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; 2.60.120.590; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008041; Peptidase_C23.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF05379; Peptidase_C23; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51492; PEPTIDASE_C23; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Dioxygenase; Helicase; Hydrolase; Iron; Metal-binding;
KW Methyltransferase; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Oxidoreductase; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..2183
FT /note="RNA replication polyprotein"
FT /id="PRO_0000401087"
FT CHAIN 1686..2177
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:Q65652"
FT /id="PRO_0000431909"
FT DOMAIN 63..256
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 762..853
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 1091..1199
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT DOMAIN 1198..1288
FT /note="Peptidase C23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00825"
FT DOMAIN 1349..1520
FT /note="(+)RNA virus helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1521..1667
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1961..2068
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 883..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1202
FT /evidence="ECO:0000250|UniProtKB:Q65652"
FT ACT_SITE 1283
FT /evidence="ECO:0000250|UniProtKB:Q65652"
FT BINDING 780
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 782
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 835
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 844
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 1374..1381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT SITE 1685..1686
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:Q65652"
SQ SEQUENCE 2183 AA; 247262 MW; 2156D7A75A548CC5 CRC64;
MALLSRTAAE EVIASFTSEE QSRISTQAVL ALTNVEKDKH DLFNYALPEL AKMRLFNSGI
YLSPHSYRPH SHPVCKTLEN NILFNILPSY LDNSFYLVSI KKNKVDFLKR RHPDLQMVET
INRYISSIDK TRYGGFFHVS PSKISAKFKC DRRTGFEDDA SLIDLIPGCM EGARKRFFFH
DELHYWTKEA LITFLDHVKP EVMLASIVFP PEILAGAKES LNPWCYTFRI VGKDLVFFPD
GEQSEAYIQP VAGSYLLRTG KITTPSGDIF QLDLLKSSFS HHLISITKGE AIGQKMRFFN
GFEAVAMKGL NPLRRKVESC LPISKNTILK IYRYLRTLKK PDLQSAMAKL SQVCKDPNGY
EIKFFEEFSK LCLKCDTLNT NMIPDMKRIV QGFFLKLFPN PISRNFKVVQ QLHLDNFIET
LEEFNFSINT ESLSLNWKDD LEFVNLTFGD TDFNVEDSFA EAWGTKKDVV NITTVHHSPY
LVSKFESYDH QFHSILSVKS ISALTRIAKI VLSLYDPCVV EAFSESRVTN LAVNVIIAAN
LRACFAVTDL WRIFEGILLK ECKRAQGKMR KRFHFELGIR WFLFVDVSNQ WFLPPCRDGL
IARSVSFDQF IKGCQRDNSL HNGRMSLRQV LKGPKLQALF DVSELSIIHN VEMENAPEAG
STLDAGIKPT SSPLEVVPIE NARCNLAPCK CDLNCFIQPA DVNSLHGNLV FLDFIGGSKG
RGASFYSRDL KGYSYTGFSH VSRGWPAFLD KFLSDNKIPL NFYNQCLVQE YSTGHGLSMH
KDDESIYDIN HQVLTVNYSG DAIFCIECLG SGFEIPLSGP QMLLMPFGFQ KEHRHGIKSP
SKGRISLTFR LTKEGDSQVP IQEVVTICDH GDSDDRAALK ALERRSHQSG GRPAVELEGH
EREKVNSDSS DSAPVQEFLI QIDSSLLEYA LKSLSGLSKN VVNCDMCLCN SPWLKNEELR
FSEALRDLAF AQGLIQLIDF LCLKVLRCAE VNRIISELPT HVFPLRGTMH IVDLDDESIR
GDVKEGSFSG FRRWKVMSCS TDLIMLAFLK PKMTLGGELR SHEDECELSD LTEKLHGCSV
ILSRKFEPDL FHSFDVEADG NCFWHSVGPL IGVDGEYLKR ILHDQAKKDG VKCPRLSKQL
EGNTWAEREA VAYFCSHYGI RLNVLYTREE CTWIFKPHEV LKAATLICQD NHFKPCMPVN
GCVIRAISSA LNRREVDVLA VLGKPAHEDL FEEVAEGRGF SIFDLTRLFE IFSICGSVDT
GGELIMVNEN GRIPAEFSLE KEHLAHIPTL SRRKFSPIVS DLNRVSNSAM RFLAINGAEV
DYRPSIDRAS TLLDSFEIGA TGVLCQGIKE AQKDLASKLI PELVHERKLI MILGTFGCGK
SSLFKKFIEK SPGKAITFVS PRRSLAESIN HDLGLARVGG KKTGKSKDLK NVRVKTFELF
ILHLDSIKEG HTVVIDEIQL FPPGYIDLII LGLKPNVNII IAGDPCQSDY DCSSDRHIFA
GSESDIMRIL SGRSYKFNIL SQRFRNPVFY GRLPCNLNKT RLTLDEEEYT LWDSIQEFSM
MGRKDCPVVL VSSFEEKKIV AAHLGLKMKC ITYGESTGLN FQKGAILVTY ESALTSDRRW
WTALSRFSHD IHFINGMGVT WDNAITHFVG KPLHKFFTKR ACNDDIIDLL PGRPELIEGF
QSQVGADEGV REAKLVGDPW LKTKIFLGQN PDFEIEIADE VEAAEDWFKT HIPIMSLEAV
RAQWVHKLIS REDREFRIGD ITTEQFTDDH SKNRGQELTN AAERYEAIYP RHKGTDTATF
LMAVKKRLSF SSPAAEHAKL RRAKPFGKFL LDTFLKRVPL NSSHDEKMMQ EAVHAFEEKK
LSKSMATIEN HSGRSCEDWP VDKALIFMKS QLCTKFDNRF RSAKAGQTLA CFQHSVLCRF
APYMRYIESK VTEVLPKNLY IHSGKNIDDL AAWVTTSKFN GVCTESDYEA FDASQDHFIL
AFELEVMKFL GLPSDLIADY TFIKTHLGSK LGSFAIMRFT GEASTFLFNT MANMLFTFLR
YDLNGREAIC FAGDDMCANS RLKVTNRFSN FLDKIKLKAK VQFTATPTFC GWGLCEHGVF
KKPDLVLERL QIARETRNLE NCIDNYAIEV SCAYKMGENL NLYLTPQEVD AHYNCVRFIV
QHNHLLKSNI RDLFKGESLP ASS
