RDRP_PVMR
ID RDRP_PVMR Reviewed; 1968 AA.
AC P17965; Q89548;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 113.
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 Potato virus M (strain Russian) (PVM).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Betaflexiviridae; Quinvirinae; Carlavirus.
OX NCBI_TaxID=12168;
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1990070; DOI=10.1099/0022-1317-72-1-9;
RA Zavriev S.K., Kanyuka K.V., Levay K.E.;
RT "The genome organization of potato virus M RNA.";
RL J. Gen. Virol. 72:9-14(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1944258;
RA Zavriev S.K., Kaniuka K.V., Levai K.E.;
RT "Complete nucleotide sequence of genomic RNA of the potato M-virus.";
RL Mol. Biol. (Mosk.) 25:761-769(1991).
CC -!- FUNCTION: [RNA replication polyprotein]: RNA-directed RNA polymerase
CC involved in viral RNA replication. {ECO:0000250|UniProtKB:Q65652,
CC ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- FUNCTION: Protease: Thiol protease that cleaves the polyprotein.
CC {ECO:0000250|UniProtKB:Q65652}.
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 -!- 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; D14449; BAA03339.1; -; Genomic_RNA.
DR PIR; PN0093; PN0093.
DR RefSeq; NP_056767.1; NC_001361.2.
DR PRIDE; P17965; -.
DR GeneID; 1493995; -.
DR KEGG; vg:1493995; -.
DR Proteomes; UP000000677; 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: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 InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR003323; OTU_dom.
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; 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; 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; Methyltransferase;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Oxidoreductase; Protease; Reference proteome; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Viral RNA replication.
FT CHAIN 1..1968
FT /note="RNA replication polyprotein"
FT /id="PRO_0000222563"
FT CHAIN 1473..1968
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:Q65652"
FT /id="PRO_0000431908"
FT DOMAIN 63..254
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 883..991
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT DOMAIN 990..1080
FT /note="Peptidase C23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00825"
FT DOMAIN 1134..1316
FT /note="(+)RNA virus helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1317..1454
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1749..1856
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 994
FT /evidence="ECO:0000250|UniProtKB:Q65652"
FT ACT_SITE 1075
FT /evidence="ECO:0000250|UniProtKB:Q65652"
FT BINDING 1166..1173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT SITE 1472..1473
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:Q65652"
SQ SEQUENCE 1968 AA; 223386 MW; 6F15A79E1AD96AAC CRC64;
MAVTYRTPME DIVNCFEPAT QAVIANSAAT LYKNFEEQHC QYFNYYLSPL AKRKLSMAGI
YLSPYSAVVH SHPVCKTLEN YILYSVLPSY INSSFYFVGI KERKLQLLKS KCKNLDSVQV
VNRYVTSADR MRYTNDFVPY GSYEHECLVH KGVGLDNEAL RGLVGPLRRH KAKNLFFHDE
LHYWSSKVLI DFLDVMRPDK LLGTVVYPPE LLFKPTRSLN EWCYTYDIVG DTLMFFPDGV
QSEGYQQPLK GGYLLGARSL KLPDGTVYMV DVLCSKFPHH LISITKGEAA APTHRAFGPF
EAVASEALKA TLSPDYPCAF PVSYEVVNKI YRYLRTLKKP DEQSAIAKLS QIIAEPSGRE
IDFVECFARL VIHNSSMCAT IMPEQLKEFM GNWLGKMPSV LARRFSSVRA VCVNKFIRGL
KPYSFTLRLN EITWWNIWEN SYAWFFDTDA EVDVPEKLDS LFMGEGAGLV AHITSRPYVG
TVPLADREWN ALLCMDSQKL LHAMRRMFMR GAWGAHMCVI SREFLLKYVE ARLKSSCLIA
KARRRGQHKE KLEAWEVLGL KSSDALFRAM TYLCNARLEP MFSESGLRFF LTRGRNNLYG
LTNYTEGKRA VTGVQNLWSN VVHEVSTKRH KGMIRLEKAR VTEQPRSEFA SCVLEPEVWR
DVEAALDIEL GEVACACNAR FVQGVVLSNQ AGLNVREQVA GASVGLYTKD RSNLKWGNSE
LLSNGWGRSL SVWMEINSVS QKFDVAVRLS YSKETQMNVL LPSLDGIERG AGATVVNLRK
CGAFIVRCAR GWRLALAWMD HICLEVMANV AYGHECYMRS WGTMDVVVFL KRATVSEQVT
FESAQEVGPI EGKSDSGAPG VGVNLDLGGV VGSEYPANGA ERYKRVSGPG DGCCCWHSFA
YLVGMHHMEL KRLCTSHVFE NAALNVELEQ CKASGAFVTH AAILATALRL RAEIRVHNAG
TGRVHRFAPK QKNMALDLWL ESEHYEPQVL RNGCVIESVA QALGTRNADI LAVVEERCCE
EVVESVQAGL GLNLHHVEIV LQCFDIVGHC NLGDKEITLN AGGKMPFCFD ISDEHMSFCG
RRKDPICKLV SGALHGKMFA ESALLDLENC GLKIDFEPNW NRAGMLADSM YQGATGVLGS
ALFNNKRNMR EKFVRNVSLS LHAIVGTFGS GKSTLFKNLL KYGAGKSLDF VSPRRALAED
FKRTVGMNER GGRAKAGQEN WRVTTLETFL ARVEFLTEGQ VVILDEMQLY PPGYFDLVVS
MLKVDVRLFL VGDPAQSDYD SEKDRLVLGA MEENMSVVLG AREYNYKVRS HRFLNCNFIG
RLPCEINKDD CTIDEPHIMR MHLENLLDVA EEYKSVVLVS SFDEKMVVCA HLPEAKVLTF
GESTGLTFMH GTIYISAVSE RTNERRWITA LRRFRFNLCF VNCSGMDYQQ LAGRYKGRVR
SKFLCKTAIP DDLNSMLPGQ ALFKSEYPRL IGKDEGVREE KLAGDPWLKT MINLYQAPEV
EIAEEPEVVM QEEWFRTHLP RDELESVRAQ WVHKILAKEY REVRMGDMVS EQFTHDHTKQ
LGAKQLTNAA ERFETIYPRH RASDTVTFLM AVKKRLSFSN PGKEKGNLFH AASYGKALLS
EFLKRVPLKP NHNVRFMEEA LWNFEEKKLS KSAATIENHS GRSCRDWPTD VAQIFSKSQL
CTKFDNRFRV AKAAQSIVCF QHAVLCRFAP YMRYIEMKVH EVLPKNYYIH SGKGLEELDA
WVKKGKFDRI CTESDYEAFD ASQDEFIMAF ELELMKYLRL PSDLIEDYKF IKTSLGSKLG
NFAIMRFSGE ASTFLFNTLA NMLFTFMRYN IRGDEFICFA GDDMCASRRL QPTKKFAHFL
DKLKLKAKVQ FVQFVNKPTF CGWHLCPDGI YKKPQLVLER MCIAKEMNNL SNCIDNYAIE
VAYAYKLGEK AVNRMDEEEV AAFYNCVRII VRNKHLIRSD VKQVFEVL
