RDRP_P1AMV
ID RDRP_P1AMV Reviewed; 1385 AA.
AC Q07518;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=RNA replication protein;
DE AltName: Full=156 kDa protein;
DE AltName: Full=ORF1 protein;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE Includes:
DE RecName: Full=Helicase;
DE EC=3.6.4.13;
OS Plantago asiatica mosaic potexvirus (P1AMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=28354;
OH NCBI_TaxID=197796; Plantago asiatica.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8113746; DOI=10.1099/0022-1317-75-2-259;
RA Solovyev A.G., Novikov V.K., Merits A., Savenkov E.I., Zelenina D.A.,
RA Tyulkina L.G., Morozov S.Y.;
RT "Genome characterization and taxonomy of Plantago asiatica mosaic
RT potexvirus.";
RL J. Gen. Virol. 75:259-267(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8477237;
RA Solovyev A.G., Novikov V.K., Morozov S.I., Kagramanov V.N., Atabekov I.G.;
RT "Primary structure of the triple block RNA genes of the Plantago asiatica
RT mosaic virus.";
RL Dokl. Akad. Nauk 328:625-628(1993).
CC -!- FUNCTION: RNA replication. The central part of this protein possibly
CC functions as an ATP-binding helicase (Probable). {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 -!- 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 -!- SIMILARITY: Belongs to the potexvirus/carlavirus RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; Z21647; CAA79761.1; -; Genomic_RNA.
DR PIR; S34230; S34230.
DR RefSeq; NP_620836.1; NC_003849.1.
DR GeneID; 944434; -.
DR KEGG; vg:944434; -.
DR Proteomes; UP000009190; Genome.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
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; Helicase; Hydrolase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT CHAIN 1..1385
FT /note="RNA replication protein"
FT /id="PRO_0000222551"
FT DOMAIN 59..224
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 635..791
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 792..925
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1164..1271
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 504..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 665..672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1385 AA; 155617 MW; 66C177E44678A94F CRC64;
MSNVRNVFSQ LTDPSLKAVI QDEAYRVLKR ELAQTRHTNP FAQSPEAADA LEALGINSHP
YAITSHTHAA AKAIESDLYE VVSHYLPKEN PVSFLFMKPA KLRFFHRGPT HGDHFLNAHV
EPKDVPRYPQ ETIINRLADI PTQIAFMGDT LHFLSPSFLT ALFAHSPRLQ TLYATLVLPP
EPSTSRSLYP QIYTLTYSED GFMYIPGGHA GASYFHKYDQ LEWLTVGHLT APGCPTVTAQ
RLETKGANHL FIFQRGNYIT PERRTFATND QYVTVPHIFL PENYNCRTPI SKTTMMQMFF
YIKSGKEAQR EGHLGQVQQL ISTKELQHYQ PSEITLLVNY FEFTATLDSH TCFEDVPPKL
APKTTPAPPL GISRILQFFR GRPSFVKLIK ALDWQPITLE FPVRDVRTTV RGPPGFKNPF
TQPQPVNPED ADISSRFQDF SRATNSTPKP TVEAVLEASA ESPDHHTQLK VLCSALSEGQ
LEAIHALGHS RCGGPLLPEL TAKSTPVEQC PDLPPCPTKS QASPASSNPS GPDAQPTAQN
PETLPWVAWL PKLNALGFEA LEVQHDPSTG EMIMPITDTQ ELPRATLPAH WQGHNLERIL
STLRSLNRFP TPWSPDRTRA RAFTSDVKNS RTGKALHRES QTWKETQTML TENTQTELAI
SVIHGAGGSG KSQALQTLLR QDHSLPIEVV LPTNELRLDW LKKLPHNPPE QFRTFERAFV
SSHSPVVIFD DYGKLPQGYL EAFALTHANL ELVILTGDPR QSTHHESNEE ALISKLPPAT
TIYSAFSRYY INATLRNSKF LANKLGVYSA NSCPLNVTYG FQPLPGLHLL VPSLMKKAAF
TDAGHKVSSY AGCQGITAPK VQILLDNDTT MCTKEVLYTA LSRAVDSIHF VNTNAQSSAF
WEKLEATPYL KTFLSLVRED KITEFQAPAD APKPVTPPVT HFPVEEPATT LDDFKEELRD
KFDREIFTSD RGHTNCVQTD DPTTQLFSHQ QAKDEALLWE MIRARLKIST PEANIEEFRA
KKDLGDILWV NYHRAMGLPK EQPDFSEDLW NRCAEEVQNT YLKKTMAQLK GGERRQSPDF
HEHQILIFLK SQWVKKMEKL GAKEIKPGQT IASFQQHAVM LYGTMARYMR RFRDALSPNN
IMINCEKTPQ DLSRWVLNYW DFSKPSYAND FTAFDQSQDG AMLQFEILKA KYFNLPEWVI
EGYLDIKLSP KIFLGTLSIM RLTGEGPTFD ANTECNIAYT HTRFDIPEGT AQIYAGDDCA
IAQVCPEKPS FALLKNRIAL QAKPAYTPQE RGQWAEFCGY LITPKGLIKD PLKLHASLEL
AKAQKKAGVR DAITNVVANY SLDAKLAYSL GDDLQDLLSP HQAHLHQVTV RDLVKFGGSP
FLNSD