RDRP_CARMV
ID RDRP_CARMV Reviewed; 763 AA.
AC P04518;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 29-SEP-2021, entry version 81.
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=Protein p88;
DE Contains:
DE RecName: Full=Protein p28;
GN ORFNames=ORF1;
OS Carnation mottle virus (CarMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC Tolivirales; Tombusviridae; Procedovirinae; Alphacarmovirus.
OX NCBI_TaxID=11986;
OH NCBI_TaxID=3681; Begonia.
OH NCBI_TaxID=278075; Dianthus barbatus.
OH NCBI_TaxID=3570; Dianthus caryophyllus (Carnation) (Clove pink).
OH NCBI_TaxID=118431; Dianthus chinensis.
OH NCBI_TaxID=288950; Dianthus superbus.
OH NCBI_TaxID=3750; Malus domestica (Apple) (Pyrus malus).
OH NCBI_TaxID=3572; Saponaria officinalis (Common soapwort) (Lychnis saponaria).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3840587; DOI=10.1093/nar/13.18.6663;
RA Guilley H., Carrington J.C., Balazs E., Jonard G., Richards K.,
RA Morris T.J.;
RT "Nucleotide sequence and genome organization of carnation mottle virus
RT RNA.";
RL Nucleic Acids Res. 13:6663-6677(1985).
CC -!- FUNCTION: RNA-dependent RNA polymerase that plays an essential role in
CC the virus replication. {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 -!- MISCELLANEOUS: Readthrough of the terminator UAG occurs at position
CC 246.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26726.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X02986; CAA26726.1; ALT_SEQ; Genomic_RNA.
DR PIR; A04208; RRVECV.
DR RefSeq; YP_009032645.1; NC_001265.2.
DR RefSeq; YP_009032646.1; NC_001265.2.
DR PRIDE; P04518; -.
DR GeneID; 1724754; -.
DR GeneID; 1724755; -.
DR KEGG; vg:1724754; -.
DR KEGG; vg:1724755; -.
DR Proteomes; UP000201784; Genome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR Pfam; PF00998; RdRP_3; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 4: Predicted;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA suppression of termination; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication.
FT CHAIN 1..763
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000222895"
FT CHAIN 1..245
FT /note="Protein p28"
FT /id="PRO_0000398299"
FT DOMAIN 466..579
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 763 AA; 85776 MW; 197256D8B4B61A38 CRC64;
MGLPSLLVEG VIGCTLVGGL VAVGSAALAV RATIGVVEFN RECVRGARRI VSSGGRCLVV
QSPYGNPNQG LIRGEDEEID NVEESTPVEL TPLIEVKAEV DGKEVVVSKK RVVNRHLRQR
FVRSIAIEAK NHFGGDISPS KANYLSVSKF LTGKCKERHV VPAHTRDCVS AAMVLVFTPD
VHEIRMMAGL ASDAAYGIKI AMASILNRKG WCWRLMVNPL DRARWWEMWC VVNGFDSNKP
VTFPKXGGLF YLNGVETKIR RGGHPSVIEV DGQCPLKERK LYVQNAITTG YEYRVHNHSY
ANLRRGLLER VFYVERNKEL VSCPQPEPGS FKEMGYLRRR FHRVCGNHTR ISANDLVDCY
QGRKRTIYEN AAASLLDRAI ERKDGDLKTF IKAEKFNVNL KSDPAPRVIQ PRSPRYNVEL
GRYLKKYEHH AYKALDKIWG GPTVMKGYTT EEVAQHIWSA WNQFQTPVAI GFDMSRFDQH
VSVAALEFEH SCYLACFEGD AHLANLLKMQ LVNHGVGFAS NGMLRYTKEG CRMSGDMNTA
LGNCLLACLI TKHLMKIRSR LINNGDDCVL ICERTDIDYV VSNLTTGWSR FGFNCIAEEP
VYEMEKIRFC QMAPVFDGAG WLMVRDPLVS MSKDSHSLVH WNNETNAKQW LKSVGMCGLR
IAGGVPVVQE FYQKYVETAG NVRENKNITE KSSSGFFMMA DRAKRGYSAV SEVCRFSFYQ
AFGITPDQQI ALEGEIRSLT INTNVGPQCE AADSLWILNR KYQ