ID RDRP_CGMVS Reviewed; 1648 AA.
AC P69514; P19523; P89877; P90356; Q83208;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Replicase large subunit;
DE EC=2.7.7.48;
DE AltName: Full=186 kDa protein;
DE Contains:
DE RecName: Full=Replicase small subunit;
DE EC=3.6.4.13;
DE AltName: Full=129 kDa protein;
DE AltName: Full=Methyltransferase/RNA helicase;
DE Short=MT/HEL;
OS Cucumber green mottle mosaic virus (strain watermelon SH) (CGMMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Tobamovirus;
OC Cucumber green mottle mosaic virus.
OX NCBI_TaxID=12236;
OH NCBI_TaxID=3653; Citrullus.
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH NCBI_TaxID=3668; Lagenaria siceraria (Bottle gourd) (Lagenaria leucantha).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1856687; DOI=10.1099/0022-1317-72-7-1487;
RA Ugaki M., Tomiyama M., Kakutani T., Hidaka S., Kiguchi T., Nagata R.,
RA Sato T., Motoyoshi F., Nishiguchi M.;
RT "The complete nucleotide sequence of cucumber green mottle mosaic virus (SH
RT strain) genomic RNA.";
RL J. Gen. Virol. 72:1487-1495(1991).
RN [2]
RP SEQUENCE REVISION.
RA Ugaki M., Tomiyama M., Kakutani T., Hidaka S., Kiguchi T., Nagata R.,
RA Sato T., Motoyoshi F., Nishiguchi M.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The replicase large subunit is an RNA-dependent RNA
CC polymerase active in viral RNA replication. {ECO:0000250}.
CC -!- FUNCTION: The replicase small subunit is a methyltransferase active in
CC RNA capping and an RNA helicase. It also acts as a suppressor of RNA-
CC mediated gene silencing, also known as post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs. May mediate silencing suppression through
CC either inhibition of HEN1-mediated siRNA or siRNA demethylation (By
CC similarity). {ECO:0000250}.
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 -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC -!- MISCELLANEOUS: Readthrough of the terminator codon UAG occurs between
CC codons for Lys-1144 and Gln-1146.
CC -!- SIMILARITY: Belongs to the tobamovirus RNA-directed RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; D12505; BAA18895.1; -; Genomic_RNA.
DR EMBL; D12505; BAA18896.1; -; Genomic_RNA.
DR PIR; JQ1157; WMTMS2.
DR RefSeq; NP_044577.1; NC_001801.1.
DR RefSeq; NP_044578.1; NC_001801.1.
DR GeneID; 1494061; -.
DR GeneID; 1494064; -.
DR KEGG; vg:1494061; -.
DR KEGG; vg:1494064; -.
DR Proteomes; UP000008447; Segment.
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-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.30.450.420; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR001788; RNA-dep_RNA_pol_alsuvir.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA suppression of termination;
KW RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW Viral immunoevasion; Viral RNA replication.
FT CHAIN 1..1648
FT /note="Replicase large subunit"
FT /id="PRO_0000041172"
FT CHAIN 1..1144
FT /note="Replicase small subunit"
FT /id="PRO_0000041173"
FT DOMAIN 72..287
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 831..991
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 992..1144
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1413..1526
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 863..870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1648 AA; 186551 MW; 1D1AFFEEE7B65595 CRC64;
MANINEQINN QRDAAASGRN NLVSQLASKR VYDEAVRSLD HQDRRPKMNF SRVVSTEHTR
LVTDAYPEFS ISFTATKNSV HSLAGGLRLL ELEYMMMQVP YGSPCYDIGG NYTQHLFKGR
SYVHCCNPCL DLKDVARNVM YNDMITQHVQ RHKGSGGCRP LPTFQIDAFR RYDSSPCAVT
CSDVFQECSY DFGSGRDNHA VSLHSIYDIP YSSIGPALHR KNVRVCYAAF HFSEALLLGS
PVGNLNSIGA QFRVDGDDVH FLFSEESTLH YTHSLENIKL IVMRTYFPAD DRFVYIKEFM
VKRVDTFFFR LVRADTHMLH KSVGHYSKSK SEYFALNTPP IFQDKATFSV WFPEAKRKVL
IPKFELSRFL SGNVKISRML VDADFVHTII NHISTYDNKA LVWKNVQSFV ESIRSRVIVN
GVSVKSEWNV PVDQLTDISF SIFLLVKVRK VQIELMSDKV VIEARGLLRR FADSLKSAVE
GLGDCVYDAL VQTGWFDTSS DELKVLLPEP FMTFSDYLEG MYEADAKIER ESVSELLASG
DDLFKKIDEI RNNYSGVEFD VEKFQEFCKE LNVNPMLIGH VIEAIFSQKA GVTVTGLGTL
SPEMGASVAL SSTSVDTCED MDVTEDMEDI VLMADKSHSY MSPEMARWAD VKYGNNKGAL
VEYKVGTSMT LPATWAEKGK AVLPLSGICV RKPQFSKPLD EEDDLRLSNM NFFKVSDLKL
KKTITPVVYT GTIRERQMKN YIDYLSASLG STLGNLERIV RSDWNGTEES MQTFGLYDCE
KCKWLLLPAE KKHAWAVVLA SDDTTRIIFL SYDESGSPII DKKNWKRFAV CSETKVYSVI
RSLEVLNKEA IVDPGVHITL VDGVPGCGKT AEIIARVNWK TDLVLTPGRE AAAMIRRRAC
ALHKSPVATN DNVRTFDSFV MNRKIFKFDA VYVDEGLMVH TGLLNFALKI SGCKKAFVFG
DAKQIPFINR VMNFDYPKEL RTLIVDNVER RYVTHRCPRD VTSFLNTIYK AAVATTSPVV
HSVKAIKVSG AGILRPELTK IKGKIITFTQ SDKQSLIKSG YNDVNTVHEI QGETFEETAV
VRATPTPIGL IARDSPHVLV ALTRHTKAMV YYTVVFDAVT SIIADVEKVD QSILTMFATT
VPTKXQLMQN SLYVHRNIFL PVSKTGFYTD MQEFYDRCLP GNSFVLNDFD AVTMRLRDNE
FNLQPCRLTL SNLDPVPALI KNEAQNFLIP VLRTACERPR IPGLLENLVA MIKRNMNTPD
LAGTVDITNM SISIVDNFFS SFVRDEVLLD HLDCVRASSI QSFSDWFSCQ PTSAVGQLAN
FNFIDLPAFD TYMHMIKRQP KSRLDTSIQS EYPALQTIVY HPKVVNAVFG PVFKYLTTKF
LSMVDSSKFF FYTRKKPEDL QEFFSDLSSH SDYEILELDV SKYDKSQSDF HFSIEMAIWE
KLGLDDILAW MWSMGHKRTI LQDFQAGIKT LIYYQRKSGD VTTFIGNTFI IAACVASMLP
LDKCFKASFC GDDSLIYLPK GLEYPDIQAT ANLVWNFEAK LFRKKYGYFC GKYIIHHANG
CIVYPDPLKL ISKLGNKSLV GYEHVEEFRI SLLDVAHSLF NGAYFHLLDD AIHELFPNAG
GCSFVINCLC KYLSDKRLFR SLYIDVSK
//
