RDRP_SBWMN
ID RDRP_SBWMN Reviewed; 1828 AA.
AC Q89249; Q06359;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 105.
DE RecName: Full=Replicase large subunit;
DE EC=2.1.1.-;
DE EC=2.7.7.-;
DE EC=2.7.7.48;
DE EC=3.6.4.13;
DE AltName: Full=209 kDa readthrough protein;
DE AltName: Full=RNA-directed RNA polymerase;
DE Contains:
DE RecName: Full=Replicase small subunit;
DE EC=2.1.1.-;
DE EC=2.7.7.-;
DE EC=3.6.4.13;
DE AltName: Full=150 kDa protein;
DE AltName: Full=Methyltransferase/RNA helicase;
GN Name=rep; ORFNames=ORF1-1bis;
OS Soil-borne wheat mosaic virus (strain United States/Nebraska/1981) (SBWMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Furovirus.
OX NCBI_TaxID=652673;
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH NCBI_TaxID=4564; Triticum.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8317092; DOI=10.1006/viro.1993.1342;
RA Shirako Y., Wilson T.M.;
RT "Complete nucleotide sequence and organization of the bipartite RNA genome
RT of soil-borne wheat mosaic virus.";
RL Virology 195:16-32(1993).
CC -!- FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase
CC active in viral RNA replication. {ECO:0000250}.
CC -!- FUNCTION: [Replicase small subunit]: Is a methyltransferase active in
CC RNA capping and an RNA helicase. Methyltransferase displays a
CC cytoplasmic capping enzyme activity. This function is necessary since
CC all viral RNAs are synthesized in the cytoplasm, and host capping
CC enzymes are restricted to the nucleus. Helicase region probably
CC exhibits NTPase and RNA unwinding activities (Potential).
CC {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 -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC -!- MISCELLANEOUS: The replicase large subunit is translated as a fusion
CC protein by episodic readthrough of a termination codon. When
CC readthrough of the terminator codon TGA occurs between the codons for
CC 1320-Lys and 1322-Arg, this results in the addition of the RdRp region.
CC -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; L07937; AAA48492.1; -; Genomic_RNA.
DR EMBL; L07937; AAA48491.1; -; Genomic_RNA.
DR RefSeq; NP_049335.1; NC_002041.1.
DR PRIDE; Q89249; -.
DR GeneID; 991048; -.
DR KEGG; vg:991048; -.
DR Proteomes; UP000009270; 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:UniProtKB-KW.
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; -; 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; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR InterPro; IPR013664; Virgavirus_MeTrfase_C.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR Pfam; PF08456; Vmethyltransf_C; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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; Coiled coil; Helicase; Hydrolase; Methyltransferase;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-binding; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1828
FT /note="Replicase large subunit"
FT /id="PRO_0000409449"
FT CHAIN 1..1320
FT /note="Replicase small subunit"
FT /id="PRO_0000409450"
FT DOMAIN 82..302
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 996..1154
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1155..1320
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1581..1694
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 61..812
FT /note="Methyltransferase"
FT REGION 1026..1289
FT /note="Helicase"
FT COILED 701..728
FT /evidence="ECO:0000255"
FT COILED 1432..1496
FT /evidence="ECO:0000255"
SQ SEQUENCE 1828 AA; 209206 MW; C964ACC9044AAC45 CRC64;
MPIDSSSILG IISEEDVIRA AISTSATKFG SQLHSTVCDH VKETYLDAVE RQKVKKKIDV
RRDLSQEQLQ LLNDLYPERH IVSSNCERGT HSFAAASRKI ETDLLLSRIP KRSWVYDIGG
NWATHVKRND GRKVHCCCPT VDIRDSARKT VRWASIEKYL DEKEEIPPEI GERIKRLQAD
EDRIYANLKS EKAQPEDLDG KWYCGNRFED CVFRADRAYA MAIHSIYDID LSDLANALEE
KRIKVMSGTF LFSVDLLLGK KSGTLPTMDG FFEVEDGYVK YGFHNDTNPG YKHNLNQLMK
YLTKTFVVAK GGTIYYLELT EQRGDVMFFT MTDATEARMN GVVADESFKC IPIDNKDEVV
FPIFEVDQKT DALVFSEILL SRDFVQRAIE YTGRLKPAQL TSDNVNTYLT STNNTIIIGG
SSKKNATKVD ATLIQQITTT LIVWTELMNQ RQKRVLEKLR MQMKDDVDFM TLAHATFLKM
FGKVSYYQRA LRCFANWISY VHGADAIQFR NVPLYAEVTD RIKLWKNYAP NQGFVLDLEE
LDVKIKLHEI TEREKRDVSR CIVSGKLGEL SSVDNTECGA VLDGKDYKDS RRKTTFEDLL
DGEVATNFLD NWCDKTDHFN FSRSDAVSKY AWGMKLLKGV WEFLLPPLHF APVYVDAEQA
RIRLNAEIVT VVEHAVTESN VGLTGVEKAE FADAMSFLVG AAKHLEKRKE VAQQAVVEAV
EAVRELRKVH SPADVCNAVD LWSAFEKDLD DDDETGTTAT IVEKGKAVCD DDVQVVLCGS
SSTSSVEEVS KEAELFVETI ESQASSVTET SDVTTEVAAS SSDESVMSEV PEKSWASVAE
DESDDSYYLR SMIISDKVQK SALPKRPDFS KYSTLQQKAK QEALWYLQCK IVSDRTTLRS
IIDDHLRGMF HNGNCELPKD SAFLDYTVDN CGTWMYGKPS RPGHSYGVGF SLDTKQRITK
CELVKLMWNR DCRGQMNQKP VNTRAFQYLL LSDLSFMMNE LVIYRNLQQV VKKKERTKQA
RITLRDGVPG CGKSTWILNN ANPMKDMVLC VGKEATEDLK EKFMKKHKCA ESDLKRIRTV
DSFLMHDYDK FRAATVHFDE ALMAHAGIVY FCADILGAKK VICQGDSQQI PFINRVESIT
LQYAKLAIDE TEYVRLTYRS PVDVAHYLTK KSWYSGGRVT TKNSVLRSMK VVGPRDAKPM
TSVHCVPYHR DAQYLTFTQS EKADLYKALR AKGPVEVNTV HETQGKTFDD VIVVRLKTTE
NEIYPGGRKG QPYEIVATTR HRRSLVYYTA IEDRLFEDIS DMQDVMESKL MKNLCSELTK
XRFGSKYESI LICDREVRVP DVGTPVIIQD FYDRVLPGNS TMDSHFDGYE VSTSDISIEL
ENCTVQPNKN VKVWQDKRGL VPVLRTAMPP KRQNLPVEAM LALKKRNMAA PKLQEAVNEF
EVIERTVNRA KEIFFDTSLI DDSEVSTRES NLRWWKRQST TAKAQLKKET RLLHELDLCY
YNYCIKGDEK PKMDRSPQHE YGALQTVVFP DKIVNALFGP AMKEINERIR LALKPHVVYN
SRMNAEELNR TVEFLDPEED FNAFEIDFSK FDKSKTSLHI RAVIELYKLF GLNDLFALLW
EKSQCQTKIR DFVNGITAYL LYQQKSGNCD TYGSNTWSAA LALLESMPLE KAKFMIFGGD
DSLILFPKHL TIEDPCRRLA SLWNFDCKLF DFKHNMFCGK FLLKVGDRFK FAPDPMKLIT
KLGRKDIVDG RLLSEIFVSV GDNYRSYRDY RILEQLTYAL RERYRTTEDP TAALVALKKY
IFDFKLWASM FNYKGEFVEC RVDRNFEW
