ID   RDRP_SHMV               Reviewed;        1629 AA.
AC   P89202; Q88624;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 96.
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=183 kDa 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=126 kDa protein;
DE     AltName: Full=Methyltransferase/RNA helicase;
DE              Short=MT/HEL;
OS   Sunn-hemp mosaic virus (SHMV) (TMV strain cowpea).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Tobamovirus.
OX   NCBI_TaxID=12240;
OH   NCBI_TaxID=3829; Crotalaria juncea (Sunn hemp).
OH   NCBI_TaxID=35936; Lablab purpureus (Hyacinth bean) (Dolichos lablab).
OH   NCBI_TaxID=40336; Mucuna.
OH   NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-1536.
RX   PubMed=8938983; DOI=10.1007/bf00576982;
RA   Silver S., Quan S., Deom C.M.;
RT   "Completion of the nucleotide sequence of sunn-hemp mosaic virus: a
RT   tobamovirus pathogenic to legumes.";
RL   Virus Genes 13:83-85(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1538-1629.
RX   PubMed=6292867; DOI=10.1093/nar/10.19.6111;
RA   Meshi T., Ohno T., Okada Y.;
RT   "Nucleotide sequence of the 30K protein cistron of cowpea strain of tobacco
RT   mosaic virus.";
RL   Nucleic Acids Res. 10:6111-6117(1982).
CC   -!- FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase
CC       active in viral RNA replication.
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). It also acts
CC       as a suppressor of RNA-mediated gene silencing, also known as post-
CC       transcriptional gene silencing (PTGS), a mechanism of plant viral
CC       defense that limits the accumulation of viral RNAs. May mediate
CC       silencing suppression through either inhibition of HEN1-mediated siRNA
CC       or siRNA demethylation (By similarity). {ECO:0000250, 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: This protein is translated as a fusion protein by
CC       episodic readthrough of a termination codon. When readthrough of the
CC       terminator codon TGA occurs between the codons for Lys-1130 and Gln-
CC       1132, this results in the addition of the RdRp region to the replicase.
CC   -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC       RNA polymerase family. {ECO:0000305}.
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DR   EMBL; U47034; AAB38492.1; -; mRNA.
DR   EMBL; J02413; AAA46585.1; -; Genomic_RNA.
DR   Proteomes; UP000007218; 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; -; 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   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; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA suppression of termination;
KW   RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1629
FT                   /note="Replicase large subunit"
FT                   /id="PRO_0000041184"
FT   CHAIN           1..1130
FT                   /note="Replicase small subunit"
FT                   /id="PRO_0000041185"
FT   DOMAIN          69..292
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          821..976
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          977..1130
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1396..1509
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          48..473
FT                   /note="Methyltransferase"
FT   REGION          845..1099
FT                   /note="Helicase"
FT   BINDING         849..856
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1629 AA;  186516 MW;  C928BC9AF95FE8A5 CRC64;
     MSTSTLINKA QTNSCGDVGV VDLLKRKVYD DTVKTMQGLD RRAKYRLNQC LGPEQCRTVR
     GGYPEFQIEF TGASNTSHAM AAGLRGLELE YLYTLVPYGA VSYDIGGNFP AHMMKGRSYV
     HCCNPALDAR DLARNENYRI SIENYLSRFE DKSGDYCQWQ RKKPKVSKPL PRYQKACFDR
     YNEDPEHVTC SETFEKCRIS PPAERDDIYA TSLHSLYDIP YQNLGPALAR KRIKVLHAAF
     HFSEDLLLGA SEGLLTQIGG TFQRNGDVLT FSFLDESSLI YTHSFRNVFE YVTRTFFVAC
     NRYAYMKEFR SRRVDTVFCS FIRIDTYCLY RSVFKDCDEH VFAAMDDAWE FKKKRVMLEA
     SRPIFNDVAQ FNVYFPNAKD KVCLPIFAVK SVSGAPVTTR HILVEKDFYW TALNHILTYP
     DGKADFRGVM SFLESIRSRV VINGTTTASQ WEVDKSQLKD IALSLLLIAK LEKLKISVIE
     KRIKIERQGL VSLLKEFLHG LLDEYTQTMA EWVVEKGWVK SVDQVLQVTI PDLVLNFRDH
     FRCEFRTSAN VSEVNVSEHL VATNEYYAKV SDLVDRNPTL AFDFEKFQDY CEKLGVDIDT
     VTELIDAIST GRAGITLDHT DDKEEQLPRT LAGSSSYLEE EPSDDLVCLS DKAIVNRSTI
     LGELKNNVVI FEGTLPKNSV FVSAPDDPSV TIELSELHAR PVSDFLSMQK PVNIVYTGEV
     QICQMQNYLD YLSASLVACI SNLKKYLQDQ WLNPGEKFQK IGVWDNLNNK WIVVPQKKKY
     AWGLAADVDG NQKTVILNYD EHGMPILEKS YVRLVVSTDT YLFTVVSMLG YLRHLDQKKP
     TATITLVDGV PGCGKTQEIL SRFDANSDLI LVQGREACEM IRRRANDNVP GSATKENVRT
     FDSFVMNRKP GKFKTLWVDE GLMVHPGLIN FCINISCVSS VYIFGDRKQI PFINRVMNFS
     IPDNLAKLYY DEIVSRDTTK RCPLDVTHFL NSVYEKRVMS YSNVQRSLEC KMISGKAKIN
     DYRSILAEGK LLTFTQEDKE YLLKAGFKDV NTVHEAQGET YRDVNLIRVT ATPLTIVSAG
     SPHVTVALSR HTNRFVYYTV VPDVVMTTVQ KTQCVSNFLL DMYAVAYTQK XQLQISPFYT
     HDIPFVETNK VGQISDLQYF YDSWLPGNSF VQNNHDQWSI ISSDINLHSE AVRLDMNKRH
     IPRTKGEFLR PLLNTAVEPP RIPGLLENLL ALIKRNFNAP DLAGQLDYDF LSRKVCDGFF
     GKLLPPDVEA SELLRLPVDH MYSVQNFDDW LNKQEPGVVG QLANWDHIGM PAADQYRHMI
     KRTPKAKLDL SIQSEYPALQ TIVYHSKHVN AVFGPIFSCL TERLLSVVDP LRFKFFTRTT
     PADLEFFFRD MVVGDMEILE LDISKYDKSQ NKFHFEVEMR IWEMLGIDKY IEKVWENGHR
     KTHLRDYTAG IKTVIEYQRK SGDVTTFIGN TIIIAACLCS ILPMEKVFKA GFCGDDSIIY
     LPRNLLYPDI QSVSNNMWNF EAKLFKKLHG YFCGRYXLRN GRYLRLLPDP LKIITKLGCK
     AIKDWDHLEE FRISMFDMAC EYKNCFGFDV LESAVKESFP KAEGCNVAFC AIYKFLSNKY
     LFRTLFSDV