194K_TRVSY
ID 194K_TRVSY Reviewed; 1707 AA.
AC P05080;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 23-FEB-2022, entry version 97.
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=194 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=134 kDa protein;
DE AltName: Full=Methyltransferase/RNA helicase;
OS Tobacco rattle virus (strain SYM).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Tobravirus.
OX NCBI_TaxID=12298;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH NCBI_TaxID=82024; Hyacinthus.
OH NCBI_TaxID=39639; Narcissus pseudonarcissus (Daffodil).
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH NCBI_TaxID=13274; Stellaria media (Common chickweed) (Alsine media).
OH NCBI_TaxID=13305; Tulipa.
OH NCBI_TaxID=97415; Viola arvensis (European field pansy) (Field violet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3668507; DOI=10.1099/0022-1317-68-10-2563;
RA Hamilton W.D.O., Boccara M., Robinson D.J., Baulcombe D.C.;
RT "The complete nucleotide sequence of tobacco rattle virus RNA-1.";
RL J. Gen. Virol. 68:2563-2575(1987).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE.
RX PubMed=16453668; DOI=10.1002/j.1460-2075.1986.tb04202.x;
RA Boccara M., Hamilton W.D.O., Baulcombe D.C.;
RT "The organisation and interviral homologies of genes at the 3' end of
RT tobacco rattle virus RNA1.";
RL EMBO J. 5:223-229(1986).
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=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 -!- 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 -!- 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 1187-Lys and 1189-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; X06172; CAA29537.1; -; Genomic_RNA.
DR EMBL; D00155; BAA00110.1; -; Genomic_RNA.
DR PIR; S01865; S01865.
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 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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Methyltransferase;
KW Nucleotide-binding; Nucleotidyltransferase; RNA-binding;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT CHAIN 1..1707
FT /note="Replicase large subunit"
FT /id="PRO_0000040215"
FT CHAIN 1..1187
FT /note="Replicase small subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040216"
FT DOMAIN 86..300
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 872..1033
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1034..1187
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1449..1562
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 65..425
FT /note="Methyltransferase"
FT /evidence="ECO:0000250"
FT REGION 901..1155
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT COILED 601..622
FT /evidence="ECO:0000255"
SQ SEQUENCE 1707 AA; 194330 MW; F4DABDB6C7F51F04 CRC64;
MANGNFKLSQ LLNVDEMSAE QRSHFFDLML TKPDCEIGQM MQRVVVDKVD DMIRERKTKD
PVIVHEVLSQ KEQNKLMEIY PEFNIVFKDD KNMVHGFAAA ERKLQALLLL DRVPALQEVD
DIGGQWSFWV TRGEKRIHSC CPNLDIRDDQ REISRQIFLT AIGDQARSGK RQMSENELWM
YDQFRKNIAA PNAVRCNNTY QGCTCRGFSD GKKKGAQYAI ALHSLYDFKL KDLMATMVEK
KTKVVHAAML FAPESMLVDE GPLPSVDGYY MKKNGKIYFG FEKDPSFSYI HDWEEYKKYL
LGKPVSYQGN VFYFEPWQVR GDTMLFSIYR IAGVPRRSLS SQEYYRRIYI SRWENMVVVP
IFDLVESTRE LVKKDLFVEK QFMDKCLDYI ARLSDQQLTI SNVKSYLSSN NWVLFINGAA
VKNKQSVDSR DLQLLAQTLL VKEQVARPVM RELREAILTE TKPITSLTDV LGLISRKLWK
QFANKIAVGG FVGMVGTLIG FYPKKVLTWA KDTPNGPELC YENSHKTKVI VFLSVVYAIG
GITLMRRDIR DGLVKKLCDM FDIKRGAHVL DVENPCRYYE INDFFSSLYS ASESGETVLP
DLSEVKAKSD KLLQQKKEIA DEFLSAKFSN YSGSSVRTSP PSVVGSSRSG LGLLLEDSNV
LTQARVGVSR KVDDEEIMEQ FLSGLIDTEA EIDEVVSAFS AECERGETSG TKVLCKPLTP
PGFENVLPAV KPLVSKGKTV KRVDYFQVMG GERLPKRPVV SGDNSVDARR EFLYYLDAER
VAQNDEIMSL YRDYSRGVIR TGGQNYPHGL GVWDVEMKNW CIRPVVTEHA YVFQPDKRMD
DWSGYLEVAV WERGMLVNDF AVERMSDYVI VCDQTYLCNN RLILDNLSAL DLGPVNCSFE
LVDGVPGCGK STMIVNSANP CVDVVLSTGR AATDDLIERF ASKGFPCKLK RRVKTVDSFL
MHCVDGSLTG DVLHFDEALM AHAGMVYFCA QIAGAKRCIC QGDQNQISFK PRVSQVDLRF
SSLVGKFDIV TEKRETYRSP ADVAAVLNKY YTGDVRTHNA TANSMTVRKI VSKEQVSLKP
GAQYITFLQS EKKELVNLLA LRKVAAKVST VHESQGETFK DVVLVRTKPT DDSIARGREY
LIVALSRHTQ SLVYETVKED DVSKEIRESA ALTKAALARF FVTETVLXRF RSRFDVFRHH
EGPCAVPDSG TITDLEMWYD ALFPGNSLRD SSLDGYLVAT TDCNLRLDNV TIKSGNWKDK
FAEKETFLKP VIRTAMPDKR KTTQLESLLA LQKRNQAAPD LQENVHATVL IEETMKKLKS
VVYDVGKIRA DPIVNRAQME RWWRNQSTAV QAKVVADVRE LHEIDYSSYM YMIKSDVKPK
TDLTPQFEYS ALQTVVYHEK LINSLFGPIF KEINERKLDA MQPHFVFNTR MTSSDLNDRV
KFLNTEAAYD FVEIDMSKFD KSANRFHLQL QLEIYRLFGL DEWAAFLWEV SHTQTTVRDI
QNGMMAHIWY QQKSGDADTY NANSDRTLCA LLSELPLEKA VMVTYGGDDS LIAFPRGTQF
VDPCPKLATK WNFECKIFKY DVPMFCGKFL LKTSSCYEFV PDPVKVLTKL GKKSIKDVQH
LAEIYISLND SNRALGNYMV VSKLSESVSD RYLYKGDSVH ALCALWKHIK SFTALCTLFR
DENDKELNPA KVDWKKAQRA VSNFYDW
