RDRP_BNYVS
ID RDRP_BNYVS Reviewed; 2109 AA.
AC Q65667;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Replicase;
DE AltName: Full=237 kDa protein;
DE Contains:
DE RecName: Full=Replicase large subunit;
DE EC=2.1.1.-;
DE EC=2.7.7.-;
DE EC=3.4.22.-;
DE EC=3.6.4.13;
DE AltName: Full=150 kDa protein;
DE Contains:
DE RecName: Full=Replicase small subunit;
DE EC=2.7.7.48;
DE AltName: Full=66 kDa protein;
DE AltName: Full=RdRp;
GN ORFNames=ORF1;
OS Beet necrotic yellow vein virus (isolate Japan/S) (BNYVV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Benyviridae; Benyvirus.
OX NCBI_TaxID=652670;
OH NCBI_TaxID=343494; Beta macrocarpa (Beet) (Beta vulgaris subsp. macrocarpa).
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8973531; DOI=10.1007/bf01718223;
RA Saito M., Kiguchi T., Kusume T., Tamada T.;
RT "Complete nucleotide sequence of the Japanese isolate S of beet necrotic
RT yellow vein virus RNA and comparison with European isolates.";
RL Arch. Virol. 141:2163-2175(1996).
RN [2]
RP PROTEOLYTIC PROCESSING.
RX PubMed=9191870; DOI=10.1007/s007050050141;
RA Hehn A., Fritsch C., Richards K.E., Guilley H., Jonard G.;
RT "Evidence for in vitro and in vivo autocatalytic processing of the primary
RT translation product of beet necrotic yellow vein virus RNA 1 by a papain-
RT like proteinase.";
RL Arch. Virol. 142:1051-1058(1997).
CC -!- FUNCTION: [Replicase small subunit]: Is an RNA-dependent RNA polymerase
CC active in viral RNA replication. {ECO:0000305}.
CC -!- FUNCTION: [Replicase large 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. Contains a cysteine
CC protease activity responsible for autocatalytic processing of the 237
CC kDa protein (Potential). {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;
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 -!- PTM: Autocatalytically cleaved by the cysteine protease.
CC {ECO:0000269|PubMed:9191870}.
CC -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC RNA polymerase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84410; BAA12339.1; -; Genomic_RNA.
DR RefSeq; NP_612615.1; NC_003514.1.
DR MEROPS; C36.001; -.
DR PRIDE; Q65667; -.
DR GeneID; 991082; -.
DR KEGG; vg:991082; -.
DR Proteomes; UP000001100; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; 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; IPR008746; Peptidase_C36.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF05415; Peptidase_C36; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Methyltransferase;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..2109
FT /note="Replicase"
FT /id="PRO_0000409655"
FT CHAIN 1..?1540
FT /note="Replicase large subunit"
FT /id="PRO_0000409656"
FT CHAIN ?1541..2109
FT /note="Replicase small subunit"
FT /id="PRO_0000409657"
FT DOMAIN 209..421
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 911..1063
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1064..1214
FT /note="(+)RNA virus helicase C-terminal"
FT REGION 939..1181
FT /note="Helicase"
FT REGION 1285..1388
FT /note="Protease"
FT REGION 1390..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2109 AA; 237518 MW; 4F4915CBD6C6947C CRC64;
MADSFGFTPM EVLLFGGESV QLLTSDMPID VQWGFVHSTR CYALWKDDLI HLNPLLKYSQ
RIAKRWERLV SGFVGPVPLD KLLSLLAKLM RYCVNMGVSV QEIYLSDAIV SSSYMLHVSR
SAGCVSFSWL YAKLSMFASC GKFWVGSSHH TAANMIEGSR AVNGPDVAIS EMVEAFHLEV
KSSLVVTVSL TPREKKILER ELGFVPLYKQ KSRAPRNHPV LAALREVMRQ EYSASCNILN
TKLKTLVVGA ASREVNCYSS NPSVHYYFAN KDSKDLVRTT LELLHSALAT KYRNMESGER
ELMNNLKGCG YIVKRSVENA VYEVVSDKDV AEVLRYAQTV ASTKKEAKKK PNTGKRKMVM
SEATRRTIEL HELSRIVAEE KKIPNHFHFD ESDFASVGNF TQLVCEDVGY NFSVDAWLHL
FEATGAQTAV GYMALPNELL FEHYPISDYY DYWEGVEKHG SLGGITISPL RNGQVVGMPT
GVFQPVHFDK TSAGLGIPGS KMGAAERVIC HMSDGLGNGY NHVKSDWQTL LKHPILSSSK
YNFAVEVDLT GRYGCLATFR LTRVTGVKYV ARTIKLRPED RYVRVLDLLH IVRSIRLKGH
AGLKEPYQYF PVYKREVDTP VSYCFSIAEK SLTVQNIANF IRHHIGGVSL VNKELVSAWR
LNPQLVPSFA YAVYFYVVNL RGELDGMLQK LMKKGITWAD RLKANVSAFL RDMVDPISFL
WTWLFERRLV DQIFQDGTDV FYQMDRACVD EKALRLNDHI KITRDFLPAD TLLPEGWSLD
DWEKAPDSLK TLSAAASLPV ECGAVNCVGK SFKSVRTLLP PSVVTSPVEQ FFKSGGKFRD
DAEFAELLSA HYRWQMDNSF CACQVCAALT GKTGSQVVEC RWKAESMYTF SMSQTEVDDF
RNEIKAQSIE KGNRFGEMLI GVHQKIPTQA FEVSVRLEYV KGGPGTGKSF LIRSLADPIR
DLVVAPFIKL RSDYQNQRVG DELLSWDFHT PHKALDVTGK QIIFVDEFTA YDWRLLAVLA
YRNHAHTIYL VGDEQQTGIQ EGRGEGISIL NKVDLSKVST HVPIMNFRNP VRDVKVLNYL
FGSRMVPMSS VEKGFSFGDV KEFSSLSNIP DTKIIHYSDE TGEHMMPDYV RGVSKTTVRA
NQGSTYDNVV LPVLPSDLNL INSAELNLVA LSRHRNKLTI LLDNDGMNIG AVLKGMLEGV
PEELERRDYI VGMYLGLHLP IKKEFFFPES EFAKSFRLMV AKYEAFVPYD SNLPTLVLQG
DVVVLDIARV ENDINDAFNC PDFYNLVSRP NNCLVVAISE CLGVTLEKLD NLMQANAVTL
DKYHAWLSKK SPSTWQDCRM FADALKVSMY VKVLSDKPYD LTYEVDGAGS SVTLHLVGKE
SDGHFIAAPL SPSLSTNERE SGHDSKKPAD DSDTFDAANL FADKGVSSAD IEAFCAYLEK
TLMATIMEYD LRLQSWANVV DDTDDFYQIN ISEFRQSTCF GKLLSALEVL KVDVSRKRFI
SDWLCKNLEN KQFRWRWSSS VASTSSAGSN VDDDFVNMAG GKTDANVDPA DVLRQSFMDY
ASEFVPILIA ESPILMPLVE PEPILSKCMV PEFDAFLLIK EFDLDNGADE YQCAYLNESV
ANRVGDKFVS GVLDTDIISP LNLRGHPIAE NVKYHSMCVA PAQIYFKRNQ WQELQVQQAR
YLFRKVRNSP SSTQDSVARM VAQLFVSDCL VPNVADTFSA SNLWRIMDKA MHDMVTKNYQ
GQMEEEFTRN AKLYRFQLKD IEKPLKDPET DLAKAGQGIL AWSKEAHVKF MVAFRVLNDL
LLKSLNSNVV YDNTMSETEF VGKINAAMNI VPDSAINGVI DAAACDSGQG VFTQLIERHI
YAALGISDFF LDWYFSFREK YVMQSRYVRA HMSYVKTSGE PGTLLGNTIL MGAMLNAMLR
GTGPFCMAMK GDDGFKRQAN LKINDQMLKL IKKETVLDFK LDLNVPITFC GYALSNGHLF
PSVSRKLTKI AAHRFREYKH FCEYQESLRD WIKNLPKDPA VYADFLECNA SLSCRNVDDV
QRWLDAIISV SRIGREQFMM MFPIREVFMS LPPVEDSLGE LSSTKVAVSI GDNVSNVVRK
VARVDMKKF
