RDRP_BBSCV
ID RDRP_BBSCV Reviewed; 1967 AA.
AC Q65652;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=RNA replication polyprotein {ECO:0000303|PubMed:7871721};
DE AltName: Full=223 kDa protein {ECO:0000303|PubMed:7871721};
DE AltName: Full=ORF1 protein {ECO:0000303|PubMed:7871721};
DE Includes:
DE RecName: Full=Viral methyltransferase {ECO:0000255};
DE EC=2.1.1.- {ECO:0000305};
DE Includes:
DE RecName: Full=Putative Fe(2+) 2-oxoglutarate dioxygenase {ECO:0000255};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE Includes:
DE RecName: Full=Protease {ECO:0000303|PubMed:7871721};
DE EC=3.4.22.- {ECO:0000269|PubMed:7871721};
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE Contains:
DE RecName: Full=Helicase {ECO:0000303|PubMed:7871721};
DE EC=3.6.4.13 {ECO:0000305};
GN ORFNames=ORF1 {ECO:0000303|PubMed:7871721};
OS Blueberry scorch virus (BBScV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Betaflexiviridae; Quinvirinae; Carlavirus.
OX NCBI_TaxID=31722;
OH NCBI_TaxID=69266; Vaccinium corymbosum (Highbush blueberry).
OH NCBI_TaxID=13750; Vaccinium macrocarpon (Large cranberry) (Oxycoccus macrocarpus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=NJ-2 {ECO:0000312|EMBL:AAA68984.1};
RX PubMed=8151289; DOI=10.1099/0022-1317-75-4-711;
RA Cavileer T.D., Halpern B.T., Lawrence D.M., Podleckis E.V., Martin R.R.,
RA Hillman B.I.;
RT "Nucleotide sequence of the carlavirus associated with blueberry scorch and
RT similar diseases.";
RL J. Gen. Virol. 75:711-720(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION (PROTEASE), ACTIVE SITE
RP (PROTEASE), AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC STRAIN=NJ-2 {ECO:0000312|EMBL:AAA68984.1};
RX PubMed=7871721; DOI=10.1006/viro.1995.1058;
RA Lawrence D.M., Rozanov M.N., Hillman B.I.;
RT "Autocatalytic processing of the 223-kDa protein of blueberry scorch
RT carlavirus by a papain-like proteinase.";
RL Virology 207:127-135(1995).
CC -!- FUNCTION: [RNA replication polyprotein]: RNA-directed RNA polymerase
CC involved in viral RNA replication. {ECO:0000255|PROSITE-
CC ProRule:PRU00539, ECO:0000305}.
CC -!- FUNCTION: Protease: Thiol protease that cleaves the polyprotein.
CC {ECO:0000269|PubMed:7871721}.
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 Evidence={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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. {ECO:0000269|PubMed:7871721}.
CC -!- SIMILARITY: Belongs to the potexviruses/carlaviruses RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; L25658; AAA68984.1; -; Genomic_RNA.
DR RefSeq; NP_612579.1; NC_003499.1.
DR PRIDE; Q65652; -.
DR GeneID; 935434; -.
DR KEGG; vg:935434; -.
DR Proteomes; UP000030600; 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; IDA:UniProtKB.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008041; Peptidase_C23.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF05379; Peptidase_C23; 1.
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; PS50802; OTU; 1.
DR PROSITE; PS51492; PEPTIDASE_C23; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Dioxygenase; Helicase; Hydrolase; Iron; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Oxidoreductase; Protease; Reference proteome; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Viral RNA replication.
FT CHAIN 1..1967
FT /note="RNA replication polyprotein"
FT /id="PRO_0000431910"
FT CHAIN 1473..1967
FT /note="Helicase"
FT /evidence="ECO:0000269|PubMed:7871721"
FT /id="PRO_0000431911"
FT DOMAIN 63..252
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 750..841
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 884..991
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT DOMAIN 990..1080
FT /note="Peptidase C23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00825"
FT DOMAIN 1133..1308
FT /note="(+)RNA virus helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1309..1455
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1748..1855
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 994
FT /evidence="ECO:0000269|PubMed:7871721"
FT ACT_SITE 1075
FT /evidence="ECO:0000269|PubMed:7871721"
FT BINDING 768
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 770
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 823
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 832
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 1166..1173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT SITE 1472..1473
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:7871721"
SQ SEQUENCE 1967 AA; 223431 MW; 4CEDD6AF14980188 CRC64;
MALTYRSPVE EVLTLFEPTA QSLIASAAVS AFQRHEKDNF EWFRYSVPAF AKEHLSKAGI
YLSPYAGFPH SHPVCKTLEN YILYVVVPSI VNSTFFFVGI KDFKINFLKS RFDKLNMISA
LNRYVSSADK IRYGNDFVIR AGVEHRALKR HRGLVDSPTL KALMPNVKSG SKLFLHDELH
YWSKEELIGF LEICEPEVLL GTVIYPPELL IGSDCSLNPW CYEYEVKKKK LLFYPDGVRS
EGYEQPLSGG YLLQTSRIKL PNAGIYCVDL LCSRFAHHLF SITRGDLITP DNRSFGPFEA
VHSGALAGIS RGKPNFYPVS QHTILRVYRY LRSLKKPDKQ SAMAKFSQIV HEPCGRAVKF
MEEFSDLIIN TGTLRTVINP EQVKLFFGNL GRCMPPCFAS KLKGTRTVCL DEFISMLRPL
SVDVTLETIS MHSMTMVVTT WSQEAEEGVD LPKIFEEKWE GKQSLDRTEA PYLGLAPFVD
YKIQWRLQFN IPKFLNQLAE LFVNSCSVNG GVRSMSIPAY LRRLATCRSC VGRAMLCCLT
EVDIASLRVV VRNRYPYTED FYRCRRRWFL RIGAQRRPSF YIEDAKHLER LGQFEEEQFQ
RPMSRRSLYT LASVSMNGTD DPFCSDCFYD PVPVARAKIV PTPTVIVERA LEPLAIDTGT
TSDAPCDAPG ATCLRGAQAV VCACGLSMAV SAVPYAELKM DFYPDALKGR DAAWYSKEDR
EYKYNGGSHL CRGWPKWLQL WMQANGVDET YDCMLAQRYG AQGKIGFHAD NEEIFMRGAP
VHTVSMDGNA DFGTECAAGR QYTTLRGNVQ FTMPSGFQET HKHAVRNTTA GRVSYTFRRL
AKKDESRVIE EVVEVETKDM GFSSSLFGVQ IIVDEPCDGV EETFNVQCVP GDGNCFWHSL
GSFTGLTVEC MKAGIKNFAC GPEGAEKLSR QLEPNVWAED EALCAACAHL GVDLVIFDED
QGFKMLYRYP GNKREALLRL KGSHFEPLEP KEMCVVKAIA QAVKRSPMDV LRVALKKMGE
DFKEQICRGK GVMLDVFMVL AKIFDVSACV LQGTEQIMIN PKGRIKGLFR MTTDHLSYDG
VPDKVKHSEV NVYKHDVALQ IEDLIELREL SSLVEYTPSF SRAKLLADCL HDGSTGVMCS
ELYNDKGHLC PEGRETTRVT IGVLLGTFGC GKSRLFKEIL FKLCGKSVCY ISPRKALCDS
FDDEIRKARG NMGERGIKHY KSLTFEKAIL QASKLHKGSL VIIDEIQLYP PGYLDLLLLL
AGPTMKYFAL GDPCQSDYDS EKDRTILGSV RSDVFELLDG IEYKFNILSR RFQSSLFRGR
LPCLMYEEDL EAGAPLRLID GLESIDTSAA YSRCCLVSSF EEKKIVNAYF GERTKCLTFG
ESTGMTFDVG CVLITSISAH TSEQRWITAL SRFRKDIVFV NAASVAWDTL QSVYANRWLG
RFLNRSARQE DLRRMLPGTP LFVEGFQKNL LGADEGKREC KLEGDPWLKT MVDLLQVEDM
EDIEIAKEVL QDEWCKTHLP QCELESVRAR WVHKILAKEF REKRMGCLVS EQFTDQHSKQ
MGKHLTNSAE RFETIYPRHR AADTVTFIMA VRKRLSFSCP IKESAKLNQA LPYGPFLLKE
FLKRVPLKPM HDRKMMEQAK FDFEEKKTSK SAATIENHSN RSCRDWLIDV GLVFSKSQLC
TKFDNRFRDA KRAQTIVCFQ HAVLCRFAPY MRYIEKKLNE VLPSKYYIHS GKGLEELNRW
VIEGRFEGVC TESDYEAFDA SQDHYIVAFE ICLMRYLGLP NDLIEDYKFI KTHLGSKLGN
FAIMRFSGEA STFLFNTMAN MLFTFLQYDL KGNERICFAG DDMCANGRLH VSSKHKNFMS
KLKLKAKVSN TMNPTFCGWN LSSDGIFKKP QLVLERLCIA KETNNLANCI DNYAIEVSFA
YLMGERAKQR MDEEEVEAFY NCVRIIVKSK HLLKSDVATI YQTARVD
