ID   RDRP_CLBVS              Reviewed;        1962 AA.
AC   Q91QZ3;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=RNA replication polyprotein {ECO:0000250|UniProtKB:Q65652};
DE   AltName: Full=ORF1 protein {ECO:0000250|UniProtKB:Q65652};
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:0000250|UniProtKB:Q65652};
DE              EC=3.4.22.- {ECO:0000250|UniProtKB:Q65652};
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   Includes:
DE     RecName: Full=Helicase {ECO:0000250|UniProtKB:Q65652};
DE              EC=3.6.4.13 {ECO:0000305};
GN   ORFNames=ORF1 {ECO:0000250|UniProtKB:Q65652};
OS   Citrus leaf blotch virus (isolate Nagami kumquat/France/SRA-153/1984)
OS   (CLBV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Betaflexiviridae; Trivirinae; Citrivirus.
OX   NCBI_TaxID=686981;
OH   NCBI_TaxID=2706; Citrus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11504557; DOI=10.1006/viro.2001.1040;
RA   Vives M.C., Galipienso L., Navarro L., Moreno P., Guerri J.;
RT   "The nucleotide sequence and genomic organization of Citrus leaf blotch
RT   virus: candidate type species for a new virus genus.";
RL   Virology 287:225-233(2001).
CC   -!- FUNCTION: RNA replication polyprotein: RNA-directed RNA polymerase
CC       involved in viral RNA replication. {ECO:0000250|UniProtKB:Q65652}.
CC   -!- FUNCTION: Protease: Thiol protease that cleaves the polyprotein.
CC       {ECO:0000250|UniProtKB:Q65652}.
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   -!- 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:0000250|UniProtKB:Q65652}.
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DR   EMBL; AJ318061; CAC39422.1; -; Genomic_RNA.
DR   RefSeq; NP_624333.1; NC_003877.1.
DR   PRIDE; Q91QZ3; -.
DR   GeneID; 944478; -.
DR   KEGG; vg:944478; -.
DR   Proteomes; UP000006933; 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: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   Gene3D; 3.40.50.300; -; 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; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
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; PF03171; 2OG-FeII_Oxy; 1.
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; PS51471; FE2OG_OXY; 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   3: Inferred from homology;
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..1962
FT                   /note="RNA replication polyprotein"
FT                   /id="PRO_0000401088"
FT   DOMAIN          64..261
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          683..794
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   DOMAIN          874..963
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   DOMAIN          978..1067
FT                   /note="Peptidase C23"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00825"
FT   DOMAIN          1122..1297
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          1298..1445
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1739..1846
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ACT_SITE        982
FT                   /evidence="ECO:0000250|UniProtKB:Q65652"
FT   ACT_SITE        1062
FT                   /evidence="ECO:0000250|UniProtKB:Q65652"
FT   BINDING         892
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         894
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         946
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         954
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         1164..1171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
SQ   SEQUENCE   1962 AA;  227379 MW;  138CC30DD43916D5 CRC64;
     MALMSNKTAI ESILGNFEKK HVDAIYNAAA QTILSHSEFR NKHFAYSLNS YQKKIASKVG
     IELYPNGYLP HSHPLSKIFE NHLLFDVLPG VVNTSRLVMC SIKESKVLVF KGIRDKSRRQ
     VSDLNALNSL NNSHTSFINR LVASKDVSRY TEEADAFFQS KKGSPELFSR NFIKSLENKE
     AVFFHDEVHH WTKAQMFSFL KSTKVKRFIF TVVYPPEILK KFANSQNPKV YDFKVDKGRL
     FFFPDGVKTE AYEQKLNMEW LFSASHLRSG DCVWTVTRHK SIYAHHLFEI SIGELVTDSK
     LFFSDYNSID MSKIFLDRFR SYEVFPISIE HLYKVYSYLL CLKKPDLESG LAKLRQIIGD
     DVEIKEFLFF EQFCKRLIER QTSWGLFGHS FFEKLTDMAL SSLPNSIARI FPQWKKKNTF
     EFLFSLGTLV VDVERKVCFE HVLEEWGFEV VITDENAYLD PLSIFAINEN FNEDRVDDGY
     LERIRLPFWN LNDYDLKRKR VNAYNILSYR FEEERKIESA QKGPNKMLQI EWYGIKEFKV
     DPFISNSITE FTLLEALLGK RIDPKKYSYS KQACTLSNYL TFLCAEGLDG FNLEEHLERR
     LKAAGHDVSD DEEEELTSAE QAGPIKILAD PLGFMKECLE EIPIETEPSL EERGQFSTDY
     HSEKFEINYN DIFNPHNCMN THGDEIPTPS DGNCFFSAFT ETFEVERPDT LRSDFSDWLM
     EFNGGSYASL AEMIRPNGVF MEAELIYLFC VFRGVTLIIH DRTHEKENVY AVHRGFEEGH
     MVHRGNHFVG IETYNISTLT SDPLLGDIPC GFSEEITKFH FRPDHFNCAQ FRGRKAAFIT
     KVDADYGHNG MVYPHNSWVP SLEEIIQICG QGDDFNCALI NFYEANSSLG FHRDNERVYN
     DDPILTVCTF GEGRFTIEFK DQVTSFLMTA GSFFLMPKGF QKKARHSVSN EMSRVSITFR
     KHVRRLNGSP IAIREENYKN TCLINAFSKA MKRSKQAIIA KLKTVNSPFW SRYLSEGNGG
     SIEDCQSACE ALDVTVDLNV NGKCVVLGKG ALRISMALRN NHFSVINAAQ LMERTFVSHL
     LEKGNVNVLE GFDAMLSGDV GAAGVNKIQF AANFEFARIL ANSFLNMTTG ICLGKALDNG
     EKYFLHILKD RVKQIGIDVT MVCGFAGSGK SRKLQSWLHS RKKGNFCVVS PRTNLAADWA
     FKLELEPNEQ RKVSTFEKFI KTDKSKLDLI VIDELTLFPN GYLDLLVYEL ADVNRHCQII
     LLFDPLQARY HNKMDESILT FEHDVDRLIG GQNIEYIYST HRMSRYFNRF FDVPCFNQAD
     RTEEQRLWIF DDVYSIPSIC SDRQEPCDVL LVESDLEKKA FSPIINVMTF GESQGLTFNH
     VCILLSESSA ASNEFRWMVA LTRARTRFSL CSTFLGGIEE FKVKRKESLI TSILQGEKIT
     FNRLNLMLKC NLIRREKENG CRDEVDREER LEGDPFLKPF IFLGQRVEKD EDEVEEVKIR
     EPTCQTHLYI TEPNFGLCYN FDFIREKEQR EYREDMLVTN QFCDSYDKVH INGKRETPGP
     LRFKAIYPKH SADDDMTFWM AVRKRLVFRE EEENYQRLSR AHLVGGLLYT NFKKKMGLEF
     TFDQGLLEES INAFEKKKLE KSCGTIKSHS IRSDIDWALN DVFLFMKSQL CTKYEKQFVD
     AKAGQTLACF QHLILVQFAP WCRYLETQIR NQLPEEIYIH SNKNFDDLNA WVKKFFQRDI
     CVESDYEAFD ASQDEYILSF EIHLMKDAHF PQKIIDAYID LKCKLGCKLG HFSIMRFTGE
     FCTFLFNTLA NMAFTMCRYE WRRGQPIAFA GDDMCALNNL AVCHDFDDLF ELISLKAKVE
     RTETPMFCGW RLTPYGIVKE PELVYNRFQV AIEEGKVLEC LENYAIEVSY AYSLSERLYE
     VLKSERQVQY HQAVVRFIVT HIDKLKTKVR DLFLEQSSDE DI