RDRP_ICRSV
ID RDRP_ICRSV Reviewed; 1658 AA.
AC Q918W3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=RNA replication protein;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE Includes:
DE RecName: Full=Helicase;
DE EC=3.6.4.13;
GN ORFNames=ORF1;
OS Indian citrus ringspot virus (isolate Kinnow mandarin/India/K1/1996)
OS (ICRSV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus; Mandarivirus.
OX NCBI_TaxID=651357;
OH NCBI_TaxID=2706; Citrus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11043949; DOI=10.1007/s007050070064;
RA Rustici G., Accotto G.P., Noris E., Masenga V., Luisoni E., Milne R.G.;
RT "Indian citrus ringspot virus: a proposed new species with some affinities
RT to potex-, carla-, fovea- and allexiviruses.";
RL Arch. Virol. 145:1895-1908(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12417955; DOI=10.1007/s00705-002-0875-6;
RA Rustici G., Milne R.G., Accotto G.P.;
RT "Nucleotide sequence, genome organisation and phylogenetic analysis of
RT Indian citrus ringspot virus.";
RL Arch. Virol. 147:2215-2224(2002).
CC -!- FUNCTION: RNA replication. The central part of this protein possibly
CC functions as an ATP-binding helicase (Probable). {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 -!- 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 -!- SIMILARITY: Belongs to the potexvirus/carlavirus RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; AF406744; AAK97522.1; -; Genomic_RNA.
DR RefSeq; NP_203553.1; NC_003093.1.
DR PRIDE; Q918W3; -.
DR GeneID; 922105; -.
DR KEGG; vg:922105; -.
DR Proteomes; UP000000394; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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: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; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51471; FE2OG_OXY; 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; Reference proteome; RNA-directed RNA polymerase;
KW Transferase; Viral RNA replication.
FT CHAIN 1..1658
FT /note="RNA replication protein"
FT /id="PRO_0000401078"
FT DOMAIN 59..224
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 574..665
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 910..1065
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1066..1199
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1437..1544
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 462..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 592
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 594
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 647
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 656
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 1658 AA; 187256 MW; 801A6ED698812DD7 CRC64;
MATIRGAIDR ITDTTVRTTL QEEACRQIRT ELKNVEHVNR YAIPPDAADA LEHLGIGTNP
FSVKLHTHGA CKAIENQLLY VVGTLLPKER VTMLFLKKAK LNFMKRCPKF QDIFLNQHIE
PRDVSRYCDF NVQSTSTSIP THTAYISDTL HFMDRKDLVR LFINSPNLDT LYATIVLPVE
AAYRQPSRYP DLYQINYDFD GFQYIPGGHG GGAYHHEFSH LEWLDVGHIH WRGPDNKDIQ
LTITAQMIES LGANHLFCFR RGNLRTPRVR TFGRDTQVLL PKIFRPVDKN FNRAIPLTLA
NKMLLYAKSI NTVTFRDVVA KTRQLMKDKE LETYTGADLL HMANYFFVVG ALSGVNSYDQ
MLGLSAWEAC TMALKNTVTN LWERITGKRE FGKLLEALEW ETLTYSRQVT QKYVGGTPAR
LPLPDITDQE EIFAQQEALD ALTSGATKIT THHLMSAAAR RSTEGPTMPT PAAQVPPTQN
PKHTIDEVAS RALVTKLQKN KRVYIQDDGP EYIMGHMAEV PAWYLEQDET TTRLRNRCAW
FFGPPTHRYG HNDIEYHTTE YYPWVERIGN IFGKFNTCLA QTHDQGARIG YHADDEDCYD
KDVTVATVNL TGNATFSLKT ATGTRTWKLK PGDFIVLKPG AQGCTKHAIS DCTTNRTSLT
FRWQARPCPS QLRRVVNLGN VNNPKRKSKA QQWTPKTSNS DSPRLTQTPN SPTPKDVPVV
SPKLADATAP TIRAVPENGA HTNMACVELT DLPETTTTHR PGKEPINDLT DSEPETESEQ
TENLVLNRFI QDLPTTSTHA WASETDSICS FQAEALGPSS VEALPWHEHL ELINSLGFTG
LERQYGPDNN LIWPITHYRT LPKSRTIEAP TDLVELLDTI DRHPTDVPYS KTRASAFGSD
VKNLRIGALV KNQDKQWRAS LALLCEENEH VLPTTVIHGA GGSGKSHLLQ QWVSSTERGN
VVVILPTIEL LRDWLNKCPT TPKDSFKTFE KALVQNSAPV VIMDDYSKLP PGYIEAYVAL
KGQCKLLVLT GDPRQSHYHE ENPEALISTL DPATDYFSKY CTYNINATHR NATTFANALG
VYSERKLPVS VTCSSYQKSG WPTLVPSILK KTALNDMGQR SLTYAGCQGL TTPKVQIVLD
NATPLCSEQV MYTALSRAVD QIHFFNTGPN HSDYWEKMNA TPFLKTFIDH TREENLKEHQ
PAEPTVREHT PATHFPPANE ALALEPWVEP LTDKHSRELH HKALGHSNCV QTDNPVVQLF
PHQQAKDETL FWKTIDARIK ITTPEENVRN FNMASDIGDI LFLNYKEAMC LPADPIPFQQ
SLWDSCQAEV QQTYLSKPLA ALANAAQRQD PDFDSNKIQL FLKSQWVKKV EKLGCLKIKP
GQTIASFMQQ TVMLYGTMAR YMRRIRISLC PSHIMINCET NPTQISSWVR ENWDFSGQSH
ENDFEAFDQS QDANMLQFEL IKAKFHSIPE EIIAGYKHLK CHAHIFLGTI AIMRLSGEGP
TFDANTECSI AYNHTRYFVP KGCAQLYAGD DSACAAPLSE KPSFQHISPE LSLKSKAKIR
SQTKGDYATF CGWLITPKGF IKNPTQLYAS WLLAKHNKDL QDVARNYALD LRIAYQLKDE
LYELLSPEEL DHHQLLVREM VKHKMGHLLN LPEGFKQT
