RDRP_LOLV
ID RDRP_LOLV Reviewed; 1729 AA.
AC B1PS76;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Name=ORF1;
OS Lolium latent virus (isolate Lolium/USA/US1/-) (LoLV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Lolavirus.
OX NCBI_TaxID=686945;
OH NCBI_TaxID=480553; Lolium multiflorum x Lolium perenne.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Vaira A.M.V., Maroon-Lango C.J., Hammond J.;
RT "Molecular characterization of Lolium latent virus, proposed type member of
RT a new genus in the family Flexiviridae.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; EU489641; ACA53374.1; -; Genomic_RNA.
DR RefSeq; YP_001718499.1; NC_010434.1.
DR PRIDE; B1PS76; -.
DR GeneID; 6000098; -.
DR KEGG; vg:6000098; -.
DR Proteomes; UP000008689; 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; 1.
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 Nucleotide-binding; Nucleotidyltransferase; Oxidoreductase;
KW Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1729
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000401073"
FT DOMAIN 59..232
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 741..834
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 957..1111
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1112..1247
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1492..1599
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 528..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 759
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 761
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 816
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 825
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 1729 AA; 196119 MW; 2DA0091740FF7866 CRC64;
MTTLALNLAQ YNDPITKGII AQESLRRVRP DLKAVVNVNP YAIPTSAALV LEKLGIGTHP
MSLAVHPHAP CKAIENQILN TVGHLLPKEQ PVTFMAMKKS KLNMLRRHPS RADTFINPIY
HPRDNVRYGL DPDPDQDASI TASFLEVKTS TAFMQDTLHY LTPEDLLDIF ETSPKLENLI
ASFVLPVEAT RNMKSLYPDL YSIHYTHGGF QWAPSGHLGD AYFHEPWQLY WLRCGSLTRL
IEEETTTTVQ PPPGFEGEAY TRVRKEVREL KIYAERVTSI GAHHLFIFSR NAKATPRVRS
YSQNGKWVTL PRIFRPVSHN VQTPLKQEVA NSLMLYTYAV RPSLKDVAAK VRQKFDEKDL
AEHSPLEITH LINYIYYIDQ RAYLTNDDDI LSDNLLKRWI FTPIQAAYKK AKGFLLGPDD
FQKLLKALEW QPVTFDYAVD HYKSNPWRIH ASRTGAKMRQ LKNFLSRTTG LCEAVEDDAL
EGSELLKELE GNMWFRNPSE VEKEVFDAIV ADLPPDSQRS ELILEDPNSN ARDYLPIQQD
QPSVTQGPDE AAQTQTPTAT SMVTNSVAAR MPPPVPRTLR EHHEQFPTTV RASFEQPSST
RAPETSENNT PAESVTPSPR AIYVGDFAIM DANASTSRAS SPSPRRTVVS PRQPEAQNET
LGRQIVSRVS PAHGCQMSPY AAQLAHQLSE QTAYTDVIGQ RMVAFYSQHS RSYKYGRHEH
RSQSWLPVID SLQVALGLDE SYDHCLIQRY RKHARVGLHA DDEECYEPDS TIVTLNLYGN
ADFLIERNTD KASETITLQH NDMLFMPSGM QVTHRHAVCS LYEGRVSITF RNKTKDYLRK
SAPDMNPVEQ PGASAGQLTG PLDHRPEELP WEHWIPRLNR LGFTGLQKQT DPEGKLIYPI
TEIRQDMVYV PFPNCCPGPL RKDLEAMGRR PVRYTVDTGR ALTLASDIKN NRVGALLQNA
DLTWKTLLVE YCRMEPTSVP MTVIHGAGGS GKSKLLQDHL NRAELNVVII VPTRVLQQDW
RNKMTEFPSF LVQTYEAAMM ESAPQMVVFD DYGKLPHGYI DLFCQFHPSV EYVILTGDAR
QSTYYEYNSD AGIRNLPTNI EVFKQYCGYY INCTHRNKQD LANMLGVYSE KMGSTHFTFG
NTCETGSLLL VPSGTQKTVM GEAGHKTETY AGCQGITADK VQIMIDHDTH KSADSHMYTA
LSRATEHIHF YNSIAGLNTA RFHAKLNLTP YLKTFIQVIT ERAAAETEPA EYTVQAPTAR
THIPVENCST FLEKDLEEQR AKEDREVYTQ AGATNVFQTN SPIVQCFQHQ QPKDGALSII
THAKRLQYAS AEANQAEYRA KLQIGAALWE NFKTAMEIPD EPVPFIRDLW EQSEAEVLST
YLSKSEMAIK NGKNRQDPDW QDERMFVYLK AQWVTKASKF NLPTAKAGQT ISAFKQAVVM
KFGAMARYLR RITPKPDNIR INCEMQPQDI SKWALGLDSH NRPTKQKWNF ERPAFASDFE
AFDQSQDGAM LHFEALWARH FNVPSSLIEE YLFLKMHAQA PKGYLTIMRL TGEGPTFDAN
TACSIAYNHT RYEIPKSCMQ LYAGDDMLLD QVPVEKTGFK NIAAGLKLTA KTEIFEQKRG
KWGEFCSWWM TPYGLVKDPI TLYHRILLAS EIGDLSKKID AYAIEAEPAY ALQGRLFDCF
NEEQMTAHYG TIRRLIIEGK TNFSLDDQAP RHQDLQGILN CMDAKFMYH
