RDRP_FXMV
ID RDRP_FXMV Reviewed; 1335 AA.
AC P22168;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=RNA replication protein;
DE AltName: Full=152 kDa protein;
DE AltName: Full=ORF1 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;
OS Foxtail mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12179;
OH NCBI_TaxID=4555; Setaria italica (Foxtail millet) (Panicum italicum).
OH NCBI_TaxID=4556; Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1840610; DOI=10.1099/0022-1317-72-9-2173;
RA Bancroft J.B., Rouleau M., Johnston R., Prins L., Mackie G.A.;
RT "The entire nucleotide sequence of foxtail mosaic virus RNA.";
RL J. Gen. Virol. 72:2173-2181(1991).
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 -!- SIMILARITY: Belongs to the potexviruses/carlaviruses RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; M62730; AAA43826.1; -; Genomic_RNA.
DR PIR; JQ1258; JQ1258.
DR RefSeq; NP_040988.1; NC_001483.1.
DR SMR; P22168; -.
DR PRIDE; P22168; -.
DR GeneID; 1494009; -.
DR KEGG; vg:1494009; -.
DR Proteomes; UP000008623; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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; 3.40.50.300; -; 1.
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; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
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; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT CHAIN 1..1335
FT /note="RNA replication protein"
FT /id="PRO_0000222548"
FT DOMAIN 58..225
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 564..729
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 730..863
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1102..1209
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 428..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 603..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1335 AA; 152318 MW; D2ECBBA932F49DB9 CRC64;
MSIEAVFDQV TDPSLRAVIQ EEAHKQIKDL FKETTRCNPY SIPQAGRKVL EKYAIPYNPY
SLKLHPHAAS KAFEVSLYEA ASNYLPSTSS TPVTFMFTKP GKLRFFRRRG HVDKFVNADI
VPRDLARYPR DTVYSYLPEI TTTHAFIGDT LHHFGEDFLV EVFSRSPKLE VLLATMVLPP
EAFYRMESLH PSVYTLLYRD DRFLYLPGGL SGGEYEHRYK DLNWLTFGTV THGGITITGE
RIETKAANHL FLFRRGRLAT PKFRSFDMPE PMVLLPKVFR PAKYNVQKPI PREKANKWLM
YVKSIGNATI RDVWAKLRQT IANADIGLFS PTELVHLTNY FLLLGRLDSH NSFDQVLADS
VLKAWFRPMV AKLQEIKHKL MGQTQFMQLC QALEMTEVDL VFEVRDSKTP HKQAVPLDRE
IENVLLEGVS SEPTYTETEG VADGPLPPPM QTAAEPSATS DEPESSSSRE IEHQPAPEIT
LDEEEPQRDD LPWDAWRTQL RALGFEASER QYDPDGELIS PILSTRRLPK TPIDTTLYAT
LDKIARCPTF YKPDTDRAQT YARDVMAGKT GAILKQQPFE WKTTLKRKTK EEPKEIHLAV
LHGAGGSGKS YALQEFMRNN SDTPITVILP TNELRADWKK KLPAHDKDTF MTYENALLCP
RGDIFIMDDY TKLPRGYIEA FVQNAPALSL LILTGDPNQA EHFETTEDNE INSLAPASVV
FGKFSRYHIN ATHRNPRNLA NALGVYSETP GEVKVLYTRN IKTGYHNLVP SQMKMRNYAS
LGQRASTYAG CQGITAPRVQ IILDSDTPRC TRQVMYTALS RATTEVVLCN TMPDEKSFFQ
KVEATPYLKA ILNLNKEIKV TEGDLTEEPP REPAPPTTHL PVENRIILNE ALVEPLPDKH
DREIYSNSTG FSNCIQTQDP YIQAFQHQQA KDETLFWATV EKRLAASTPK DNWTEFKTKR
PLGDVLWLAY KRAMVLPDEP IKFNPELWWA CADEVQKTYL SKPIHALKNG ILRQSPDFDW
NKLQIFLKSQ WVKKIDKIGK IDVNAGQTIA AFYQPTVMLF GTMARYMRRI RDTYQPGEIL
INCEKNQKHI SKWVESNWNH RLPAYTNDFT AYDQSQDGAM LQFEVLKALH HDIPHEVVEA
YVALKLNSKM FLGTLAIMRL TGEGPTFDAN TECNIAYTHA RFEIPKNVAQ MYAGDDCALN
CRPVERQSFL PLVEKFTLKS KPKVFEQKVG SWPEFCGNLI TPRGYLKDPM KLQHCLQLAQ
RKKPSEPGSL KDVAENYAMD LLPTYELGDA LYEIFDERQM NAHYQSVRTL ITCAHTKVLR
VAQALQEDCT FFSSI