RDRP_NMV
ID RDRP_NMV Reviewed; 1643 AA.
AC P15095;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=RNA replication protein;
DE AltName: Full=186 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 Narcissus mosaic virus (NMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12180;
OH NCBI_TaxID=39639; Narcissus pseudonarcissus (Daffodil).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2732689; DOI=10.1099/0022-1317-70-2-267;
RA Zuidema D., Linthorst H.J.M., Huisman M.J., Asjes C.J., Bol J.F.;
RT "Nucleotide sequence of narcissus mosaic virus RNA.";
RL J. Gen. Virol. 70:267-276(1989).
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 potexvirus/carlavirus RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; D13747; BAA02891.1; -; Genomic_RNA.
DR PIR; JT0470; RRWGNV.
DR RefSeq; NP_040778.1; NC_001441.1.
DR PRIDE; P15095; -.
DR GeneID; 1494016; -.
DR KEGG; vg:1494016; -.
DR Proteomes; UP000008865; 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 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; 1.
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..1643
FT /note="RNA replication protein"
FT /id="PRO_0000222549"
FT DOMAIN 59..224
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 828..996
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 997..1132
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1372..1479
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 686..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 868..875
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1643 AA; 186305 MW; ADAE6FCF0FF2EC43 CRC64;
MAKVRAALER IRDPSVQTAL SEAAYTHVRP VLKESLVNCP YALSNDEADC LESFGITVNP
YANQTHTHAA CKVIENRMLE IVGMHLPKHS CTMLFLKRSK LRYMRRAAIL KDVFLNKDVE
PKDLFRYDRD TIRSRLQDID TKIAYMSDTL HFMSRREIVQ LFEDSPKLET LLATVVLPVE
ALHKRTSLYP SLYSINYSAK GFEYIPGNHG GGSYFHPYTT LEWLKVRMIN AEDFHKLSTG
FILTFQLVES LGANHLFIVQ KAKLLTPQMR TFCRDSLVTL PQVFCPAAMN ANRPLSKTKA
MQMLLYCKSV KQVTERDIYA KIRQIIPTSE LELYDPDEIV HLANYFFFVS SLDSITCYED
LLSSDIWMRL TRPLRTAVRK FVELFKGKQD FDKLLIALKW QPFSYSLEPV DFTAYFVSRR
VRTLAKMEDI SWHQAAELAR RLESEPDLLS WEDLCSKPIA DPLASVSTPP LATLTSPAIS
ESRVTDTSSP KLTNISVESI LHPTSSNHAT IAESLNPKFC GWTRGDFHHM IVNQPSDRLK
GCRSWSYTTS PDVDLMLENL LLTPIPWESR LSDILLTLNT PANACCIQIL DCSAASAWVD
WSVQPIKTFP VAFVGMGETT LTFEDDSTLP LKEGEFVFFP PEWLARHKYQ IKTASNLHLC
ATFLVLDTTL LGETLANNCI EPEPLRPTAS RKSCQPTPSV DKSGADSPPE KQIVTPIVDA
AVLSCRPKLQ DVTKPTKVLM AAETSDSVAD SLPWASWVNL LQKHGFKGNQ QQIAQDGQLI
IPISDIRKLP HIPFPEEVPE TLRETLKNIK RFPVEITMQH KRAGSYDSDI KNNRTGKLLS
QMDNKWKAAF AYKLQQEDRK VCGTIIHGCG GSGKSFAIQE WMRSLKEDQS VVTVVTPTVL
LRNDWQTKLP ILPADVFKTF EKSVIQPCNP ILVFDDYTKL PPGLIESVVM HHQNVVFIIL
TGDNRQSVYH ETNPEAYIAA LPEAVEIFSP YCEFYLNATH RNVKDLANKL GVYSEREGKL
KVNFASHHLK ASRIPMLVPS TMKRNAMFDM GHHSMTYAGC QGLTAPKIQI LLDNHTQFCS
ERVLYTCLSR AVDRIHFINT GPTTGDYWAK LESTPYLKAF IDTYRDEKTE VYNSQPASAE
PTEPEAPATH FPTAPKPLLE PLVEKLTDKE AREIFSPAFG HSNAIQTEDS VVQLFQHQQA
KDETLYWATI DTRLAISTPE ANLREFNMKR DIGDILFMNY AKLMCLPPEP VPFEERLWKI
SADEVRNTYI SKPIGNLVNA ASRQSPDFPK NKIALFLKSQ WVKKTEKLGT LKVKPGQTIA
SFMQETVMLY GTMARYLRKM RRRFQPDNIF INCETTPEDL DKFIKSQWDF SRPAHTNDFT
AFDQSQDGAM LQFEVIKAKF FNIPAEIIEG YIYIKLNAAI FLGTLGIMRL SGEGPTFDAN
TECSIAYNAT RFHITDDTAQ VYAGDDMALD RVSIEKDSFN RLEKQLKLTS KPMFPKQVKG
DYAEFCGWVM TPAGIIKHSL KMHASIQLQK KINNIKESAR SYALDLRYAY KLGDELQEHL
NEVEADYHQQ SVRDMHLLHQ QDVLNKGSAS PPHVFEKTAD ANTAGSSKTH KRNALKKKKQ
TRIAEILPSP DATGLSSLPF RFF