RDRP_PVX
ID RDRP_PVX Reviewed; 1456 AA.
AC P09395;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=RNA replication protein;
DE AltName: Full=165 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 Potato virus X (PVX).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12183;
OH NCBI_TaxID=3711; Brassica campestris (Field mustard).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3205733; DOI=10.1093/nar/16.22.10929;
RA Skryabin K.G., Kraev A.S., Morozov S.Y., Rozanov M.N., Chernov B.K.,
RA Lukasheva L.I., Atabekov J.G.;
RT "The nucleotide sequence of potato virus X RNA.";
RL Nucleic Acids Res. 16:10929-10930(1988).
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; M72416; AAA47167.1; -; Genomic_RNA.
DR Proteomes; UP000006841; 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..1456
FT /note="RNA replication protein"
FT /id="PRO_0000222553"
FT DOMAIN 59..224
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 695..862
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 863..997
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1236..1343
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 537..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 735..742
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1456 AA; 165407 MW; F09FDF47E298988C CRC64;
MAKVREVYQS FTDSTTKTLI QDEAYRNIRP IMEKHKLANP YAQTVEAAND LEGFGIATNP
YSIELHTHAA AKTIENKLLE VLGSILPQEP VTFMFLKPRK LNYMRRNPRI KDIFHNVAIE
PRDVARYPKE TIIDKLTEIT TDTAYIGDTL HFLDPSYIVE TFQNCPKLQT LYATLVLPVE
AAFKMESTHP NIYSLKYFGD GFQYIPGNHG GGAYHHEFSH LQWLKVGKIK WRDPKDSFLG
HLNYTTEQVE MHTVTVQLQE SFAANHLYCI RRGDLLTPEV RTFGQPDRYV IPPQIFLPKV
HNCKKPILKK TMMQLFLYVR TVKVAKNCDI FAKVRQLIKS SDLDKYSAVE LVYLVSYMEF
LADLQATTCF SDTLSGGLLT KTLAPVRAWI QEKKMQLFGL EDYAKLVKAV DFHPVDFSFK
VETWDFRFHP LQAWKAFRPR EVSDVEEMEN LFSDGDLLDC FTRMPAYAVN AEEDLAAIRK
TPEMDAGQEV KEPAGDRNQY SNPAETFLSK LHRKHSREVK HQAAKKAKRL AEIQESMRAE
GEAESNEMSG GMGAIPSNAE LPSTSGARQE LTLPTTKPVP ARWEDASFTD SSVEEEQVKL
PGKEAVETAT QQVIEGLPWK HWIPQLNAVG FKALEIQRDR SGTMIMPITE MVSGLEKEDF
PEGTPKELAR ELLAMNRSPA TIPLDLLRAR DYGSDVKNKR IGAITKTQAA SWGEYLTGKI
ESLTERKVAA CVIHGAGGSG KSHAIQKALR EIGKGSDITV VLPTNELRLD WSKKVPNTEP
YMFKTYEKAL IGGTGSIVIF DDYSKLPPGY IEALICFYSK IKLVILTGDS RQSVYHETAE
DASIRHLGPA TEYFSKYCRY YLNATHRNKK DLANMLGVYS ERTGVTEISM SAEFLEGIPT
LVPSDEKRRL YMGTGRNDTF TYAGCQGLTK PKVQIVLDHN TQVCSANVMY TALSRATDRI
HFVNTSANSS AFWEKLDSTP YLKTFLSVVR EQALKEYEPA EAEPIREPEP QTHMCVENEE
SVLEEYKEEL LEKFDREIHS ESHGHSNCVQ TEDTTIQLFS HQQAKDETLL WATIDARLKT
SNQETNFREF LSKKDIGDVL FLNYQKAMGL PKERIPFSQE VWEACAHEVQ SKYLSKSKCN
LINGTVRQSP DFDENKIMVF LKSQWVTKVE KLGLPKIKPG QTIAAFYQQT VMLFGTMARY
MRWFRQAFQP KEVFINCETT PEDMSAWALN NWNFSRPSLA NDYTAFDQSQ DGAMLQFEVL
KAKHHCIPEE IIQAYIDIKT NAHIFLGTLS IMRLTGEGPT FDANTECNIA YTHTKFDIPA
GTAQVYAGDD SALDCVPEVK HSFHRLEDKL LLKSKPVITQ QKKGSWPEFC GWLITPKGVM
KDPIKLHVSL KLAEAKGELK KCQDSYEIDL SYAYDHKDSL HDLFDEKQCQ AHTLTCRTLI
KSGRGTVSLP RLRNFL