RDRP_PVXCP
ID RDRP_PVXCP Reviewed; 1456 AA.
AC P22591;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 (strain CP) (PVX).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12184;
OH NCBI_TaxID=3711; Brassica campestris (Field mustard).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2392880; DOI=10.1016/0168-1702(90)90054-f;
RA Orman B.E., Celnik R.M., Mandel A.M., Torres H.N., Mentaberry A.N.;
RT "Complete cDNA sequence of a South American isolate of potato virus X.";
RL Virus Res. 16:293-305(1990).
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; M31541; AAA47178.1; -; Genomic_RNA.
DR EMBL; X55802; CAA39324.1; -; Genomic_RNA.
DR PIR; S14005; S14005.
DR Proteomes; UP000008615; 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_0000222554"
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 474..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
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; 165301 MW; 489BA57EA070BD2E CRC64;
MAKVREVYQS FTDSTTKTLI QDEAYRNIRP IMEKHKLSNP YAQTIEAAND LEGFGIATNP
YSIELHTHAA AKTIENKLLE VLGSLLPQEP VTFMFLKPRK LNFMRRNPRI KDIFHNVAIE
PRDVARYPKE TIIHKLAEIE TDTAYISDTL HFLDPSYIVE TFQNCPKLQT LYATLVLPSE
AAFKMESTHP NIYSLKYFGD GFQYIPGNHG GGAYHHEFTD LQWLKVGKIK WRDPKDGLLG
HLNYTHEQVD THTVTVQLQE SFAANHLYCI RRGNMMTPEV RTFGQPDRYV LPPQIFLPKV
HNCKKPILKK TMMQLFLYVR TVKVAKNCDI FAKVRQLIKS SDRDKFSAVE LVYLVSYMEF
LAALQATTCF SDTLSGGLLT KTLAPVRAWI QEKKMQLCGL EDYVKLVKAV DWRPVDFSFK
VETWDFRFTQ LGMWKAFQPS ELSDVEEMNN FFDDGDLLDC FTRMPAYAVN AEEDLAGMRG
NNQEETSTAP REPEGEKKEY INPAETFLDK LTRKHNRETR SRAAKKAKRL AEIQDSMNRD
RTEEGSHKTP NMGEAPSNAD LPGVNEVEAG TTFPTLKALP QKWEDASSTD SSTIDPTEII
PGEEDDKAAT QKVVVGLPWK HWLPQLNAVG FKALEIQRDR NGTMIMPITE MVFGLDKEEF
PEGTPEALAR ELKAMNRSPT TIPLDLLRAR DYGSDVKNKR IGAITKTQAA SWGEYLTGKI
ESLPERKVAA CVIHGAGGSG KSHAIQKALR EIGKGSDITV VLPTNELRLD WSKKVPNTEP
YMFKTYEKAL IGGTGSIVIF DDYSKLPPGY IEALVSFSTK IKLIILTGDS RQSVYHETSD
DASIRHLGPA TEVFAKYCRY YLNATHRNKK DLANMLGVYS ERTGTTEISM SSEFLEGVPT
LVPSDEKRRL YMGTGRNDTF TYAGCQGLTK PKVQIVLDHN TQVCSANVMY SALSRATDRI
HFINTSANSS AFWEKLDSTP YLKTFLSVVR EHALKEYEPA EAEPIKEPEP QTHMCVENEE
SVLEEYKEEL LEKFDREIHS DAHGHSNCVQ TEDTTIQLFS HQEAKDETLL WATIDARLKT
SNQESNFREF LSKRDIGDVL FLNYQKAMGL PKEPIPFSQE VWEACAHEVQ SKYLSKSKCN
LINGTVRQSP DFDENKIMVF LKSQWVTKVE KLGLPKIKPG QTIAAFYQQT VMLFGTMARY
MRWFRQAFQP KEVFINCETT PEDMSAWALS NWNFTRPSLA NDYTAFDQSQ DGAMLQFEVL
KAKHHCIPEE IIQAYIDIKT NAQIFLGTLS IMRLTGEGPT FDANTECNIA FTHTKFDIPA
GTAQVYAGDD SALDCVPEVK QSFHRLEDKL LLKSKPVITQ QKKGSWPEFC GWLITPKGVM
KDPIKLHVSL KLAEAKGELR KCQDSYEIDL SYAYDHKDSL HDLFDEKQCQ AHTLTCRTLI
KSGRGTVSLP RLKNFL