RDRP_SMYEA
ID RDRP_SMYEA Reviewed; 1323 AA.
AC P28897;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=RNA replication protein;
DE AltName: Full=150 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 Strawberry mild yellow edge-associated virus (SMYEaV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12187;
OH NCBI_TaxID=63459; Chenopodium quinoa (Quinoa).
OH NCBI_TaxID=57918; Fragaria vesca (Woodland strawberry) (Potentilla vesca).
OH NCBI_TaxID=59498; Rubus rosifolius.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=MY-18;
RX PubMed=1339469; DOI=10.1099/0022-1317-73-2-475;
RA Jelkmann W., Maiss E., Martin R.R.;
RT "The nucleotide sequence and genome organization of strawberry mild yellow
RT edge-associated potexvirus.";
RL J. Gen. Virol. 73:475-479(1992).
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; D12517; BAA02082.1; -; Genomic_RNA.
DR PIR; JQ1426; RRWGSM.
DR RefSeq; NP_620642.1; NC_003794.1.
DR GeneID; 944372; -.
DR KEGG; vg:944372; -.
DR Proteomes; UP000007225; 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; 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..1323
FT /note="RNA replication protein"
FT /id="PRO_0000222557"
FT DOMAIN 60..224
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 572..733
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 734..867
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1104..1211
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 432..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 605..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1323 AA; 149594 MW; D6BC35133E3CAD26 CRC64;
MATRVASVFS SLTDVGIKAA LQDEAYKRIK SNLREAEIIN PYSVDARGAE ALEELAIITN
PHSIRLHTHA AAKSIENQML NIVGHALPKE PVTFLFLKRG KLRYLSRGRI KDIFQNQEIE
PRDVARYEHK TIVQKSLLLN TRVAYISDTL HFLRPRYIID LFSQNVFLDV LYATVVLPVE
ASFKHPSQNP AIYTINYNYG GFQYLPGNHG GGAYSHEFED LDWLKYGKFI YRWVDYRTDP
ISGKRVGTPK ELVVTCQLVE SLGANHLFIF KRGDLKTPRV RTFAKDKSVT FPDLFYPEEE
NANFPVDAEL ATKLFLYVKT LKTVTSQDVH GKLRQLLRSD ELTRFSPMQL THMVNYFMVV
AHLDSCNDYS MLLGSSVWTQ LTAPIQSKLR KLTEFFKGKS SFGKFCAALK WKTATYSLEV
VDYVETRRDS FEPHPLDSLP DADDRDVNYD TDVSEDEADE KPAPKAPTST PVPDTTPPAS
PAAPADAEYT QCWAAWDTVI RKHGFKGNQA QFDDDGNLIT PIAEIKSLPK DSPRCAPELI
KSLQEIARTP TLVEIDSKRS NAFGSDVKNG RIGMILKKQP NDWRLSFAAK CEHTSRKVHA
CVIHGAGGSG KSQRLQDWMR SLKKNSRECT VILPTAELRT DWVNKVPKQS LDTFKTWEKG
LVQPPNRVVI LDDYGKLPAG YPEALCANYP NIELLILTGD SRQSVHNEHN KQAATASLES
NIEFWTQYCR FYVNATHRNV KRLANALGVY GERDEPLKVT CSSHVYDGWP VLAPGLLKAG
NLAECGRRAF TYAGCQGLTA PRVQILLDND TPLCSQRVMY TALSRAVNEI HFVNTGPSGD
DFWTKLDCTP FLKTFLELSR EIEIPEAKCQ ETAPAEATVK THFPVENPNL VLEPYVEKMA
EKFDRELYSK EYGYSNAIQT EDPVIQLFPH QQAKDDTLMW ATIDQRLAIT TKSENETEFA
LKKDIGDLLF INYHRAMKLP KNPIPFDKDL WQSCKNEVQK TYLSKDVGSI VNGVARQDPD
FPINEIKLFL KSQWVKKVEK LGMVVKPGQT IASFAQAPVM LYGTMARYMR RMREVYQPSN
IFINCEKTPA DLDEWAKANW NFEGLAHSND FTAFDQSQDG AMLQFEVIKA KFHNIPSDII
NSYVELKTNA KVFLGVLKIM RLSGEGPTFD ANTECSIAYH HTKYWVEPDV AQVYAGDDSA
QDRTPVPRPS FNKIKDRLGL VSKPLTHRQV PGDFATFCGW IITPKGVIKD PLKLYASLQL
AIRRGKSHEV ALSYAHDAGL AYRLGDDLHS VLTFDEAHAH QCTVRDLVKL NKVEVLRPIW
ALD
