ID   POLR_ELV                Reviewed;        1748 AA.
AC   P35928;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=RNA replicase polyprotein;
DE            EC=2.7.7.48;
OS   Erysimum latent virus (ELV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Tymoviridae; Tymovirus.
OX   NCBI_TaxID=12152;
OH   NCBI_TaxID=65352; Erysimum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1607861; DOI=10.1099/0022-1317-73-6-1437;
RA   Srifah P., Keese P., Weiller G., Gibbs A.;
RT   "Comparisons of the genomic sequences of erysimum latent virus and other
RT   tymoviruses: a search for the molecular basis of their host
RT   specificities.";
RL   J. Gen. Virol. 73:1437-1447(1992).
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   -!- SIMILARITY: Belongs to the tymovirus NS35 RNA replicase polyprotein
CC       family. {ECO:0000305}.
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DR   PIR; JQ1555; JQ1555.
DR   RefSeq; NP_047920.1; NC_001977.1.
DR   GeneID; 1493964; -.
DR   KEGG; vg:1493964; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; 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   Gene3D; 3.90.70.100; -; 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; IPR008043; Peptidase_C21.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR043629; Salyut_dom.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   InterPro; IPR043181; TYMV_endopept_dom.
DR   Pfam; PF05381; Peptidase_C21; 1.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF19227; Salyut; 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; PS51738; PEPTIDASE_C21; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW   Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1748
FT                   /note="RNA replicase polyprotein"
FT                   /id="PRO_0000222933"
FT   DOMAIN          58..219
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          627..781
FT                   /note="Peptidase C21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   DOMAIN          844..1001
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          1002..1138
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1474..1580
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          433..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..598
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        680
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   ACT_SITE        766
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   BINDING         874..881
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1748 AA;  193908 MW;  A9CA5DE87D64A3AA CRC64;
     MAFQLALDAL SSTTHRDSIS APLLDSSVSQ LQSSLELFPY TVPKELVPQL NRMGIQVSGL
     TSTPHPHAAH KTLELNLLFN HWAKSCNVDS AVVFMKPSKF FKLQEKNSHF KSLHNYRLHP
     HDSNRYPHPS TSLPTEKRFY IHDSLMYFTP HQISGLFESC PNLLSLYASL VVPPESSMTD
     LSLNPDLYRY SIHKSTLHYT PEGHSAGSYN QPVNALDWLK ISAIQTPSLS LSVSVLESWG
     PLHSLLIERS SQTQNPDSQK IKDLISFQTP QALILPNPDS LAVPLRHRLV PQKTYDALFT
     YTRATRTLRT SDPAGFVRTQ SNKPEFNWVT SQAWDNLQTY ALLTASYRPP VSYTLHRSPL
     TKLKELLTRN ALKLAAMASP ALTLAIFTTM TALNTNSSKA LSFSALKIHL LNPLTGPELL
     HFQTSVLQQK NSAPLSQAEA KQELDKSAVP APSEHDSSAS QSTSLSLSAS SQLLSTEKHP
     GSELSSKAIP VSTSCPSASK QLAPPLTAES HSSVNALLRK FLGPNSPQSN LDNYNLHLHP
     ESFTLGWKRR PLLLDSHSSF LPSSCLQPPA SPSIAAAPHP LPPAQKPPRP PTTVPTPKPL
     ASPSQTQAAQ PATQSPPSIP QTAPVTSLLP APLETDDSCA GPISTFQDLF PASYYPHTAN
     FPCRSKIPGY LEAPYPPLDC MLVALSAQMP QSPQELWSAL NTLMPLSALT SPSLRVLGLG
     TEELTALSYY YHFQAEIHSD NEIYRFGIQT ASTKLCLIRD SGPPAHFTAP DPLRAGSPPS
     RSQTNENSLR RSLLGFRLNG NLLPIDQVHS FTSEPSRAKN LASNMKNGFD GILTTLAALS
     SLSSGPSPRD RIFTLDGICD FALPKTVDLI HLSGFAGCGK THPIQQLLKT PHFHNFRVVT
     PTTNLRSEWK SDMALPAHHN WRFSTWESAL LKHAEILVID EIYKLPRGYL DLSLIADPTV
     KLVILLGDPL QGEYHSTSAH SSNLRLSSEI PRLLPFIDYY CYWSYRVPKC VAKLFSLPCF
     NPSEGFIKTT LDFFPSANNL VNSHSVVHIS EACGWNAVTI SSSQGCTFSD PAFIHLDRNT
     ALLSPSNCLV ALTRSRSGVY FKGDFTFLSS LSGSSRMFSL AYSGQPIHLP DFFPEIVFQL
     NMITAPLTKR SSSFRSGFQP NISSAPKIPA PPNLPCPPHI PTNYSKDVIV NNQALYGESL
     ERRLSVLHLP PTRMTLHSDI NITAPSSSSF QPSDEPVPSD HTAVYPGFDF FTLAAHFLPA
     HDPEVKEIEL KDQTSQQFPW LNLDFHISCQ TSSLISARHQ PGSDSTLLPA SLHKRLRFRP
     TAAPYQITPS DSFLGNCLYR SWCQVYRRDP NVRLPFNEAL FLECIAVNDY AQLSSKTQAT
     IVANASRSDP DWRHTFVKIF AKSQHKVNDG SIFGPWKACQ TLALMHDYVI LTLGPVKKYQ
     RLFDQLERPS HIYYHAGNTP HDLRRWCSKH LETSHCTTND YTAFDQSQHG EAVVFEVLKM
     RRLSIPENLI SLHVHLKTNV ETQFGPLTCM RLTGEPGTYD DNTDYNLAVL NLQYDLRKTP
     TLVSGDDSYL SGTLSPRSNW PFVKELLHLR LKPSSLIDGL FCGYYLGPQG CIRNPLALFA
     KLMIAEDDGS AFDKLPSYLT EFSIGHGLGD SLWQLLPSDL VLYQSACFDY FCRKATRSQK
     ILLQPGLVDQ ETLDKIALSA KFISRPFYSM LSSHARSLIS TKFKLDSSLT TLQDPMVEFE
     LLPFSNVQ