ID   POLN_TYMVA              Reviewed;        1844 AA.
AC   P20128;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Non-structural replication polyprotein {ECO:0000305};
DE   AltName: Full=206 kDa polyprotein;
DE   AltName: Full=206K;
DE   Contains:
DE     RecName: Full=Methyltransferase/Protease/Ubiquitinyl hydrolase;
DE              EC=2.1.1.-;
DE              EC=3.4.19.12 {ECO:0000250|UniProtKB:P10358};
DE              EC=3.4.22.-;
DE     AltName: Full=98 kDa protein;
DE     AltName: Full=MET/PRO;
DE   Contains:
DE     RecName: Full=Putative helicase;
DE              EC=3.6.4.-;
DE     AltName: Full=42 kDa protein;
DE     AltName: Full=HEL;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE     AltName: Full=66 kDa protein;
DE     AltName: Full=POL;
OS   Turnip yellow mosaic virus (isolate Australia).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Tymoviridae; Tymovirus; Tymovirus brassicae.
OX   NCBI_TaxID=12155;
OH   NCBI_TaxID=3705; Brassica.
OH   NCBI_TaxID=82359; Cardamine lilacina.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2800335; DOI=10.1016/0042-6822(89)90196-7;
RA   Keese P., Mackenzie A., Gibbs A.;
RT   "Nucleotide sequence of the genome of an Australian isolate of turnip
RT   yellow mosaic tymovirus.";
RL   Virology 172:536-546(1989).
CC   -!- FUNCTION: [Methyltransferase/Protease/Ubiquitinyl hydrolase]: Acts as a
CC       cysteine protease, methyltransferase and deubiquitinase. The cysteine
CC       protease activity cleaves the polyprotein giving rise to mature
CC       proteins. The protease has the ability to process substrates in trans.
CC       The methyltransferase domain is probably involved in viral RNA capping.
CC       The deubiquitylating activity counteracts the degradation of the viral
CC       polymerase mediated by the host ubiquitin-proteasome system. The
CC       polymerase is thus stabilized and infectivity is increased. Favors K63
CC       poly-Ub linkage. {ECO:0000250|UniProtKB:P10358}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: RNA-directed RNA polymerase is
CC       responsible for the replication and transcription of the genome.
CC       {ECO:0000250|UniProtKB:P10358}.
CC   -!- CATALYTIC ACTIVITY: [Methyltransferase/Protease/Ubiquitinyl hydrolase]:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:P10358};
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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   -!- SUBUNIT: [Methyltransferase/Protease/Ubiquitinyl hydrolase]: Interacts
CC       with host ubiquitin. {ECO:0000250|UniProtKB:P10358}.
CC   -!- SUBCELLULAR LOCATION: [Methyltransferase/Protease/Ubiquitinyl
CC       hydrolase]: Host chloroplast envelope {ECO:0000250|UniProtKB:P10358}.
CC   -!- SUBCELLULAR LOCATION: [Putative helicase]: Host chloroplast envelope
CC       {ECO:0000250|UniProtKB:P10358}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host chloroplast
CC       envelope {ECO:0000250|UniProtKB:P10358}.
CC   -!- DOMAIN: [Methyltransferase/Protease/Ubiquitinyl hydrolase]: The viral
CC       OTU domain (vOTU) is responsible for the deubiquitination activity.
CC       Both protease (PRO) and deubiquitination (DUB) activities rely on the
CC       single catalytic site of the cysteine proteinase. The switch in the
CC       PRO/DUB activities is due to the mobility of a GPP flap.
CC       {ECO:0000250|UniProtKB:P10358}.
CC   -!- PTM: Specific enzymatic cleavages by the host yield mature proteins.
CC       {ECO:0000250|UniProtKB:P10358}.
CC   -!- MISCELLANEOUS: [Methyltransferase/Protease/Ubiquitinyl hydrolase]: The
CC       deubiquitinase activity is low compared to that of Bunyaviruses or
CC       coronaviruses. {ECO:0000250|UniProtKB:P10358}.
CC   -!- SIMILARITY: Belongs to the Tymoviridae non-structural replication
CC       polyprotein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J04373; AAA46592.1; -; Genomic_RNA.
DR   PIR; JQ0109; RRWPTM.
DR   MEROPS; C21.001; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
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 RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0016556; P:mRNA modification; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0039648; P:symbiont-mediated perturbation of host ubiquitin-like protein modification; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23247; Tymoviridae_RdRp; 1.
DR   Gene3D; 3.90.70.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR001788; RNA-dep_RNA_pol_alsuvir.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR043629; Salyut_dom.
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; SSF56672; DNA/RNA polymerases; 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; Host-virus interaction; Hydrolase; Methyltransferase;
KW   Modulation of host ubiquitin pathway by viral deubiquitinase;
KW   Modulation of host ubiquitin pathway by virus; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Protease;
KW   RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1844
FT                   /note="Non-structural replication polyprotein"
FT                   /id="PRO_0000222939"
FT   CHAIN           1..879
FT                   /note="Methyltransferase/Protease/Ubiquitinyl hydrolase"
FT                   /evidence="ECO:0000250|UniProtKB:P10358"
FT                   /id="PRO_0000455969"
FT   CHAIN           880..1259
FT                   /note="Putative helicase"
FT                   /evidence="ECO:0000250|UniProtKB:P10358"
FT                   /id="PRO_0000455970"
FT   CHAIN           1260..1844
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000250|UniProtKB:P10358"
FT                   /id="PRO_0000455971"
FT   DOMAIN          58..219
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          728..879
FT                   /note="OTU"
FT                   /evidence="ECO:0000250|UniProtKB:P10358"
FT   DOMAIN          730..884
FT                   /note="Peptidase C21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   DOMAIN          946..1103
FT                   /note="(+)RNA virus helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          1104..1236
FT                   /note="(+)RNA virus helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          1572..1678
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          571..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           865..867
FT                   /note="GPP flap"
FT                   /evidence="ECO:0000250|UniProtKB:P10358"
FT   COMPBIAS        631..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..736
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        783
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   ACT_SITE        869
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   BINDING         976..983
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   SITE            879..880
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P10358"
FT   SITE            1259..1260
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P10358"
SQ   SEQUENCE   1844 AA;  206511 MW;  CB447EF05F199A18 CRC64;
     MAFQLALDAL APTTHRDPSL HPILESTVDS IRSSIQTYPW SIPKELLPLL NSYGIPTSGL
     GTSHHPHAAH KTIETFLLCT HWSFQATTPS SVMFMKPSKF NKLAQVNSNF RELKNYRLHP
     NDSTRYPFTS PDLPVFPTIF MHDALMYYHP SQIMDLFLQK PNLERLYASL VVPPEAHLSD
     QSFFPKLYTY TTTRHTLHYV PEGHEAGSYN QPSDAHSWLR INSIRLGNHH LSVTILESWG
     PVHSLLIQRG TPPPDPSLQA PSTPMASDLF RSYQEPRLDV VSFRIPDAIE LPQATFLQQP
     LRDRLVPRAV YNALFTYTRA VRTLRTSDPA AFVRMHSSKP DHDWVTSNAW DNLQTFALLN
     VPLRPNVVYH VLQSPIASLA LYLRQHWRRL TATAVPILSF LTLLQRFLPL PIPLAEVKSI
     TAFRRELYRK KAPHHPLDVF HLQQHLRNHH SAISAVRPAS PPHQRLPHAL QKAALLLLRP
     ISPLLTATPF FRSEQKSMLP NAELSWTLKR FALPWQASLV LLSLSESSVL LHKLFSPPTL
     QAQHDTYHRH LHPGSYSLQW ERTPLSIPRT TAFLPFTPTT STAPPDHSEA SLPPAFASTS
     VPRPPPVASS LGAQPPTTTA APPTPIEPTQ RAHQNSDLTL ESSTPIEPPP PPIQSSDIPP
     SAPVLFPEIN SPHRFSPKLP TTPDFEPTRT SPPPSTSHQD STDPADPLMG SHLLHHSLPA
     PPTHPLQSSQ LLPAPLTNDP TAIGPVLPFE ELHPRRYPEN TATFLTRLRS LPSNHLPQPT
     LNCLLSAVSD QTKVSEDHLW ESLQTILPDS QLRNEEINSL GLSTEHLTAL AHLYNFQATI
     YSDRGPILFG PSDTIKRIDI THTTGPPSHF SPGKRLLGSQ PSAKGHPSDS LIRAMKSFKV
     SGNYLPFSEA HNHPTSISHA KNLVSNMKNG FDGILSLLDV STGQRTGPTP KDAIIQIDHY
     LDTNPGKTTP VVHFAGFAGC GKTYPIQQLL KTKLFKDFRV SCPTTELRTE WKTAMELHGS
     QSWRFNTWES SILKSSRILV IDEIYKMPRG YLDLSILADP ALELVIILGD PLQGEYHSQS
     KDSSNHRLPS ETLRLLPYID MYCWWSYRIP QCIARLFQIH SFNAWQGIIG SVSTPQDQSP
     VLTNSHASSL TFNSLGYRSC TISSSQGLTF CDPAIIVLDN YTKWLSSANG LVALTRSRSG
     VQFMGPSSYV GGTNGSSAMF SDAFNNSLII MDRYFPSLFP QLKLITSPLT TRSPKLNGAT
     PSASPTHRSP NFHLPPHIPL SYDRDFVTVN PTLPDQGPET RLDTHFLPPS RLPLHFDLPP
     AITPPPISTS VDPPQAKASP VYPGEFFDSL AAFFLPAHDP STREVLHKDQ SSNQFPWFDR
     PFSLSCQPSS LISAKHAPNH DPTLLPASIN KRLRFRPSEA PHQITADDVV LGLQLFHSLC
     RAYSRQPNIT VPFNPELFAE CISLNEYAQL SSKTQSTIVA NASRSDPDWR HTTVKIFAKA
     QHKVNDGSIF GSWKACQTLA LMHDYVILVL GPVKKYQRIF DNVDRPSHIY SHCGKTPNQL
     RDWCQEHLTH STPKIANDYT AFDQSQHGES VVLEALKMKR LNIPSHLIQL HVHLKTNVST
     QFGPLTCMRL TGEPGTYDDN TDYNLAVIYS QYDVGSCPIM VSGDDSLIDH PLPTRHDWPS
     VLKRLHLRFK LELTSHPLFC GYYVGPAGCI RNPLALFCKL MIAVDDDALD DRRLSYLTEF
     TTGHLLGESL WHLLPETHVQ YQSACFDFFC RRCPKHEKML LDDSTPTLSL LERITSSPRW
     LTKNAMYLLP AKLRLAITSL SQTQSFPESI EVSHAESELL HYVQ
//