POLR_TYMVA
ID POLR_TYMVA Reviewed; 1844 AA.
AC P20128;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=RNA replicase polyprotein;
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.
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: Acts as a cysteine protease, methyltransferase and
CC deubiquitinase. The cysteine protease activity cleaves the polyprotein
CC giving rise to mature proteins. The methyltransferase domain is
CC probably involved in viral RNA capping. The deubiquitylating activity
CC counteracts the degradation of the viral polymerase mediated by the
CC host ubiquitin-proteasome system. The polymerase is thus stabilized and
CC infectivity is increased. Favors K63 poly-Ub linkage.
CC {ECO:0000250|UniProtKB:P10358}.
CC -!- FUNCTION: RNA-directed RNA polymerase is responsible for the
CC replication and transcription of the genome.
CC {ECO:0000250|UniProtKB:P10358}.
CC -!- CATALYTIC ACTIVITY:
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:
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 -!- SUBUNIT: Interacts 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 -!- MISCELLANEOUS: The deubiquitinase activity is low compared to that of
CC Bunyaviruses or coronaviruses. {ECO:0000250|UniProtKB:P10358}.
CC -!- SIMILARITY: Belongs to the tymovirus NS35 RNA replicase polyprotein
CC family. {ECO:0000305}.
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DR EMBL; J04373; AAA46592.1; -; Genomic_RNA.
DR PIR; JQ0109; RRWPTM.
DR MEROPS; C21.001; -.
DR Proteomes; UP000008268; Genome.
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; 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; 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="RNA replicase 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 571..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..736
FT /note="Polar residues"
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
