POLN_RUBVT
ID POLN_RUBVT Reviewed; 2116 AA.
AC P13889;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 5.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Non-structural polyprotein p200;
DE Short=p200;
DE Contains:
DE RecName: Full=Protease/methyltransferase p150;
DE Short=p150;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase p90;
DE Short=p90;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE EC=3.6.1.15;
DE EC=3.6.4.13;
OS Rubella virus (strain Therien) (RUBV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Matonaviridae; Rubivirus; Rubivirus rubellae.
OX NCBI_TaxID=11045;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2353453; DOI=10.1016/0042-6822(90)90476-8;
RA Dominguez G., Wang C.Y., Frey T.K.;
RT "Sequence of the genome RNA of rubella virus: evidence for genetic
RT rearrangement during togavirus evolution.";
RL Virology 177:225-238(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1738-2116.
RX PubMed=2836271; DOI=10.1016/0378-1119(88)90582-3;
RA Frey T.K., Marr L.D.;
RT "Sequence of the region coding for virion proteins C and E2 and the carboxy
RT terminus of the nonstructural proteins of rubella virus: comparison with
RT alphaviruses.";
RL Gene 62:85-99(1988).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=9229006; DOI=10.1007/s007050050150;
RA Pugachev K.V., Abernathy E.S., Frey T.K.;
RT "Genomic sequence of the RA27/3 vaccine strain of rubella virus.";
RL Arch. Virol. 142:1165-1180(1997).
RN [4]
RP SEQUENCE REVISION TO 2087-2088.
RA Zhou Y., Frey T.K.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION (PROTEASE/METHYLTRANSFERASE P150).
RX PubMed=10438871; DOI=10.1128/jvi.73.9.7805-7811.1999;
RA Kujala P., Ahola T., Ehsani N., Auvinen P., Vihinen H., Kaeaeriaeinen L.;
RT "Intracellular distribution of rubella virus nonstructural protein P150.";
RL J. Virol. 73:7805-7811(1999).
RN [6]
RP SUBCELLULAR LOCATION (PROTEASE/METHYLTRANSFERASE P150).
RX PubMed=8128633; DOI=10.1006/viro.1994.1192;
RA Lee J.Y., Marshall J.A., Bowden D.S.;
RT "Characterization of rubella virus replication complexes using antibodies
RT to double-stranded RNA.";
RL Virology 200:307-312(1994).
CC -!- FUNCTION: [Non-structural polyprotein p200]: Probable principal
CC replicase for the negative-strand DNA, which replicates the 40S (+)
CC genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into
CC (+) until cleaved into p150 and p90 mature proteins.
CC {ECO:0000250|UniProtKB:Q86500}.
CC -!- FUNCTION: [Protease/methyltransferase p150]: Protease that cleaves the
CC precursor polyprotein into two mature products. Together with RNA-
CC directed RNA polymerase p90, replicates the 40S genomic and antigenomic
CC RNA by recognizing replications specific signals. The heterodimer
CC P150/p90 is probably the principal replicase for positive-strand
CC genomic RNA and the 24S subgenomic RNA, which codes for structural
CC proteins. Responsible for the mRNA-capping of the viral mRNAs. This
CC function is necessary since all viral RNAs are synthesized in the
CC cytoplasm, and host capping enzymes are restricted to the nucleus.
CC Forms fibers late in the infection that may be involved in cell-to-cell
CC spread of the virus RNA in the absence of virus particle formation.
CC {ECO:0000250|UniProtKB:Q86500}.
CC -!- FUNCTION: [RNA-directed RNA polymerase p90]: Together with
CC protease/methyltransferase p150, replicates the 40S genomic and
CC antigenomic RNA by recognizing replications specific signals. The
CC heterodimer P150/p90 is probably the principal replicase for positive-
CC strand genomic RNA and the 24S subgenomic RNA, which codes for
CC structural proteins. A helicase activity is probably also present.
CC {ECO:0000250|UniProtKB:Q86500}.
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:0000250|UniProtKB:Q86500,
CC ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q86500};
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 Evidence={ECO:0000250|UniProtKB:Q86500};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01237};
CC Note=Zn(2+) is necessary for the protease activity. The protease can
CC also function efficiently with Cd(2+) and Co(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU01237};
CC -!- SUBUNIT: [Protease/methyltransferase p150]: Interacts with RNA-directed
CC RNA polymerase p90. Interacts with host CALM1; this interaction is
CC necessary for the protease activity and viral infectivity. Interacts
CC with host C1QBP. Interacts with the capsid protein. {ECO:0000305}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase p90]: Interacts with human
CC RB1/retinoblastoma protein. Interacts with protease/methyltransferase
CC p150. {ECO:0000250|UniProtKB:Q86500}.
CC -!- SUBCELLULAR LOCATION: [Non-structural polyprotein p200]: Host membrane
CC {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at
CC 24 hpi. {ECO:0000250|UniProtKB:Q86500}.
CC -!- SUBCELLULAR LOCATION: [Protease/methyltransferase p150]: Host membrane
CC {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host
CC cytoplasm, probably in vesicles inside host vacuoles of endosomal and
CC lysosomal origin (PubMed:10438871, PubMed:8128633). At 72 hpi,
CC localizes to filamentous structures in the host cytoplasm (By
CC similarity). {ECO:0000250|UniProtKB:Q86500,
CC ECO:0000269|PubMed:10438871, ECO:0000269|PubMed:8128633}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase p90]: Host membrane
CC {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to
CC the cytoplasmic fibers formed by protease/methyltransferase p150.
CC {ECO:0000250|UniProtKB:Q86500}.
CC -!- DOMAIN: [Protease/methyltransferase p150]: The N-terminus has a
CC methyltransferase activity for mRNA-capping. The C-terminus harbors a
CC protease active in cis or in trans which specifically cleaves and
CC releases the two mature proteins. Both the N-terminus and C-terminus
CC are required for fiber formation. The N-terminus is involved in
CC associating with membranes. An EF-hand Ca(2+)-binding motif is present
CC in the protease. Also contains 3 SH3-binding motifs that are
CC responsible for the interaction with host C1QBP.
CC {ECO:0000250|UniProtKB:Q86500}.
CC -!- PTM: [Non-structural polyprotein p200]: Specific enzymatic cleavage by
CC its own cysteine protease yield mature proteins p150 and p90.
CC {ECO:0000250|UniProtKB:Q86500}.
CC -!- MISCELLANEOUS: Rubella virus in utero infection has frequently severe
CC consequences on normal fetal development, collectively known as
CC congenital rubella syndrome (CRS). The teratogenicity of the virus is
CC possibly due to the interaction between the p90 protein and the human
CC RB1/retinoblastoma protein. {ECO:0000250|UniProtKB:Q86500}.
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DR EMBL; M15240; AAA88528.2; -; Genomic_RNA.
DR PIR; A35320; MNWVRN.
DR RefSeq; NP_062883.2; NC_001545.2.
DR SMR; P13889; -.
DR ELM; P13889; -.
DR MEROPS; C27.001; -.
DR GeneID; 1502161; -.
DR KEGG; vg:1502161; -.
DR Proteomes; UP000000571; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 CDD; cd21557; Macro_X_Nsp3-like; 1.
DR Gene3D; 3.40.220.10; -; 1.
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; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008738; Peptidase_C27.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR022245; Rubi_NSP_C.
DR InterPro; IPR044070; RUBV_NS_PRO.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05407; Peptidase_C27; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF12601; Rubi_NSP_C; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51889; RUBV_NS_PRO; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Helicase; Host cytoplasm; Host membrane; Hydrolase;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Protease; Reference proteome; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Viral RNA replication; Zinc.
FT CHAIN 1..2116
FT /note="Non-structural polyprotein p200"
FT /id="PRO_0000249223"
FT CHAIN 1..1301
FT /note="Protease/methyltransferase p150"
FT /id="PRO_0000041226"
FT CHAIN 1302..2116
FT /note="RNA-directed RNA polymerase p90"
FT /id="PRO_0000041227"
FT DOMAIN 57..247
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 806..985
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1000..1301
FT /note="Peptidase C27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT DOMAIN 1320..1468
FT /note="(+)RNA virus helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1469..1609
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1870..1981
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 36..49
FT /note="Required for efficient proteolysis and P150-P90
FT interaction"
FT /evidence="ECO:0000250|UniProtKB:Q86500"
FT REGION 457..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1183
FT /note="Interaction with host CALM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT REGION 1193..1228
FT /note="EF-hand-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT REGION 1700..1900
FT /note="Involved in P150-P90 interaction"
FT /evidence="ECO:0000250|UniProtKB:Q86500"
FT MOTIF 727..732
FT /note="PxxPxR; class II SH3-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86500"
FT MOTIF 747..752
FT /note="PxxPxR; class II SH3-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86500"
FT MOTIF 761..766
FT /note="PxxPxR; class II SH3-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86500"
FT MOTIF 1902..1906
FT /note="Human RB1 binding"
FT /evidence="ECO:0000250|UniProtKB:Q86500"
FT COMPBIAS 747..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1152
FT /note="For cysteine protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT ACT_SITE 1273
FT /note="For cysteine protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT BINDING 1175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT BINDING 1178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT BINDING 1227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT BINDING 1273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT BINDING 1352..1359
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT SITE 1301..1302
FT /note="Cleavage; autocatalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01237"
FT CONFLICT 410
FT /note="Missing (in Ref. 1; AAA88528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2116 AA; 230546 MW; 3B283DED68B25DBE CRC64;
MEKLLDEVLA PGGPYNLTVG SWVRDHVRSI VEGAWEVRDV VTAAQKRAIV AVIPRPVFTQ
MQVSDHPALH AISRYTRRHW IEWGPKEALH VLIDPSPGLL REVARVERRW VALCLHRTAR
KLATALAETA SEAWHADYVC ALRGAPSGPF YVHPEDVPHG GRAVADRCLL YYTPMQMCEL
MRTIDATLLV AVDLWPVALA AHVGDDWDDL GIAWHLDHDG GCPADCRGAG AGPTPGYTRP
CTTRIYQVLP DTAHPGRLYR CGPRLWTRDC AVAELSWEVA QHCGHQARVR AVRCTLPIRH
VRSLQPSARV RLPDLVHLAE VGRWRWFSLP RPVFQRMLSY CKTLSPDAYY SERVFKFKNA
LCHSITLAGN VLQEGWKGTC AEEDALCAYV AFRAWQSNAR LAGIMKGAKR CAADSLSVAG
WLDTIWDAIK RFLGSVPLAE RMEEWEQDAA VAAFDRGPLE DGGRHLDTVQ PPKSPPRPEI
AATWIVHAAS EDRHCACAPR CDVPRERPSA PAGQPDDEAL IPPWLFAERR ALRCREWDFE
ALRARADTAA APAPPAPRPA RYPTVLYRHP AHHGPWLTLD EPGEADAALV LCDPLGQPLR
GPERHFAAGA HMCAQARGLQ AFVRVVPPPE RPWADGGARA WAKFFRGCAW AQRLLGEPAV
MHLPYTDGDV PQLIALALRT LAQQGAALAL SVRDLPGGAA FDANAVTAAV RAGPRQSAAA
SPPPGDPPPP RRARRSQRHS DARGTPPPAP ARDPPPPAPS PPAPPRAGDP VPPIPAGPAD
RARDAELEVA CEPSGPPTST RADPDSDIVE SYARAAGPVH LRVRDIMDPP PGCKVVVNAA
NEGLLAGSGV CGAIFANATA ALAANCRRLA PCPTGEAVAT PGHGCGYTHI IHAVAPRRPR
DPAALEEGEA LLERAYRSIV ALAAARRWAC VACPLLGAGV YGWSAAESLR AALAATRTEP
VERVSLHICH PDRATLTHAS VLVGAGLAAR RVSPPPTEPL ASCPAGDPGR PAQRSASPPA
TPLGDATAPE PRGCQGCELC RYTRVTNDRA YVNLWLERDR GATSWAMRIP EVVVYGPEHL
ATHFPLNHYS VLKPAEVRPP RGMCGSDMWR CRGWHGMPQV RCTPSNAHAA LCRTGVPPRA
STRGGELDPN TCWLRAAANV AQAARACGAY TSAGCPKCAY GRALSEARTH EDFAALSQRW
SASHADASPD GTGDPLDPLM ETVGCACSRV WVGSEHEAPP DHLLVSLHRA PNGPWGVVLE
VRARPEGGNP TGHFVCAVGG GPRRVSDRPH LWLAVPLSRG GGTCAATDEG LAQAYYDDLE
VRRLGDDAMA RAALASVQRP RKGPYNIRVW NMAAGAGKTT RILAAFTRED LYVCPTNALL
HEIQAKLRAR DIDIKNAATY ERRLTKPLAA YRRIYIDEAF TLGGEYCAFV ASQTTAEVIC
VGDRDQCGPH YANNCRTPVP DRWPTERSRH TWRFPDCWAA RLRAGLDYDI EGERTGTFAC
NLWDGRQVDL HLAFSRETVR RLHEAGIRAY TVREAQGMSV GTACIHVGRD GTDVALALTR
DLAIVSLTRA SDALYLHELE DGSLRAAGLS AFLDAGALAE LKEVPAGIDR VVAVEQAPPP
LPPADGIPEA QDVPPFCPRT LEELVFGRAG HPHYADLNRV TEGEREVRYM RISRHLLNKN
HTEMPGTERV LSAVCAVRRY RAGEDGSTLR TAVARQHPRP FRQIPPPRVT AGVAQEWRMT
YLRERIDLTD VYTQMGVAAR ELTDRYARRY PEIFAGMCTA QSLSVPAFLK ATLKCVDAAL
GPRDTEDCHA AQGKAGLEIR AWAKEWVQVM SPHFRAIQKI IMRALRPQFL VAAGHTEPEV
DAWWQAHYTT NAIEVDFTEF DMNQTLATRD VELEISAALL GLPCAEDYRA LRAGSYCTLR
ELGSTETGCE RTSGEPATLL HNTTVAMCMA MRMVPKGVRW AGIFQGDDMV IFLPEGARSA
ALKWTPAEVG LFGFHIPVKH VSTPTPSFCG HVGTAAGLFH DVMHQAIKVL CRRFDPDVLE
EQQVALLDRL RGVYAALPDT VAANAAYYDY SAERVLAIVR ELTAYARGRG LDHPATIGAL
EEIQTPYARA NLHDAD
