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Non-structural polyprotein p200 (p200) [Cleaved into: Protease p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase/triphosphatase/helicase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]

 POLN_RUBVM              Reviewed;        2116 AA.
Q86500;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 2.
15-MAR-2017, entry version 110.
RecName: Full=Non-structural polyprotein p200;
Short=p200;
Contains:
RecName: Full=Protease p150;
Short=p150;
EC=3.4.22.-;
Contains:
RecName: Full=RNA-directed RNA polymerase/triphosphatase/helicase p90;
Short=p90;
EC=2.7.7.48;
EC=3.6.1.15;
EC=3.6.4.13;
Rubella virus (strain M33) (RUBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Rubivirus.
NCBI_TaxID=11043;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND MUTAGENESIS OF CYS-1152 AND
GLY-1300.
PubMed=9656995; DOI=10.1006/viro.1998.9179;
Yao J., Yang D., Chong P., Hwang D., Liang Y., Gillam S.;
"Proteolytic processing of rubella virus nonstructural proteins.";
Virology 246:74-82(1998).
[2]
INTERACTION WITH HUMAN RB1/RETINOBLASTOMA PROTEIN.
PubMed=9608663; DOI=10.1023/A:1007998023047;
Atreya C.D., Lee N.S., Forng R.Y., Hofmann J., Washington G.,
Marti G., Nakhasi H.L.;
"The rubella virus putative replicase interacts with the
retinoblastoma tumor suppressor protein.";
Virus Genes 16:177-183(1998).
[3]
MUTAGENESIS OF CYS-1904.
PubMed=10073691; DOI=10.1099/0022-1317-80-2-327;
Forng R.Y., Atreya C.D.;
"Mutations in the retinoblastoma protein-binding LXCXE motif of
rubella virus putative replicase affect virus replication.";
J. Gen. Virol. 80:327-332(1999).
[4]
FUNCTION.
PubMed=10823845; DOI=10.1128/JVI.74.12.5412-5423.2000;
Liang Y., Yao J., Gillam S.;
"Rubella virus nonstructural protein protease domains involved in
trans-and cis-cleavage activities.";
J. Virol. 74:5412-5423(2000).
[5]
MUTAGENESIS OF GLY-1966; ASP-1967 AND ASP-1968.
PubMed=11437666; DOI=10.1006/viro.2001.0939;
Wang X., Gillam S.;
"Mutations in the GDD motif of rubella virus putative RNA-dependent
RNA polymerase affect virus replication.";
Virology 285:322-331(2001).
[6]
FUNCTION.
PubMed=11289813; DOI=10.1006/viro.2001.0862;
Liang Y., Gillam S.;
"Rubella virus RNA replication is cis-preferential and synthesis of
negative- and positive-strand RNAs is regulated by the processing of
nonstructural protein.";
Virology 282:307-319(2001).
[7]
FUNCTION.
PubMed=12076835; DOI=10.1016/S0168-1702(02)00077-1;
Wang X., Liang Y., Gillam S.;
"Rescue of rubella virus replication-defective mutants using vaccinia
virus recombinant expressing rubella virus nonstructural proteins.";
Virus Res. 86:111-122(2002).
-!- FUNCTION: Non-structural polyprotein p200 replicates the 40S (+)
genomic RNA into (-) antigenomic RNA. It cannot replicate the (-)
into (+) until cleaved in p150 and p90 (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protease p150 has 2 separate domains with different
biological activities. The N-terminal section has presumably a
cytoplasmic mRNA-capping activity. This function is necessary
since all viral RNAs are synthesized in the cytoplasm, and host
capping enzymes are restricted to the nucleus. The C-terminal
section harbors a protease active in cis or in trans which
specifically cleaves and releases the two mature proteins (By
similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase/triphosphatase/helicase p90
replicates the 40S genomic and antigenomic RNA by recognizing
replications specific signals. Transcribes also a subgenomic mRNA
by initiating RNA synthesis internally on antigenomic RNA. This
24S mRNA codes for structural proteins (By similarity).
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: p90 interacts with human RB1/retinoblasstoma protein.
{ECO:0000269|PubMed:9608663}.
-!- SUBCELLULAR LOCATION: Non-structural polyprotein p200: Host
endosome membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host lysosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cytoplasmic vesicle
{ECO:0000250}. Note=Located in vesicles at the cytoplasmic surface
of modified endosomes and lysosomes, also called replication
complexes. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protease p150: Host endosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cytoplasmic vesicle
{ECO:0000250}. Note=Located in vesicles at the cytoplasmic surface
of modified endosomes and lysosomes, also called replication
complexes. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA
polymerase/triphosphatase/helicase p90: Host endosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cytoplasmic vesicle
{ECO:0000250}. Note=Located in vesicles at the cytoplasmic surface
of modified endosomes and lysosomes, also called replication
complexes. {ECO:0000250}.
-!- PTM: Specific enzymatic cleavage by its own cysteine protease
yield mature proteins. Uncleaved p200 functions in minus-strand
RNA synthesis, whereas cleavage of p200 into p150 and p90 converts
the complex to the capacity for efficient synthesis of positive-
strand genomic RNA both in cis and in trans (By similarity).
{ECO:0000250}.
-!- MISCELLANEOUS: Rubella virus in utero infection has frequently
severe consequences on normal fetal development, collectively
known as congenital rubella syndrome (CRS). The teratogenicity of
the virus possibly due to the interaction between the p90 protein
and the human RB1/retinoblastoma protein.
-!- SEQUENCE CAUTION:
Sequence=CAA51087.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X72393; CAA51087.1; ALT_SEQ; Genomic_RNA.
PIR; S38480; S38480.
ProteinModelPortal; Q86500; -.
IntAct; Q86500; 22.
OrthoDB; VOG0900000T; -.
Proteomes; UP000007143; Genome.
GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0044188; C:host cell lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006396; P:RNA processing; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR002588; Alphavirus-like_MT_dom.
InterPro; IPR002589; Macro_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008738; Peptidase_C27.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR022245; Rubi_NSP_C.
InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
Pfam; PF01661; Macro; 1.
Pfam; PF05407; Peptidase_C27; 1.
Pfam; PF00978; RdRP_2; 1.
Pfam; PF12601; Rubi_NSP_C; 1.
Pfam; PF01443; Viral_helicase1; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51743; ALPHAVIRUS_MT; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Helicase; Host cytoplasmic vesicle;
Host endosome; Host lysosome; Host membrane; Hydrolase; Membrane;
Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Protease;
RNA-directed RNA polymerase; Thiol protease; Transferase; Zinc.
CHAIN 1 2116 Non-structural polyprotein p200.
/FTId=PRO_0000249224.
CHAIN 1 1301 Protease p150.
/FTId=PRO_0000041224.
CHAIN 1302 2116 RNA-directed RNA
polymerase/triphosphatase/helicase p90.
/FTId=PRO_0000041225.
DOMAIN 57 247 Alphavirus-like MT. {ECO:0000255|PROSITE-
ProRule:PRU01079}.
DOMAIN 806 985 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1109 1274 Peptidase C27.
DOMAIN 1320 1468 (+)RNA virus helicase ATP-binding.
DOMAIN 1469 1609 (+)RNA virus helicase C-terminal.
DOMAIN 1870 1981 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
MOTIF 1902 1906 Human RB1 binding motif. {ECO:0000250}.
ACT_SITE 1152 1152 For cysteine protease activity.
{ECO:0000250}.
ACT_SITE 1273 1273 For cysteine protease activity.
{ECO:0000250}.
METAL 1175 1175 Zinc. {ECO:0000250}.
METAL 1178 1178 Zinc. {ECO:0000250}.
METAL 1227 1227 Zinc. {ECO:0000250}.
METAL 1273 1273 Zinc. {ECO:0000250}.
SITE 1301 1302 Cleavage; by p150.
MUTAGEN 1152 1152 C->S: Complete loss of protease activity.
{ECO:0000269|PubMed:9656995}.
MUTAGEN 1300 1300 G->S: Complete loss of polyprotein
cleavage. {ECO:0000269|PubMed:9656995}.
MUTAGEN 1904 1904 C->G: Partial loss of human RB1 binding
and 47% loss of virus replication.
{ECO:0000269|PubMed:10073691}.
MUTAGEN 1904 1904 C->R: Complete loss of human RB1 binding
and virus replication.
{ECO:0000269|PubMed:10073691}.
MUTAGEN 1966 1966 G->A: Reduces virus infectivity.
{ECO:0000269|PubMed:11437666}.
MUTAGEN 1967 1967 D->A: Complete loss of virus replication.
{ECO:0000269|PubMed:11437666}.
MUTAGEN 1968 1968 D->A: Complete loss of virus replication.
{ECO:0000269|PubMed:11437666}.
SEQUENCE 2116 AA; 230910 MW; 04DD4C97B704EC8E 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 VGWWRWFSLP RPVFQRMLSY CKTLSPDAYY SERVFKFKNA
LSHSITLAGN VLQEGWKGTC AEEDALCAYV AFRAWQSNAR LAGIMKSAKR CAADSLSVAG
WLDTIWDAIK RFFGSVPLAE RMEEWEQDAA VAAFDRGPLE DGGRHLDTVQ PPKSPPRPEI
AATWIVHAAS ADRHCACAPR CDVPRERPSA PAGPPDDEAL IPPWLFAERR ALRCREWDFE
ALRARADTAA APAPLAPRPA RYPTVLYRHP AHHGPWLTLD EPGGADAALV LCDPLGQPLR
GPERHYAAGA HMCAQARGLQ AFVRVVPPPE RPWADGGARA WAKFFRGCAW AQRLLGEPAV
MHLPYTDGDV PKLIALALRT LAQQGAALAL SVRDLPRGTA FEANAVTAAV RAGPGQLAAT
SPPPGDPPPP RRARRSQRHS DARGTPPPAP VRDPPRPQPS PPAPPRVGDP VPPTTAEPAD
RARHAELEVV YEPSGPPTST KADPDSDIVE SYARAAGPVH LRVRDIMDPP PGCKVVVNAA
NEGLLAGSGV CGAIFANATA ALAADCRRLA PCPIGEAVAT PGHGCGYTHI IHAVAPRRPR
DPAALEEGEA LLERAYRSIV ALAAARRWAR VACPLLGAGV YGWSAAESLR AALAATRAEP
AERVSLHICH PDRATLTHAS VLVGAGLAAR RVSPPPTEPL ASCPAGDPGR PAQRSASPPA
TPLGDATAPE PRGCQGCELC RYTRVTNDRA YVNLWLERDR GATSWAMRIP EVVVYGPEHL
ATHFPLNHYS VLKPAEVRPP RGMCGSDMWR CRGWQGMPQV RCTPSNAHAA LCRTGVPPRV
STRGGELDPN TCWLRAAANV AQAARACGAY TSAGCPKCAY GRALSEARTH EDFAALSQWW
SASHADASPD GTGDPLDPLM ETVGCACSRV WVGSEHEAPP DHLLVSLHRA PNGPWGVVLE
VRARPEGGNP TGHFVCAVGG GPRRVSDRPH LWLAVPLSRG GGTCAATDEG LAQAYYDDLE
VRRLGDDAMA RAALASIQRP RKGPYNIRVW NMAAGAGKTT RILAAFTRED LYVCPTNALL
HEIQAKLRAR DIDIKNAATY ERALTKPLAA YRRIYIDEAF TLGGEYCAFV ASQTTAEVIC
VGDRDQCGPH YANNCRTPVP DRWPTGRSRH TWRFPDCWAA RLRAGLDYDI EGERTGTFAC
NLWDGRQVDL HLAFSRETVR RLHEAGIRAY TVREAQGMSV GTACIHVGRD GTDVALALTR
DLAIVSLTRA SDALYLHELE DGLLRAAGLS AFLDAGALAE LKEVPAGIDR VVAVEQAPPP
LPPADGIPEA QDVPPFCPRT LEELVFGRAG HPHYADLNRV TEGEREVRYM RISRHLLNKN
HTEMPGTERV LSAVCAVRRY RAGEDGSTLR TAVARQHPRP FRQIPPPRVT AGVAQEWRMT
YLRERIDLTD VYTQMGVAAR ELTDRYTRRY PEIFAGMCTA QSLSVPAFLK ATLKCVDAAL
GPRDTEDCHA AQGKAGLEIR AWAKEWVQVM SPHFRAIQKI IMRALRPQFL VAAGHTEPEV
DAWWQAHYTT NAIEVDFTEF DMNQTLATRD VELEISAALL GLPCAEDYRA LRAGSYCTLR
ELGSTETGCE RTSGEPATLL HNTTVAMCMA MRMVPKGVRW AGIFQGDDMV IFLPEGARNA
ALKWTPAEVG LFGFHIPVKH VSTPTPSFCG HVGTAAGLFH DVMHQAIKVL CRRFDPDVLE
EQQVALLDRL RGVYAALPDT VAANAAYYDY SAERVLAIVR ELTAYARGRG LDHPATIGAL
EEIQTPYARA NLHDAD


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