Reviewed, UniProtKB/Swiss-Prot P03317 (POLN_SINDV)

Names and origin

Protein names	Recommended name:     Non-structural polyprotein Alternative name(s):     Polyprotein nsP1234       Short name=P1234 Cleaved into the following 7 chains:     1- Recommended name:             P123     2- Recommended name:             P123'     3- Recommended name:             mRNA-capping enzyme nsP1               EC=2.1.1.-               EC=2.7.7.-         Alternative name(s):             Non-structural protein 1     4- Recommended name:             Protease/triphosphatase/NTPase/helicase nsP2               EC=3.4.22.-               EC=3.1.3.33               EC=3.6.1.15               EC=3.6.1.-         Alternative name(s):             Non-structural protein 2               Short name=nsP2     5- Recommended name:             Non-structural protein 3                 Short name=nsP3     6- Recommended name:             Non-structural protein 3'                 Short name=nsP3'     7- Recommended name:             RNA-directed RNA polymerase nsP4               EC=2.7.7.48         Alternative name(s):             Non-structural protein 4               Short name=nsP4
Organism	Sindbis virus (SINV)
Taxonomic identifier	11034 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Togaviridae › Alphavirus › WEEV complex
Virus host	Aedes [TaxID: 7158] Homo sapiens (Human) [TaxID: 9606] Motacilla alba (White wagtail) (Pied wagtail) [TaxID: 45807] Acrocephalus scirpaceus [TaxID: 48156] Culex [TaxID: 53527] Streptopelia turtur [TaxID: 177155]

Protein attributes

Sequence length	2512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	P123 and P123' are short-lived polyproteins, accumulating during early stage of infection. P123 is directly translated from the genome, whereas P123' is a product of the cleavage of P1234. They localize the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, they start viral genome replication into antigenome. After these early events, P123 and P123' are cleaved sequentially into nsP1, nsP2 and nsP3/nsP3'. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex. Ref.11 Ref.12 nsP1 is a cytoplasmic capping enzyme. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping would consist in the following reactions: GTP is first methylated and then forms the m7GMp-nsP1 complex, from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell. Ref.11 Ref.12 nsP2 has two separate domain with different biological activities. The N-terminal section is part of the RNA polymerase complex and has RNA trisphosphatase and RNA helicase activity. The C-terminal section harbors a protease that specifically cleaves and releases the four mature proteins. Ref.11 Ref.12 nsP3 and nsP3' are essential for minus strand and subgenomic 26S mRNA synthesis. Ref.11 Ref.12 nsP4 is a RNA dependent RNA polymerase. It replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a 26S subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 26S mRNA encodes for structural proteins. nsP4 is a short-lived protein regulated by several ways: the opal codon readthrough and degradation by ubiquitin pathway. Ref.11 Ref.12
Catalytic activity	S-adenosyl-L-methionine + GTP = m7GTP. m7GTP + (5')pp-Pur-mRNA = diphosphate + m7G(5')ppp-Pur-mRNA. (5')ppp-mRNA + H2O = (5')pp-mRNA + phosphate. A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate. NTP + H2O = NDP + phosphate. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	P123 interacts with nsP4; nsP1, nsP2, nsP3 and nsP4 interact with each other, and with uncharacterized host factors.
Subcellular location	Non-structural polyprotein: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Located on the cytoplasmic surface of modified endosomes and lysosomes, also called cytopathic vacuoles type I (CPVI). These vacuoles contain numerous small circular invaginations (spherules) which may be the sites of RNA synthesis. Ref.5 P123: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Ref.5 P123': Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Ref.5 mRNA-capping enzyme nsP1: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Host cell membrane; Peripheral membrane protein; Cytoplasmic side. Host cell projection › host filopodium. Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then a fraction of nsP1 localizes to the inner surface of the plasma membrane and its filopodial extensions. Ref.5 Protease/triphosphatase/NTPase/helicase nsP2: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus. Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then approximately half of nsP2 is found in the nucleus. Ref.5 Non-structural protein 3: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Host cytoplasm. Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' seems to aggregate in cytoplasm. Ref.5 Non-structural protein 3': Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Host cytoplasm. Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' seems to aggregate in cytoplasm. Ref.5 RNA-directed RNA polymerase nsP4: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Host lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Ref.5
Induction	Viral replication produces dsRNA in the late phase of infection, resulting in a strong activation of host EIF2AK2/PKR, leading to almost complete phosphorylation of EIF2A. This inactivates completely cellular translation initiation, resulting in a dramatic shutoff of proteins synthesis. Translation of viral non-structural polyprotein and all cellular proteins are stopped in infected cell between 2 and 4 hours post infection. Only the 26S mRNA is still translated into viral structural proteins, presumably through a unique mechanism of enhancer element which counteract the translation inhibition mediated by EIF2A. By doing this, the virus uses the cellular defense for its own advantage: shutoff of cellular translation allows to produce big amounts of structural proteins needed for the virus to bud out of the doomed cell. Ref.16
Post-translational modification	Specific enzymatic cleavages in vivo yield mature proteins. The polyprotein is synthesized as P123, or P1234 by stop codon readthrough. These polyproteins are processed differently depending on the stage of infection. In early stages, P1234 is first cleaved in trans, through its nsP2 protease activity, releasing P123' and nsP4. P123/P123' and nsP4 start to replicate the viral genome into its antigenome. After these early events, nsP1 is cleaved in cis by nsP2 protease, releasing the P23/P23' polyprotein. Cleavage of nsP1 exposes an 'activator' at the N-terminus of P23/P23' which induces its cleavage into nsP2 and nsP3 by the viral protease. This sequence of delayed processing would allow correct assembly and membrane association of the RNA-polymerase complex. In the late stage of infection, the presence of free nsP2 in the cytoplasm cleaves P1234 quickly into P12 and P34, then into the four nsP. Ref.6 Ref.8 nsP1 is palmitoylated by host. Ref.15 nsP4 is ubiquitinated; targets the protein for rapid degradation via the ubiquitin system.
Miscellaneous	The genome encodes for P123, but readthrough of a terminator codon UGA occurs between the codons for Tyr-1896 and Leu-1897. This readthrough produces P1234, cleaved quickly by nsP2 into P123' and nsP4. Further processing of p123' gives nsP1, nsP2 and nsP3' which is 6 amino-acids longer than nsP3 since the cleavage site is after the readthrough. This unusual molecular mechanism ensures that few nsP4 are produced compared to other non-structural proteins. Mutant viruses with no alternative termination site grow significantly slower than wild-type virus.
Sequence similarities	Contains 1 Macro domain. Contains 1 peptidase C9 domain. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	RNA replication mRNA capping mRNA processing
Cellular component	Host cell membrane Host cell projection Host cytoplasm Host endosome Host lysosome Host membrane Host nucleus Membrane
Ligand	ATP-binding GTP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase Methyltransferase Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase
PTM	Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW transcription, RNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular component	cell projection Inferred from electronic annotation. Source: UniProtKB-KW endosome Inferred from electronic annotation. Source: UniProtKB-KW host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide 5'-phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2512	2512	Non-structural polyprotein		PRO_0000308405
	Chain	1 – 1902	1902	P123'		PRO_0000227771
	Chain	1 – 1896	1896	P123		PRO_0000227772
	Chain	1 – 540	540	mRNA-capping enzyme nsP1		PRO_0000041236
	Chain	541 – 1347	807	Protease/triphosphatase/NTPase/helicase nsP2		PRO_0000041237
	Chain	1348 – 1902	555	Non-structural protein 3'		PRO_0000041238
	Chain	1348 – 1896	549	Non-structural protein 3		PRO_0000227773
	Chain	1903 – 2512	610	RNA-directed RNA polymerase nsP4		PRO_0000041239
Regions
	Domain	972 – 1179	208	Peptidase C9
	Domain	1348 – 1507	160	Macro
	Domain	2266 – 2381	116	RdRp catalytic
	Nucleotide binding	726 – 733	8	ATP Potential
	Region	245 – 264	20	nsP1 membrane-binding By similarity
	Region	1013 – 1032	20	Nucleolus localization signal By similarity
	Motif	1196 – 1200	5	Nuclear localization signal By similarity
Sites
	Active site	1021	1	For cysteine protease nsP2 activity
	Active site	1098	1	For cysteine protease nsP2 activity
	Site	540 – 541	2	Cleavage; by nsP2
	Site	1347 – 1348	2	Cleavage; by nsP2
	Site	1902 – 1903	2	Cleavage; by nsP2
Amino acid modifications
	Lipidation	420	1	S-palmitoyl cysteine; by host Ref.15
Experimental info
	Mutagenesis	39	1	H → A: Complete loss of methyl transferase activity or viral infectivity. Ref.13
	Mutagenesis	81	1	H → A: Complete loss of methyl transferase activity or viral infectivity. Ref.13
	Mutagenesis	91	1	D → A: Complete loss of methyl transferase activity or viral infectivity. Ref.13
	Mutagenesis	94	1	R → A: Complete loss of methyl transferase activity or viral infectivity. Ref.13
	Mutagenesis	249	1	Y → A: Complete loss of methyl transferase activity or viral infectivity. Ref.13
	Mutagenesis	369	1	I → V: No effect on methyl transferase activity or viral infectivity. Ref.13
	Mutagenesis	420	1	C → A: Complete loss of palmitoylation. Ref.15
	Mutagenesis	1021	1	C → A: Complete loss of nsP2 protease activity. Ref.10
	Mutagenesis	1098	1	H → A: Complete loss of nsP2 protease activity. Ref.10
	Mutagenesis	1099	1	W → A: Complete loss of nsP2 protease activity. Ref.10
	Mutagenesis	1896	1	Y → YR, YS or YW: Reduces RNA synthesis in early phase of infection. Ref.7
	Mutagenesis	1903	1	Y → A: No effect on nsP4 cleavage. Ref.14
	Mutagenesis	1903	1	Y → C: Destabilizes nsP4. Ref.14
	Mutagenesis	1903	1	Y → E: Reduces nsP4 cleavage. Ref.14
	Mutagenesis	1903	1	Y → F: Destabilizes nsP4. Ref.14
	Mutagenesis	1903	1	Y → L: Reduces nsP4 cleavage and destabilizes nsP4. Ref.14
	Mutagenesis	1903	1	Y → M: Reduces nsP4 cleavage. Ref.14
	Mutagenesis	1903	1	Y → N: Reduces nsP4 cleavage. Ref.14
	Mutagenesis	1903	1	Y → P: Complete loss of nsP4 cleavage. Ref.14
	Mutagenesis	1903	1	Y → Q: Reduces nsP4 cleavage. Ref.14
	Mutagenesis	1903	1	Y → R: Destabilizes nsP4. Ref.14
	Mutagenesis	1903	1	Y → T: Reduces nsP4 cleavage. Ref.14

Sequences

	Sequence		Length	Mass (Da)
	P03317-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: F3656FC8BB495726	FASTA	2,512	279,549
	10 20 30 40 50 60 MEKPVVNVDV DPQSPFVVQL QKSFPQFEVV AQQVTPNDHA NARAFSHLAS KLIELEVPTT 70 80 90 100 110 120 ATILDIGSAP ARRMFSEHQY HCVCPMRSPE DPDRMMKYAS KLAEKACKIT NKNLHEKIKD 130 140 150 160 170 180 LRTVLDTPDA ETPSLCFHND VTCNMRAEYS VMQDVYINAP GTIYHQAMKG VRTLYWIGFD 190 200 210 220 230 240 TTQFMFSAMA GSYPAYNTNW ADEKVLEARN IGLCSTKLSE GRTGKLSIMR KKELKPGSRV 250 260 270 280 290 300 YFSVGSTLYP EHRASLQSWH LPSVFHLNGK QSYTCRCDTV VSCEGYVVKK ITISPGITGE 310 320 330 340 350 360 TVGYAVTHNS EGFLLCKVTD TVKGERVSFP VCTYIPATIC DQMTGIMATD ISPDDAQKLL 370 380 390 400 410 420 VGLNQRIVIN GRTNRNTNTM QNYLLPIIAQ GFSKWAKERK DDLDNEKMLG TRERKLTYGC 430 440 450 460 470 480 LWAFRTKKVH SFYRPPGTQT CVKVPASFSA FPMSSVWTTS LPMSLRQKLK LALQPKKEEK 490 500 510 520 530 540 LLQVSEELVM EAKAAFEDAQ EEARAEKLRE ALPPLVADKG IEAAAEVVCE VEGLQADIGA 550 560 570 580 590 600 ALVETPRGHV RIIPQANDRM IGQYIVVSPN SVLKNAKLAP AHPLADQVKI ITHSGRSGRY 610 620 630 640 650 660 AVEPYDAKVL MPAGGAVPWP EFLALSESAT LVYNEREFVN RKLYHIAMHG PAKNTEEEQY 670 680 690 700 710 720 KVTKAELAET EYVFDVDKKR CVKKEEASGL VLSGELTNPP YHELALEGLK TRPAVPYKVE 730 740 750 760 770 780 TIGVIGTPGS GKSAIIKSTV TARDLVTSGK KENCREIEAD VLRLRGMQIT SKTVDSVMLN 790 800 810 820 830 840 GCHKAVEVLY VDEAFACHAG ALLALIAIVR PRKKVVLCGD PMQCGFFNMM QLKVHFNHPE 850 860 870 880 890 900 KDICTKTFYK YISRRCTQPV TAIVSTLHYD GKMKTTNPCK KNIEIDITGA TKPKPGDIIL 910 920 930 940 950 960 TCFRGWVKQL QIDYPGHEVM TAAASQGLTR KGVYAVRQKV NENPLYAITS EHVNVLLTRT 970 980 990 1000 1010 1020 EDRLVWKTLQ GDPWIKQPTN IPKGNFQATI EDWEAEHKGI IAAINSPTPR ANPFSCKTNV 1030 1040 1050 1060 1070 1080 CWAKALEPIL ATAGIVLTGC QWSELFPQFA DDKPHSAIYA LDVICIKFFG MDLTSGLFSK 1090 1100 1110 1120 1130 1140 QSIPLTYHPA DSARPVAHWD NSPGTRKYGY DHAIAAELSR RFPVFQLAGK GTQLDLQTGR 1150 1160 1170 1180 1190 1200 TRVISAQHNL VPVNRNLPHA LVPEYKEKQP GPVKKFLNQF KHHSVLVVSE EKIEAPRKRI 1210 1220 1230 1240 1250 1260 EWIAPIGIAG ADKNYNLAFG FPPQARYDLV FINIGTKYRN HHFQQCEDHA ATLKTLSRSA 1270 1280 1290 1300 1310 1320 LNCLNPGGTL VVKSYGYADR NSEDVVTALA RKFVRVSAAR PDCVSSNTEM YLIFRQLDNS 1330 1340 1350 1360 1370 1380 RTRQFTPHHL NCVISSVYEG TRDGVGAAPS YRTKRENIAD CQEEAVVNAA NPLGRPGEGV 1390 1400 1410 1420 1430 1440 CRAIYKRWPT SFTDSATETG TARMTVCLGK KVIHAVGPDF RKHPEAEALK LLQNAYHAVA 1450 1460 1470 1480 1490 1500 DLVNEHNIKS VAIPLLSTGI YAAGKDRLEV SLNCLTTALD RTDADVTIYC LDKKWKERID 1510 1520 1530 1540 1550 1560 AALQLKESVT ELKDEDMEID DELVWIHPDS CLKGRKGFST TKGKLYSYFE GTKFHQAAKD 1570 1580 1590 1600 1610 1620 MAEIKVLFPN DQESNEQLCA YILGETMEAI REKCPVDHNP SSSPPKTLPC LCMYAMTPER 1630 1640 1650 1660 1670 1680 VHRLRSNNVK EVTVCSSTPL PKHKIKNVQK VQCTKVVLFN PHTPAFVPAR KYIEVPEQPT 1690 1700 1710 1720 1730 1740 APPAQAEEAP EVVATPSPST ADNTSLDVTD ISLDMDDSSE GSLFSSFSGS DNSITSMDSW 1750 1760 1770 1780 1790 1800 SSGPSSLEIV DRRQVVVADV HAVQEPAPIP PPRLKKMARL AAARKEPTPP ASNSSESLHL 1810 1820 1830 1840 1850 1860 SFGGVSMSLG SIFDGETARQ AAVQPLATGP TDVPMSFGSF SDGEIDELSR RVTESEPVLF 1870 1880 1890 1900 1910 1920 GSFEPGEVNS IISSRSAVSF PLRKQRRRRR SRRTEYLTGV GGYIFSTDTG PGHLQKKSVL 1930 1940 1950 1960 1970 1980 QNQLTEPTLE RNVLERIHAP VLDTSKEEQL KLRYQMMPTE ANKSRYQSRK VENQKAITTE 1990 2000 2010 2020 2030 2040 RLLSGLRLYN SATDQPECYK ITYPKPLYSS SVPANYSDPQ FAVAVCNNYL HENYPTVASY 2050 2060 2070 2080 2090 2100 QITDEYDAYL DMVDGTVACL DTATFCPAKL RSYPKKHEYR APNIRSAVPS AMQNTLQNVL 2110 2120 2130 2140 2150 2160 IAATKRNCNV TQMRELPTLD SATFNVECFR KYACNDEYWE EFARKPIRIT TEFVTAYVAR 2170 2180 2190 2200 2210 2220 LKGPKAAALF AKTYNLVPLQ EVPMDRFVMD MKRDVKVTPG TKHTEERPKV QVIQAAEPLA 2230 2240 2250 2260 2270 2280 TAYLCGIHRE LVRRLTAVLL PNIHTLFDMS AEDFDAIIAE HFKQGDPVLE TDIASFDKSQ 2290 2300 2310 2320 2330 2340 DDAMALTGLM ILEDLGVDQP LLDLIECAFG EISSTHLPTG TRFKFGAMMK SGMFLTLFVN 2350 2360 2370 2380 2390 2400 TVLNVVIASR VLEERLKTSR CAAFIGDDNI IHGVVSDKEM AERCATWLNM EVKIIDAVIG 2410 2420 2430 2440 2450 2460 ERPPYFCGGF ILQDSVTSTA CRVADPLKRL FKLGKPLPAD DEQDEDRRRA LLDETKAWFR 2470 2480 2490 2500 2510 VGITGTLAVA VTTRYEVDNI TPVLLALRTF AQSKRAFQAI RGEIKHLYGG PK

References

[1]	"Complete nucleotide sequence of the genomic RNA of Sindbis virus." Strauss E.G., Rice C.M., Strauss J.H. Virology 133:92-110(1984) [PubMed: 6322438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"The 5'-terminal sequences of the genomic RNAs of several alphaviruses." Ou J.H., Strauss E.G., Strauss J.H. J. Mol. Biol. 168:1-15(1983) [PubMed: 6308269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-54.
[3]	"Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon." Strauss E.G., Rice C.M., Strauss J.H. Proc. Natl. Acad. Sci. U.S.A. 80:5271-5275(1983) [PubMed: 6577423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1429-2512.
[4]	"Sequence studies of several alphavirus genomic RNAs in the region containing the start of the subgenomic RNA." Ou J.-H., Rice C.M., Dalgarno L., Strauss E.G., Strauss J.H. Proc. Natl. Acad. Sci. U.S.A. 79:5235-5239(1982) [PubMed: 6291034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2431-2512.
[5]	"Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes." Froshauer S., Kartenbeck J., Helenius A. J. Cell Biol. 107:2075-2086(1988) [PubMed: 2904446] [Abstract] Cited for: SUBCELLULAR LOCATION OF NON-STRUCTURAL PROTEINS.
[6]	"Processing the nonstructural polyproteins of sindbis virus: nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans." Hardy W.R., Strauss J.H. J. Virol. 63:4653-4664(1989) [PubMed: 2529379] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[7]	"Mutagenesis of the in-frame opal termination codon preceding nsP4 of Sindbis virus: studies of translational readthrough and its effect on virus replication." Li G.P., Rice C.M. J. Virol. 63:1326-1337(1989) [PubMed: 2521676] [Abstract] Cited for: MUTAGENESIS OF OPAL STOP CODON BETWEEN TYR-1896 AND LEU-1897.
[8]	"Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo." de Groot R.J., Hardy W.R., Shirako Y., Strauss J.H. EMBO J. 9:2631-2638(1990) [PubMed: 2142454] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN BY NSP2.
[9]	"Sindbis virus RNA polymerase is degraded by the N-end rule pathway." de Groot R.J., Ruemenapf T., Kuhn R.J., Strauss E.G., Strauss J.H. Proc. Natl. Acad. Sci. U.S.A. 88:8967-8971(1991) [PubMed: 1924357] [Abstract] Cited for: UBIQUITIN DEGRADATION OF NSP4.
[10]	"Identification of the active site residues in the nsP2 proteinase of Sindbis virus." Strauss E.G., De Groot R.J., Levinson R., Strauss J.H. Virology 191:932-940(1992) [PubMed: 1448929] [Abstract] Cited for: MUTAGENESIS OF CYS-1021; HIS-1098 AND TRP-1099.
[11]	"Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus- and plus-strand RNA synthesis." Lemm J.A., Ruemenapf T., Strauss E.G., Strauss J.H., Rice C.M. EMBO J. 13:2925-2934(1994) [PubMed: 7517863] [Abstract] Cited for: FUNCTION.
[12]	"Regulation of Sindbis virus RNA replication: uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis." Shirako Y., Strauss J.H. J. Virol. 68:1874-1885(1994) [PubMed: 8107248] [Abstract] Cited for: FUNCTION OF P123.
[13]	"Mutagenesis of the Sindbis virus nsP1 protein: effects on methyltransferase activity and viral infectivity." Wang H.-L., O'Rear J., Stollar V. Virology 217:527-531(1996) [PubMed: 8610444] [Abstract] Cited for: MUTAGENESIS OF HIS-39; HIS-81; ASP-91; ARG-94; TYR-249 AND ILE-369.
[14]	"Requirement for an aromatic amino acid or histidine at the N-terminus of Sindbis virus RNA polymerase." Shirako Y., Strauss J.H. J. Virol. 72:2310-2315(1998) [PubMed: 9499091] [Abstract] Cited for: MUTAGENESIS OF TYR-1903.
[15]	"Effects of palmitoylation of replicase protein nsP1 on alphavirus infection." Ahola T., Kujala P., Tuittila M., Blom T., Laakkonen P., Hinkkanen A., Auvinen P. J. Virol. 74:6725-6733(2000) [PubMed: 10888610] [Abstract] Cited for: PALMITOYLATION AT CYS-420, MUTAGENESIS OF CYS-420.
[16]	"Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR." Ventoso I., Sanz M.A., Molina S., Berlanga J.J., Carrasco L., Esteban M. Genes Dev. 20:87-100(2006) [PubMed: 16391235] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02363 Genomic RNA. Translation: AAA96975.1. Sequence problems.
PIR	MNWVS. A03917.
RefSeq	NP_062889.1.
3D structure databases
HSSP	HSSP built from PDB template 1FW5 based on UniProtKB P08411.
ModBase	Search...
Protein family/group databases
MEROPS	C09.001.
Genome annotation databases
GeneID	1502154.
Enzyme and pathway databases
BRENDA	2.7.7.48. 18664. 3.1.3.33. 18664. 3.6.1.15. 18664.
Family and domain databases
InterPro	IPR002589. A1pp. IPR002620. Peptidase_C9. IPR001788. RNA-dep_RNA_pol_vir-typ. IPR007094. RNA-dir_pol_PSvirus. IPR000606. RNA_helicase1_vir. [Graphical view]
Pfam	PF01661. Macro. 1 hit. PF01707. Peptidase_C9. 1 hit. PF00978. RdRP_2. 1 hit. PF01443. Viral_helicase1. 1 hit. [Graphical view]
SMART	SM00506. A1pp. 1 hit. [Graphical view]
PROSITE	PS51154. MACRO. 1 hit. PS50507. RDRP_SSRNA_POS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
PMAP-CutDB	P03317.

Entry information

Entry name

POLN_SINDV

Accession

Primary (citable) accession number: P03317

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 3, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)