Q99D35 (POLG_DEN3C) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 14 chains: Capsid protein C Alternative name(s): Core protein prM Peptide pr Small envelope protein M Alternative name(s): Matrix protein Envelope protein E Non-structural protein 1 Short name=NS1 Non-structural protein 2A Short name=NS2A Non-structural protein 2A-alpha Short name=NS2A-alpha Serine protease subunit NS2B Alternative name(s): Flavivirin protease NS2B regulatory subunit Non-structural protein 2B Serine protease NS3 EC=3.4.21.91 EC=3.6.1.15 EC=3.6.4.13 Alternative name(s): Flavivirin protease NS3 catalytic subunit Non-structural protein 3 Non-structural protein 4A Short name=NS4A Peptide 2k Non-structural protein 4B Short name=NS4B RNA-directed RNA polymerase NS5 EC=2.1.1.56 EC=2.1.1.57 EC=2.7.7.48 Alternative name(s): Non-structural protein 5
Organism	Dengue virus type 3 (strain China/80-2/1980) (DENV-3) [Complete proteome]
Taxonomic identifier	408690 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group
Virus host	Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538] Homo sapiens (Human) [TaxID: 9606] Diceromyia [TaxID: 53539] Aedimorphus [TaxID: 53540] Stegomyia [TaxID: 53541]

Protein attributes

Sequence length	3390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity. prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated By similarity. Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as an homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes By similarity. Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome By similarity. Non-structural protein 2A may be involved viral RNA replication and capsid assembly Potential. Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity. Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction By similarity. Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functionning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase By similarity. Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter By similarity. Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway By similarity. RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway By similarity.
Catalytic activity	Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). NTP + H2O = NDP + phosphate. ATP + H2O = ADP + phosphate. S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA. S-adenosyl-L-methionine + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA.
Subunit structure	Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity. NS5 interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation By similarity.
Subcellular location	Capsid protein C: Virion Potential. Peptide pr: Secreted By similarity. Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential. Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential. Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity. Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Located in RE-associated vesicles hosting the replication complex. Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus By similarity. Note: Located in RE-associated vesicles hosting the replication complex.
Domain	Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals By similarity.
Post-translational modification	Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site By similarity. RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization By similarity. Envelope protein E and non-structural protein 1 are N-glycosylated By similarity.
Sequence similarities	Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 peptidase S7 domain. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	Clathrin-mediated endocytosis of virus by host Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Host-virus interaction Inhibition of host STAT2 by virus Inhibition of host TYK2 by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Initiation of viral infection RNA replication Transcription Transcription regulation Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Virus endocytosis by host
Cellular component	Host endoplasmic reticulum Host membrane Host nucleus Membrane Secreted Viral envelope protein Virion
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding
Molecular function	Capsid protein Helicase Hydrolase Methyltransferase Nucleotidyltransferase Protease RNA-directed RNA polymerase Serine protease Transferase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	evasion by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular component	host cell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: InterPro virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW double-stranded RNA binding Inferred from electronic annotation. Source: InterPro mRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: EC mRNA (nucleoside-2'-O-)-methyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type exopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3390	3390	Genome polyprotein		PRO_0000405222
	Chain	1 – 100	100	Capsid protein C By similarity		PRO_0000268043
	Propeptide	101 – 114	14	ER anchor for the protein C, removed in mature form by serine protease NS3		PRO_0000268044
	Chain	115 – 280	166	prM By similarity		PRO_0000268045
	Chain	115 – 205	91	Peptide pr By similarity		PRO_0000268046
	Chain	206 – 280	75	Small envelope protein M By similarity		PRO_0000268047
	Chain	281 – 773	493	Envelope protein E By similarity		PRO_0000268048
	Chain	774 – 1125	352	Non-structural protein 1 By similarity		PRO_0000268049
	Chain	1126 – 1343	218	Non-structural protein 2A By similarity		PRO_0000268050
	Chain	1126 – 1313	188	Non-structural protein 2A-alpha By similarity		PRO_0000268051
	Chain	1344 – 1473	130	Serine protease subunit NS2B By similarity		PRO_0000268052
	Chain	1474 – 2092	619	Serine protease NS3 By similarity		PRO_0000268053
	Chain	2093 – 2219	127	Non-structural protein 4A By similarity		PRO_0000268054
	Peptide	2220 – 2242	23	Peptide 2k		PRO_0000268055
	Chain	2243 – 2490	248	Non-structural protein 4B By similarity		PRO_0000268056
	Chain	2491 – 3390	900	RNA-directed RNA polymerase NS5 By similarity		PRO_0000268057
Regions
	Topological domain	1 – 100	100	Cytoplasmic Potential
	Transmembrane	101 – 118	18	Helical; Potential
	Topological domain	119 – 243	125	Extracellular Potential
	Transmembrane	244 – 264	21	Helical; Potential
	Topological domain	265	1	Cytoplasmic Potential
	Transmembrane	266 – 280	15	Helical; Potential
	Topological domain	281 – 723	443	Extracellular Potential
	Intramembrane	724 – 744	21	Helical; Potential
	Topological domain	745 – 750	6	Extracellular Potential
	Intramembrane	751 – 771	21	Helical; Potential
	Topological domain	772 – 1123	352	Extracellular Potential
	Transmembrane	1124 – 1144	21	Helical; Potential
	Topological domain	1145 – 1154	10	Cytoplasmic Potential
	Transmembrane	1155 – 1175	21	Helical; Potential
	Topological domain	1176 – 1196	21	Lumenal Potential
	Transmembrane	1197 – 1217	21	Helical; Potential
	Topological domain	1218 – 1282	65	Cytoplasmic Potential
	Transmembrane	1283 – 1303	21	Helical; Potential
	Topological domain	1304 – 1315	12	Lumenal Potential
	Transmembrane	1316 – 1336	21	Helical; Potential
	Topological domain	1337 – 1344	8	Cytoplasmic Potential
	Transmembrane	1345 – 1365	21	Helical; Potential
	Topological domain	1366 – 1368	3	Lumenal Potential
	Transmembrane	1369 – 1389	21	Helical; Potential
	Topological domain	1390 – 1443	54	Cytoplasmic Potential
	Intramembrane	1444 – 1464	21	Helical; Potential
	Topological domain	1465 – 2146	682	Cytoplasmic Potential
	Transmembrane	2147 – 2167	21	Helical; Potential
	Topological domain	2168 – 2169	2	Lumenal Potential
	Intramembrane	2170 – 2190	21	Helical; Potential
	Topological domain	2191	1	Lumenal Potential
	Transmembrane	2192 – 2212	21	Helical; Potential
	Topological domain	2213 – 2227	15	Cytoplasmic Potential
	Transmembrane	2228 – 2248	21	Helical; Note=Signal for NS4B; Potential
	Topological domain	2249 – 2273	25	Lumenal Potential
	Intramembrane	2274 – 2294	21	Helical; Potential
	Topological domain	2295 – 2305	11	Lumenal Potential
	Intramembrane	2306 – 2326	21	Helical; Potential
	Topological domain	2327 – 2346	20	Lumenal Potential
	Transmembrane	2347 – 2367	21	Helical; Potential
	Topological domain	2368 – 2412	45	Cytoplasmic Potential
	Transmembrane	2413 – 2433	21	Helical; Potential
	Topological domain	2434 – 2458	25	Lumenal Potential
	Transmembrane	2459 – 2479	21	Helical; Potential
	Topological domain	2480 – 3390	911	Cytoplasmic Potential
	Domain	1474 – 1651	178	Peptidase S7
	Domain	1654 – 1810	157	Helicase ATP-binding
	Domain	1821 – 1986	166	Helicase C-terminal
	Domain	3018 – 3168	151	RdRp catalytic
	Nucleotide binding	1667 – 1674	8	ATP Potential
	Region	33 – 74	42	Hydrophobic; homodimerization of capsid protein C By similarity
	Region	1396 – 1435	40	Interacts with and activates NS3 protease By similarity
	Motif	1758 – 1761	4	DEAH box
Sites
	Active site	1524	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1548	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1608	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	2551	1	For 2'-O-methyltransferase activity By similarity
	Active site	2636	1	For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
	Active site	2670	1	For 2'-O-methyltransferase activity By similarity
	Active site	2706	1	For 2'-O-methyltransferase activity By similarity
	Site	100 – 101	2	Cleavage; by viral protease NS3 Potential
	Site	114 – 115	2	Cleavage; by host signal peptidase By similarity
	Site	205 – 206	2	Cleavage; by host furin Potential
	Site	280 – 281	2	Cleavage; by host signal peptidase Potential
	Site	773 – 774	2	Cleavage; by host signal peptidase Potential
	Site	1125 – 1126	2	Cleavage; by host By similarity
	Site	1343 – 1344	2	Cleavage; by viral protease NS3 Potential
	Site	1473 – 1474	2	Cleavage; by autolysis Potential
	Site	2092 – 2093	2	Cleavage; by autolysis Potential
	Site	2219 – 2220	2	Cleavage; by viral protease NS3 Potential
	Site	2242 – 2243	2	Cleavage; by host signal peptidase Potential
	Site	2490 – 2491	2	Cleavage; by viral protease NS3 Potential
Amino acid modifications
	Glycosylation	183	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	347	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	433	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	980	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2300	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2304	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2456	1	N-linked (GlcNAc...); by host Potential
	Disulfide bond	283 ↔ 310		By similarity
	Disulfide bond	340 ↔ 401		By similarity
	Disulfide bond	354 ↔ 385		By similarity
	Disulfide bond	372 ↔ 396		By similarity
	Disulfide bond	463 ↔ 563		By similarity
	Disulfide bond	580 ↔ 611		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99D35 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: C52C2725C6A103AD	FASTA	3,390	378,159
	10 20 30 40 50 60 MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSRGLLNG QGPMKLVMAF IAFLRFLAIP 70 80 90 100 110 120 PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK TSLCLMMMLP ATLAFHLTSR 130 140 150 160 170 180 DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC 190 200 210 220 230 240 WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW 250 260 270 280 290 300 ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW 310 320 330 340 350 360 VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA 370 380 390 400 410 420 ILPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLESIEGKVV QHENLKYTVI 430 440 450 460 470 480 ITVHTGDQHQ VGNETQGVTA EITSQASTAE AILPEYGTLG LECSPRTGLD FNEMILLTMK 490 500 510 520 530 540 NKAWMVHRQW FFDLPLPWTS GATTKTPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT 550 560 570 580 590 600 ALTGATEIQT LGGTSIFAGH LKCRLKMDKL ELKGMSYAMC LNTFVLKKEV SETQHGTILI 610 620 630 640 650 660 KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI 670 680 690 700 710 720 GDKALKINWY RKGSSIGKMF EATARGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS 730 740 750 760 770 780 AYTALFSGVS WIMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGVV VQADMGCVIN 790 800 810 820 830 840 WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL 850 860 870 880 890 900 WKQIANELNY ILWENNIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE 910 920 930 940 950 960 TQNSSFIIDG PSTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA 970 980 990 1000 1010 1020 VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWSNGVL ESDMIIPKSL 1030 1040 1050 1060 1070 1080 AGPISQHNHR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI SENCGTRGPS LRTTTVSGKL 1090 1100 1110 1120 1130 1140 IHEWCCRSCT LPPLRYMGED GCWYGMEIRP INEKEENMVK SLASAGSGKV DNFTMGVLCL 1150 1160 1170 1180 1190 1200 AILFEEVMRG KFGKKHMIAG VLFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL 1210 1220 1230 1240 1250 1260 ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMAATLR LPEDIEQMAN GIALGLMALK 1270 1280 1290 1300 1310 1320 LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGI SLLPVCQSSS MRKTDWLPMT 1330 1340 1350 1360 1370 1380 VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL 1390 1400 1410 1420 1430 1440 LIACYVITGT SADLTVEKAA DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV 1450 1460 1470 1480 1490 1500 LLKTALLIVS GIFPCSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ 1510 1520 1530 1540 1550 1560 QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI SYGGGWRLSA 1570 1580 1590 1600 1610 1620 QWQKGEEVQV IAVEPGKNPK NFQTMPGIFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV 1630 1640 1650 1660 1670 1680 GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA 1690 1700 1710 1720 1730 1740 IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT 1750 1760 1770 1780 1790 1800 MRLLSPVRVP NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP 1810 1820 1830 1840 1850 1860 QSNAPIQDEE RDIPERSWNS GNEWITDFVG KTVWFVPSIK AGNDIANCLR KNGKKVIQLS 1870 1880 1890 1900 1910 1920 RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR RCLKPVILTD GPERVILAGP 1930 1940 1950 1960 1970 1980 MPVTVASAAQ RRGRVGRNPQ KENDQYIFMG QPLNKDEDHA HWTEAKMLLD NINTPEGIIP 1990 2000 2010 2020 2030 2040 ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG 2050 2060 2070 2080 2090 2100 ERNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT 2110 2120 2130 2140 2150 2160 EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL GLMILLTGGA 2170 2180 2190 2200 2210 2220 MLFLISGKGI GKTSIGLICV IASSGMLWMA DVPLQWIASA IVLEFFMMVL LIPEPEKQRT 2230 2240 2250 2260 2270 2280 PQDNQLAYVV IGILTLAAIV AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW 2290 2300 2310 2320 2330 2340 TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC 2350 2360 2370 2380 2390 2400 YSQVNPLTLI AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV 2410 2420 2430 2440 2450 2460 IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEVLTLAT GPITTLWEGS PGKFWNTTIA 2470 2480 2490 2500 2510 2520 VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK 2530 2540 2550 2560 2570 2580 SGITEVDRTE AKEGLKRGEI THHAVSRGSA KLQWFVERNM VIPEGRVIDL GCGRGGWSYY 2590 2600 2610 2620 2630 2640 CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES 2650 2660 2670 2680 2690 2700 SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS 2710 2720 2730 2740 2750 2760 RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET 2770 2780 2790 2800 2810 2820 PNMDVIGERI KRIKEEHSST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP 2830 2840 2850 2860 2870 2880 WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRPMPGTR KVMEITAEWL WRTLGRNKRP 2890 2900 2910 2920 2930 2940 RLCTREEFTK KVRTNAAMGA VFTEENQWDS ARAAVEDEEF WKLVDREREL HKLGKCGSCV 2950 2960 2970 2980 2990 3000 YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG 3010 3020 3030 3040 3050 3060 LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH RQLANAIFKL 3070 3080 3090 3100 3110 3120 TYQNKVVKVQ RPTPKGTVMD IISRKDQRGS GQVGTYGLNT FTNMEAQLIR QMEGEGVLSK 3130 3140 3150 3160 3170 3180 ADLENPHPLE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD 3190 3200 3210 3220 3230 3240 IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE 3250 3260 3270 3280 3290 3300 TACLGKAYAQ MWTLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML 3310 3320 3330 3340 3350 3360 TVWNRVWIED NPWMEDKTPI TTWEDVPYLG KREDQWCGSL IGLTSRATWA QNILTAIQQV 3370 3380 3390 RSLIGNEEFL DYMPSMKRFR KEEESEGAIW

References

[1]	"Complete sequence of dengue virus type 3 strain 80-2 isolated from Guangxi China." Yuan X., Geng L., Li X., Yu M., Qin E. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+	Additional computationally mapped references.

Web resources

Virus Pathogen Resource

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF317645 Genomic RNA. Translation: AAK01920.1.
3D structure databases
HSSP	HSSP built from PDB template 1UZG based on UniProtKB P27915.
ProteinModelPortal	Q99D35.
SMR	Q99D35. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.
ModBase	Search...
Protein family/group databases
MEROPS	S07.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR014001. DEAD-like_helicase. IPR011492. DEAD_Flavivir. IPR000069. Env_glycoprot_M_flavivir. IPR013756. Flav_glyE_cen_dom_subdom2. IPR013754. Flav_glyE_dim. IPR001122. Flavi_capsidC. IPR001157. Flavi_NS1. IPR000752. Flavi_NS2A. IPR000487. Flavi_NS2B. IPR000404. Flavi_NS4A. IPR001528. Flavi_NS4B. IPR002535. Flavi_propep. IPR000336. Flv_glyE_Ig-like. IPR014412. Gen_Poly_FLV. IPR011999. GlycoprotE_cen/dimer_Flavivir. IPR011998. GlycoprotE_cen/dimer_vir. IPR001650. Helicase_C. IPR014756. Ig_E-set. IPR009003. Pept_cys/ser_Trypsin-like. IPR001850. Peptidase_S7. IPR000208. RNA-dir_pol_flavivirus. IPR007094. RNA-dir_pol_PSvirus. IPR002877. rRNA_MeTrfase_RrmJ/FtsJ. [Graphical view]
Gene3D	G3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit. G3DSA:2.60.98.10. Flav_glyE_dim. 3 hits. G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
Pfam	PF01003. Flavi_capsid. 1 hit. PF07652. Flavi_DEAD. 1 hit. PF02832. Flavi_glycop_C. 1 hit. PF00869. Flavi_glycoprot. 1 hit. PF01004. Flavi_M. 1 hit. PF00948. Flavi_NS1. 1 hit. PF01005. Flavi_NS2A. 1 hit. PF01002. Flavi_NS2B. 1 hit. PF01350. Flavi_NS4A. 1 hit. PF01349. Flavi_NS4B. 1 hit. PF00972. Flavi_NS5. 1 hit. PF01570. Flavi_propep. 1 hit. PF01728. FtsJ. 1 hit. PF00271. Helicase_C. 1 hit. PF00949. Peptidase_S7. 1 hit. [Graphical view]
PIRSF	PIRSF003817. Gen_Poly_FLV. 1 hit.
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
SUPFAM	SSF56983. Flavi_glycoprotE. 1 hit. SSF81296. Ig_E-set. 1 hit. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS51527. FLAVIVIRUS_NS2B. 1 hit. PS51528. FLAVIVIRUS_NS3PRO. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS50507. RDRP_SSRNA_POS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLG_DEN3C

Accession

Primary (citable) accession number: Q99D35

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program