P33478 (POLG_DEN1S) 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 1 (strain Singapore/S275/1990) (DENV-1) [Complete proteome]
Taxonomic identifier	33741 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group › Dengue virus › Dengue virus 1
Virus host	Aedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159] Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160] Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	3396 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 a 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, functioning 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	In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 mRNA cap 0-1 NS5-type MT domain. Contains 1 peptidase S7 domain. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	Activation of host autophagy by virus 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 Transcription Transcription regulation Viral RNA replication Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell mRNA capping mRNA processing
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 S-adenosyl-L-methionine
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	RNA (guanine-N7)-methylation Inferred from electronic annotation. Source: GOC induction by virus of host autophagy 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 suppression by virus of host STAT2 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host TYK2 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis 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: UniProtKB-KW 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 – 3396	3396	Genome polyprotein		PRO_0000405206
	Chain	1 – 100	100	Capsid protein C By similarity		PRO_0000037894
	Propeptide	101 – 114	14	ER anchor for the protein C, removed in mature form by serine protease NS3		PRO_0000037895
	Chain	115 – 280	166	prM By similarity		PRO_0000264654
	Chain	115 – 205	91	Peptide pr By similarity		PRO_0000264655
	Chain	206 – 280	75	Small envelope protein M By similarity		PRO_0000037896
	Chain	281 – 774	494	Envelope protein E By similarity		PRO_0000037897
	Chain	775 – 1126	352	Non-structural protein 1 By similarity		PRO_0000037898
	Chain	1127 – 1344	218	Non-structural protein 2A By similarity		PRO_0000037899
	Chain	1127 – 1315	189	Non-structural protein 2A-alpha By similarity		PRO_0000264656
	Chain	1345 – 1474	130	Serine protease subunit NS2B By similarity		PRO_0000037900
	Chain	1475 – 2093	619	Serine protease NS3 By similarity		PRO_0000037901
	Chain	2094 – 2220	127	Non-structural protein 4A By similarity		PRO_0000037902
	Peptide	2221 – 2243	23	Peptide 2k		PRO_0000264657
	Chain	2244 – 2492	249	Non-structural protein 4B By similarity		PRO_0000037903
	Chain	2493 – 3396	904	RNA-directed RNA polymerase NS5 By similarity		PRO_0000037904
Regions
	Topological domain	1 – 101	101	Cytoplasmic Potential
	Transmembrane	102 – 119	18	Helical; Potential
	Topological domain	120 – 242	123	Extracellular Potential
	Transmembrane	243 – 260	18	Helical; Potential
	Topological domain	261	1	Cytoplasmic Potential
	Transmembrane	262 – 280	19	Helical; Potential
	Topological domain	281 – 725	445	Extracellular Potential
	Intramembrane	726 – 746	21	Helical; Potential
	Topological domain	747 – 752	6	Extracellular Potential
	Intramembrane	753 – 775	23	Helical; Potential
	Topological domain	776 – 1124	349	Extracellular Potential
	Transmembrane	1125 – 1145	21	Helical; Potential
	Topological domain	1146 – 1156	11	Cytoplasmic Potential
	Transmembrane	1157 – 1177	21	Helical; Potential
	Topological domain	1178 – 1198	21	Lumenal Potential
	Transmembrane	1199 – 1219	21	Helical; Potential
	Topological domain	1220 – 1288	69	Cytoplasmic Potential
	Transmembrane	1289 – 1309	21	Helical; Potential
	Topological domain	1310 – 1314	5	Lumenal Potential
	Transmembrane	1315 – 1335	21	Helical; Potential
	Topological domain	1336 – 1345	10	Cytoplasmic Potential
	Transmembrane	1346 – 1366	21	Helical; Potential
	Topological domain	1367 – 1369	3	Lumenal Potential
	Transmembrane	1370 – 1390	21	Helical; Potential
	Topological domain	1391 – 1446	56	Cytoplasmic Potential
	Intramembrane	1447 – 1467	21	Helical; Potential
	Topological domain	1468 – 2147	680	Cytoplasmic Potential
	Transmembrane	2148 – 2168	21	Helical; Potential
	Topological domain	2169 – 2170	2	Lumenal Potential
	Intramembrane	2171 – 2191	21	Helical; Potential
	Topological domain	2192	1	Lumenal Potential
	Transmembrane	2193 – 2213	21	Helical; Potential
	Topological domain	2214 – 2228	15	Cytoplasmic Potential
	Transmembrane	2229 – 2249	21	Helical; Note=Signal for NS4B; Potential
	Topological domain	2250 – 2275	26	Lumenal Potential
	Intramembrane	2276 – 2296	21	Helical; Potential
	Topological domain	2297 – 2348	52	Lumenal Potential
	Transmembrane	2349 – 2369	21	Helical; Potential
	Topological domain	2370 – 2414	45	Cytoplasmic Potential
	Transmembrane	2415 – 2435	21	Helical; Potential
	Topological domain	2436 – 2460	25	Lumenal Potential
	Transmembrane	2461 – 2481	21	Helical; Potential
	Topological domain	2482 – 3396	915	Cytoplasmic Potential
	Domain	1475 – 1652	178	Peptidase S7
	Domain	1655 – 1811	157	Helicase ATP-binding
	Domain	1821 – 1988	168	Helicase C-terminal
	Domain	2494 – 2755	262	mRNA cap 0-1 NS5-type MT
	Domain	3019 – 3168	150	RdRp catalytic
	Nucleotide binding	1668 – 1675	8	ATP By similarity
	Region	33 – 74	42	Hydrophobic; homodimerization of capsid protein C By similarity
	Region	1397 – 1436	40	Interacts with and activates NS3 protease By similarity
	Motif	1759 – 1762	4	DEAH box
Sites
	Active site	1525	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1549	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1609	1	Charge relay system; for serine protease NS3 activity By similarity
	Binding site	2506	1	mRNA cap By similarity
	Binding site	2509	1	mRNA cap; via carbonyl oxygen By similarity
	Binding site	2510	1	mRNA cap By similarity
	Binding site	2512	1	mRNA cap; via carbonyl oxygen By similarity
	Binding site	2521	1	mRNA cap By similarity
	Binding site	2548	1	S-adenosyl-L-methionine By similarity
	Binding site	2578	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	2579	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	2596	1	S-adenosyl-L-methionine By similarity
	Binding site	2597	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	2623	1	S-adenosyl-L-methionine By similarity
	Binding site	2624	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	2642	1	mRNA cap By similarity
	Binding site	2703	1	mRNA cap By similarity
	Binding site	2705	1	mRNA cap By similarity
	Binding site	2710	1	S-adenosyl-L-methionine 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	774 – 775	2	Cleavage; by host signal peptidase Potential
	Site	1126 – 1127	2	Cleavage; by host By similarity
	Site	1344 – 1345	2	Cleavage; by viral protease NS3 Potential
	Site	1474 – 1475	2	Cleavage; by autolysis Potential
	Site	2093 – 2094	2	Cleavage; by autolysis Potential
	Site	2220 – 2221	2	Cleavage; by viral protease NS3 Potential
	Site	2243 – 2244	2	Cleavage; by host signal peptidase Potential
	Site	2492 – 2493	2	Cleavage; by viral protease NS3 Potential
	Site	2517	1	mRNA cap binding By similarity
	Site	2553	1	Essential for 2'-O-methyltransferase activity By similarity
	Site	2638	1	Essential for 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
	Site	2639	1	S-adenosyl-L-methionine binding By similarity
	Site	2672	1	Essential for 2'-O-methyltransferase activity By similarity
	Site	2708	1	Essential for 2'-O-methyltransferase activity By similarity
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	981	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2302	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2306	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2458	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	465 ↔ 565		By similarity
	Disulfide bond	582 ↔ 613		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P33478 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: C53E75F3E424367D	FASTA	3,396	379,564
	10 20 30 40 50 60 MNNQRKKTAR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP 70 80 90 100 110 120 PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLLP TALAFHLTTR 130 140 150 160 170 180 GGEPHMIVSK QEREKSLLFK TSVGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC 190 200 210 220 230 240 WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQRVETW 250 260 270 280 290 300 ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGSRD FVEGLSGATW 310 320 330 340 350 360 VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA 370 380 390 400 410 420 TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK CVTKLEGKIV QYENLKYSVI 430 440 450 460 470 480 VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT 490 500 510 520 530 540 MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM 550 560 570 580 590 600 HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV 610 620 630 640 650 660 LVQVKYEGTD APCKIPFSTQ DEKGVTQNRL ITANPIVTDK EKPVNIETEP PFGESYIVVG 670 680 690 700 710 720 AGEKALKQCW FKKGSSIGKM FEATARGARR MAILGDTAWD FGSIGGVFTS VGKLVHQVFG 730 740 750 760 770 780 TAYGVLFSGV SWTMKIGIGI LLTWLGLNSR STSLSMTCIA VGMVTLYLGV MVQADSGCVI 790 800 810 820 830 840 NWKGRELKCG SGIFVTNEVH TWTEQYKFQA DSPKRLSAAI GKAWEEGVCG IRSATRLENI 850 860 870 880 890 900 MWKQISNELN HILLENDMKF TVVVGDVVGI LAQGKKMIRP QPMEHKYSWK SWGKAKIIGA 910 920 930 940 950 960 DIQNTTFIID GPDTPECPDD QRAWNIWEVE DYGFGIFTTN IWLKLRDSYT QMCDHRLMSA 970 980 990 1000 1010 1020 AIKDSKAVHA DMGYWIESEK NETWKLARAS FIEVKTCVWP KSHTLWSNGV LESEMIIPKI 1030 1040 1050 1060 1070 1080 YGGPISQHNY RPGYFTQTAG PWHLGKLELD FDLCEGTTVV VDEHCGNRGP SLRTTTVTGK 1090 1100 1110 1120 1130 1140 IIHEWCCRSC TLPPLRFKGE DGCWYGMEIR PVKEKEENLV KSMVSAGSGE VDSFSLGLLC 1150 1160 1170 1180 1190 1200 ISIMIEEVMR SRWSRKMLMT GTLAVFLLLI MGQLTWNDLI RLCIMVGANA SDRMGMGTTY 1210 1220 1230 1240 1250 1260 LALMATFKMR PMFAVGLLFR RLTSREVLLL TIGLSLVASV ELPNSLEELG DGLAMGIMIL 1270 1280 1290 1300 1310 1320 KLLTDFQSHQ LWATLLSLTF VKTTFSLHYA WKTMAMVLSI VSLFPLCLST TSQKTTWLPV 1330 1340 1350 1360 1370 1380 LLGSLGCKPL TMFLIAENKI WGRKSWPLNE GIMAVGIVSI LLSSLLKNDV PLAGPLIAGG 1390 1400 1410 1420 1430 1440 MLIACYVISG SSADLSLEKA AEVSWEEEAE HSGASHNILV EVQDDGTMKI KDEERDDTLT 1450 1460 1470 1480 1490 1500 ILLKATLLAV SGVYPLSIPA TLFVWYFWQK KKQRSGVLWD TPSPPEVERA VLDDGIYRIM 1510 1520 1530 1540 1550 1560 QRGLLGRSQV GVGVFQDGVF HTMWHVTRGA VLMYQGKRLE PSWASVKKDL ISYGGGWRFQ 1570 1580 1590 1600 1610 1620 GSWNTGEEVQ VIAVEPGKNP KNVQTAPGTF KTPEGEVGAI ALDFKPGTSG SPIVNREGKI 1630 1640 1650 1660 1670 1680 VGLYGNGVVT TSGTYVSAIA QAKASQEGPL PEIEDEVFRK RNLTIMDLHP GSGKTRRYLP 1690 1700 1710 1720 1730 1740 AIVREAIRRN VRTLILAPTR VVASEMAEAL KGMPIRYQTT AVKSEHTGKE IVDLMCHATF 1750 1760 1770 1780 1790 1800 TMRLLSPVRV PNYNMIIMDE AHFTDPASIA RRGYISTRVG MGEAAAIFMT ATPPGSVEAF 1810 1820 1830 1840 1850 1860 PQSNAVIQDE ERDIPERSWN SGYEWITDFP GKTVWFVPSI KSGNDIANCL RKNGKRVIQL 1870 1880 1890 1900 1910 1920 SRKTFDTEYQ KTKNNDWDYV VTTDISEMGA NFRADRVIDP RRCLKPVILK DGPERVILAG 1930 1940 1950 1960 1970 1980 PMPVTVASAA QRRGRIGRNQ NKEGDQYVYM GQPLNNDEDH AHWTEAKMLL DNINTPEGII 1990 2000 2010 2020 2030 2040 PALFEPEREK SAAIDGEYRL RGEARKTFVE LMRRGDLPVW LSYKVASEGF QYSDRRWCFD 2050 2060 2070 2080 2090 2100 GERNNQVLEE NMDVEMWTKE GERKKLRPRW LDARTYSDPL ALREFKEFAA GRRSVSGDLI 2110 2120 2130 2140 2150 2160 LEIGKLPQHL TQRAQNALDN LVMLHNSEQG GRAYRHAMEE LPDTIETLML LALIAVLTGG 2170 2180 2190 2200 2210 2220 VTLFFLSGKG LGKTSIGLLC VMASSVLLWM ASVEPHWIAA SIILEFFLMV LLIPEPDRQR 2230 2240 2250 2260 2270 2280 TPQDNQLAYV VIGLLFMILT VAANEMGLLE TTKKDLGIGH VAAENHHHAT MLDVDLRPAS 2290 2300 2310 2320 2330 2340 AWTLYAVATT VITPMMRHTI ENTTANISLT AIANQAAILM GLDKGWPISK MDIGVPLLAL 2350 2360 2370 2380 2390 2400 GCYSQVNPLT LTAAVLMLVA HYAIIGPGLQ AKATREAQKR TAAGIMKNPT VDGIVAIDLD 2410 2420 2430 2440 2450 2460 PVVYDAKFEK QLGQIMLLIL CTSQILLMRT TWALCESITL ATGPLTTLWE GSPGKFWNTT 2470 2480 2490 2500 2510 2520 IAVSMANIFR GSYLAGAGLA FSLMKSLGGG RRGTGAKGKH WERNGKDRLN QLSKSEFNTY 2530 2540 2550 2560 2570 2580 KRSGIMEVDR SEAKEGLKRG ETTKHAVSRG TAKLRWFVER NLVKPEGKVI DLGCGRGGWS 2590 2600 2610 2620 2630 2640 YYCAGLKKVT EVKGYTKGGP GHEEPIPMAT YGWNLVKLYS GKDVFFTPPE KCDTLLCDIG 2650 2660 2670 2680 2690 2700 ESSPNPTIEE GRTLRVLKMV EPWLRGNQFC IKILNPYMPS VVETLEQMQR KHGGMLVRNP 2710 2720 2730 2740 2750 2760 LSRNSTHEMY WVSCGTGNIV SAVNMTSRML LNRFTMAHRK PTYERDVDLG AGTRHVAVEP 2770 2780 2790 2800 2810 2820 EVANLDIIGQ RIENIKHEHK STWHYDEDNP YKTWAYHGSY EVKPSGSASS MVNGVVKLLT 2830 2840 2850 2860 2870 2880 KPWDAIPMVT QIAMTDTTPF GQQRVFKEKV DTRTPKAKRG TAQIMEVTAR WLWGFLSRNK 2890 2900 2910 2920 2930 2940 KPRICTREEF TRKVRSNAAI GAVFVDENQW NSAKEAVEDE RFWDLVHRER ELHKQGKCAT 2950 2960 2970 2980 2990 3000 CVYNMMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFMNEDHWFS RENSLSGVEG 3010 3020 3030 3040 3050 3060 EGLHKLGYIL RDISKIPGGN MYADDTAGWD TRITEDDLQN EAKITDIMEP EHALLATSIF 3070 3080 3090 3100 3110 3120 KLTYQNKVVR VQRPAKNGTV MDVISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMESEGIF 3130 3140 3150 3160 3170 3180 SPSELETPNL AERVLDWLEK YGVERLKRMA ISGDDCVVKP IDDRFATALT ALNDMGKVRK 3190 3200 3210 3220 3230 3240 DIPQWEPSKG WNDWQQVPFC SHHFHQLIMK DGREIVVPCR NQDELVGRAR VSQGAGWSLR 3250 3260 3270 3280 3290 3300 ETACLGKSYA QMWQLMYFHR RDLRLAANAI CSAVPVDWVP TSRTTWSIHA HHQWMTTEDM 3310 3320 3330 3340 3350 3360 LSVWNRVWIE ENPWMEDKTH VSSWEDVPYL GKREDQWCGS LIGLTARATW ATNIQVAINQ 3370 3380 3390 VRRLIGNENY LDYMTSMKRF KNESDPKGHS GESTHL

References

[1]	"Full-length cDNA sequence of dengue type 1 virus (Singapore strain S275/90)." Fu J., Tan B.H., Yap E.H., Chan Y.C., Tan Y.H. Virology 188:953-958(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Web resources

Virus Pathogen Resource

Cross-references

Sequence databases
EMBL GenBank DDBJ	M87512 Genomic RNA. No translation available.
PIR	A42551.
3D structure databases
ProteinModelPortal	P33478.
SMR	P33478. Positions 21-100, 115-195, 281-673, 1494-2093, 2498-2759, 2765-3374.
ModBase	Search...
Protein family/group databases
MEROPS	S07.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.60.40.350. 1 hit. 2.60.98.10. 2 hits. 3.30.387.10. 1 hit.
InterPro	IPR011492. DEAD_Flavivir. IPR000069. Env_glycoprot_M_flavivir. IPR013755. Flav_gly_cen_dom_subdom1. IPR001122. Flavi_capsidC. IPR026470. Flavi_E_Stem/Anchor_dom. IPR001157. Flavi_NS1. IPR000752. Flavi_NS2A. IPR000487. Flavi_NS2B. IPR000404. Flavi_NS4A. IPR001528. Flavi_NS4B. IPR002535. Flavi_propep. IPR000336. Flavivir/Alphavir_Ig-like. IPR001850. Flavivirus_NS3_S7. IPR027287. Flavovir_Ig-like. IPR014412. Gen_Poly_FLV. IPR011998. Glycoprot_cen/dimer. IPR013754. GlyE_dim. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR014756. Ig_E-set. IPR026490. mRNA_cap_0/1_MeTrfase. IPR027417. P-loop_NTPase. IPR000208. RNA-dir_pol_flavivirus. IPR007094. RNA-dir_pol_PSvirus. IPR002877. rRNA_MeTrfase_FtsJ_dom. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
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. SSF52540. SSF52540. 2 hits.
TIGRFAMs	TIGR04240. flavi_E_stem. 1 hit.
PROSITE	PS00690. DEAH_ATP_HELICASE. False negative. 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. PS51591. RNA_CAP01_NS5_MT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLG_DEN1S

Accession

Primary (citable) accession number: P33478

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 29, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program