Reviewed, UniProtKB/Swiss-Prot Q2YHF0 (POLG_DEN4T)

Names and origin

Protein names	Recommended name:     Genome polyprotein Cleaved into the following 14 chains:     1- Recommended name:             Protein C         Alternative name(s):             Core protein             Capsid protein     2- Recommended name:             prM     3- Recommended name:             Peptide pr     4- Recommended name:             Small envelope protein M         Alternative name(s):             Matrix protein     5- Recommended name:             Envelope protein E     6- Recommended name:             Non-structural protein 1                 Short name=NS1     7- Recommended name:             Non-structural protein 2A                 Short name=NS2A     8- Recommended name:             Non-structural protein 2A-alpha     9- Recommended name:             Serine protease subunit NS2B         Alternative name(s):             Non-structural protein 2B     10- Recommended name:             Serine protease subunit NS3               EC=3.4.21.91         Alternative name(s):             Non-structural protein 3     11- Recommended name:             Non-structural protein 4A                 Short name=NS4A     12- Recommended name:             Peptide 2k     13- Recommended name:             Non-structural protein 4B                 Short name=NS4B     14- Recommended name:             RNA-directed RNA polymerase NS5               EC=2.7.7.48               EC=2.1.1.56         Alternative name(s):             Non-structural protein 5
Organism	Dengue virus type 4 (strain Thailand/0348/1991) (DENV-4) [Complete proteome]
Taxonomic identifier	408688 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group
Virus host	Aedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159] Aedes albopictus (Asian tiger mosquito) (Culex albopictus) [TaxID: 7160] Homo sapiens (Human) [TaxID: 9606] Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]

Protein attributes

Sequence length	3387 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	Protein C packages viral RNA to form a viral nucleocapsid, and promotes virion budding 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 binds cell surface receptor and is involved in membrane fusion between virion and target cell. 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 slowly secreted from mammalian cells, but not from mosquito cells. Secreted form elicits protective immune response and plays an essential role in RNA replication. 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 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, 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 plays a role in RNA replication. Enhances inhibition of cell antiviral response by non-structural protein 4B By similarity. Non-structural protein 4B prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways By similarity. RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and assure the capping of genomes in the cytoplasm. May be involved in methylation of 5'RNA cap structure 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). S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
Subunit structure	prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. Envelope protein E forms homodimers. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form an heterodimer. NS3 interacts with unphosphorylated NS5 By similarity.
Subcellular location	Protein C: Virion By similarity. Peptide pr: Secreted By similarity. Small envelope protein M: Virion membrane; Single-pass type I membrane protein By similarity. Envelope protein E: Virion membrane; Single-pass type I 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 By similarity. Non-structural protein 2A: Host endoplasmic reticulum membrane By similarity. Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Serine protease subunit NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Non-structural protein 4A: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: The C-terminal transmembrane domain of non-structural protein 4B is presumably reoriented after cleavage on the lumenal side By similarity. RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus By similarity.
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 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.
Miscellaneous	The virion is assembled in the endoplasmic reticulum lumen, transported by vesicles to the Golgi, then transported again to the cell membrane where it is released outside the cell.
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	RNA replication Transcription Transcription regulation
Cellular component	Capsid protein Envelope protein Host endoplasmic reticulum Host membrane Host nucleus Membrane Secreted Virion
Domain	Transmembrane
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Viral nucleoprotein
Molecular function	Helicase Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Ribonucleoprotein Serine protease Transferase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	RNA metabolic process Inferred from electronic annotation. Source: InterPro methylation Inferred from electronic annotation. Source: InterPro regulation of transcription 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	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoprotein complex 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
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase 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 – 99

99

Protein C

PRO_0000268131

Propeptide

100 – 113

14

ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity

PRO_0000268132

Chain

114 – 279

166

prM

PRO_0000268133

Chain

114 – 204

91

Peptide pr

PRO_0000268134

Chain

205 – 279

75

Small envelope protein M

PRO_0000268135

Chain

280 – 774

495

Envelope protein E

PRO_0000268136

Chain

775 – 1126

352

Non-structural protein 1

PRO_0000268137

Chain

1127 – 1344

218

Non-structural protein 2A

PRO_0000268138

Chain

1127 – ?

Non-structural protein 2A-alpha

PRO_0000304550

Chain

1345 – 1474

130

Serine protease subunit NS2B

PRO_0000268139

Chain

1475 – 2092

618

Serine protease subunit NS3

PRO_0000268140

Chain

2093 – 2219

127

Non-structural protein 4A

PRO_0000268141

Peptide

2220 – 2242

23

Peptide 2k

PRO_0000268142

Chain

2243 – 2487

245

Non-structural protein 4B

PRO_0000268143

Chain

2488 – 3387

900

RNA-directed RNA polymerase NS5

PRO_0000268144

Regions

Topological domain

1 – 100

100

Cytoplasmic Potential

Transmembrane

101 – 121

21

Potential

Topological domain

122 – 237

116

Extracellular Potential

Transmembrane

238 – 258

21

Potential

Topological domain

259 – 264

6

Cytoplasmic Potential

Transmembrane

265 – 285

21

Potential

Topological domain

286 – 724

439

Extracellular Potential

Transmembrane

725 – 745

21

Potential

Topological domain

746 – 751

6

Cytoplasmic Potential

Transmembrane

752 – 772

21

Potential

Topological domain

773 – 1155

383

Extracellular Potential

Transmembrane

1156 – 1176

21

Potential

Topological domain

1177 – 1446

270

Cytoplasmic Potential

Transmembrane

1447 – 1467

21

Potential

Topological domain

1468 – 2191

724

Lumenal Potential

Transmembrane

2192 – 2212

21

Potential

Topological domain

2213 – 2219

7

Cytoplasmic Potential

Transmembrane

2220 – 2239

20

Potential

Topological domain

2240 – 2343

104

Lumenal Potential

Transmembrane

2344 – 2364

21

Potential

Topological domain

2365 – 2409

45

Cytoplasmic Potential

Transmembrane

2410 – 2430

21

Potential

Topological domain

2431 – 2455

25

Lumenal Potential

Transmembrane

2456 – 2476

21

Potential

Topological domain

2477 – 3387

911

Cytoplasmic Potential

Domain

1654 – 1810

157

Helicase ATP-binding

Domain

1820 – 1987

168

Helicase C-terminal

Domain

3016 – 3166

151

RdRp catalytic

Nucleotide binding

1667 – 1674

8

ATP Potential

Motif

1758 – 1761

4

DEAH box By similarity

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

Site

99 – 100

2

Cleavage; by serine protease NS3 By similarity

Site

113 – 114

2

Cleavage; by host signal peptidase By similarity

Site

204 – 205

2

Cleavage; by host furin By similarity

Site

279 – 280

2

Cleavage; by host signal peptidase By similarity

Site

774 – 775

2

Cleavage; by host signal peptidase By similarity

Site

1126 – 1127

2

Cleavage; by host By similarity

Site

1344 – 1345

2

Cleavage; by serine protease NS3 By similarity

Site

1474 – 1475

2

Cleavage; by serine protease NS3 By similarity

Site

2092 – 2093

2

Cleavage; by serine protease NS3 By similarity

Site

2219 – 2220

2

Cleavage; by host signal peptidase By similarity

Site

2242 – 2243

2

Cleavage; by serine protease NS3 By similarity

Site

2487 – 2488

2

Cleavage; by serine protease NS3 By similarity

Amino acid modifications

Glycosylation

182

1

N-linked (GlcNAc...); by host Potential

Glycosylation

346

1

N-linked (GlcNAc...); by host Potential

Glycosylation

432

1

N-linked (GlcNAc...); by host Potential

Glycosylation

981

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2297

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2301

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2453

1

N-linked (GlcNAc...); by host Potential

Disulfide bond

282 ↔ 309

By similarity

Disulfide bond

339 ↔ 400

By similarity

Disulfide bond

353 ↔ 384

By similarity

Disulfide bond

371 ↔ 395

By similarity

Disulfide bond

464 ↔ 564

By similarity

Disulfide bond

581 ↔ 612

By similarity

Secondary structure

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3387

Helix Strand Turn

Details...

Helix

1654 – 1657

4

Beta strand

1662 – 1665

4

Helix

1677 – 1687

11

Beta strand

1692 – 1698

7

Helix

1699 – 1708

10

Beta strand

1714 – 1716

3

Beta strand

1731 – 1735

5

Helix

1736 – 1745

10

Beta strand

1753 – 1758

6

Turn

1759 – 1761

3

Helix

1765 – 1770

6

Helix

1774 – 1779

6

Beta strand

1784 – 1788

5

Beta strand

1806 – 1810

5

Helix

1823 – 1827

5

Beta strand

1832 – 1835

4

Beta strand

1837 – 1839

3

Helix

1844 – 1850

7

Beta strand

1856 – 1859

4

Turn

1861 – 1863

3

Helix

1864 – 1867

4

Helix

1868 – 1872

5

Beta strand

1877 – 1881

5

Helix

1883 – 1886

4

Beta strand

1896 – 1898

3

Beta strand

1901 – 1908

8

Beta strand

1914 – 1918

5

Beta strand

1920 – 1922

3

Helix

1925 – 1931

7

Beta strand

1944 – 1948

5

Helix

1960 – 1969

10

Helix

1987 – 1989

3

Helix

2003 – 2012

10

Helix

2018 – 2026

9

Helix

2035 – 2037

3

Helix

2042 – 2044

3

Beta strand

2054 – 2056

3

Beta strand

2062 – 2064

3

Helix

2072 – 2074

3

Helix

2078 – 2088

11

Sequences

	Sequence		Length	Mass (Da)
	Q2YHF0-1 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 1FEDC2D663A0F945	FASTA	3,387	378,438
	10 20 30 40 50 60 MNQRKKVARP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI TFLRVLSIPP 70 80 90 100 110 120 TAGILKRWGQ LKKNKAIKIL TGFRKEIGRM LNILNGRKRS TITLLCLIPT VMAFHLSTRD 130 140 150 160 170 180 GEPLMIVAKH ERGRPLLFKT TEGINKCTLI AMDLGEMCED TVTYKCPLLV NTEPEDIDCW 190 200 210 220 230 240 CNLTSAWVMY GTCTQSGERR REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI 250 260 270 280 290 300 LRNPGFALLA GFMAYMIGQT GIQRTVFFIL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV 310 320 330 340 350 360 DLVLEHGGCV TTMAQGKPTL DFELIKTTAK EVALLRTYCI EASISNITTA TRCPTQGEPY 370 380 390 400 410 420 LKEEQDQQYI CRRDMVDRGW GNGCGLFGKG GVVTCAKFSC SGKITGNLVQ IENLEYTVVV 430 440 450 460 470 480 TVHNGDTHAV GNDTSNHGVT ATITPRSPSV EVKLPDYGEL TLDCEPRSGI DFNEMILMKM 490 500 510 520 530 540 KTKTWLVHKQ WFLDLPLPWT AGADTLEVHW NHKERMVTFK VPHAKRQDVT VLGSQEGAMH 550 560 570 580 590 600 SALAGATEVD SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV 610 620 630 640 650 660 VKVKYEGTGA PCKVPIEIRD VNKEKVVGRI ISSTPFAENT NSVTNIELEP PFGDSYIVIG 670 680 690 700 710 720 VGDSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD FGSVGGLLTS LGKAVHQVFG 730 740 750 760 770 780 SVYTTMFGGV SWMVRILIGL LVLWIGTNSR NTSMAMSCIA VGGITLFLGF TVHADMGCAV 790 800 810 820 830 840 SWSGKELKCG SGIFVIDNVH TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV 850 860 870 880 890 900 MWKQITNELN YVLWEGGHDL TVVAGDVKGV LSKGKRALAP PVNDLKYSWK TWGKAKIFTP 910 920 930 940 950 960 ETRNSTFLVD GPDTSECPNE RRAWNFLEVE DYGFGMFTTN IWMKFREGSS EVCDHRLMSA 970 980 990 1000 1010 1020 AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP KTHTLWSNGV LESQMLIPKA 1030 1040 1050 1060 1070 1080 YAGPISQHNY RQGYATQTVG PWHLGKLEID FGECPGTTVT IQEDCDHRGP SLRTTTASGK 1090 1100 1110 1120 1130 1140 LVTQWCCRSC TMPPLRFLGE DGCWYGMEIR PLNEKEENMV KSQVSAGQGT SETFSMGLLC 1150 1160 1170 1180 1190 1200 LTLFVEECLR RRVTRKHMIL VVVTTLCAII LGGLTWMDLL RALIMLGDTM SGRMGGQIHL 1210 1220 1230 1240 1250 1260 AIMAVFKMSP GYVLGIFLRK LTSRETALMV IGMAMTTVLS IPHDLMEFID GISLGLILLK 1270 1280 1290 1300 1310 1320 MVTHFDNTQV GTLALSLTFI KSTMPLVMAW RTIMAVLFVV TLIPLCRTSC LQKQSHWVEI 1330 1340 1350 1360 1370 1380 TALILGAQAL PVYLMTLMKG ASKRSWPLNE GIMAVGLVSL LGSALLKNDV PLAGPMVAGG 1390 1400 1410 1420 1430 1440 LLLAAYVMSG SSADLSLEKA ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDVEETNMIT 1450 1460 1470 1480 1490 1500 LLVKLALITV SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAAAQKA TLTEGVYRIM 1510 1520 1530 1540 1550 1560 QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHESGRLE PSWADVRNDM ISYGGGWRLG 1570 1580 1590 1600 1610 1620 DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV TLDFKPGTSG SPIINRKGKV 1630 1640 1650 1660 1670 1680 IGLYGNGVVT KSGDYVSAIT QAERIGEPDY EVDEDIFRKK RLTIMDLHPG AGKTKRILPS 1690 1700 1710 1720 1730 1740 IVREALKRRL RTLILAPTRV VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT 1750 1760 1770 1780 1790 1800 TRLLSSTRVP NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGTTDPFP 1810 1820 1830 1840 1850 1860 QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR KSGKKVIQLS 1870 1880 1890 1900 1910 1920 RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR RCLKPVILTD GPERVILAGP 1930 1940 1950 1960 1970 1980 IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG DPLRNDEDHA HWTEAKMLLD NIYTPEGIIP 1990 2000 2010 2020 2030 2040 TLFGPEREKT QAIDGEFRLR GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG 2050 2060 2070 2080 2090 2100 ERNNQILEEN MEVEIWTREG EKKKLRPKWL DARVYADPMA LKDFKEFASG RKSITLDILT 2110 2120 2130 2140 2150 2160 EIASLPTYLS SRAKLALDNI VMLHTTERGG KAYQHALNEL PESLETLMLV ALLGAMTAGI 2170 2180 2190 2200 2210 2220 FLFFMQGKGI GKLSMGLIAI AVASGLLWVA EIQPQWIAAS IILEFFLMVL LVPEPEKQRT 2230 2240 2250 2260 2270 2280 PQDNQLIYVI LTILTIIALV AANEMGLIEK TKTDFGFYQA KTETTILDVD LRPASAWTLY 2290 2300 2310 2320 2330 2340 AVATTILTPM LRHTIENTSA NLSLAAIANQ AAVLMGLGKG WPLHRMDLGV PLLAMGCYSQ 2350 2360 2370 2380 2390 2400 VNPTTLTASL VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD 2410 2420 2430 2440 2450 2460 PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPI LTLWEGNPGR FWNTTIAVST 2470 2480 2490 2500 2510 2520 ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW KRQLNSLDRK EFEEYKRSGI 2530 2540 2550 2560 2570 2580 LEVDRTEAKS ALKDGSKIKY AVSRGTSKIR WIVERGMVKP KGKVVDLGCG RGGWSYYMAT 2590 2600 2610 2620 2630 2640 LKNVTEVKGY TKGGPGHEEP IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN 2650 2660 2670 2680 2690 2700 PTIEEGRTLR VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG SLVRCPLSRN 2710 2720 2730 2740 2750 2760 STHEMYWVSG VSGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDADLGAGTR SVSTETEKPD 2770 2780 2790 2800 2810 2820 MTIIGRRLQR LQEEHKETWH YDHENPYRTW AYHGSYEAPS TGSASSMVNG VVKLLTKPWD 2830 2840 2850 2860 2870 2880 VVPMVTQLAM TDTTPFGQQR VFKEKVDTRT PQPKPGTRVV MTTTANWLWA LLGRKKNPRL 2890 2900 2910 2920 2930 2940 CTREEFISKV RSNAAIGAVF QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGKCESCVYN 2950 2960 2970 2980 2990 3000 MMGKREKKLG EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH 3010 3020 3030 3040 3050 3060 RLGYILEDID KKDGDLIYAD DTAGWDTRIT EDDLLNEELI TEQMAPHHKI LAKAIFKLTY 3070 3080 3090 3100 3110 3120 QNKVVKVLRP TPKGAVMDII SRKDQRGSGQ VGTYGLNTFT NMEVQLIRQM EAEGVITRDD 3130 3140 3150 3160 3170 3180 MHNPKGLKER VEKWLKECGV DRLKRMAISG DDCVVKPLDE RFSTSLLFLN DMGKVRKDIP 3190 3200 3210 3220 3230 3240 QWEPSKGWKN WQEVPFCSHH FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA 3250 3260 3270 3280 3290 3300 CLGKAYAQMW SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV 3310 3320 3330 3340 3350 3360 WNRVWIEDNP NMIDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN IQTAITQVRN 3370 3380 LIGKEEYVDY MPVMKRYSAH FESEGVL

References

[1]	"The molecular epidemiology of dengue virus serotype 4 in Bangkok, Thailand." Klungthong C., Zhang C., Mammen M.P. Jr., Ubol S., Holmes E.C. Virology 329:168-179(2004) [PubMed: 15476884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AY618990 Genomic RNA. Translation: AAU89377.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JLQ	X-ray	1.67	A	1646-2092	[»]
2JLR	X-ray	2.00	A	1646-2092	[»]
2JLS	X-ray	2.23	A	1646-2092	[»]
2JLU	X-ray	2.04	A/B	1646-2092	[»]
2JLV	X-ray	2.30	A/B	1646-2092	[»]
2JLW	X-ray	2.60	A/B	1646-2092	[»]
2JLX	X-ray	2.20	A/B	1646-2092	[»]
2JLY	X-ray	2.40	A/B	1646-2092	[»]
2JLZ	X-ray	2.20	A/B	1646-2092	[»]

SMR

Q2YHF0. Positions 1647-2092, 2494-2755, 2761-3371.

ModBase

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Protein family/group databases

MEROPS

S07.001.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR011492. DEAD_Flavivir.
IPR001650. DNA/RNA_helicase_C.
IPR000069. Env_glycoprot_M_flavivir.
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.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR001850. Peptidase_S7.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
[Graphical view]

Gene3D

G3DSA:2.60.98.10. Flav_glyE_dim. 1 hit.
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.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]

PIRSF

PIRSF003817. Gen_Poly_FLV. 1 hit.

ProDom

PD001496. Flavi_NS1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00487. DEXDc. 1 hit.
[Graphical view]

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. False negative.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

POLG_DEN4T

Accession

Primary (citable) accession number: Q2YHF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 20, 2005
Last modified:	November 3, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)