Reviewed, UniProtKB/Swiss-Prot P09866 (POLG_DEN4D)

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                 Short name=NS2A-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 Dominica/814669/1981) (DENV-4) [Complete proteome]
Taxonomic identifier	408871 [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 By similarity		PRO_0000038000
	Propeptide	100 – 113	14	ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity		PRO_0000038001
	Chain	114 – 279	166	prM By similarity		PRO_0000308297
	Chain	114 – 204	91	Peptide pr By similarity		PRO_0000308298
	Chain	205 – 279	75	Small envelope protein M By similarity		PRO_0000038002
	Chain	280 – 774	495	Envelope protein E By similarity		PRO_0000038003
	Chain	775 – 1126	352	Non-structural protein 1 By similarity		PRO_0000038004
	Chain	1127 – 1344	218	Non-structural protein 2A By similarity		PRO_0000038005
	Chain	1127 – ?		Non-structural protein 2A-alpha By similarity		PRO_0000308299
	Chain	1345 – 1474	130	Serine protease subunit NS2B By similarity		PRO_0000038006
	Chain	1475 – 2092	618	Serine protease subunit NS3 By similarity		PRO_0000038007
	Chain	2093 – 2219	127	Non-structural protein 4A By similarity		PRO_0000038008
	Peptide	2220 – 2242	23	Peptide 2k By similarity		PRO_0000308300
	Chain	2243 – 2487	245	Non-structural protein 4B By similarity		PRO_0000038009
	Chain	2488 – 3387	900	RNA-directed RNA polymerase NS5 By similarity		PRO_0000038010
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
	Glycosylation	346	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	432	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	904	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
Experimental info
	Sequence conflict	780	1	A → V in AAG45436. Ref.2
	Sequence conflict	780	1	A → V in AAK01233. Ref.2
	Sequence conflict	1418	1	I → V in AAG45435. Ref.2
	Sequence conflict	1909	1	P → T in AAK01233. Ref.2
	Sequence conflict	2032	1	K → E in AAG45435. Ref.2
	Sequence conflict	2351	1	V → A in AAG45436. Ref.2
	Sequence conflict	2354	1	L → F in AAG45437. Ref.2
	Sequence conflict	2510	1	K → R in AAK01233. Ref.2
	Sequence conflict	2736	1	K → R in AAG45436. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P09866-1 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: 0CE81B6E7DEFDB5E	FASTA	3,387	378,385
	10 20 30 40 50 60 MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI TFLRVLSIPP 70 80 90 100 110 120 TAGILKRWGQ LKKNKAIKIL IGFRKEIGRM LNILNGRKRS TITLLCLIPT VMAFSLSTRD 130 140 150 160 170 180 GEPLMIVAKH ERGRPLLFKT TEGINKCTLI AMDLGEMCED TVTYKCPLLV NTEPEDIDCW 190 200 210 220 230 240 CNLTSTWVMY GTCTQSGERR REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI 250 260 270 280 290 300 LRNPGFALLA GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV 310 320 330 340 350 360 DLVLEHGGCV TTMAQGKPTL DFELTKTTAK EVALLRTYCI EASISNITTA TRCPTQGEPY 370 380 390 400 410 420 LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC SGKITGNLVQ IENLEYTVVV 430 440 450 460 470 480 TVHNGDTHAV GNDTSNHGVT AMITPRSPSV EVKLPDYGEL TLDCEPRSGI DFNEMILMKM 490 500 510 520 530 540 KKKTWLVHKQ WFLDLPLPWT AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH 550 560 570 580 590 600 SALAGATEVD SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV 610 620 630 640 650 660 VKVKYEGAGA PCKVPIEIRD VNKEKVVGRI ISSTPLAENT NSVTNIELEP PFGDSYIVIG 670 680 690 700 710 720 VGNSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD FGSVGGLFTS LGKAVHQVFG 730 740 750 760 770 780 SVYTTMFGGV SWMIRILIGF LVLWIGTNSR NTSMAMTCIA VGGITLFLGF TVQADMGCVA 790 800 810 820 830 840 SWSGKELKCG SGIFVVDNVH TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV 850 860 870 880 890 900 MWKQITNELN YVLWEGGHDL TVVAGDVKGV LTKGKRALTP PVSDLKYSWK TWGKAKIFTP 910 920 930 940 950 960 EARNSTFLID GPDTSECPNE RRAWNSLEVE DYGFGMFTTN IWMKFREGSS EVCDHRLMSA 970 980 990 1000 1010 1020 AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP KTHTLWSNGV LESQMLIPKS 1030 1040 1050 1060 1070 1080 YAGPFSQHNY RQGYATQTVG PWHLGKLEID FGECPGTTVT IQEDCDHRGP SLRTTTASGK 1090 1100 1110 1120 1130 1140 LVTQWCCRSC TMPPLRFLGE DGCWYGMEIR PLSEKEENMV KSQVTAGQGT SETFSMGLLC 1150 1160 1170 1180 1190 1200 LTLFVEECLR RRVTRKHMIL VVVITLCAII LGGLTWMDLL RALIMLGDTM SGRIGGQIHL 1210 1220 1230 1240 1250 1260 AIMAVFKMSP GYVLGVFLRK LTSRETALMV IGMAMTTVLS IPHDLMELID GISLGLILLK 1270 1280 1290 1300 1310 1320 IVTQFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV TLIPLCRTSC LQKQSHWVEI 1330 1340 1350 1360 1370 1380 TALILGAQAL PVYLMTLMKG ASRRSWPLNE 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 VPSPAATKKA ALSEGVYRIM 1510 1520 1530 1540 1550 1560 QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHETGRLE 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 TPPGATDPFP 1810 1820 1830 1840 1850 1860 QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR KSGKKVIQLS 1870 1880 1890 1900 1910 1920 RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR RCLKPVILPD GPERVILAGP 1930 1940 1950 1960 1970 1980 IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP 1990 2000 2010 2020 2030 2040 TLFGPEREKT QAIDGEFRLR GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG 2050 2060 2070 2080 2090 2100 ERNNQILEEN MEVEIWTREG EKKKLRPRWL DARVYADPMA LKDFKEFASG RKSITLDILT 2110 2120 2130 2140 2150 2160 EIASLPTYLS SRAKLALDNI VMLHTTERGG RAYQHALNEL PESLETLMLV ALLGAMTAGI 2170 2180 2190 2200 2210 2220 FLFFMQGKGI GKLSMGLITI AVASGLLWVA EIQPQWIAAS IILEFFLMVL LIPEPEKQRT 2230 2240 2250 2260 2270 2280 PQDNQLIYVI LTILTIIGLI AANEMGLIEK TKTDFGFYQV 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 ALKDGSKIKH AVSRGSSKIR 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 NLVRCPLSRN 2710 2720 2730 2740 2750 2760 STHEMYWVSG ASGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR SVSTETEKPD 2770 2780 2790 2800 2810 2820 MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS TGSASSMVNG VVKLLTKPWD 2830 2840 2850 2860 2870 2880 VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT PQPKPGTRMV MTTTANWLWA LLGKKKNPRL 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 RLGYILEEID KKDGDLMYAD DTAGWDTRIT EDDLQNEELI TEQMAPHHKI LAKAIFKLTY 3070 3080 3090 3100 3110 3120 QNKVVKVLRP TPRGAVMDII SRKDQRGSGQ VGTYGLNTFT NMEVQLIRQM EAEGVITQDD 3130 3140 3150 3160 3170 3180 MQNPKGLKER VEKWLKECGV DRLKRMAISG DDCVVKPLDE RFGTSLLFLN 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 NMTDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN IHTAITQVRN 3370 3380 LIGKEEYVDY MPVMKRYSAP SESEGVL

References

[1]	Yamashiro T., Shameem G., Lai C.-J. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION.
[2]	"A live attenuated dengue virus type 4 vaccine candidate with a 30 nucleotide deletion in the 3' untranslated region is highly attenuated and immunogenic in humans." Durbin A.P., Karron R.A., Sun W., Vaughn D.W., Reynolds M.J., Perreault J.R., Men R.H., Lai C.-J., Elkins W.R., Chanock R.M., Murphy B.R., Whitehead S.S. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Cloning full-length dengue type 4 viral DNA sequences: analysis of genes coding for structural proteins." Zhao B., Mackow E., Buckler-White A., Markoff L., Chancock R.M., Lai C.-J., Makino Y. Virology 155:77-88(1986) [PubMed: 3022479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-777.
[4]	"The nucleotide sequence of dengue type 4 virus: analysis of genes coding for nonstructural proteins." Mackow E., Makino Y., Zhao B., Zhang Y.M., Markoff L., Buckler-White A., Guiler M., Chanock R., Lai C.-J. Virology 159:217-228(1987) [PubMed: 3039728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 775-3387.
[5]	"In vitro processing of dengue virus structural proteins: cleavage of the pre-membrane protein." Markoff L. J. Virol. 63:3345-3352(1989) [PubMed: 2501515] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF THE M PROTEIN. Strain: 814669.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14931 Genomic RNA. Translation: AAA42964.2.
AF326825 Genomic RNA. Translation: AAG45435.1.
AF326826 Genomic RNA. Translation: AAG45436.1.
AF326827 Genomic RNA. Translation: AAG45437.1.
AF326573 Genomic RNA. Translation: AAK01233.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H0P	NMR	-	A	568-679	[»]

SMR

P09866. Positions 1647-2092, 2494-2755, 2761-3371.

ModBase

Search...

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR011492. DEAD_Flavivir.
IPR001650. DNA/RNA_helicase_C.
IPR002464. DNA/RNA_helicase_DEAH_CS.
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

PS00690. DEAH_ATP_HELICASE. False negative.
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_DEN4D

Accession

Primary (citable) accession number: P09866
Secondary accession number(s): Q88661 , Q88662, Q88663, Q88664, Q88665, Q88666, Q88667, Q88668, Q88669, Q88670, Q88671, Q99BK4, Q9DKQ5, Q9DKQ6, Q9DKQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 16, 2004
Last modified:	November 3, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)