Reviewed, UniProtKB/Swiss-Prot P14340 (POLG_DEN2N)

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             Flavivirin protease NS2B regulatory subunit     10- Recommended name:             Serine protease/NTPase/helicase NS3               EC=3.4.21.91               EC=3.6.1.15               EC=3.6.1.-         Alternative name(s):             Flavivirin protease NS3 catalytic subunit             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:             Methyltransferase/RNA-directed RNA polymerase NS5               EC=2.7.7.48               EC=2.1.1.56               EC=2.1.1.57         Alternative name(s):             Non-structural protein 5
Organism	Dengue virus type 2 (strain Thailand/NGS-C/1944) (DENV-2) [Complete proteome]
Taxonomic identifier	11065 [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	3391 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 performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions 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. 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	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 Ref.4. Peptide pr: Secreted By similarity Ref.4. Small envelope protein M: Virion membrane; Single-pass type I membrane protein By similarity Ref.4. Envelope protein E: Virion membrane; Single-pass type I membrane protein By similarity Ref.4. Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity Ref.4. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane By similarity Ref.4. Non-structural protein 2A: Host endoplasmic reticulum membrane By similarity Ref.4. Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity Ref.4. Serine protease/NTPase/helicase 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 Ref.4. 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. Ref.4 Methyltransferase/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. Ref.3 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 Methyltransferase 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	extrinsic to 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-SubCell 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 protein binding Inferred from physical interaction. Source: IntAct serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NRBP1	Q9UHY1	1	EBI-465733,EBI-749731	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 100	100	Protein C		PRO_0000037958
	Propeptide	101 – 114	14	ER anchor for the protein C, removed in mature form by serine protease NS3		PRO_0000261388
	Chain	115 – 280	166	prM		PRO_0000261389
	Chain	115 – 205	91	Peptide pr		PRO_0000037959
	Chain	206 – 280	75	Small envelope protein M		PRO_0000037960
	Chain	281 – 775	495	Envelope protein E		PRO_0000037961
	Chain	776 – 1127	352	Non-structural protein 1		PRO_0000037962
	Chain	1127 – 1315	189	Non-structural protein 2A-alpha		PRO_0000261390
	Chain	1128 – 1345	218	Non-structural protein 2A		PRO_0000037963
	Chain	1346 – 1475	130	Serine protease subunit NS2B		PRO_0000037964
	Chain	1476 – 2093	618	Serine protease/NTPase/helicase NS3		PRO_0000037965
	Chain	2094 – 2220	127	Non-structural protein 4A		PRO_0000037966
	Peptide	2221 – 2243	23	Peptide 2k		PRO_0000261391
	Chain	2244 – 2491	248	Non-structural protein 4B		PRO_0000037967
	Chain	2492 – 3391	900	Methyltransferase/RNA-directed RNA polymerase NS5		PRO_0000037968
Regions
	Topological domain	1 – 101	101	Cytoplasmic Potential
	Transmembrane	102 – 122	21	Potential
	Topological domain	123 – 238	116	Extracellular Potential
	Transmembrane	239 – 259	21	Potential
	Topological domain	260 – 265	6	Cytoplasmic Potential
	Transmembrane	266 – 286	21	Potential
	Topological domain	287 – 725	439	Extracellular Potential
	Transmembrane	726 – 746	21	Potential
	Topological domain	747 – 752	6	Cytoplasmic Potential
	Transmembrane	753 – 773	21	Potential
	Topological domain	774 – 1156	383	Extracellular Potential
	Transmembrane	1157 – 1177	21	Potential
	Topological domain	1178 – 1447	270	Cytoplasmic Potential
	Transmembrane	1448 – 1468	21	Potential
	Topological domain	1469 – 2192	724	Lumenal Potential
	Transmembrane	2193 – 2213	21	Potential
	Topological domain	2214 – 2220	7	Cytoplasmic Potential
	Transmembrane	2221 – 2240	20	Potential
	Topological domain	2241 – 2347	107	Lumenal Potential
	Transmembrane	2348 – 2368	21	Potential
	Topological domain	2369 – 2413	45	Cytoplasmic Potential
	Transmembrane	2414 – 2434	21	Potential
	Topological domain	2435 – 2459	25	Lumenal Potential
	Transmembrane	2460 – 2480	21	Potential
	Topological domain	2481 – 3391	911	Cytoplasmic Potential
	Domain	1655 – 1811	157	Helicase ATP-binding
	Domain	1821 – 1988	168	Helicase C-terminal
	Domain	3019 – 3168	150	RdRp catalytic
	Nucleotide binding	1668 – 1675	8	ATP Potential
	Motif	1759 – 1762	4	DEAH box
Sites
	Active site	1526	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1550	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1610	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	2552	1	For 2'-O-methyltransferase activity By similarity
	Active site	2637	1	For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
	Active site	2672	1	For 2'-O-methyltransferase activity By similarity
	Active site	2708	1	For 2'-O-methyltransferase activity By similarity
	Site	100 – 101	2	Cleavage; by serine protease NS3 By similarity
	Site	114 – 115	2	Cleavage; by host signal peptidase By similarity
	Site	205 – 206	2	Cleavage; by host furin By similarity
	Site	280 – 281	2	Cleavage; by host signal peptidase By similarity
	Site	775 – 776	2	Cleavage; by host signal peptidase By similarity
	Site	1127 – 1128	2	Cleavage; by host By similarity
	Site	1315 – 1316	2	Cleavage; by serine protease NS3 By similarity
	Site	1345 – 1346	2	Cleavage; by serine protease NS3 By similarity
	Site	1475 – 1476	2	Cleavage; by serine protease NS3 By similarity
	Site	2093 – 2094	2	Cleavage; by serine protease NS3 By similarity
	Site	2220 – 2221	2	Cleavage; by host signal peptidase By similarity
	Site	2243 – 2244	2	Cleavage; by serine protease NS3 By similarity
	Site	2491 – 2492	2	Cleavage; by serine protease NS3 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	982	1	N-linked (GlcNAc...); by host
	Glycosylation	2301	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2305	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2457	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)
	P14340-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: FFF98B4FF5B4BC57	FASTA	3,391	379,501
	10 20 30 40 50 60 MNNQRKKARN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP 70 80 90 100 110 120 PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR TAGMIIMLIP TVMAFHLTTR 130 140 150 160 170 180 NGEPHMIVSR QEKGKSLLFK TEDGVNMCTL MAMDLGELCE DTITYKCPFL KQNEPEDIDC 190 200 210 220 230 240 WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW 250 260 270 280 290 300 ILRHPGFTIM AAILAYTIGT THFQRALIFI LLTAVAPSMT MRCIGISNRD FVEGVSGGSW 310 320 330 340 350 360 VDIVLEHGSC VTTMAKNKPT LDFELIETEA KQPATLRKYC IEAKLTNTTT DSRCPTQGEP 370 380 390 400 410 420 SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMKGKVV QPENLEYTIV 430 440 450 460 470 480 ITPHSGEEHA VGNDTGKHGK EIKITPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ 490 500 510 520 530 540 MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM 550 560 570 580 590 600 HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI 610 620 630 640 650 660 VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII 670 680 690 700 710 720 GVEPGQLKLN WFKKGSSIGQ MIETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF 730 740 750 760 770 780 GAIYGAAFSG VSWIMKILIG VIITWIGMNS RSTSLSVSLV LVGVVTLYLG VMVQADSGCV 790 800 810 820 830 840 VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN 850 860 870 880 890 900 LMWKQITPEL NHILSENEVK LTIMTGDIKG IMQAGKRSLQ PQPTELKYSW KTWGKAKMLS 910 920 930 940 950 960 TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLREKQ DVFCDSKLMS 970 980 990 1000 1010 1020 AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW PKSHTLWSNG VLESEMIIPK 1030 1040 1050 1060 1070 1080 NFAGPVSQHN YRPGYHTQTA GPWHLGKLEM DFDFCEGTTV VVTEDCGNRG PSLRTTTASG 1090 1100 1110 1120 1130 1140 KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QIDNFSLGVL 1150 1160 1170 1180 1190 1200 GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT 1210 1220 1230 1240 1250 1260 YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ STIPETILEL TDALALGMMV 1270 1280 1290 1300 1310 1320 LKMVRKMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKADWIP 1330 1340 1350 1360 1370 1380 LALTIKGLNP TAIFLTTLSR TNKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG 1390 1400 1410 1420 1430 1440 GLLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL 1450 1460 1470 1480 1490 1500 TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVGK AELEDGAYRI 1510 1520 1530 1540 1550 1560 KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL 1570 1580 1590 1600 1610 1620 EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNAGTIGA VSLDFSPGTS GSPIIDKKGK 1630 1640 1650 1660 1670 1680 VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RKLTIMDLHP GAGKTKRYLP 1690 1700 1710 1720 1730 1740 AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF 1750 1760 1770 1780 1790 1800 TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF 1810 1820 1830 1840 1850 1860 PQSNAPIMDE EREIPERSWS SGHEWVTDFK GKTVWFVPSI KAGNDIAACL RKNGKKVIQL 1870 1880 1890 1900 1910 1920 SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG 1930 1940 1950 1960 1970 1980 PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII 1990 2000 2010 2020 2030 2040 PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD 2050 2060 2070 2080 2090 2100 GIKNNQILEE NVEVEIWTKE GERKKLKPRW LDAKIYSDPL ALKEFKEFAA GRKSLTLNLI 2110 2120 2130 2140 2150 2160 TEMGRLPTFM TQKARDALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG 2170 2180 2190 2200 2210 2220 IFLFLMSGRG IGKMTLGMCC IITASILLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR 2230 2240 2250 2260 2270 2280 TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS ITTQQPESNI LDIDLRPASA 2290 2300 2310 2320 2330 2340 WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG 2350 2360 2370 2380 2390 2400 CYSQVNPITL TAALFLLVAH YAIIGPGLQA KATREAQKRA AAGIMKNPTV DGITVIDLDP 2410 2420 2430 2440 2450 2460 IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPISTLWEG NPGRFWNTTI 2470 2480 2490 2500 2510 2520 AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RGTGNIGETL GEKWKSRLNA LGKSEFQIYK 2530 2540 2550 2560 2570 2580 KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY 2590 2600 2610 2620 2630 2640 YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFTPPEK CDTLLCDIGE 2650 2660 2670 2680 2690 2700 SSPNPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP 2710 2720 2730 2740 2750 2760 LSRNSTHEMY WLSNASGNIV SSVNMISRML INRFTMRHKK ATYEPDVDLG SGTRNIGIES 2770 2780 2790 2800 2810 2820 EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MGNGVVRLLT 2830 2840 2850 2860 2870 2880 KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK 2890 2900 2910 2920 2930 2940 TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET 2950 2960 2970 2980 2990 3000 CVYNMMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG 3010 3020 3030 3040 3050 3060 EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG EHKKLAEAIF 3070 3080 3090 3100 3110 3120 KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF 3130 3140 3150 3160 3170 3180 KSIQHLTVTE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRFASALT ALNDMGKVRK 3190 3200 3210 3220 3230 3240 DIQQWEPSRG WNDWTQVPFC SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR 3250 3260 3270 3280 3290 3300 ETACLGKSYA QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM 3310 3320 3330 3340 3350 3360 LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW AKNIQTAINQ 3370 3380 3390 VRSLIGNEEY TDYMPSMKRF RKEEEEAGVL W

References

[1]	"Sequence analysis of cloned dengue virus type 2 genome (New Guinea-C strain)." Irie K., Mohan P.M., Sasaguri Y., Putnak R., Padmanabhan R. Gene 75:197-211(1989) [PubMed: 2714651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Functional and antigenic domains of the dengue-2 virus nonstructural glycoprotein NS-1." Putnak J.R., Charles P.C., Padmanabhan R., Irie K., Hoke C.H., Burke D.S. Virology 163:93-103(1988) [PubMed: 2964755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 749-1225.
[3]	"Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5." Kapoor M., Zhang L., Ramachandra M., Kusukawa J., Ebner K.E., Padmanabhan R. J. Biol. Chem. 270:19100-19106(1995) [PubMed: 7642575] [Abstract] Cited for: PHOSPHORYLATION OF NS5.
[4]	"Subcellular localization and membrane topology of the Dengue virus type 2 Non-structural protein 4B." Miller S., Sparacio S., Bartenschlager R. J. Biol. Chem. 281:8854-8863(2006) [PubMed: 16436383] [Abstract] Cited for: SUBCELLULAR LOCATION OF NON-STRUCTURAL PROTEIN 4B, MEMBRANE TOPOLOGY OF NON-STRUCTURAL PROTEIN 4B.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29095 Genomic RNA. Translation: AAA42941.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DF9	X-ray	2.10	A/B	1476-1660	[»]
2QID	X-ray	2.10	A/B	1476-1660	[»]
2R69	X-ray	3.80	A	578-674	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P14340. 1 interaction.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
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.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR014756. Ig_E-set.
IPR001850. Peptidase_S7.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[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.
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]

PROSITE

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_DEN2N

Accession

Primary (citable) accession number: P14340
Secondary accession number(s): Q66347 , Q66348, Q66349, Q66350, Q66351, Q66352, Q66353, Q66354, Q66355, Q66356, Q89579

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)