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     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 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 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 Endoplasmic reticulum Envelope protein Membrane Nucleus 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, DNA-dependent 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-KW 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 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: UniProtKB-KW
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 subunit 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

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

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

3391

Helix Strand Turn

Details...

Helix

1485 – 1491

7

Beta strand

1515 – 1517

3

Beta strand

1520 – 1522

3

Helix

1525 – 1528

4

Beta strand

1536 – 1538

3

Turn

1547 – 1550

4

Beta strand

1568 – 1573

6

Beta strand

1575 – 1577

3

Turn

1584 – 1586

3

Beta strand

1592 – 1598

7

Beta strand

1603 – 1605

3

Beta strand

1613 – 1619

7

Beta strand

1621 – 1629

9

Beta strand

1637 – 1642

6

Helix

1643 – 1646

4

Turn

1647 – 1649

3

Turn

1653 – 1655

3

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.
[5]	"Crystal structure of Dengue virus NS3 protease in complex with a Bowman-Birk inhibitor: implications for flaviviral polyprotein processing and drug design." Krishna Murthy H.M., Judge K., DeLucas L., Padmanabhan R. J. Mol. Biol. 301:759-767(2000) [PubMed: 10966782] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1470-1660 IN COMPLEX WITH A BOWMAN-BIRK INHIBITOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M29095 Genomic RNA. Translation: AAA42941.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BEF	X-ray	2.10	A	1476-1656	[»]
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	[»]

SMR

P14340. Positions 21-100, 281-674, 1646-2093, 2498-2759, 2765-3374.

ModBase

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Protein-protein interaction databases

IntAct

P14340. 1 interaction.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR011492. DEAD_Flavivir.
IPR001650. DNA/RNA_helicase_C.
IPR000069. Env_glycoprot_M_flavivir.
IPR011999. Flav_glyE_cen_dm.
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.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR001850. Peptidase_S7.
IPR000208. RNA_pol_flaviviral.
IPR007094. RNA_pol_PSvir.
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.
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

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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:	June 16, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)