Reviewed, UniProtKB/Swiss-Prot P12823 (POLG_DEN2P)

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 Puerto Rico/PR159-S1/1969) (DENV-2) [Complete proteome]
Taxonomic identifier	11066 [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	3388 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 serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 100

100

Protein C By similarity

PRO_0000037969

Propeptide

101 – 114

14

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

PRO_0000037970

Chain

115 – 280

166

prM By similarity

PRO_0000308286

Chain

115 – 205

91

Peptide pr By similarity

PRO_0000308287

Chain

206 – 280

75

Small envelope protein M By similarity

PRO_0000037971

Chain

281 – 775

495

Envelope protein E By similarity

PRO_0000037972

Chain

776 – 1127

352

Non-structural protein 1 By similarity

PRO_0000037973

Chain

1128 – 1345

218

Non-structural protein 2A By similarity

PRO_0000037974

Chain

1128 – 1315

188

Non-structural protein 2A-alpha By similarity

PRO_0000308288

Chain

1346 – 1475

130

Serine protease subunit NS2B By similarity

PRO_0000037975

Chain

1476 – 2090

615

Serine protease subunit NS3 By similarity

PRO_0000037976

Chain

2091 – 2217

127

Non-structural protein 4A By similarity

PRO_0000037977

Peptide

2218 – 2240

23

Peptide 2k By similarity

PRO_0000308289

Chain

2241 – 2488

248

Non-structural protein 4B By similarity

PRO_0000037978

Chain

2489 – 3388

900

RNA-directed RNA polymerase NS5 By similarity

PRO_0000037979

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 – 2189

721

Lumenal Potential

Transmembrane

2190 – 2210

21

Potential

Topological domain

2211 – 2217

7

Cytoplasmic Potential

Transmembrane

2218 – 2237

20

Potential

Transmembrane

2345 – 2365

21

Potential

Topological domain

2366 – 2410

45

Cytoplasmic Potential

Transmembrane

2411 – 2431

21

Potential

Topological domain

2432 – 2456

25

Lumenal Potential

Transmembrane

2457 – 2477

21

Potential

Topological domain

2478 – 3388

911

Cytoplasmic Potential

Domain

1655 – 1811

157

Helicase ATP-binding

Domain

1821 – 1988

168

Helicase C-terminal

Domain

3017 – 3166

150

RdRp catalytic

Nucleotide binding

1668 – 1675

8

ATP Potential

Motif

1759 – 1762

4

DEAH box By similarity

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

2090 – 2091

2

Cleavage; by serine protease NS3 By similarity

Site

2217 – 2218

2

Cleavage; by host signal peptidase By similarity

Site

2240 – 2241

2

Cleavage; by serine protease NS3 By similarity

Site

2488 – 2489

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

905

1

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

Glycosylation

982

1

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

Glycosylation

1134

1

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

Glycosylation

2298

1

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

Glycosylation

2302

1

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

Glycosylation

2454

1

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

Disulfide bond

283 ↔ 310

Ref.4

Disulfide bond

340 ↔ 401

Ref.4

Disulfide bond

354 ↔ 385

Ref.4

Disulfide bond

372 ↔ 396

Ref.4

Disulfide bond

465 ↔ 565

Ref.4

Disulfide bond

582 ↔ 613

Ref.4

Experimental info

Sequence conflict

351

1

D → E Ref.4

Sequence conflict

615

1

T → I Ref.4

Sequence conflict

632

1

T → I Ref.4

Sequence conflict

670

1

D → N Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

3388

Helix Strand Turn

Details...

Beta strand

23 – 25

3

Helix

27 – 32

6

Beta strand

34 – 36

3

Helix

45 – 57

13

Helix

63 – 69

7

Helix

75 – 95

21

Helix

288 – 290

3

Beta strand

291 – 293

3

Beta strand

295 – 306

12

Beta strand

311 – 315

5

Beta strand

320 – 332

13

Beta strand

334 – 352

19

Helix

363 – 366

4

Beta strand

370 – 379

10

Helix

381 – 383

3

Beta strand

389 – 409

21

Helix

412 – 414

3

Beta strand

415 – 424

10

Turn

428 – 432

5

Beta strand

440 – 444

5

Beta strand

450 – 455

6

Turn

456 – 458

3

Beta strand

459 – 467

9

Turn

473 – 475

3

Beta strand

476 – 481

6

Beta strand

484 – 489

6

Helix

490 – 495

6

Beta strand

500 – 502

3

Helix

514 – 516

3

Beta strand

518 – 520

3

Beta strand

530 – 532

3

Helix

537 – 543

7

Turn

544 – 546

3

Beta strand

547 – 550

4

Beta strand

552 – 559

8

Beta strand

562 – 571

10

Beta strand

586 – 594

9

Beta strand

600 – 606

7

Beta strand

608 – 610

3

Beta strand

612 – 614

3

Beta strand

617 – 624

8

Beta strand

631 – 633

3

Beta strand

645 – 649

5

Beta strand

653 – 661

9

Beta strand

667 – 673

7

Helix

2497 – 2507

11

Helix

2510 – 2517

8

Turn

2518 – 2520

3

Beta strand

2522 – 2525

4

Helix

2527 – 2535

9

Helix

2546 – 2554

9

Turn

2555 – 2557

3

Beta strand

2563 – 2568

6

Turn

2571 – 2573

3

Helix

2574 – 2579

6

Beta strand

2585 – 2591

7

Helix

2609 – 2611

3

Beta strand

2612 – 2615

4

Helix

2620 – 2622

3

Beta strand

2629 – 2633

5

Helix

2642 – 2657

16

Beta strand

2665 – 2671

7

Helix

2676 – 2688

13

Beta strand

2692 – 2694

3

Beta strand

2706 – 2709

4

Helix

2716 – 2729

14

Beta strand

2739 – 2742

4

Sequences

	Sequence		Length	Mass (Da)
	P12823-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 79B7C87BE64D2D8F	FASTA	3,388	379,219
	10 20 30 40 50 60 MNDQRKKARN 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 TKDGTNMCTL MAMDLGELCE DTITYKCPFL KQNEPEDIDC 190 200 210 220 230 240 WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW 250 260 270 280 290 300 ILRHPGFTIM AAILAYTIGT THFQRVLIFI LLTAIAPSMT MRCIGISNRD FVEGVSGGSW 310 320 330 340 350 360 VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT DSRCPTQGEP 370 380 390 400 410 420 TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKIV QPENLEYTVV 430 440 450 460 470 480 ITPHSGEEHA VGNDTGKHGK EVKITPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ 490 500 510 520 530 540 MKDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM 550 560 570 580 590 600 HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI 610 620 630 640 650 660 VIRVQYEGDG SPCKTPFEIM DLEKRHVLGR LTTVNPIVTE KDSPVNIEAE PPFGDSYIII 670 680 690 700 710 720 GVEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF 730 740 750 760 770 780 GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV LVGIVTLYLG VMVQADSGCV 790 800 810 820 830 840 VSWKNKELKC GSGIFVTDNV HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN 850 860 870 880 890 900 LMWKQITSEL NHILSENEVK LTIMTGDIKG IMQVGKRSLR PQPTELRYSW KTWGKAKMLS 910 920 930 940 950 960 TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLRLREKQ DAFCDSKLMS 970 980 990 1000 1010 1020 AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW PKSHTLWSNG VLESEMVIPK 1030 1040 1050 1060 1070 1080 NFAGPVSQHN NRPGYHTQTA GPWHLGKLEM DFDFCEGTTV VVTEDCGNRG PSLRTTTASG 1090 1100 1110 1120 1130 1140 KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VSSLVTAGHG QIDNFSLGIL 1150 1160 1170 1180 1190 1200 GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT 1210 1220 1230 1240 1250 1260 YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ SSIPETILEL TDALALGMMV 1270 1280 1290 1300 1310 1320 LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKADWIP 1330 1340 1350 1360 1370 1380 LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND TPMTGPLVAG 1390 1400 1410 1420 1430 1440 GLLTVCYVLT GRSADLELER ATDVKWDDQA 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 FRTNTGTIGA VSLDFSPGTS GSPIVDKKGK 1630 1640 1650 1660 1670 1680 VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP 1690 1700 1710 1720 1730 1740 AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF 1750 1760 1770 1780 1790 1800 TMRLLSPIRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF 1810 1820 1830 1840 1850 1860 PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL RKNGKRVIQL 1870 1880 1890 1900 1910 1920 SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG 1930 1940 1950 1960 1970 1980 PMPVTHSSAA QRRGRIGRNP RNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII 1990 2000 2010 2020 2030 2040 PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRRWCFD 2050 2060 2070 2080 2090 2100 GTRNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFAAGRK SLTLNLITEM 2110 2120 2130 2140 2150 2160 GRLPTFMTQK ARDALDNLAV LHTAEAGGKA YNHALSELPE TLETLLLLTL LATVTGGIFL 2170 2180 2190 2200 2210 2220 FLMSGRGIGK MTLGMCCIIT ASILLWYAQI QPHWIAASII LEFFLIVLLI PEPEKQRTPQ 2230 2240 2250 2260 2270 2280 DNQLTYVIIA ILTVVAATMA NEMGFLEKTK KDLGLGNIAT QQPESNILDI DLRPASAWTL 2290 2300 2310 2320 2330 2340 YAVATTFITP MLRHSIENSS VNVSLTAIAN QATVLMGLGK GWPLSKMDIG VPLLAIGCYS 2350 2360 2370 2380 2390 2400 QVNPITLTAA LLLLVAHYAI IGPGLQAKAT REAQKRAAAG IMKNPTVDGI TVIDLDPIPY 2410 2420 2430 2440 2450 2460 DPKFEKQLGQ VMLLVLCVTQ VLMMRTTWAL CEALTLATGP VSTLWEGNPG RFWNTTIAVS 2470 2480 2490 2500 2510 2520 MANIFRGSYL AGAGLLFSIM KNTTSTRRGT GNIGETLGEK WKSRLNALGK SEFQIYKKSG 2530 2540 2550 2560 2570 2580 IQEVDRTLAK EGIKRGETDH HAVSRGSAKL RWFVERNLVT PEGKVVDLGC GRGGWSYYCG 2590 2600 2610 2620 2630 2640 GLKNVREVKG LTKGGPGHEE PIPMSTYGWN LVRLQSGVDV FFVPPEKCDT LLCDIGESSP 2650 2660 2670 2680 2690 2700 NPTVEAGRTL RVLNLVENWL NNNTQFCVKV LNPYMPSVIE RMETLQRKYG GALVRNPLSR 2710 2720 2730 2740 2750 2760 NSTHEMYWVS NASGNIVSSV NMISRMLINR FTMRHKKATY EPDVDLGSGT RNIGIESETP 2770 2780 2790 2800 2810 2820 NLDIIGKRIE KIKQEHETSW HYDQDHPYKT WAYHGSYETK QTGSASSMVN GVVRLLTKPW 2830 2840 2850 2860 2870 2880 DVVPMVTQMA MTDTTPFGQQ RVFKEKVDTR TQEPKEGTKK LMKITAEWLW KELGKKKTPR 2890 2900 2910 2920 2930 2940 MCTREEFTKK VRSNAALGAI FTDENKWKSA REAVEDSRFW ELVDKERNLH LEGKCETCVY 2950 2960 2970 2980 2990 3000 NMMGKREKKL GEFGKAKGSR AIWYMWLGAR FLEFEALGFL NEDHWFSREN SLSGVEGEGL 3010 3020 3030 3040 3050 3060 HKLGYILREV SKKEGGAMYA DDTAGWDTRI TIEDLKNEEM ITNHMAGEHK KLAEAIFKLT 3070 3080 3090 3100 3110 3120 YQNKVVRVQR PTPRGTVMDI ISRRDQRGSG QVGTYGLNTF TNMEAQLIRQ MEGEGIFKSI 3130 3140 3150 3160 3170 3180 QHLTASEEIA VQDWLARVGR ERLSRMAISG DDCVVKPLDD RFARALTALN DMGKVRKDIQ 3190 3200 3210 3220 3230 3240 QWEPSRGWND WTQVPFCSHH FHELIMKDGR TLVVPCRNQD ELIGRARISQ GAGWSLRETA 3250 3260 3270 3280 3290 3300 CLGKSYAQMW SLMYFHRRDL RLAANAICSA VPSHWVPTSR TTWSIHASHE WMTTEDMLTV 3310 3320 3330 3340 3350 3360 WNKVWILENP WMEDKTPVES WEEIPYLGKR EDQWCGSLIG LTSRATWAKN IQTAINQVRS 3370 3380 LIGNEEYTDY MPSMKRFRRE EEEAGVLW

References

[1]	"Nucleotide sequence of dengue 2 RNA and comparison of the encoded proteins with those of other flaviviruses." Hahn Y.S., Galler R., Hunkapiller T., Dalrymple J.M., Strauss J.H., Strauss E.G. Virology 162:167-180(1988) [PubMed: 2827375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Definition of the carboxy termini of the three glycoproteins specified by dengue virus type 2." Wright P.J., Cauchi M.R., Ng M.L. Virology 171:61-67(1989) [PubMed: 2741348] [Abstract] Cited for: C-TERMINUS OF M; E AND NS1. Strain: New-Guinea.
[3]	"An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization." Egloff M.P., Benarroch D., Selisko B., Romette J.L., Canard B. EMBO J. 21:2757-2768(2002) [PubMed: 12032088] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2494-2783.
[4]	"A ligand-binding pocket in the dengue virus envelope glycoprotein." Modis Y., Ogata S., Clements D., Harrison S.C. Proc. Natl. Acad. Sci. U.S.A. 100:6986-6991(2003) [PubMed: 12759475] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 281-674, DISULFIDE BONDS.
[5]	"Structures of immature flavivirus particles." Zhang Y., Corver J., Chipman P.R., Zhang W., Pletnev S.V., Sedlak D., Baker T.S., Strauss J.H., Kuhn R.J., Rossmann M.G. EMBO J. 22:2604-2613(2003) [PubMed: 12773377] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16 ANGSTROMS) OF IMMATURE PARTICLES.
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBLGenBankDDBJ

M19197 Genomic RNA. Translation: AAA42962.1.

PIR

GNWVDP. A29972.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L9K	X-ray	2.40	A	2492-2784	[»]
1OAN	X-ray	2.75	A/B	281-674	[»]
1OK8	X-ray	2.00	A	281-674	[»]
1OKE	X-ray	2.40	A/B	281-674	[»]
1P58	electron microscopy	9.50	A/B/C	281-775	[»]
			D/E/F	206-280	[»]
1R6A	X-ray	2.60	A	2492-2784	[»]
1R6R	NMR	-	A/B	1-100	[»]
1THD	electron microscopy	9.50	A/B/C	281-675	[»]
2P1D	X-ray	2.90	A	2492-2784	[»]
2P3L	X-ray	2.20	A	2492-2784	[»]
2P3O	X-ray	2.76	A	2492-2784	[»]
2P3Q	X-ray	2.75	A	2492-2784	[»]
2P40	X-ray	2.70	A	2492-2784	[»]
2P41	X-ray	1.80	A	2492-2784	[»]

SMR

P12823. Positions 1480-1656, 1646-2090, 2762-3371.

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.
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

PS00690. DEAH_ATP_HELICASE. False negative.
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_DEN2P

Accession

Primary (citable) accession number: P12823
Secondary accession number(s): Q88646 , Q88647, Q88648, Q88649, Q88650, Q88651, Q88652, Q88653, Q88654, Q88655

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)