Reviewed, UniProtKB/Swiss-Prot P27909 (POLG_DEN1B)

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 1 (strain Brazil/97-11/1997) (DENV-1) [Complete proteome]
Taxonomic identifier	408685 [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] Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	3392 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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	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		PRO_0000264634
	Propeptide	101 – 114	14	ER anchor for the protein C, removed in mature form by serine protease NS3		PRO_0000264635
	Chain	115 – 280	166	prM		PRO_0000264636
	Chain	115 – 205	91	Peptide pr		PRO_0000264637
	Chain	206 – 280	75	Small envelope protein M		PRO_0000264638
	Chain	281 – 775	495	Envelope protein E		PRO_0000264639
	Chain	776 – 1127	352	Non-structural protein 1		PRO_0000264640
	Chain	1128 – 1345	218	Non-structural protein 2A		PRO_0000264641
	Chain	1128 – 1315	188	Non-structural protein 2A-alpha		PRO_0000264642
	Chain	1346 – 1475	130	Serine protease subunit NS2B		PRO_0000264643
	Chain	1476 – 2094	619	Serine protease subunit NS3		PRO_0000264644
	Chain	2095 – 2221	127	Non-structural protein 4A		PRO_0000264645
	Peptide	2222 – 2244	23	Peptide 2k		PRO_0000264646
	Chain	2245 – 2493	249	Non-structural protein 4B		PRO_0000264647
	Chain	2494 – 3392	899	RNA-directed RNA polymerase NS5		PRO_0000264648
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 – 723	437	Extracellular Potential
	Transmembrane	724 – 746	23	Potential
	Topological domain	747 – 750	4	Cytoplasmic Potential
	Transmembrane	751 – 773	23	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 – 2193	725	Lumenal Potential
	Transmembrane	2194 – 2214	21	Potential
	Topological domain	2215 – 2221	7	Cytoplasmic Potential
	Transmembrane	2222 – 2241	20	Potential
	Topological domain	2242 – 2349	108	Lumenal Potential
	Transmembrane	2350 – 2370	21	Potential
	Topological domain	2371 – 2415	45	Cytoplasmic Potential
	Transmembrane	2416 – 2436	21	Potential
	Topological domain	2437 – 2461	25	Lumenal Potential
	Transmembrane	2462 – 2482	21	Potential
	Topological domain	2483 – 3392	910	Cytoplasmic Potential
	Domain	1656 – 1812	157	Helicase ATP-binding
	Domain	1822 – 1989	168	Helicase C-terminal
	Domain	3021 – 3170	150	RdRp catalytic
	Nucleotide binding	1669 – 1676	8	ATP Potential
	Motif	1760 – 1763	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	2094 – 2095	2	Cleavage; by serine protease NS3 By similarity
	Site	2221 – 2222	2	Cleavage; by host signal peptidase By similarity
	Site	2244 – 2245	2	Cleavage; by serine protease NS3 By similarity
	Site	2493 – 2494	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 Potential
	Glycosylation	2303	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2307	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2459	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
Natural variations
	Natural variant	394	1	L → I in strain: Isolate Thailand/TH-Sman/1958.
	Natural variant	402	1	V → A in strain: Isolate Thailand/TH-Sman/1958.
	Natural variant	441	1	I → T in strain: Isolate Thailand/TH-Sman/1958.
	Natural variant	475 – 476	2	EM → RV in strain: Isolate 924-1.
	Natural variant	483	1	E → K in strain: Isolate 924-1.
	Natural variant	531	1	V → A in strain: Isolate 924-1 and Isolate Thailand/TH-Sman/1958.
	Natural variant	577	1	T → M in strain: Isolate 924-1 and Isolate Thailand/TH-Sman/1958.
	Natural variant	619	1	T → S in strain: Isolate 924-1.
	Natural variant	649	1	T → E in strain: Isolate 924-1 and Isolate Thailand/TH-Sman/1958.
	Natural variant	677	1	S → I in strain: Isolate Thailand/TH-Sman/1958n.
	Natural variant	712	1	V → M in strain: Isolate Thailand/TH-Sman/1958.
	Natural variant	716	1	V → I in strain: Isolate 924-1.
	Natural variant	719	1	V → I in strain: Isolate 924-1.
	Natural variant	752	1	S → N in strain: Isolate Thailand/TH-Sman/1958.
	Natural variant	758	1	T → M in strain: Isolate Thailand/TH-Sman/1958.

Sequences

	Sequence		Length	Mass (Da)
	P27909-1 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: BBD894175578E164	FASTA	3,392	378,905
	10 20 30 40 50 60 MNNQRKKTGR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP 70 80 90 100 110 120 PTAGILARWS SFKKNGAIKV LRGFKKEISS MLNIMNRRKR SVTMLLMLLP TALAFHLTTR 130 140 150 160 170 180 GGEPHMIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC 190 200 210 220 230 240 WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW 250 260 270 280 290 300 ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW 310 320 330 340 350 360 VDVVLEHGSC VTTMAKNKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA 370 380 390 400 410 420 TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK CVTKLEGKIV QYENLKYSVI 430 440 450 460 470 480 VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT 490 500 510 520 530 540 MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM 550 560 570 580 590 600 HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGTSYV MCTGSFKLEK EVAETQHGTV 610 620 630 640 650 660 LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR LITANPIVTD KEKPVNIETE PPFGESYIVV 670 680 690 700 710 720 GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQVF 730 740 750 760 770 780 GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV 790 800 810 820 830 840 INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGRAWEEGVC GIRSATRLEN 850 860 870 880 890 900 IMWKQISNEL NHILLENDIK FTVVVGNANG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG 910 920 930 940 950 960 ADIQNTTFII DGPDTPECPD EQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQMCDHRLMS 970 980 990 1000 1010 1020 AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK 1030 1040 1050 1060 1070 1080 MYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGSRG PSLRTTTVTG 1090 1100 1110 1120 1130 1140 KIIHEWCCRS CTLPPLRFRG EDGCWYGMEI RPVKEKEENL VRSMVSAGSG EVDSFSLGIL 1150 1160 1170 1180 1190 1200 CVSIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMVGAN ASDKMGMGTT 1210 1220 1230 1240 1250 1260 YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL GDGLAMGIMM 1270 1280 1290 1300 1310 1320 LKLLTEFQPH QLWTTLLSLT FIKTTLSLDY AWKTTAMVLS IVSLFPLCLS TTSQKTTWLP 1330 1340 1350 1360 1370 1380 VLLGSFGCKP LTMFLITENE IWGRKSWPLN EGIMAIGIVS ILLSSLLKND VPLAGPLIAG 1390 1400 1410 1420 1430 1440 GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGTSHNIL VEVQDDGTMK IKDEERDDTL 1450 1460 1470 1480 1490 1500 TILLKATLLA VSGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI 1510 1520 1530 1540 1550 1560 LQRGLLGRSQ VGVGVFQDGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRF 1570 1580 1590 1600 1610 1620 QGSWNTGEEV QVIAVEPGKN PKNVQTTPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK 1630 1640 1650 1660 1670 1680 IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFK KRNLTIMDLH PGSGKTRRYL 1690 1700 1710 1720 1730 1740 PAIVREAIKR KLRTLILAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGR EIVDLMCHAT 1750 1760 1770 1780 1790 1800 FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA 1810 1820 1830 1840 1850 1860 FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ 1870 1880 1890 1900 1910 1920 LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA 1930 1940 1950 1960 1970 1980 GPMPVTVASA AQRRGRIGRN QNKEGDQYVY MGQPLNNDED HAHWTEAKML LDNINTPEGI 1990 2000 2010 2020 2030 2040 IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF 2050 2060 2070 2080 2090 2100 DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL 2110 2120 2130 2140 2150 2160 ILEIGKLPQH LTLRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG 2170 2180 2190 2200 2210 2220 GVTLFFLSGK GLGKTSIGLL CVTASSALLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ 2230 2240 2250 2260 2270 2280 RTPQDNQLAY VVIGLLFMIL TVAANEMGLL ETTKKDLGIG HVAAENHQHA TILDVDLHPA 2290 2300 2310 2320 2330 2340 SAWTLYAVAT TVITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDLGVPLLA 2350 2360 2370 2380 2390 2400 LGCYSQVNPL TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL 2410 2420 2430 2440 2450 2460 DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT 2470 2480 2490 2500 2510 2520 TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT 2530 2540 2550 2560 2570 2580 YKRSGIMEVD RSEAKEGLKR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW 2590 2600 2610 2620 2630 2640 SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLH SGKDVFFMPP EKCDTLLCDI 2650 2660 2670 2680 2690 2700 GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN 2710 2720 2730 2740 2750 2760 PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE 2770 2780 2790 2800 2810 2820 PEVANLDIIG QRIENIKNEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL 2830 2840 2850 2860 2870 2880 TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPRAKR GTAQIMEVTA KWLWGFLSRN 2890 2900 2910 2920 2930 2940 KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA 2950 2960 2970 2980 2990 3000 TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE 3010 3020 3030 3040 3050 3060 GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI 3070 3080 3090 3100 3110 3120 FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEVQ LIRQMESEGI 3130 3140 3150 3160 3170 3180 FFPSELESPN LAERVLDWLE KHGAERLKRM AISGDDCVVK PIDDRFATAL IALNDMGKVR 3190 3200 3210 3220 3230 3240 KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL 3250 3260 3270 3280 3290 3300 RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED 3310 3320 3330 3340 3350 3360 MLSVWNRVWI EENPWMEDKT HVSSWEEVPY LGKREDQWCG SLIGLTARAT WATNIQVAIN 3370 3380 3390 QVRRLIGNEN YLDYMTSMKR FKNESDPEGA LW

References

[1]	"Genetic relatedness among structural protein genes of dengue 1 virus strains." Chu M.C., O'Rourke E.J., Trent D.W. J. Gen. Virol. 70:1701-1712(1989) [PubMed: 2738579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 232-786. Strain: Isolate Caribbean/924-1.
[2]	"Envelope protein sequences of dengue virus isolates TH-36 and TH-Sman, and identification of a type-specific genetic marker for dengue and tick-borne flaviviruses." Shiu S.Y.W., Jiang W.R., Porterfield J.S., Gould E.A. J. Gen. Virol. 73:207-212(1992) [PubMed: 1339466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 281-778. Strain: Isolate Thailand/TH-Sman/1958.
[3]	"Genome analysis of dengue type-1 virus isolated between 1990 and 2001 in Brazil reveals a remarkable conservation of the structural proteins but amino acid differences in the non-structural proteins." Duarte dos Santos C.N., Rocha C.F.S., Cordeiro M., Fragoso S.P., Rey F., Deubel V., Despres P. Virus Res. 90:197-205(2002) [PubMed: 12457974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00504 Genomic RNA. Translation: BAA00396.1. D10513 Genomic RNA. Translation: BAA01388.1. AF311956 Genomic RNA. Translation: AAN60368.1.
PIR	JQ1405.
3D structure databases
HSSP	HSSP built from PDB template 1L9K based on UniProtKB Q88653.
SMR	P27909. Positions 21-100, 281-674, 1652-2094, 2500-2760.
ModBase	Search...
Family and domain databases
InterPro	IPR014001. DEAD-like_N. IPR011492. DEAD_Flavivir. IPR001650. DNA/RNA_helicase_C. IPR000069. Env_glycoprot_M_flavivir. IPR013755. Flav_glyE_cen_1. IPR013756. Flav_glyE_cen_2. IPR011999. Flav_glyE_cen_dm. 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:3.30.387.10. Flav_glyE_cen_1. 1 hit. G3DSA:3.30.67.10. Flav_glyE_cen_2. 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	Search...

Entry information

Entry name

POLG_DEN1B

Accession

Primary (citable) accession number: P27909
Secondary accession number(s): P29983, Q8B648

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	December 12, 2006
Last modified:	June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)