Reviewed, UniProtKB/Swiss-Prot Q6YMS4 (POLG_DEN3S)

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

Gene names

Name:

pol

Organism

Dengue virus type 3 (strain Sri Lanka/1266/2000) (DENV-3) [Complete proteome]

Taxonomic identifier

408692 [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	3390 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 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. 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/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. 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. 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. 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	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 serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 100	100	Protein C		PRO_0000268088
	Propeptide	101 – 114	14	ER anchor for the protein C, removed in mature form by serine protease NS3		PRO_0000268089
	Chain	115 – 280	166	prM		PRO_0000268090
	Chain	115 – 205	91	Peptide pr		PRO_0000268091
	Chain	206 – 280	75	Small envelope protein M		PRO_0000268092
	Chain	281 – 773	493	Envelope protein E		PRO_0000268093
	Chain	774 – 1125	352	Non-structural protein 1		PRO_0000268094
	Chain	1126 – 1343	218	Non-structural protein 2A		PRO_0000268095
	Chain	1126 – 1313	188	Non-structural protein 2A-alpha		PRO_0000268096
	Chain	1344 – 1473	130	Serine protease subunit NS2B		PRO_0000268097
	Chain	1474 – 2092	619	Serine protease/NTPase/helicase NS3		PRO_0000268098
	Chain	2093 – 2219	127	Non-structural protein 4A		PRO_0000268099
	Peptide	2220 – 2242	23	Peptide 2k		PRO_0000268100
	Chain	2243 – 2490	248	Non-structural protein 4B		PRO_0000268101
	Chain	2491 – 3390	900	Methyltransferase/RNA-directed RNA polymerase NS5		PRO_0000268102
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 – 744	21	Potential
	Topological domain	745 – 750	6	Cytoplasmic Potential
	Transmembrane	751 – 771	21	Potential
	Topological domain	772 – 1154	383	Extracellular Potential
	Transmembrane	1155 – 1175	21	Potential
	Topological domain	1176 – 1445	270	Cytoplasmic Potential
	Transmembrane	1446 – 1466	21	Potential
	Topological domain	1467 – 2191	725	Lumenal Potential
	Transmembrane	2192 – 2212	21	Potential
	Topological domain	2213 – 2219	7	Cytoplasmic Potential
	Transmembrane	2220 – 2239	20	Potential
	Topological domain	2240 – 2346	107	Lumenal Potential
	Transmembrane	2347 – 2367	21	Potential
	Topological domain	2368 – 2412	45	Cytoplasmic Potential
	Transmembrane	2413 – 2433	21	Potential
	Topological domain	2434 – 2458	25	Lumenal Potential
	Transmembrane	2459 – 2479	21	Potential
	Topological domain	2480 – 3390	911	Cytoplasmic Potential
	Domain	1654 – 1810	157	Helicase ATP-binding
	Domain	1820 – 1987	168	Helicase C-terminal
	Domain	3018 – 3168	151	RdRp catalytic
	Nucleotide binding	1667 – 1674	8	ATP Potential
	Motif	1758 – 1761	4	DEAH box By similarity
Sites
	Active site	1524	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1548	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1608	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	2551	1	For 2'-O-methyltransferase activity By similarity
	Active site	2636	1	For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
	Active site	2670	1	For 2'-O-methyltransferase activity By similarity
	Active site	2706	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	773 – 774	2	Cleavage; by host signal peptidase By similarity
	Site	1125 – 1126	2	Cleavage; by host By similarity
	Site	1313 – 1314	2	Cleavage; by serine protease NS3 By similarity
	Site	1343 – 1344	2	Cleavage; by serine protease NS3 By similarity
	Site	1473 – 1474	2	Cleavage; by serine protease NS3 By similarity
	Site	2092 – 2093	2	Cleavage; by serine protease NS3 By similarity
	Site	2219 – 2220	2	Cleavage; by host signal peptidase By similarity
	Site	2242 – 2243	2	Cleavage; by serine protease NS3 By similarity
	Site	2490 – 2491	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	980	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2300	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2304	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2456	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	463 ↔ 563		By similarity
	Disulfide bond	580 ↔ 611		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6YMS4-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 14C0E2C0C9189CCB	FASTA	3,390	377,923
	10 20 30 40 50 60 MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSKGLLNG QGPMKLVMAF IAFLRFLAIP 70 80 90 100 110 120 PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINQRKK TSLCLMMILP AALAFHLTSR 130 140 150 160 170 180 DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC 190 200 210 220 230 240 WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW 250 260 270 280 290 300 ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW 310 320 330 340 350 360 VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA 370 380 390 400 410 420 VLPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLEPIEGKVV QYENLKYTVI 430 440 450 460 470 480 ITVHTGDQHQ VGNETQGVTA EITPQASTTE AILPEYGTLG LECSPRTGLD FNEMILLTMK 490 500 510 520 530 540 NKAWMVHRQW FFDLPLPWAS GATTETPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT 550 560 570 580 590 600 ALTGATEIQN SGGTSIFAGH LKCRLKMDKL ELKGMSYAMC TNTFVLKKEV SETQHGTILI 610 620 630 640 650 660 KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI 670 680 690 700 710 720 GDNALKINWY KKGSSIGKMF EATERGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS 730 740 750 760 770 780 AYTALFSGVS WVMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGAV VQADMGCVIN 790 800 810 820 830 840 WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL 850 860 870 880 890 900 WKQIANELNY ILWENNIKLT VVVGDTLGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE 910 920 930 940 950 960 TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA 970 980 990 1000 1010 1020 VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWTNGVL ESDMIIPKSL 1030 1040 1050 1060 1070 1080 AGPISQHNYR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI TESCGTRGPS LRTTTVSGKL 1090 1100 1110 1120 1130 1140 IHEWCCRSCT LPPLRYMGED GCWYGMEIRP ISEKEENMVK SLVSAGSGKV DNFTMGVLCL 1150 1160 1170 1180 1190 1200 AILFEEVLRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL 1210 1220 1230 1240 1250 1260 ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GVALGLMALK 1270 1280 1290 1300 1310 1320 LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGV SLLPVCQSSS MRKTDWLPMT 1330 1340 1350 1360 1370 1380 VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL 1390 1400 1410 1420 1430 1440 LIACYVITGT SADLTVEKAP DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV 1450 1460 1470 1480 1490 1500 LLKTALLIVS GIFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ 1510 1520 1530 1540 1550 1560 QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI SYGGGWRLSA 1570 1580 1590 1600 1610 1620 QWQKGEEVQV IAVEPGKNPK NFQTTPGTFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV 1630 1640 1650 1660 1670 1680 GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA 1690 1700 1710 1720 1730 1740 IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT 1750 1760 1770 1780 1790 1800 MRLLSPVRVP NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP 1810 1820 1830 1840 1850 1860 QSNAPIQDEE RDIPERSWNS GNEWITDFAG KTVWFVPSIK AGNDIANCLR KNGKKVIQLS 1870 1880 1890 1900 1910 1920 RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR RCLKPVILTD GPERVILAGP 1930 1940 1950 1960 1970 1980 MPVTAASAAQ RRGRVGRNPQ KENDQYIFTG QPLNNDEDHA HWTEAKMLLD NINTPEGIIP 1990 2000 2010 2020 2030 2040 ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG 2050 2060 2070 2080 2090 2100 QRNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT 2110 2120 2130 2140 2150 2160 EIGRVPSHLA HRTRNALDNL VMLHTSEDGG RAYRHAVEEL PETMETLLLL GLMILLTGGA 2170 2180 2190 2200 2210 2220 MLFLISGKGI GKTSIGLICV IASSGMLWMA EVPLQWIASA IVLEFFMMVL LIPEPEKQRT 2230 2240 2250 2260 2270 2280 PQDNQLAYVV IGILTLAATI AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW 2290 2300 2310 2320 2330 2340 TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC 2350 2360 2370 2380 2390 2400 YSQVNPLTLT AAVLLLITHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDSV 2410 2420 2430 2440 2450 2460 IFDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEALTLAT GPITTLWEGS PGKFWNTTIA 2470 2480 2490 2500 2510 2520 VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK 2530 2540 2550 2560 2570 2580 SGITEVDRTE AKEGLKRGET THHAVSRGSA KLQWFVERNM VVPEGRVIDL GCGRGGWSYY 2590 2600 2610 2620 2630 2640 CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES 2650 2660 2670 2680 2690 2700 SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS 2710 2720 2730 2740 2750 2760 RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET 2770 2780 2790 2800 2810 2820 PNMDVIGERI KRIKEEHNST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP 2830 2840 2850 2860 2870 2880 WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRPMPGTR KAMEITAEWL WRTLGRNKRP 2890 2900 2910 2920 2930 2940 RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEEF WKLVDREREL HKLGKCGSCV 2950 2960 2970 2980 2990 3000 YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG 3010 3020 3030 3040 3050 3060 LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KIIQQMDPEH RQLANAIFKL 3070 3080 3090 3100 3110 3120 TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQLGTYGLNT FTNMEAQLVR QMEGEGVLTK 3130 3140 3150 3160 3170 3180 ADLENPHLLE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD 3190 3200 3210 3220 3230 3240 IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE 3250 3260 3270 3280 3290 3300 TACLGKAYAQ MWSLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML 3310 3320 3330 3340 3350 3360 TVWNRVWIEE NPWMEDKTPV TTWENVPYLG KREDQWCGSL IGLTSRATWA QNIPTAIQQV 3370 3380 3390 RSLIGNEEFL DYMPSMKRFR KEEESEGAIW

References

[1]

"Genetic characterization of newly reintroduced dengue virus type 3 in Martinique (French West Indies)." Peyrefitte C.N., Couissinier-Paris P., Mercier-Perennec V., Bessaud M., Martial J., Kenane N., Durand J.-P.A., Tolou H.J. J. Clin. Microbiol. 41:5195-5198(2003) [PubMed: 14605161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY099336 Genomic RNA. Translation: AAM51537.1.
RefSeq	YP_001621843.1.
3D structure databases
HSSP	HSSP built from PDB template 1UZG based on UniProtKB P27915.
ModBase	Search...
Genome annotation databases
GeneID	5075727.
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_DEN3S

Accession

Primary (citable) accession number: Q6YMS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)