Q6DLV0 (Q6DLV0_9FLAV) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Polyprotein EMBL AAT75224.1
Organism	Dengue virus 3 EMBL AAT75224.1
Taxonomic identifier	11069 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group › Dengue virus

Protein attributes

Sequence length	3390 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a 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. SAAS SAAS011998
Catalytic activity	ATP + H2O = ADP + phosphate. SAAS SAAS007094 NTP + H2O = NDP + phosphate. SAAS SAAS007094 Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). SAAS SAAS007094
Subcellular location	Virion membrane; Multi-pass membrane protein. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity SAAS SAAS011998.
Sequence similarities	Contains 1 RdRp catalytic domain. Contains 1 helicase ATP-binding domain. SAAS SAAS007094 Contains 1 helicase C-terminal domain. SAAS SAAS007094

Ontologies

Keywords
Biological process	Clathrin-mediated endocytosis of virus by host SAAS SAAS011998 Fusion of virus membrane with host endosomal membrane SAAS SAAS011998 Fusion of virus membrane with host membrane Host-virus interaction Viral RNA replication SAAS SAAS007094 Viral attachment to host cell SAAS SAAS011998 Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell
Cellular component	Host endoplasmic reticulum SAAS SAAS011998 Host membrane SAAS SAAS011998 Membrane Viral envelope protein SAAS SAAS011998 Virion
Domain	Transmembrane Transmembrane helix SAAS SAAS011998
Ligand	ATP-binding GTP-binding PDB 2J7W Metal-binding PDB 2J7U PDB 2J7W Nucleotide-binding Zinc PDB 2J7U PDB 2J7W
Molecular function	Capsid protein SAAS SAAS011998 Helicase SAAS SAAS007094 Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase SAAS SAAS007094 Serine protease SAAS SAAS013754 Transferase
PTM	Disulfide bond SAAS SAAS011998
Technical term	3D-structure PDB 3VWS PDB 4HHJ PDB 2J7U PDB 2J7W
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Inferred from electronic annotation. Source: GOC RNA (guanine-N7)-methylation Inferred from electronic annotation. Source: GOC proteolysis Inferred from electronic annotation. Source: UniProtKB-KW viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane 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 virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW 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: InterPro mRNA (nucleoside-2'-O-)-methyltransferase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type exopeptidase 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
Regions
	Nucleotide binding	3284 – 3285	2	GTP PDB 2J7W
Sites
	Metal binding	2927	1	Zinc 1 PDB 2J7U PDB 2J7W
	Metal binding	2931	1	Zinc 1; via tele nitrogen PDB 2J7U PDB 2J7W
	Metal binding	2936	1	Zinc 1 PDB 2J7U PDB 2J7W
	Metal binding	2939	1	Zinc 1 PDB 2J7U PDB 2J7W
	Metal binding	3202	1	Zinc 2; via tele nitrogen PDB 2J7U PDB 2J7W
	Metal binding	3204	1	Zinc 2; via tele nitrogen PDB 2J7U PDB 2J7W
	Metal binding	3218	1	Zinc 2 PDB 2J7U PDB 2J7W
	Metal binding	3337	1	Zinc 2 PDB 2J7U PDB 2J7W
	Binding site	3200	1	GTP PDB 2J7W
	Binding site	3219	1	GTP PDB 2J7W
	Binding site	3227	1	GTP PDB 2J7W

Sequences

	Sequence		Length	Mass (Da)
	Q6DLV0 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 11781239F669266E	FASTA	3,390	377,913
	10 20 30 40 50 60 MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSKGLLNG QGPMKLVMAF IAFLRFLAIP 70 80 90 100 110 120 PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK 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 EATARGARRM 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 VVVGDTIGVL 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 SHTLWSNGVL 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 AILFEEVMRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL 1210 1220 1230 1240 1250 1260 ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GIALGLMALK 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 SADLTVEKAA 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 NFQTMPGTFQ 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 SKLNDWDFVV 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 EKRKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT 2110 2120 2130 2140 2150 2160 EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL GLMILLTGGA 2170 2180 2190 2200 2210 2220 MLFLISGKGI GKTSIGLICV IASSGMLWMA EVPLQWIASA IVLEFFMMVL LIPEPEKQRT 2230 2240 2250 2260 2270 2280 PQDNQLAYVV IGILTLAAII 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 GIMTIDLDPV 2410 2420 2430 2440 2450 2460 IYDSKFEKQL 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 RTPRPLPGTR KVMGITAEWL WRTLGRNKRP 2890 2900 2910 2920 2930 2940 RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEEF WKLVDREREL HKLGKCGSCV 2950 2960 2970 2980 2990 3000 YNMMGKREKK LGEFGKAKGS RAIWYMWLGV RYLEFEALGF LNEDHWFSRE NSYSGVEGEG 3010 3020 3030 3040 3050 3060 LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KIIQQMDPEH RQLANAIFKL 3070 3080 3090 3100 3110 3120 TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQVGTYGLNT 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]	"Full length genomic sequence of a Dengue virus of serotype 3 from Singapore." Lim S.P., Ooi E.E., Vasudevan S.G. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution." Yap T.L., Xu T., Chen Y.L., Malet H., Egloff M.P., Canard B., Vasudevan S.G., Lescar J. J. Virol. 81:4753-4765(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2763-3390 IN COMPLEX WITH GTP AND ZINC.
[3]	"Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor." Noble C.G., Lim S.P., Chen Y.L., Liew C.W., Yap L., Lescar J., Shi P.Y. J. Virol. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 2762-3390.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY662691 Genomic RNA. Translation: AAT75224.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J7U	X-ray	1.85	A	2763-3390	[»]
2J7W	X-ray	2.60	A	2763-3390	[»]
3VWS	X-ray	2.10	A	2762-3390	[»]
4HHJ	X-ray	1.79	A	2762-3390	[»]

ProteinModelPortal

Q6DLV0.

SMR

Q6DLV0. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.

ModBase

Search...

Protein family/group databases

MEROPS

S07.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.

InterPro

IPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR027287. Flavovir_Ig-like.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR026490. mRNA_cap_0/1_MeTrfase.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

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.
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]

SUPFAM

SSF56983. Flavi_glycoprotE. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.

TIGRFAMs

TIGR04240. flavi_E_stem. 1 hit.

PROSITE

PS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q6DLV0.

Entry information

Entry name

Q6DLV0_9FLAV

Accession

Primary (citable) accession number: Q6DLV0

Entry history

Integrated into UniProtKB/TrEMBL:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)