Q20IJ2 (Q20IJ2_9FLAV) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Polyprotein EMBL ABA61178.1
Organism	Dengue virus 2 EMBL ABA61178.1
Taxonomic identifier	11060 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group › Dengue virus

Protein attributes

Sequence length	3391 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. 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. SAAS SAAS007094 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 Nucleotide-binding
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 2P3Q
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 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 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
Sites
	Binding site	2547	1	S-adenosyl-L-homocysteine PDB 2P3Q
	Binding site	2578	1	S-adenosyl-L-homocysteine PDB 2P3Q
	Binding site	2596	1	S-adenosyl-L-homocysteine; via amide nitrogen PDB 2P3Q
	Binding site	2623	1	S-adenosyl-L-homocysteine; via amide nitrogen PDB 2P3Q

Sequences

	Sequence		Length	Mass (Da)
	Q20IJ2 [UniParc]. Last modified April 18, 2006. Version 1. Checksum: E78A50ADF58D2EA5	FASTA	3,391	379,453
	10 20 30 40 50 60 MNNQRKKAKN APFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP 70 80 90 100 110 120 PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR SAGMIIMLIP TVMAFHLTTR 130 140 150 160 170 180 NGEPHMIVSM QEKGKSLLFK TEDGVNMCTL MAMDLGELCE DTITYKCPLL RQNEPEDIDC 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 LDFELIKTEA KQPATLRKYC IEAKLTNTTT ESRCPTQGEP 370 380 390 400 410 420 SLKEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKIV QPENLEYTIV 430 440 450 460 470 480 VTPHSGEEHA VGNDTGKHGK EIKVTPQSSI 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 DLEKRYVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII 670 680 690 700 710 720 GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF 730 740 750 760 770 780 GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV LVGIVTLYLG VMVQADSGCV 790 800 810 820 830 840 VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAQEEGIC GIRSVTRLEN 850 860 870 880 890 900 LMWKQITPEL NHILAENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS 910 920 930 940 950 960 TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ DAFCDSKLMS 970 980 990 1000 1010 1020 AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW PKSHTLWSNG VLESEMIIPK 1030 1040 1050 1060 1070 1080 NLAGPVSQHN YRPGYHTQIA GPWHLGKLEM DFDFCDGTTV VVTEDCGNRG PSLRTTTASG 1090 1100 1110 1120 1130 1140 KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL 1150 1160 1170 1180 1190 1200 GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFKDL GRVVVMVGAT MTDDIGMGVT 1210 1220 1230 1240 1250 1260 YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ STIPETILEL TDALALGMMV 1270 1280 1290 1300 1310 1320 LKIVRKMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA AVSVSPLLLT SSQQKTDWIP 1330 1340 1350 1360 1370 1380 LALTIKGLNP TAIFLTTLSR TNKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG 1390 1400 1410 1420 1430 1440 GLLTVCYVLT GRSADLELER ATDVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL 1450 1460 1470 1480 1490 1500 TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI 1510 1520 1530 1540 1550 1560 KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL 1570 1580 1590 1600 1610 1620 EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNTGTIGA VSLDFSPGTS GSPIIDKKGK 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 TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF 1810 1820 1830 1840 1850 1860 PQSNAPIIDE EREIPERSWN 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 LAYKVAAEGI NYADRRWCFD 2050 2060 2070 2080 2090 2100 GIKNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLALNLI 2110 2120 2130 2140 2150 2160 TEMGRLPTFM TQKTRDALDN 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 IATHQPESNI LDIDLRPASA 2290 2300 2310 2320 2330 2340 WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG 2350 2360 2370 2380 2390 2400 CYSQVNPITL TAALLLLVAH 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 VDVFFIPPEK CDTLLCDIGE 2650 2660 2670 2680 2690 2700 SSPNPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP 2710 2720 2730 2740 2750 2760 LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRHKK ATYEPDVDLG SGTRNIGIES 2770 2780 2790 2800 2810 2820 EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MVNGVVRLLT 2830 2840 2850 2860 2870 2880 KPWDVLPTVT 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 RLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF 3130 3140 3150 3160 3170 3180 KNIQHLTVTE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRFASALT ALNDMGKIRK 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 AKNIQAAINQ 3370 3380 3390 VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W

References

[1]

"Structure and age of genetic diversity of dengue virus type 2 in Thailand." Zhang C., Mammen M.P. Jr., Chinnawirotpisan P., Klungthong C., Rodpradit P., Nisalak A., Vaughn D.W., Nimmannitya S., Kalayanarooj S., Holmes E.C. J. Gen. Virol. 87:873-883(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ThD2_0017_98 EMBL ABA61178.1.

[2]

"Structural and functional analysis of methylation and 5'-RNA sequence requirements of short capped RNAs by the methyltransferase domain of dengue virus NS5." Egloff M.P., Decroly E., Malet H., Selisko B., Benarroch D., Ferron F., Canard B. J. Mol. Biol. 372:723-736(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 2495-2787 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ181799 Genomic RNA. Translation: ABA61178.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P3Q	X-ray	2.75	A	2495-2787	[»]

ProteinModelPortal

Q20IJ2.

ModBase

Search...

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

Search...

Other

EvolutionaryTrace

Q20IJ2.

Entry information

Entry name

Q20IJ2_9FLAV

Accession

Primary (citable) accession number: Q20IJ2

Entry history

Integrated into UniProtKB/TrEMBL:	April 18, 2006
Last sequence update:	April 18, 2006
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)