Q89277 (POLG_YEFVF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 14 chains: Capsid protein C Alternative name(s): Core protein prM Peptide pr Small envelope protein M Alternative name(s): Matrix protein Envelope protein E Non-structural protein 1 Short name=NS1 Non-structural protein 2A Short name=NS2A Non-structural protein 2A-alpha Short name=NS2A-alpha Serine protease subunit NS2B Alternative name(s): Flavivirin protease NS2B regulatory subunit Non-structural protein 2B Serine protease NS3 EC=3.4.21.91 EC=3.6.1.15 EC=3.6.4.13 Alternative name(s): Flavivirin protease NS3 catalytic subunit Non-structural protein 3 Non-structural protein 4A Short name=NS4A Peptide 2k Non-structural protein 4B Short name=NS4B RNA-directed RNA polymerase NS5 EC=2.1.1.56 EC=2.1.1.57 EC=2.7.7.48 Alternative name(s): Non-structural protein 5
Organism	Yellow fever virus (strain French neurotropic vaccine FNV) (YFV) [Complete proteome]
Taxonomic identifier	407135 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Yellow fever virus group
Virus host	Aedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159] Aedes simpsoni [TaxID: 7161] Homo sapiens (Human) [TaxID: 9606] Aedes luteocephalus (Mosquito) [TaxID: 299629] Simiiformes [TaxID: 314293]

Protein attributes

Sequence length	3411 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	Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA 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 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 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 involved in virus replication and regulation of the innate immune response By similarity. Non-structural protein 2A may be involved viral RNA replication and capsid assembly Potential. 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, performs its autocleavage and 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 induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functionning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase By similarity. Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter By similarity. Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway 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. Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway 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. ATP + H2O = ADP + 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	Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity By similarity.
Subcellular location	Capsid protein C: Virion Potential. Peptide pr: Secreted By similarity. Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass 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; Multi-pass membrane protein Potential. Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential. Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity. Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Located in RE-associated vesicles hosting the replication complex. Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus By similarity. Note: Located in RE-associated vesicles hosting the replication complex.
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. Specific enzymatic cleavages in vivo yield mature proteins Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site By similarity. RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. Envelope protein E and non-structural protein 1 are N-glycosylated By similarity.
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	Clathrin-mediated endocytosis of virus by host Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Initiation of viral infection RNA replication Transcription Transcription regulation Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Virus endocytosis by host
Cellular component	Host endoplasmic reticulum Host membrane Host nucleus Membrane Secreted Viral envelope protein Virion
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding
Molecular function	Capsid protein Helicase Hydrolase Methyltransferase Nucleotidyltransferase Protease RNA-directed RNA polymerase 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	evasion by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent 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 host cell nucleus 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: InterPro 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: EC mRNA (nucleoside-2'-O-)-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 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
Molecule processing
	Chain	1 – 3411	3411	Genome polyprotein		PRO_0000405159
	Chain	1 – 101	101	Capsid protein C By similarity		PRO_0000261515
	Propeptide	102 – 121	20	ER anchor for the protein C, removed in mature form by serine protease NS3		PRO_0000261516
	Chain	122 – 285	164	prM By similarity		PRO_0000261517
	Chain	122 – 210	89	Peptide pr By similarity		PRO_0000261518
	Chain	211 – 285	75	Small envelope protein M By similarity		PRO_0000261519
	Chain	286 – 778	493	Envelope protein E By similarity		PRO_0000261520
	Chain	779 – 1130	352	Non-structural protein 1 By similarity		PRO_0000261521
	Chain	1131 – 1354	224	Non-structural protein 2A By similarity		PRO_0000261522
	Chain	1131 – 1320	190	Non-structural protein 2A-alpha By similarity		PRO_0000261523
	Chain	1355 – 1484	130	Serine protease subunit NS2B By similarity		PRO_0000261524
	Chain	1485 – 2107	623	Serine protease NS3 By similarity		PRO_0000261525
	Chain	2108 – 2233	126	Non-structural protein 4A By similarity		PRO_0000261526
	Peptide	2234 – 2256	23	Peptide 2k		PRO_0000261527
	Chain	2257 – 2506	250	Non-structural protein 4B By similarity		PRO_0000261528
	Chain	2507 – 3411	905	RNA-directed RNA polymerase NS5 By similarity		PRO_0000261529
Regions
	Topological domain	1 – 104	104	Cytoplasmic Potential
	Transmembrane	105 – 125	21	Helical; Potential
	Topological domain	126 – 244	119	Extracellular Potential
	Transmembrane	245 – 265	21	Helical; Potential
	Topological domain	266 – 270	5	Cytoplasmic Potential
	Transmembrane	271 – 285	15	Helical; Potential
	Topological domain	286 – 730	445	Extracellular Potential
	Intramembrane	731 – 751	21	Helical; Potential
	Topological domain	752 – 757	6	Extracellular Potential
	Intramembrane	758 – 778	21	Helical; Potential
	Topological domain	779 – 1130	352	Extracellular Potential
	Transmembrane	1131 – 1151	21	Helical; Potential
	Topological domain	1152 – 1160	9	Cytoplasmic Potential
	Transmembrane	1161 – 1181	21	Helical; Potential
	Topological domain	1182 – 1201	20	Lumenal Potential
	Transmembrane	1202 – 1222	21	Helical; Potential
	Topological domain	1223 – 1231	9	Cytoplasmic Potential
	Transmembrane	1232 – 1252	21	Helical; Potential
	Topological domain	1253 – 1262	10	Lumenal Potential
	Transmembrane	1263 – 1285	23	Helical; Potential
	Topological domain	1286 – 1355	70	Cytoplasmic Potential
	Transmembrane	1356 – 1376	21	Helical; Potential
	Topological domain	1377 – 1378	2	Lumenal Potential
	Transmembrane	1379 – 1399	21	Helical; Potential
	Topological domain	1400 – 1456	57	Cytoplasmic Potential
	Intramembrane	1457 – 1477	21	Helical; Potential
	Topological domain	1478 – 2157	680	Cytoplasmic Potential
	Transmembrane	2158 – 2178	21	Helical; Potential
	Topological domain	2179 – 2186	8	Lumenal Potential
	Intramembrane	2187 – 2207	21	Helical; Potential
	Topological domain	2208 – 2209	2	Lumenal Potential
	Transmembrane	2210 – 2230	21	Helical; Potential
	Topological domain	2231 – 2241	11	Cytoplasmic Potential
	Transmembrane	2242 – 2262	21	Helical; Note=Signal for NS4B; Potential
	Topological domain	2263 – 2293	31	Lumenal Potential
	Intramembrane	2294 – 2314	21	Helical; Potential
	Topological domain	2315 – 2338	24	Lumenal Potential
	Intramembrane	2339 – 2359	21	Helical; Potential
	Topological domain	2360	1	Lumenal Potential
	Transmembrane	2361 – 2380	20	Helical; Potential
	Topological domain	2381 – 2421	41	Cytoplasmic Potential
	Transmembrane	2422 – 2442	21	Helical; Potential
	Topological domain	2443 – 2445	3	Lumenal Potential
	Transmembrane	2446 – 2466	21	Helical; Potential
	Topological domain	2467 – 3411	945	Cytoplasmic Potential
	Domain	1485 – 1665	181	Peptidase S7
	Domain	1669 – 1825	157	Helicase ATP-binding
	Domain	1820 – 1997	178	Helicase C-terminal
	Domain	3035 – 3187	153	RdRp catalytic
	Nucleotide binding	1682 – 1689	8	ATP Potential
	Region	30 – 74	45	Hydrophobic; homodimerization of capsid protein C By similarity
	Region	383 – 396	14	Involved in fusion By similarity
	Region	1407 – 1446	40	Interacts with and activates NS3 protease By similarity
	Motif	1773 – 1776	4	DEAH box
	Motif	2878 – 2911	34	Nuclear localization signal By similarity
	Compositional bias	2656 – 2660	5	Poly-Ser
Sites
	Active site	1537	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1561	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1622	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	2567	1	For 2'-O-methyltransferase activity By similarity
	Active site	2652	1	For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
	Active site	2688	1	For 2'-O-methyltransferase activity By similarity
	Active site	2724	1	For 2'-O-methyltransferase activity By similarity
	Site	101 – 102	2	Cleavage; by viral protease NS3 Potential
	Site	121 – 122	2	Cleavage; by host signal peptidase By similarity
	Site	210 – 211	2	Cleavage; by host furin Potential
	Site	285 – 286	2	Cleavage; by host signal peptidase Potential
	Site	778 – 779	2	Cleavage; by host signal peptidase Potential
	Site	1130 – 1131	2	Cleavage; by host Potential
	Site	1354 – 1355	2	Cleavage; by viral protease NS3 Potential
	Site	1484 – 1485	2	Cleavage; by autolysis Potential
	Site	2107 – 2108	2	Cleavage; by autolysis Potential
	Site	2233 – 2234	2	Cleavage; by viral protease NS3 Potential
	Site	2256 – 2257	2	Cleavage; by host signal peptidase Potential
	Site	2506 – 2507	2	Cleavage; by viral protease NS3 Potential
Amino acid modifications
	Glycosylation	134	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	150	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	908	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	986	1	N-linked (GlcNAc...); by host Potential
	Disulfide bond	288 ↔ 315		By similarity
	Disulfide bond	345 ↔ 401		By similarity
	Disulfide bond	359 ↔ 390		By similarity
	Disulfide bond	377 ↔ 406		By similarity
	Disulfide bond	467 ↔ 568		By similarity
	Disulfide bond	585 ↔ 615		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89277 [UniParc]. Last modified December 1, 2001. Version 2. Checksum: E7A5E79C999C9D8D	FASTA	3,411	379,189
	10 20 30 40 50 60 MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK 70 80 90 100 110 120 ITAHLKRLWK MLDPRQGLAA LRKVKRVVAG LMRGLSSRKR RSHDVLTVQF LILGMLLMTG 130 140 150 160 170 180 GVTLVRKNRW LLLNVTSEDL GKTFSMGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD 190 200 210 220 230 240 DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ 250 260 270 280 290 300 KIERWFVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV 310 320 330 340 350 360 HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPVE ARKVCYNAVL THVKINDKCP 370 380 390 400 410 420 STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI 430 440 450 460 470 480 QYVIRARLHV GAKQENWKTD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFGNSYI 490 500 510 520 530 540 AEMEKESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGDQEGSLK 550 560 570 580 590 600 TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH 610 620 630 640 650 660 GTVVMQVKVP KGAPCRIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY 670 680 690 700 710 720 IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSVGKGIH 730 740 750 760 770 780 TVFGSAFQGL FGGLNWITKV IIGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ 790 800 810 820 830 840 GCAINFAKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS 850 860 870 880 890 900 LEHEMWRSRA DEINAILEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL 910 920 930 940 950 960 VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS 970 980 990 1000 1010 1020 ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK ECEWPLTHTI GTSVEESEMF 1030 1040 1050 1060 1070 1080 MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVIIDGNCD GRGKSARSTT 1090 1100 1110 1120 1130 1140 DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL 1150 1160 1170 1180 1190 1200 VSMMIALEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD 1210 1220 1230 1240 1250 1260 AMYMALIAAF SVRPGLLIGF GLRTLWSPRE RLVLALGAAM VEIALGGMMG GLWKYLNAVS 1270 1280 1290 1300 1310 1320 LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLATMLF CTVVIIGVLY QNSKDTSMQK 1330 1340 1350 1360 1370 1380 TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME 1390 1400 1410 1420 1430 1440 NFLGPIAVGG ILMMLVSVAG RVDGLELKKL GEVAWEEEAE ISGSSARYDV ALSEQGEFKL 1450 1460 1470 1480 1490 1500 LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKVIEE 1510 1520 1530 1540 1550 1560 CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE 1570 1580 1590 1600 1610 1620 DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG 1630 1640 1650 1660 1670 1680 TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGKTTIL 1690 1700 1710 1720 1730 1740 DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG 1750 1760 1770 1780 1790 1800 SGREVIDAMC HATLTYRMLE PTRIVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT 1810 1820 1830 1840 1850 1860 ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM 1870 1880 1890 1900 1910 1920 AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP 1930 1940 1950 1960 1970 1980 VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS 1990 2000 2010 2020 2030 2040 MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK 2050 2060 2070 2080 2090 2100 AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RTPGGAKKPL RPRWCDERVS SDQSALSEFI 2110 2120 2130 2140 2150 2160 KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVLLHS EEGSRAYRNA LSMMPEAMTI 2170 2180 2190 2200 2210 2220 VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV 2230 2240 2250 2260 2270 2280 LMVVVIPEPG QQRSIQDNQV AFLIIGILTL VSVVAANELG MLEKTKEDLF GKKNSIPSSA 2290 2300 2310 2320 2330 2340 SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI 2350 2360 2370 2380 2390 2400 PFMKMNISVI MLLISGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA 2410 2420 2430 2440 2450 2460 KNPVVDGNPT VDIEEAPEMP VLYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL 2470 2480 2490 2500 2510 2520 GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGTAN GKTLGEVWKR 2530 2540 2550 2560 2570 2580 ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE 2590 2600 2610 2620 2630 2640 GRVIDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR 2650 2660 2670 2680 2690 2700 LEPVKCDTLL CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK 2710 2720 2730 2740 2750 2760 LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE 2770 2780 2790 2800 2810 2820 ADVTLPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF YDNDNPYRTW HYCGSYVTKT 2830 2840 2850 2860 2870 2880 SGSAASMVNG VIKILTYPWD KIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI 2890 2900 2910 2920 2930 2940 MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE 2950 2960 2970 2980 2990 3000 LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN 3010 3020 3030 3040 3050 3060 EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI 3070 3080 3090 3100 3110 3120 LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI 3130 3140 3150 3160 3170 3180 TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL TRLEAWLTEH GCNRLRRMAV SGDDCVVRPI 3190 3200 3210 3220 3230 3240 DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE 3250 3260 3270 3280 3290 3300 QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ 3310 3320 3330 3340 3350 3360 GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTMV KEWRDVPYLT KRQDKLCGSL 3370 3380 3390 3400 3410 IGMTNRATWA SHIHLVIHRI RTLVGQEKYT DYLTVMDRYS VDADLQPGEL I

References

[1]	"Comparison of the genomes of the wild-type French viscerotropic strain of yellow fever virus with its vaccine derivative French neurotropic vaccine." Wang E., Ryman K.D., Jennings A.D., Wood D.J., Taffs F., Minor P.D., Sanders P.G., Barrett A.D. J. Gen. Virol. 76:2749-2755(1995) [PubMed: 7595382] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U21055 Genomic RNA. Translation: AAA99712.1.
3D structure databases
HSSP	HSSP built from PDB template 1YKS based on UniProtKB P19901.
ProteinModelPortal	Q89277.
SMR	Q89277. Positions 572-683, 1490-1667, 1671-2107, 2512-2772, 2780-3399.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR014001. DEAD-like_helicase. IPR011492. DEAD_Flavivir. IPR000069. Env_glycoprot_M_flavivir. IPR013756. Flav_glyE_cen_dom_subdom2. 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. IPR001650. Helicase_C. IPR014756. Ig_E-set. IPR009003. Pept_cys/ser_Trypsin-like. IPR001850. Peptidase_S7. IPR000208. RNA-dir_pol_flavivirus. IPR007094. RNA-dir_pol_PSvirus. IPR002877. rRNA_MeTrfase_RrmJ/FtsJ. [Graphical view]
Gene3D	G3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit. G3DSA:2.60.98.10. Flav_glyE_dim. 3 hits. 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. 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.
PROSITE	PS51527. FLAVIVIRUS_NS2B. 1 hit. PS51528. FLAVIVIRUS_NS3PRO. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. False negative. PS50507. RDRP_SSRNA_POS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLG_YEFVF

Accession

Primary (citable) accession number: Q89277

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	December 1, 2001
Last modified:	November 16, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program