Reviewed, UniProtKB/Swiss-Prot Q9YRV3 (POLG_YEFVT)

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
Organism	Yellow fever virus (strain Trinidad/TRINID79A/1979) (YFV) [Complete proteome]
Taxonomic identifier	407137 [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	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 heterodimers 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. The secreted form elicits protective immune response and plays an essential role in RNA replication 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 By similarity. Non-structural protein 4B plays a role in RNA replication 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
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 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
	Initiator methionine	1	1	Removed; by host Potential
	Chain	2 – 101	100	Protein C		PRO_0000261485
	Propeptide	102 – 121	20	ER anchor for the protein C, removed in mature form by serine protease NS3		PRO_0000261486
	Chain	122 – 285	164	prM		PRO_0000261487
	Chain	122 – 210	89	Peptide pr		PRO_0000261488
	Chain	211 – 285	75	Small envelope protein M		PRO_0000261489
	Chain	286 – 778	493	Envelope protein E		PRO_0000261490
	Chain	779 – 1130	352	Non-structural protein 1		PRO_0000261491
	Chain	1131 – 1354	224	Non-structural protein 2A		PRO_0000261492
	Chain	1131 – 1320	190	Non-structural protein 2A-alpha		PRO_0000261493
	Chain	1355 – 1484	130	Serine protease subunit NS2B		PRO_0000261494
	Chain	1485 – 2107	623	Serine protease/NTPase/helicase NS3		PRO_0000261495
	Chain	2108 – 2233	126	Non-structural protein 4A		PRO_0000261496
	Peptide	2234 – 2256	23	Peptide 2k		PRO_0000261497
	Chain	2257 – 2506	250	Non-structural protein 4B		PRO_0000261498
	Chain	2507 – 3411	905	Methyltransferase/RNA-directed RNA polymerase NS5		PRO_0000261499
Regions
	Topological domain	2 – 101	100	Cytoplasmic Potential
	Transmembrane	102 – 121	20	Potential
	Topological domain	122 – 244	123	Extracellular Potential
	Transmembrane	245 – 265	21	Potential
	Topological domain	266 – 269	4	Cytoplasmic Potential
	Transmembrane	270 – 287	18	Potential
	Topological domain	288 – 730	443	Extracellular Potential
	Transmembrane	731 – 751	21	Potential
	Topological domain	752 – 757	6	Cytoplasmic Potential
	Transmembrane	758 – 778	21	Potential
	Topological domain	779 – 1130	352	Extracellular Potential
	Transmembrane	1131 – 1151	21	Potential
	Topological domain	1152 – 1160	9	Cytoplasmic Potential
	Transmembrane	1161 – 1181	21	Potential
	Topological domain	1182 – 1201	20	Lumenal Potential
	Transmembrane	1202 – 1222	21	Potential
	Topological domain	1223 – 1231	9	Cytoplasmic Potential
	Transmembrane	1232 – 1252	21	Potential
	Topological domain	1253 – 1262	10	Lumenal Potential
	Transmembrane	1263 – 1285	23	Potential
	Topological domain	1286 – 1287	2	Cytoplasmic Potential
	Transmembrane	1288 – 1308	21	Potential
	Topological domain	1309 – 1321	13	Lumenal Potential
	Transmembrane	1322 – 1342	21	Potential
	Topological domain	1343 – 2186	844	Cytoplasmic Potential
	Transmembrane	2187 – 2207	21	Potential
	Topological domain	2208 – 2209	2	Lumenal Potential
	Transmembrane	2210 – 2230	21	Potential
	Topological domain	2231 – 2233	3	Cytoplasmic Potential
	Transmembrane	2234 – 2256	23	Potential
	Topological domain	2257 – 2359	103	Lumenal Potential
	Transmembrane	2360 – 2380	21	Potential
	Topological domain	2381 – 2421	41	Cytoplasmic Potential
	Transmembrane	2422 – 2442	21	Potential
	Topological domain	2443 – 2445	3	Lumenal Potential
	Transmembrane	2446 – 2466	21	Potential
	Topological domain	2467 – 3411	945	Cytoplasmic Potential
	Domain	1492 – 1666	175	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	383 – 396	14	Involved in fusion By similarity
	Motif	1773 – 1776	4	DEAH box By similarity
	Motif	2878 – 2911	34	Nuclear localization signal By similarity
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 serine protease NS3 By similarity
	Site	121 – 122	2	Cleavage; by host signal peptidase By similarity
	Site	210 – 211	2	Cleavage; by host furin By similarity
	Site	285 – 286	2	Cleavage; by host signal peptidase By similarity
	Site	778 – 779	2	Cleavage; by host signal peptidase By similarity
	Site	1130 – 1131	2	Cleavage; by host By similarity
	Site	1320 – 1321	2	Cleavage; by serine protease NS3 By similarity
	Site	1354 – 1355	2	Cleavage; by serine protease NS3 By similarity
	Site	1484 – 1485	2	Cleavage; by serine protease NS3 By similarity
	Site	2107 – 2108	2	Cleavage; by serine protease NS3 By similarity
	Site	2233 – 2234	2	Cleavage; by host signal peptidase By similarity
	Site	2256 – 2257	2	Cleavage; by serine protease NS3 By similarity
	Site	2506 – 2507	2	Cleavage; by serine protease NS3 By similarity
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)
	Q9YRV3-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 005E37E8E79AE4BD	FASTA	3,411	379,223
	10 20 30 40 50 60 MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK 70 80 90 100 110 120 ITAQLKRLWK MLDPRQGLAA LRKVKRVVAG LMRGLSSRKR RSHDVLTVQF LILGMLLMTG 130 140 150 160 170 180 GVTLMRKNRW LLLNVTSEDL GKTFSIGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD 190 200 210 220 230 240 DIDCWCYGVE NVRVTYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ 250 260 270 280 290 300 KIERWFVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG VADRDFIEGV 310 320 330 340 350 360 HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPVE ARKVCYNAVL THVKIDDKCP 370 380 390 400 410 420 STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI 430 440 450 460 470 480 QYVIKAQLHV GAKQEDWKTD IKTLKFDVLS GSQEAEFTGY GKVTLECQVQ 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 KGAPCKIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY 670 680 690 700 710 720 IIIGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSVGKGIH 730 740 750 760 770 780 TVFGSAFQGL FGGLNWITKV IMGAVLIWVG FNTRNMTMSM SMILVGVIMM FLSLGVGADQ 790 800 810 820 830 840 GCAINFGKRE 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 GRGKSTRSTT 1090 1100 1110 1120 1130 1140 DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPMKTHE SHLVRSWVTA GEIHAVPFGL 1150 1160 1170 1180 1190 1200 VSMMIAMEVV LRKRQGPKQV LVGGVVLLGA MLVGQVTLLD LLELTVAVGL HFHEMNNGGD 1210 1220 1230 1240 1250 1260 AMYMALIAAF SVRPGLLIGF GLRTLWSPRE RLVLALGAAM VEIALGGMMG GLWKYLNAVS 1270 1280 1290 1300 1310 1320 LCILTINAVA SRKASNAILP LMALLTPVTM AEVRLATMLF CTVVIIGVLH QNSKDTSMQK 1330 1340 1350 1360 1370 1380 TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAATGLVGV LAGLAFQEME 1390 1400 1410 1420 1430 1440 NFLGPIAVGG ILMMLVSVAG RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL 1450 1460 1470 1480 1490 1500 LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVR RARRSGDVLW DIPTPKIIEE 1510 1520 1530 1540 1550 1560 CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVWNGKK LIPSWASVKE 1570 1580 1590 1600 1610 1620 DLVAYGGSWK LEGRWDGEEE VQLIAAAPGK 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 SGREVIDVMC 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 GIKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK 2050 2060 2070 2080 2090 2100 AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI 2110 2120 2130 2140 2150 2160 KFAEGRRGAA DVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI 2170 2180 2190 2200 2210 2220 VMLFLLAGLL TSGMVIFFMS PKGISRMSMA KGTMAGCGYL MFLGGVEPTH ISYIMLIFFV 2230 2240 2250 2260 2270 2280 LMVVVIPEPG QQRSIQDNQV AFLIIGILTL VSVVAANELG MLEKTKEDLF GKKNLIPSGA 2290 2300 2310 2320 2330 2340 SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI 2350 2360 2370 2380 2390 2400 PFMKMNISVI MLLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA 2410 2420 2430 2440 2450 2460 KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLD EGIVLASAAL 2470 2480 2490 2500 2510 2520 GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVAYNLWK MKTARRGTAN GKTLGEVWKR 2530 2540 2550 2560 2570 2580 ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE 2590 2600 2610 2620 2630 2640 GRVIDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDVHP 2650 2660 2670 2680 2690 2700 LEPVKCDTLL CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMRDVLEK 2710 2720 2730 2740 2750 2760 LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE 2770 2780 2790 2800 2810 2820 ADVTLPIGTR SVETDKGPLD KEAIKERVER IKSEYMTSWF YDNDNPYRTW HYCGSYVTKT 2830 2840 2850 2860 2870 2880 SGSAASMVNG VIKLLTYPWD KIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI 2890 2900 2910 2920 2930 2940 MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQDQWKTAN EAVQDPKFWE 2950 2960 2970 2980 2990 3000 LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN 3010 3020 3030 3040 3050 3060 EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGLYAD DTAGWDTRIT EADLDDEQEI 3070 3080 3090 3100 3110 3120 LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI 3130 3140 3150 3160 3170 3180 TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL TRLEAWLTEH GCDRLRRMAV 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 GEWMTTEDRL EVWNRVWITN NPHMQDKTMV KEWRDVPYLT KRQDKLCGSL 3370 3380 3390 3400 3410 IGMTNRATWA SNIHLVIHRI RTLVGQEKYT DYLTVMDRYS VDADLQPGEL I

References

[1]	"Complete nucleotide sequence and phylogeny of an American strain of yellow fever virus, TRINID79A." Pisano M.R., Mercier V., Deubel V., Tolou H. Arch. Virol. 144:1837-1843(1999) [PubMed: 10542030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF094612 Genomic RNA. Translation: AAC72235.1.
3D structure databases
HSSP	HSSP built from PDB template 1YKS based on UniProtKB P19901.
ModBase	Search...
Protein family/group databases
MEROPS	S07.001.
Family and domain databases
InterPro	IPR014001. DEAD-like_N. IPR001650. DNA/RNA_helicase_C. IPR000069. Env_glycoprot_M_flavivir. IPR013755. Flav_glyE_cen_dom_subdom1. IPR013756. Flav_glyE_cen_dom_subdom2. 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: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. 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. False negative. PS50507. RDRP_SSRNA_POS. 1 hit. [Graphical view]
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Entry information

Entry name

POLG_YEFVT

Accession

Primary (citable) accession number: Q9YRV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	May 1, 1999
Last modified:	February 9, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)