P05769 (POLG_MVEV5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 13 chains: Peptide 2k 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 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 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	Murray valley encephalitis virus (strain MVE-1-51) (MVEV) [Complete proteome]
Taxonomic identifier	301478 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Japanese encephalitis virus group › Murray Valley encephalitis virus
Virus host	Homo sapiens (Human) [TaxID: 9606] Culex annulirostris (Common banded mosquito) [TaxID: 162997]

Protein attributes

Sequence length	3434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. Ref.8
Subcellular location	Capsid protein C: Virion Potential Ref.8. Peptide pr: Secreted By similarity Ref.8. Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.8. Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.8. Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity Ref.8. Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.8. Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.8. Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity. Ref.8 Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Located in RE-associated vesicles hosting the replication complex. Ref.8 Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.8. 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. Ref.8
Post-translational modification	Specific enzymatic cleavages in vivo by the viral protease NS3 and host cell enzymes 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 soluble protein C is released after cleavage by NS3 protease at a site upstream of this hydrophobic domain. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. 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. Ref.5 RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization 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	3D-structure Complete proteome Direct protein sequencing 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

Initiator methionine

1

1

Removed; by host Potential

Chain

2 – 3434

3433

Genome polyprotein

PRO_0000405163

Chain

2 – 105

104

Capsid protein C By similarity

PRO_0000037782

Propeptide

106 – 125

20

ER anchor for the protein C, removed in mature form by serine protease NS3

PRO_0000405164

Chain

126 – 292

167

prM By similarity

PRO_0000405165

Chain

126 – 217

92

Peptide pr By similarity

PRO_0000037783

Chain

218 – 292

75

Small envelope protein M By similarity

PRO_0000037784

Chain

293 – 793

501

Envelope protein E By similarity

PRO_0000037785

Chain

794 – 1145

352

Non-structural protein 1 By similarity

PRO_0000037786

Chain

1146 – 1372

227

Non-structural protein 2A By similarity

PRO_0000037787

Chain

1373 – 1503

131

Serine protease subunit NS2B By similarity

PRO_0000037788

Chain

1504 – 2122

619

Serine protease NS3 By similarity

PRO_0000037789

Chain

2123 – 2248

126

Non-structural protein 4A By similarity

PRO_0000037790

Peptide

2249 – 2271

23

Peptide 2k By similarity

PRO_0000405166

Chain

2272 – 2529

258

Non-structural protein 4B By similarity

PRO_0000037791

Chain

2530 – 3434

905

RNA-directed RNA polymerase NS5 By similarity

PRO_0000037792

Regions

Topological domain

2 – 110

109

Cytoplasmic Potential

Transmembrane

111 – 131

21

Helical; Potential

Topological domain

132 – 251

120

Extracellular Potential

Transmembrane

252 – 272

21

Helical; Potential

Topological domain

273 – 277

5

Cytoplasmic Potential

Transmembrane

278 – 292

15

Helical; Potential

Topological domain

293 – 745

453

Extracellular Potential

Intramembrane

746 – 766

21

Helical; Potential

Topological domain

767 – 772

6

Extracellular Potential

Intramembrane

773 – 793

21

Helical; Potential

Topological domain

794 – 1144

351

Extracellular Potential

Transmembrane

1145 – 1165

21

Helical; Potential

Topological domain

1166 – 1176

11

Cytoplasmic Potential

Transmembrane

1177 – 1197

21

Helical; Potential

Topological domain

1198 – 1218

21

Lumenal Potential

Transmembrane

1219 – 1239

21

Helical; Potential

Topological domain

1240 – 1249

10

Cytoplasmic Potential

Transmembrane

1250 – 1270

21

Helical; Potential

Topological domain

1271 – 1286

16

Lumenal Potential

Transmembrane

1287 – 1307

21

Helical; Potential

Topological domain

1308 – 1373

66

Cytoplasmic Potential

Transmembrane

1374 – 1394

21

Helical; Potential

Topological domain

1395 – 1397

3

Lumenal Potential

Transmembrane

1398 – 1418

21

Helical; Potential

Topological domain

1419 – 1475

57

Cytoplasmic Potential

Intramembrane

1476 – 1496

21

Helical; Potential

Topological domain

1497 – 2172

676

Cytoplasmic Potential

Transmembrane

2173 – 2193

21

Helical; Potential

Topological domain

2194 – 2197

4

Lumenal Potential

Intramembrane

2198 – 2218

21

Helical; Potential

Topological domain

2219 – 2220

2

Lumenal Potential

Transmembrane

2221 – 2241

21

Helical; Potential

Topological domain

2242 – 2256

15

Cytoplasmic Potential

Transmembrane

2257 – 2277

21

Helical; Note=Signal for NS4B; Potential

Topological domain

2278 – 2309

32

Lumenal Potential

Intramembrane

2310 – 2330

21

Helical; Potential

Topological domain

2331 – 2366

36

Lumenal Potential

Transmembrane

2367 – 2394

28

Helical; Potential

Topological domain

2395 – 2446

52

Cytoplasmic Potential

Transmembrane

2447 – 2467

21

Helical; Potential

Topological domain

2468 – 2498

31

Lumenal Potential

Transmembrane

2499 – 2519

21

Helical; Potential

Topological domain

2520 – 3434

915

Cytoplasmic Potential

Domain

1504 – 1681

178

Peptidase S7

Domain

1684 – 1840

157

Helicase ATP-binding

Domain

1851 – 2016

166

Helicase C-terminal

Domain

3059 – 3211

153

RdRp catalytic

Nucleotide binding

1697 – 1704

8

ATP Potential

Region

33 – 74

42

Hydrophobic; homodimerization of capsid protein C By similarity

Region

1426 – 1465

40

Interacts with and activates NS3 protease By similarity

Motif

1788 – 1791

4

DEAH box

Sites

Active site

1554

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1578

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1638

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

2590

1

For 2'-O-methyltransferase activity By similarity

Active site

2675

1

For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity

Active site

2711

1

For 2'-O-methyltransferase activity By similarity

Active site

2747

1

For 2'-O-methyltransferase activity By similarity

Site

105 – 106

2

Cleavage; by viral protease NS3 Potential

Site

125 – 126

2

Cleavage; by host signal peptidase By similarity

Site

217 – 218

2

Cleavage; by host furin By similarity

Site

292 – 293

2

Cleavage; by host signal peptidase Potential

Site

793 – 794

2

Cleavage; by host signal peptidase Potential

Site

1145 – 1146

2

Cleavage; by host By similarity

Site

1372 – 1373

2

Cleavage; by viral protease NS3 Potential

Site

1503 – 1504

2

Cleavage; by autolysis Potential

Site

2122 – 2123

2

Cleavage; by autolysis Potential

Site

2248 – 2249

2

Cleavage; by viral protease NS3 Potential

Site

2271 – 2272

2

Cleavage; by host signal peptidase Potential

Site

2529 – 2530

2

Cleavage; by viral protease NS3 Potential

Amino acid modifications

Glycosylation

140

1

N-linked (GlcNAc...); by host Potential

Glycosylation

446

1

N-linked (GlcNAc...); by host Potential

Glycosylation

923

1

N-linked (GlcNAc...); by host

Glycosylation

968

1

N-linked (GlcNAc...); by host

Glycosylation

1000

1

N-linked (GlcNAc...) (high mannose); by host

Glycosylation

2487

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2493

1

N-linked (GlcNAc...); by host Potential

Disulfide bond

295 ↔ 322

By similarity

Disulfide bond

352 ↔ 408

By similarity

Disulfide bond

366 ↔ 397

By similarity

Disulfide bond

384 ↔ 413

By similarity

Disulfide bond

482 ↔ 580

By similarity

Disulfide bond

597 ↔ 628

By similarity

Disulfide bond

797 ↔ 808

Ref.4

Disulfide bond

848 ↔ 936

Ref.4

Disulfide bond

972 ↔ 1016

Ref.4

Experimental info

Sequence conflict

115

1

L → V in CAA27184. Ref.2

Sequence conflict

754

1

P → Q in CAA27184. Ref.2

Sequence conflict

960

1

G → V in CAA27184. Ref.2

Sequence conflict

1485

1

R → W in CAA27184. Ref.2

Sequence conflict

1779

1

V → G in CAA27184. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

3434

Helix Strand Turn

Details...

Helix

1684 – 1687

4

Beta strand

1692 – 1695

4

Beta strand

1699 – 1701

3

Turn

1703 – 1706

4

Helix

1707 – 1717

11

Beta strand

1722 – 1728

7

Helix

1729 – 1738

10

Turn

1739 – 1741

3

Beta strand

1744 – 1746

3

Beta strand

1761 – 1765

5

Helix

1766 – 1773

8

Beta strand

1775 – 1777

3

Beta strand

1783 – 1789

7

Helix

1795 – 1809

15

Beta strand

1814 – 1818

5

Beta strand

1836 – 1840

5

Beta strand

1849 – 1851

3

Helix

1853 – 1857

5

Beta strand

1862 – 1865

4

Helix

1869 – 1881

13

Beta strand

1886 – 1889

4

Turn

1891 – 1893

3

Helix

1894 – 1901

8

Beta strand

1907 – 1911

5

Helix

1913 – 1916

4

Beta strand

1924 – 1928

5

Beta strand

1935 – 1938

4

Beta strand

1944 – 1947

4

Helix

1955 – 1962

8

Beta strand

1974 – 1978

5

Helix

1990 – 1999

10

Helix

2014 – 2016

3

Turn

2024 – 2027

4

Helix

2031 – 2042

12

Helix

2048 – 2055

8

Turn

2056 – 2058

3

Helix

2064 – 2067

4

Helix

2072 – 2074

3

Beta strand

2078 – 2081

4

Beta strand

2098 – 2101

4

Helix

2102 – 2104

3

Helix

2108 – 2118

11

Helix

2537 – 2546

10

Helix

2550 – 2557

8

Turn

2558 – 2560

3

Beta strand

2562 – 2564

3

Helix

2566 – 2568

3

Helix

2587 – 2596

10

Beta strand

2604 – 2609

6

Helix

2615 – 2620

6

Beta strand

2626 – 2632

7

Helix

2650 – 2652

3

Beta strand

2653 – 2656

4

Helix

2661 – 2663

3

Beta strand

2670 – 2674

5

Helix

2683 – 2701

19

Beta strand

2706 – 2713

8

Helix

2718 – 2731

14

Beta strand

2734 – 2736

3

Beta strand

2748 – 2751

4

Helix

2758 – 2771

14

Beta strand

2782 – 2784

3

Sequences

	Sequence		Length	Mass (Da)
	P05769 [UniParc]. Last modified December 21, 2004. Version 2. Checksum: 20D7110791C567A9	FASTA	3,434	380,577
	10 20 30 40 50 60 MSKKPGGPGK PRVVNMLKRG IPRVFPLVGV KRVVMNLLDG RGPIRFVLAL LAFFRFTALA 70 80 90 100 110 120 PTKALMRRWK SVNKTTAMKH LTSFKKELGT LIDVVNKRGK KQKKRGGSET SVLMLIFMLI 130 140 150 160 170 180 GFAAALKLST FQGKIMMTVN ATDIADVIAI PTPKGPNQCW IRAIDIGFMC DDTITYECPK 190 200 210 220 230 240 LESGNDPEDI DCWCDKQAVY VNYGRCTRAR HSKRSRRSIT VQTHGESTLV NKKDAWLDST 250 260 270 280 290 300 KATRYLTKTE NWIIRNPGYA LVAVVLGWML GSNTGQKVIF TVLLLLVAPA YSFNCLGMSS 310 320 330 340 350 360 RDFIEGASGA TWVDLVLEGD SCITIMAADK PTLDIRMMNI EATNLALVRN YCYAATVSDV 370 380 390 400 410 420 STVSNCPTTG ESHNTKRADH NYLCKRGVTD RGWGNGCGLF GKGSIDTCAK FTCSNSAAGR 430 440 450 460 470 480 LILPEDIKYE VGVFVHGSTD STSHGNYSTQ IGANQAVRFT ISPNAPAITA KMGDYGEVTV 490 500 510 520 530 540 ECEPRSGLNT EAYYVMTIGT KHFLVHREWF NDLLLPWTSP ASTEWRNREI LVEFEEPHAT 550 560 570 580 590 600 KQSVVALGSQ EGALHQALAG AIPVEFSSST LKLTSGHLKC RVKMEKLKLK GTTYGMCTEK 610 620 630 640 650 660 FTFSKNPADT GHGTVVLELQ YTGSDGPCKI PISSVASLND MTPVGRMVTA NPYVASSTAN 670 680 690 700 710 720 AKVLVEIEPP FGDSYIVVGR GDKQINHHWH KEGSSIGKAF STTLKGAQRL AALGDTAWDF 730 740 750 760 770 780 GSVGGVFNSI GKAVHQVFGG AFRTLFGGMS WISPGLLGAL LLWMGVNARD KSIALAFLAT 790 800 810 820 830 840 GGVLLFLATN VHADTGCAID ITRRELKCGS GIFIHNDVEA WIDRYKYLPE TPKQLAKVVE 850 860 870 880 890 900 NAHKSGICGI RSVNRFEHQM WESVRDELNA LLKENAIDLS VVVEKQKGMY RAAPNRLRLT 910 920 930 940 950 960 VEELDIGWKA WGKSLLFAAE LANSTFVVDG PETAECPNSK RAWNSFEIED FGFGITSTRG 970 980 990 1000 1010 1020 WLKLREENTS ECDSTIIGTA VKGNHAVHSD LSYWIESGLN GTWKLERAIF GEVKSCTWPE 1030 1040 1050 1060 1070 1080 THTLWGDAVE ETELIIPVTL AGPRSKHNRR EGYKVQVQGP WDEEDIKLDF DYCPGTTVTV 1090 1100 1110 1120 1130 1140 SEHCGKRGPS VRTTTDSGKL VTDWCCRSCT LPPLRFTTAS GCWYGMEIRP MKHDESTLVK 1150 1160 1170 1180 1190 1200 SRVQAFNGDM IDPFQLGLLV MFLATQEVLR KRWTARLTLP AAVGALLVLL LGGITYTDLV 1210 1220 1230 1240 1250 1260 RYLILVGSAF AESNNGGDVI HLALIAVFKV QPAFLVASLT RSRWTNQENL VLVLGAAFFQ 1270 1280 1290 1300 1310 1320 MAASDLELTI PGLLNSAATA WMVLRAMAFP STSAIAMPML AMLAPGMRML HLDTYRIVLL 1330 1340 1350 1360 1370 1380 LIGICSLLNE RRRSVEKKKG AVLIGLALTS TGYFSPTIMA AGLMICNPNK KRGWPATEVL 1390 1400 1410 1420 1430 1440 TAVGLMFAIV GGLAELDIDS MSVPFTIAGL MLVSYVISGK ATDMWLERAA DVSWEAGAAI 1450 1460 1470 1480 1490 1500 TGTSERLDVQ LDDDGDFHLL NDPGVPWKIW VLRMTCLSVA AITPRAILPS AFGYWLTLKY 1510 1520 1530 1540 1550 1560 TKRGGVFWDT PSPKVYPKGD TTPGVYRIMA RGILGRYQAG VGVMHEGVFH TLWHTTRGAA 1570 1580 1590 1600 1610 1620 IMSGEGRLTP YWGNVKEDRV TYGGPWKLDQ KWNGVDDVQM IVVEPGKPAI NVQTKPGIFK 1630 1640 1650 1660 1670 1680 TAHGEIGAVS LDYPIGTSGS PIVNSNGEII GLYGNGVILG NGAYVSAIVQ GERVEEPVPE 1690 1700 1710 1720 1730 1740 AYNPEMLKKR QLTVLDLHPG AGKTRRILPQ IIKDAIQKRL RTAVLAPTRV VAAEMAEALR 1750 1760 1770 1780 1790 1800 GLPVRYLTPA VQREHSGNEI VDVMCHATLT HRLMSPLRVP NYNLFVMDEA HFTDPASIAA 1810 1820 1830 1840 1850 1860 RGYIATRVEA GEAAAIFMTA TPPGTSDPFP DTNSPVHDVS SEIPDRAWSS GFEWITDYAG 1870 1880 1890 1900 1910 1920 KTVWFVASVK MSNEIAQCLQ RAGKRVIQLN RKSYDTEYPK CKNGDWDFVI TTDISEMGAN 1930 1940 1950 1960 1970 1980 FGASRVIDCR KSVKPTILDE GEGRVILSVP SAITSASAAQ RRGRVGRNPS QIGDEYHYGG 1990 2000 2010 2020 2030 2040 GTSEDDTMLA HWTEAKILLD NIHLPNGLVA QLYGPERDKT YTMDGEYRLR GEERKTFLEL 2050 2060 2070 2080 2090 2100 IKTADLPVWL AYKVASNGIQ YNDRKWCFDG PRSNIILEDN NEVEIITRIG ERKVLKPRWL 2110 2120 2130 2140 2150 2160 DARVYSDHQS LKWFKDFAAG KRSAIGFFEV LGRMPEHFAG KTREALDTMY LVATSEKGGK 2170 2180 2190 2200 2210 2220 AHRMALEELP DALETITLIA ALGVMTAGFF LLMMQRKGIG KLGLGALVLV VATFFLWMSD 2230 2240 2250 2260 2270 2280 VSGTKIAGVL LLALLMMVVL IPEPEKQRSQ TDNQLAVFLI CVLLVVGLVA ANEYGMLERT 2290 2300 2310 2320 2330 2340 KTDIRNLFGK SLIEENEVHI PPFDFFTLDL KPATAWALYG GSTVVLTPLI KHLVTSQYVT 2350 2360 2370 2380 2390 2400 TSLASINAQA GSLFTLPKGI PFTDFDLSVA LVFLGCWGQV TLTTLIMATI LVTLHYGYLL 2410 2420 2430 2440 2450 2460 PGWQAEALRA AQKRTAAGIM KNAVVDGIVA TDVPELERTT PQMQKRLGQI LLVLASVAAV 2470 2480 2490 2500 2510 2520 CVNPRITTIR EAGILCTAAA LTLWDNNASA AWNSTTATGL CHVMRGSWIA GASIAWTLIK 2530 2540 2550 2560 2570 2580 NAEKPAFKRG RAGGRTLGEQ WKEKLNAMGK EEFFSYRKEA ILEVDRTEAR RARREGNKVG 2590 2600 2610 2620 2630 2640 GHPVSRGTAK LRWLVERRFV QPIGKVVDLG CGRGGWSYYA ATMKNVQEVR GYTKGGPGHE 2650 2660 2670 2680 2690 2700 EPMLMQSYGW NIVTMKSGVD VFYKPSEISD TLLCDIGESS PSAEIEEQRT LRILEMVSDW 2710 2720 2730 2740 2750 2760 LSRGPKEFCI KILCPYMPKV IEKLESLQRR FGGGLVRVPL SRNSNHEMYW VSGASGNIVH 2770 2780 2790 2800 2810 2820 AVNMTSQVLI GRMDKKIWKG PKYEEDVNLG SGTRAVGKGV QHTDYKRIKS RIEKLKEEYA 2830 2840 2850 2860 2870 2880 ATWHTDDNHP YRTWTYHGSY EVKPSGSAST LVNGVVRLLS KPWDAITGVT TMAMTDTTPF 2890 2900 2910 2920 2930 2940 GQQRVFKEKV DTKAPEPPQG VKTVMDETTN WLWAYLARNK KARLCTREEF VKKVNSHAAL 2950 2960 2970 2980 2990 3000 GAMFEEQNQW KNAREAVEDP KFWEMVDEER ECHLRGECRT CIYNMMGKRE KKPGEFGKAK 3010 3020 3030 3040 3050 3060 GSRAIWFMWL GARFLEFEAL GFLNEDHWMS RENSGGGVEG AGIQKLGYIL RDVAQKPGGK 3070 3080 3090 3100 3110 3120 IYADDTAGWD TRITQADLEN EAKVLELMEG EQRTLARAII ELTYRHKVVK VMRPAAGGKT 3130 3140 3150 3160 3170 3180 VMDVISREDQ RGSGQVVTYA LNTFTNIAVQ LVRLMEAEAV IGPDDIESIE RKKKFAVRTW 3190 3200 3210 3220 3230 3240 LFENAEERVQ RMAVSGDDCV VKPLDDRFST ALHFLNAMSK VRKDIQEWKP SQGWYDWQQV 3250 3260 3270 3280 3290 3300 PFCSNHFQEV IMKDGRTLVV PCRGQDELIG RARISPGSGW NVRDTACLAK AYAQMWLVLY 3310 3320 3330 3340 3350 3360 FHRRDLRLMA NAICSSVPVD WVPTGRTTWS IHGKGEWMTT EDMLSVWNRV WILENEWMED 3370 3380 3390 3400 3410 3420 KTTVSDWTEV PYVGKREDIW CGSLIGTRTR ATWAENIYAA INQVRSVIGK EKYVDYVQSL 3430 RRYEETHVSE DRVL

References

[1]	"Characterization of infectious Murray Valley encephalitis virus derived from a stably cloned genomic-length cDNA." Hurrelbrink R.J., Nestorowicz A., McMinn P.C. J. Gen. Virol. 80:3115-3125(1999) [PubMed: 10567642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins." Dalgarno L., Trent D.W., Strauss J.H., Rice C.M. J. Mol. Biol. 187:309-323(1986) [PubMed: 3009829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1780.
[3]	"Sequence of the 3' half of the Murray Valley encephalitis virus genome and mapping of the nonstructural proteins NS1, NS3, and NS5." Lee E., Fernon C., Simpson R., Weir R.C., Rice C.M., Dalgarno L. Virus Genes 4:197-213(1990) [PubMed: 1702914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1773-3434, PROTEIN SEQUENCE OF 794-807; 1504-1519 AND 2530-2537.
[4]	"Determination of the intramolecular disulfide bond arrangement and biochemical identification of the glycosylation sites of the nonstructural protein NS1 of Murray Valley encephalitis virus." Blitvich B.J., Scanlon D., Shiell B.J., Mackenzie J.S., Pham K., Hall R.A. J. Gen. Virol. 82:2251-2256(2001) [PubMed: 11514736] [Abstract] Cited for: GLYCOSYLATION OF NS1, DISULFIDE BONDS.
[5]	"A flavivirus signal peptide balances the catalytic activity of two proteases and thereby facilitates virus morphogenesis." Lobigs M., Lee E., Ng M.L., Pavy M., Lobigs P. Virology 401:80-89(2010) [PubMed: 20207389] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF CAPSID PROTEIN C.
[6]	"Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Angstrom resolution." Mancini E.J., Assenberg R., Verma A., Walter T.S., Tuma R., Grimes J.M., Owens R.J., Stuart D.I. Protein Sci. 16:2294-2300(2007) [PubMed: 17893366] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1681-2122.
[7]	"Crystal structure of the Murray Valley encephalitis virus NS5 methyltransferase domain in complex with cap analogues." Assenberg R., Ren J., Verma A., Walter T.S., Alderton D., Hurrelbrink R.J., Fuller S.D., Bressanelli S., Owens R.J., Stuart D.I., Grimes J.M. J. Gen. Virol. 88:2228-2236(2007) [PubMed: 17622627] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2530-2798.
[8]	"Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication." Assenberg R., Mastrangelo E., Walter T.S., Verma A., Milani M., Owens R.J., Stuart D.I., Grimes J.M., Mancini E.J. J. Virol. 83:12895-12906(2009) [PubMed: 19793813] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1421-2122, SUBUNIT, TOPOLOGY OF SERINE PROTEASE SUBUNIT NS2B, SUBCELLULAR LOCATION OF SERINE PROTEASE NS3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF161266 Genomic RNA. Translation: AAF05296.1.
X03467 Unassigned RNA. Translation: CAA27184.1.

PIR

GNWVMV. A24635.

RefSeq

NP_051124.1. NC_000943.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PX2	X-ray	2.00	A/B	2530-2798	[»]
2PX4	X-ray	2.20	A	2530-2798	[»]
2PX5	X-ray	2.30	A/B	2530-2798	[»]
2PX8	X-ray	2.20	A/B	2530-2798	[»]
2PXA	X-ray	2.30	A/B	2530-2798	[»]
2PXC	X-ray	2.80	A	2530-2798	[»]
2V8O	X-ray	1.90	A	1681-2122	[»]
2WV9	X-ray	2.75	A	1421-2122	[»]

ProteinModelPortal

P05769.

SMR

P05769. Positions 27-97, 293-691, 1422-1464, 1513-2122, 2532-2796, 2803-3426.

ModBase

Search...

Protein family/group databases

MEROPS

S07.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1489715.

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

PS00690. DEAH_ATP_HELICASE. False negative.
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.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

POLG_MVEV5

Accession

Primary (citable) accession number: P05769
Secondary accession number(s): Q9Q9F7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	December 21, 2004
Last modified:	November 16, 2011
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program