Reviewed, UniProtKB/Swiss-Prot P03314 (POLG_YEFV1)

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     10- Recommended name:             Serine protease subunit NS3               EC=3.4.21.91         Alternative name(s):             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:             RNA-directed RNA polymerase NS5               EC=2.7.7.48               EC=2.1.1.56         Alternative name(s):             Non-structural protein 5
Organism	Yellow fever virus (strain 17D vaccine) (YFV) [Complete proteome]
Taxonomic identifier	11090 [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	Evidence at protein level.

General annotation (Comments)

Function	Protein C packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Ref.14 Ref.18 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. Ref.14 Ref.18 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. Ref.14 Ref.18 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. Ref.14 Ref.18 Non-structural protein 2B is a required cofactor for the serine protease function of NS3. Ref.14 Ref.18 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. Ref.14 Ref.18 Non-structural protein 4A plays a role in RNA replication. Ref.14 Ref.18 Non-structural protein 4B plays a role in RNA replication. Ref.14 Ref.18 RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and assure the capping of genomes in the cytoplasm. May be involved in methylation of 5'RNA cap structure. Ref.14 Ref.18
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). S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-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. Ref.20
Subcellular location	Protein C: Virion. Ref.25 Peptide pr: Secreted. Ref.25 Small envelope protein M: Virion membrane; Single-pass type I membrane protein. Ref.25 Envelope protein E: Virion membrane; Single-pass type I membrane protein. Ref.25 Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Ref.25 Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane. Ref.25 Non-structural protein 2A: Host endoplasmic reticulum membrane. Ref.25 Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Ref.25 Serine protease subunit NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Ref.25 Non-structural protein 4A: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Ref.25 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. RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus. Ref.25
Domain	Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals.
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. Ref.13 RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. Ref.19 Envelope protein E and non-structural protein 1 are N-glycosylated.
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 Endoplasmic reticulum Envelope protein Membrane Nucleus Secreted Virion
Domain	Transmembrane
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Viral nucleoprotein
Molecular function	Helicase Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Ribonucleoprotein 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	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	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW
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

Chain

2 – 101

100

Protein C

PRO_0000037754

Propeptide

102 – 121

20

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

PRO_0000261384

Chain

122 – 285

164

prM

PRO_0000261385

Chain

122 – 210

89

Peptide pr

PRO_0000037755

Chain

211 – 285

75

Small envelope protein M

PRO_0000037756

Chain

286 – 778

493

Envelope protein E

PRO_0000037757

Chain

779 – 1130

352

Non-structural protein 1

PRO_0000037758

Chain

1131 – 1354

224

Non-structural protein 2A

PRO_0000037759

Chain

1131 – 1320

190

Non-structural protein 2A-alpha

PRO_0000261386

Chain

1355 – 1484

130

Serine protease subunit NS2B

PRO_0000037760

Chain

1485 – 2107

623

Serine protease subunit NS3

PRO_0000037761

Chain

2108 – 2233

126

Non-structural protein 4A

PRO_0000037762

Peptide

2234 – 2256

23

Peptide 2k

PRO_0000261387

Chain

2257 – 2506

250

Non-structural protein 4B

PRO_0000037763

Chain

2507 – 3411

905

RNA-directed RNA polymerase NS5

PRO_0000037764

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

Motif

1773 – 1776

4

DEAH box

Motif

2878 – 2911

34

Nuclear localization signal By similarity

Sites

Active site

1537

1

Charge relay system; for serine protease NS3 activity

Active site

1561

1

Charge relay system; for serine protease NS3 activity

Active site

1622

1

Charge relay system; for serine protease NS3 activity

Site

101 – 102

2

Cleavage; by serine protease NS3

Site

121 – 122

2

Cleavage; by host signal peptidase

Site

210 – 211

2

Cleavage; by host furin

Site

285 – 286

2

Cleavage; by host signal peptidase

Site

778 – 779

2

Cleavage; by host signal peptidase

Site

1130 – 1131

2

Cleavage; by host

Site

1320 – 1321

2

Cleavage; by serine protease NS3

Site

1354 – 1355

2

Cleavage; by serine protease NS3

Site

1484 – 1485

2

Cleavage; by serine protease NS3

Site

2107 – 2108

2

Cleavage; by serine protease NS3

Site

2233 – 2234

2

Cleavage; by host signal peptidase

Site

2256 – 2257

2

Cleavage; by serine protease NS3

Site

2506 – 2507

2

Cleavage; by serine protease NS3

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

Natural variations

Natural variant

341

1

V → A in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.

Natural variant

438

1

N → T in strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine.

Natural variant

440

1

D → S in strain: Isolate 17DD vaccine.

Natural variant

610

1

S → P in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.

Natural variant

629

1

I → V in strain: Isolate Brazil/YF-VAVD/75 vaccine.

Natural variant

701

1

T → V in strain: Isolate 17DD vaccine.

Natural variant

744

1

A → V in strain: Isolate 17D-204-South Africa vaccine large plaque variant.

Natural variant

764

1

L → M in strain: Isolate 17D-204-South Africa vaccine large plaque variant.

Natural variant

1299

1

F → L in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.

Natural variant

1666

1

Q → R in strain: Isolate 17DD vaccine.

Natural variant

1669

1

P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine.

Natural variant

1679

1

V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.

Natural variant

2214

1

V → I in strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine.

Natural variant

2277

1

P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine.

Natural variant

2401

1

E → K in strain: Isolate 17D-204-South Africa vaccine large plaque variant, Isolate 17D-204-South Africa vaccine medium plaque variant, Isolate 17D-204-South Africa vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine.

Natural variant

2460

1

L → S in strain: Isolate 17D-204-USA HONG vaccine1, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine.

Natural variant

2528

1

R → Q in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.

Natural variant

2643

1

P → S in strain: Isolate 17D-204-South Africa vaccine medium plaque variant.

Natural variant

2661

1

V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine.

Natural variant

2897

1

N → S in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.

Natural variant

3110

1

G → R in strain: Isolate 17D-204-USA HONG2 vaccine.

Natural variant

3135

1

M → N in strain: Isolate Brazil/YF-VAVD/75 vaccine.

Natural variant

3163

1

D → N in strain: Isolate 17D-204-South Africa vaccine large plaque variant, Isolate 17D-204-South Africa vaccine medium plaque variant, Isolate 17D-204-South Africa vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine.

Natural variant

3222

1

H → R in strain: Isolate Brazil/YF-VAVD/75 vaccine.

Experimental info

Mutagenesis

98 – 101

4

RKRR → AAAA: Complete loss of NS2B-NS3 cleavage.

Mutagenesis

98 – 101

4

RKRR → AKAA: Complete loss of NS2B-NS3 cleavage.

Mutagenesis

98 – 101

4

RKRR → AKRA: Reduces NS2B-NS3 cleavage efficiency.

Mutagenesis

98 – 100

3

RKR → AAA: Complete loss of NS2B-NS3 cleavage.

Mutagenesis

98 – 100

3

RKR → AKA: Complete loss of NS2B-NS3 cleavage.

Mutagenesis

98 – 99

2

RK → AA: Reduces NS2B-NS3 cleavage efficiency.

Mutagenesis

99 – 101

3

KRR → ARA: Complete loss of NS2B-NS3 cleavage. Ref.21

Mutagenesis

99 – 100

2

KR → AA: Complete loss of NS2B-NS3 cleavage.

Mutagenesis

100 – 101

2

RR → AA: Reduces NS2B-NS3 cleavage efficiency.

Mutagenesis

116 – 121

6

LLMTGG → VPQAQA: Complete loss of infectious virus production. Enhances signal peptidase cleavage in vitro of nascent protein C. Ref.22

Mutagenesis

908

1

N → A: Reduces viral RNA accumulation and NS1 secretion. Ref.16

Mutagenesis

910

1

S → A: Reduces viral RNA accumulation and NS1 secretion. Ref.16

Mutagenesis

986

1

N → A: No effect. Ref.16

Mutagenesis

988

1

T → A: No effect. Ref.16

Mutagenesis

1077

1

R → A: Blocks RNA replication. Ref.17

Mutagenesis

1319 – 1321

3

QKT → RRS: Increases NS2A-alpha processing, complete loss of NS2A. Ref.24

Mutagenesis

1319

1

Q → S: Complete loss of cleavage and NS2A alpha. Complete loss of infectivity. Ref.24

Mutagenesis

1320

1

K → E, I, Q or S: Complete loss of cleavage and NS2A-alpha processing. Complete loss of infectivity. Ref.24

Mutagenesis

1320

1

K → R: No effect on NS2A-alpha processing. Ref.24

Mutagenesis

1321

1

T → V: Complete loss of cleavage and NS2A alpha synthesis. Complete loss of infectivity. Ref.24

Mutagenesis

1351

1

F → C, I or V: Enhances NS2A-NS2B cleavage efficiency. Ref.15

Mutagenesis

1351

1

F → G: No effect on NS2A-NS2B cleavage efficiency. Ref.15

Mutagenesis

1352

1

G → A or K: Enhances NS2A-NS2B cleavage efficiency. Ref.15

Mutagenesis

1352

1

G → E or V: Reduces NS2A-NS2B cleavage efficiency. Ref.15

Mutagenesis

1353

1

R → H, K, R or T: Reduces NS2A-NS2B cleavage efficiency. Ref.15

Mutagenesis

1353

1

R → L or P: Complete loss of NS2A-NS2B cleavage. Ref.15

Mutagenesis

1354

1

R → I, N, S or T: Complete loss of NS2A-NS2B cleavage. Ref.15

Mutagenesis

1354

1

R → K: Reduces of NS2A-NS2B cleavage efficiency. Ref.15

Mutagenesis

1355

1

S → D, K, R or V: Complete loss of NS2A-NS2B cleavage. Ref.15

Mutagenesis

1355

1

S → G: Reduces of NS2A-NS2B cleavage efficiency. Ref.15

Mutagenesis

1406 – 1409

4

ELKK → ALAA: Complete loss of polyprotein cleavage. Ref.23

Mutagenesis

1537

1

H → A: Complete loss NS3 protease activity. Ref.10

Mutagenesis

1561

1

D → A or N: Complete loss NS3 protease activity. Ref.10

Mutagenesis

1622

1

S → A: Complete loss NS3 protease activity. Ref.10

Mutagenesis

1622

1

S → C: Diminishes NS3 protease activity. Ref.10

Mutagenesis

2107

1

R → A, L, M, T or V: Reduces NS4A-NS4B cleavage efficiency. Ref.12

Mutagenesis

2107

1

R → E or P: Complete loss of NS4A-NS4B cleavage. Ref.12

Mutagenesis

2107

1

R → K: No effect on NS4A-NS4B cleavage efficiency. Ref.12

Mutagenesis

2505

1

R → A, I, L, Q, S or T: No effect on NS4B-NS5 cleavage efficiency. Ref.12

Mutagenesis

2505

1

R → P: Reduces NS4B-NS5 cleavage efficiency. Ref.12

Mutagenesis

2506

1

R → E or Y: Complete loss of NS4B-NS5 cleavage. Ref.12

Mutagenesis

2506

1

R → H, N or Q: Reduces NS4B-NS5 cleavage efficiency. Ref.12

Mutagenesis

2506

1

R → K: No effect on NS4B-NS5 cleavage efficiency. Ref.12

Mutagenesis

2507

1

G → A or S: Reduces NS4B-NS5 cleavage efficiency.

Mutagenesis

2507

1

G → E, K, L, M, N or V: Reduces NS4B-NS5 cleavage efficiency.

Secondary structure

1

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3411

Helix Strand Turn

Details...

Beta strand

1677 – 1680

4

Turn

1688 – 1691

4

Helix

1692 – 1702

11

Beta strand

1707 – 1713

7

Helix

1714 – 1723

10

Turn

1724 – 1726

3

Beta strand

1729 – 1731

3

Beta strand

1746 – 1750

5

Helix

1751 – 1758

8

Beta strand

1760 – 1762

3

Beta strand

1768 – 1772

5

Turn

1773 – 1776

4

Helix

1780 – 1794

15

Beta strand

1799 – 1803

5

Beta strand

1821 – 1825

5

Beta strand

1834 – 1836

3

Helix

1839 – 1842

4

Beta strand

1847 – 1850

4

Helix

1854 – 1866

13

Beta strand

1871 – 1873

3

Beta strand

1876 – 1878

3

Beta strand

1892 – 1899

8

Beta strand

1909 – 1913

5

Beta strand

1916 – 1923

8

Turn

1924 – 1927

4

Beta strand

1928 – 1936

9

Helix

1939 – 1946

8

Beta strand

1958 – 1962

5

Helix

1974 – 1983

10

Helix

1989 – 1991

3

Helix

2000 – 2003

4

Beta strand

2004 – 2006

3

Turn

2008 – 2011

4

Helix

2015 – 2026

12

Helix

2032 – 2040

9

Helix

2049 – 2051

3

Helix

2056 – 2058

3

Beta strand

2069 – 2071

3

Beta strand

2077 – 2079

3

Beta strand

2083 – 2086

4

Helix

2087 – 2089

3

Beta strand

2090 – 2092

3

Helix

2093 – 2103

11

Turn

2104 – 2106

3

Sequences

	Sequence		Length	Mass (Da)
	P03314-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 680E0FACD23DCFA6	FASTA	3,411	379,518
	10 20 30 40 50 60 MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK 70 80 90 100 110 120 ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSHDVLTVQF LILGMLLMTG 130 140 150 160 170 180 GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN 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 ETVAIDRPAE VRKVCYNAVL THVKINDKCP 370 380 390 400 410 420 STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI 430 440 450 460 470 480 QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEVEFIGY GKATLECQVQ TAVDFGNSYI 490 500 510 520 530 540 AEMETESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK 550 560 570 580 590 600 TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKICTDKMF FVKNPTDTGH 610 620 630 640 650 660 GTVVMQVKVS KGAPCRIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY 670 680 690 700 710 720 IIVGRGDSRL TYQWHKEGSS IGKLFTQTMK GVERLAVMGD TAWDFSSAGG FFTSVGKGIH 730 740 750 760 770 780 TVFGSAFQGL FGGLNWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ 790 800 810 820 830 840 GCAINFGKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS 850 860 870 880 890 900 LEHEMWRSRA DEINAIFEEN 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 DSGKVIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL 1150 1160 1170 1180 1190 1200 VSMMIAMEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD 1210 1220 1230 1240 1250 1260 AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGVMG GLWKYLNAVS 1270 1280 1290 1300 1310 1320 LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMFF CAVVIIGVLH QNFKDTSMQK 1330 1340 1350 1360 1370 1380 TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME 1390 1400 1410 1420 1430 1440 NFLGPIAVGG LLMMLVSVAG RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL 1450 1460 1470 1480 1490 1500 LSEEKVPWDQ VVMTSLALVG AALHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKIIEE 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 MLKKGMTTVL 1690 1700 1710 1720 1730 1740 DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG 1750 1760 1770 1780 1790 1800 SGREVIDAMC HATLTYRMLE PTRVVNWEVI 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 YYSEPTSENN AHHVCWLEAS 1990 2000 2010 2020 2030 2040 MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK 2050 2060 2070 2080 2090 2100 AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI 2110 2120 2130 2140 2150 2160 KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI 2170 2180 2190 2200 2210 2220 VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYVMLIFFV 2230 2240 2250 2260 2270 2280 LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSAVAANELG MLEKTKEDLF GKKNLIPSSA 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 ENPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL 2470 2480 2490 2500 2510 2520 GPLIEGNTSL LWNGPMAVSM TGVMRGNHYA FVGVMYNLWK MKTGRRGSAN GKTLGEVWKR 2530 2540 2550 2560 2570 2580 ELNLLDKRQF 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 ADVILPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF YDNDNPYRTW HYCGSYVTKT 2830 2840 2850 2860 2870 2880 SGSAASMVNG VIKILTYPWD RIEEVTRMAM 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 GCDRLKRMAV 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 KKWRDVPYLT KRQDKLCGSL 3370 3380 3390 3400 3410 IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQLGEL I

References

[1]	"Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution." Rice C.M., Lenches E.M., Eddy S.R., Shin S.J., Sheets R.L., Strauss J.H. Science 229:726-733(1985) [PubMed: 4023707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Complete nucleotide sequence of yellow fever virus vaccine strains 17DD and 17D-213." dos Santos C.N., Post P.R., Carvalho R., Ferreira I.I., Rice C.M., Galler R. Virus Res. 35:35-41(1995) [PubMed: 7754673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate 17D-213 vaccine and Isolate 17DD vaccine.
[3]	"Yellow fever 17D vaccine virus isolated from healthy vaccinees accumulates very few mutations." Xie H., Cass A.R., Barrett A.D.T. Virus Res. 55:93-99(1998) [PubMed: 9712515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine.
[4]	"Nucleotide sequence comparison of the genome of two 17D-204 yellow fever vaccines." Dupuy A., Despres P., Cahour A., Girard M., Bouloy M. Nucleic Acids Res. 17:3989-3989(1989) [PubMed: 2734112] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate Pasteur 17D-204 vaccine.
[5]	"Mutation in NS5 protein attenuates mouse neurovirulence of yellow fever 17D vaccine virus." Xie H., Ryman K.D., Campbell G.A., Barrett A.D.T. J. Gen. Virol. 79:1895-1899(1998) [PubMed: 9714237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate 17D-204-South Africa vaccine, Isolate 17D-204-South Africa vaccine large plaque variant and Isolate 17D-204-South Africa vaccine medium plaque variant.
[6]	"Yellow fever vaccine-associated viscerotropic disease and death in Spain." Doblas A., Domingo C., Bae H.G., Bohorquez C.L., de Ory F., Niedrig M., Mora D., Carrasco F.J., Tenorio A. J. Clin. Virol. 36:156-158(2006) [PubMed: 16597510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate Spain/AVD2791-93F/2004 vaccine.
[7]	"Characterization of a viscerotropic yellow fever vaccine variant from a patient in Brazil." Engel A.R., Vasconcelos P.F., McArthur M.A., Barrett A.D. Vaccine 24:2803-2809(2006) [PubMed: 16464518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate Brazil/YF-VAVD/1975 vaccine.
[8]	"Partial N-terminal amino acid sequences of three nonstructural proteins of two flaviviruses." Rice C.M., Aebersold R., Teplow D.B., Pata J., Bell J.R., Vorndam A.V., Trent D.W., Brandriss M.W., Schlesinger J.J., Strauss J.H. Virology 151:1-9(1986) [PubMed: 3008425] [Abstract] Cited for: PROTEIN SEQUENCE OF 779-798; 1485-1497 AND 2507-2510.
[9]	"Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and partial N-terminal amino acid sequence analysis." Chambers T.J., McCourt D.W., Rice C.M. Virology 169:100-109(1989) [PubMed: 2922923] [Abstract] Cited for: PROTEIN SEQUENCE OF 2257-2276.
[10]	"Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein." Chambers T.J., Weir R.C., Grakoui A., McCourt D.W., Bazan J.F., Fletterick R.J., Rice C.M. Proc. Natl. Acad. Sci. U.S.A. 87:8898-8902(1990) [PubMed: 2147282] [Abstract] Cited for: CHARACTERIZATION OF NS2B-NS3 PROTEASE, MUTAGENESIS OF HIS-1537; ASP-1561 AND SER-1622.
[11]	"Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants of cleavage site specificity and effects on polyprotein processing and viral replication." Chambers T.J., Nestorowicz A., Rice C.M. J. Virol. 69:1600-1605(1995) [PubMed: 7853494] [Abstract] Cited for: CHARACTERIZATION OF NS2B/NS3 PROTEASE.
[12]	"Mutagenesis of conserved residues at the yellow fever virus 3/4A and 4B/5 dibasic cleavage sites: effects on cleavage efficiency and polyprotein processing." Lin C., Chambers T.J., Rice C.M. Virology 192:596-604(1993) [PubMed: 8421901] [Abstract] Cited for: MUTAGENESIS OF ARG-2107; ARG-2505 AND ARG-2506.
[13]	"Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site." Lin C., Amberg S.M., Chambers T.J., Rice C.M. J. Virol. 67:2327-2335(1993) [PubMed: 8445732] [Abstract] Cited for: CLEAVAGE OF NS4A/NS4B.
[14]	"NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies." Amberg S.M., Nestorowicz A., McCourt D.W., Rice C.M. J. Virol. 68:3794-3802(1994) [PubMed: 8189517] [Abstract] Cited for: FUNCTION OF NS2B/NS3 PROTEASE.
[15]	"Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects on proteolytic processing, viral replication, and evidence for alternative processing of the NS2A protein." Nestorowicz A., Chambers T.J., Rice C.M. Virology 199:114-123(1994) [PubMed: 8116234] [Abstract] Cited for: MUTAGENESIS OF PHE-1351; GLY-1352; ARG-1353; ARG-1354 AND SER-1355.
[16]	"Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence." Muylaert I.R., Chambers T.J., Galler R., Rice C.M. Virology 222:159-168(1996) [PubMed: 8806496] [Abstract] Cited for: MUTAGENESIS OF ASN-908; SER-910; ASN-986 AND THR-988.
[17]	"Genetic analysis of the yellow fever virus NS1 protein: identification of a temperature-sensitive mutation which blocks RNA accumulation." Muylaert I.R., Galler R., Rice C.M. J. Virol. 71:291-298(1997) [PubMed: 8985349] [Abstract] Cited for: MUTAGENESIS OF ARG-1077.
[18]	"trans-Complementation of yellow fever virus NS1 reveals a role in early RNA replication." Lindenbach B.D., Rice C.M. J. Virol. 71:9608-9617(1997) [PubMed: 9371625] [Abstract] Cited for: FUNCTION OF NS1.
[19]	"The NS5A/NS5 proteins of viruses from three genera of the family flaviviridae are phosphorylated by associated serine/threonine kinases." Reed K.E., Gorbalenya A.E., Rice C.M. J. Virol. 72:6199-6206(1998) [PubMed: 9621090] [Abstract] Cited for: PHOSPHORYLATION OF NS5.
[20]	"Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function." Lindenbach B.D., Rice C.M. J. Virol. 73:4611-4621(1999) [PubMed: 10233920] [Abstract] Cited for: INTERACTION OF NS1 WITH NS4A.
[21]	"Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus capsid protein demonstrates a requirement for coordinated processing." Amberg S.M., Rice C.M. J. Virol. 73:8083-8094(1999) [PubMed: 10482557] [Abstract] Cited for: MUTAGENESIS OF 99-ARG--ARG-101.
[22]	"Mutagenesis of the signal sequence of yellow fever virus prM protein: enhancement of signalase cleavage In vitro is lethal for virus production." Lee E., Stocks C.E., Amberg S.M., Rice C.M., Lobigs M. J. Virol. 74:24-32(2000) [PubMed: 10590087] [Abstract] Cited for: MUTAGENESIS OF 116-LEU--GLY-121.
[23]	"Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function." Droll D.A., Krishna Murthy H.M., Chambers T.J. Virology 275:335-347(2000) [PubMed: 10998334] [Abstract] Cited for: MUTAGENESIS OF 1406-GLU--LYS-1409.
[24]	"Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles." Kummerer B.M., Rice C.M. J. Virol. 76:4773-4784(2002) [PubMed: 11967294] [Abstract] Cited for: MUTAGENESIS OF GLN-1319; LYS-1320 AND THR-1321.
[25]	"The transmembrane domains of the prM and E proteins of yellow fever virus are endoplasmic reticulum localization signals." Op De Beeck A., Rouille Y., Caron M., Duvet S., Dubuisson J. J. Virol. 78:12591-12602(2004) [PubMed: 15507646] [Abstract] Cited for: SUBCELLULAR LOCATION OF SMALL ENVELOPE PROTEIN M AND ENVELOPE PROTEIN E.
[26]	"Structures of immature flavivirus particles." Zhang Y., Corver J., Chipman P.R., Zhang W., Pletnev S.V., Sedlak D., Baker T.S., Strauss J.H., Kuhn R.J., Rossmann M.G. EMBO J. 22:2604-2613(2003) [PubMed: 12773377] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) OF IMMATURE PARTICLES.
[27]	"Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing." Wu J., Bera A.K., Kuhn R.J., Smith J.L. J. Virol. 79:10268-10277(2005) [PubMed: 16051820] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1671-2107.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X03700 Genomic RNA. Translation: CAA27332.1.
X15062 Genomic RNA. Translation: CAB37419.1.
U17066 Genomic RNA. Translation: AAC54267.1.
U17067 Genomic RNA. Translation: AAC54268.1.
AF052437 Genomic RNA. Translation: AAC35899.1.
AF052438 Genomic RNA. Translation: AAC35900.1.
AF052439 Genomic RNA. Translation: AAC35901.1.
AF052444 Genomic RNA. Translation: AAC35906.1.
AF052445 Genomic RNA. Translation: AAC35907.1.
AF052446 Genomic RNA. Translation: AAC35908.1.
DQ118157 Genomic RNA. Translation: AAZ31436.1.
DQ100292 Genomic RNA. Translation: AAZ07885.1.

PIR

GNWVY. A03914.
GNWVYP. S07757.

RefSeq

NP_041726.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NA4	electron microscopy	-
1YKS	X-ray	1.80	A	1671-2107	[»]
1YMF	X-ray	2.60	A	1671-2107	[»]
3EVA	X-ray	1.50	A	2507-2772	[»]
3EVB	X-ray	1.85	A	2507-2772	[»]
3EVC	X-ray	1.60	A	2507-2772	[»]
3EVD	X-ray	1.50	A	2507-2772	[»]
3EVE	X-ray	1.70	A	2507-2772	[»]
3EVF	X-ray	1.45	A	2507-2772	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR011492. DEAD_Flavivir.
IPR001650. DNA/RNA_helicase_C.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_glyE_cen_1.
IPR013756. Flav_glyE_cen_2.
IPR011999. Flav_glyE_cen_dm.
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.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR001850. Peptidase_S7.
IPR000208. RNA_pol_flaviviral.
IPR007094. RNA_pol_PSvir.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
[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.
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.

ProDom

PD001496. Flavi_NS1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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]

ProtoNet

Search...

Entry information

Entry name

POLG_YEFV1

Accession

Primary (citable) accession number: P03314
Secondary accession number(s): O42028 , O91857, P19901, Q102J3, Q45RQ2, Q89275, Q89276, Q9W878, Q9YWN0, Q9YWN1, Q9YWN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)