Protein C
     (Core protein)
     (Capsid protein)
prM
Peptide pr
Small envelope protein M
     (Matrix protein)
Envelope protein E
Non-structural protein 1
     (NS1)
Non-structural protein 2A
     (NS2A)
Non-structural protein 2A-alpha
     (NS2A-alpha)
Serine protease subunit NS2B
     (Non-structural protein 2B)
Serine protease subunit NS3
     (EC 3.4.21.91)
     (Non-structural protein 3)
Non-structural protein 4A
     (NS4A)
Peptide 2k
Non-structural protein 4B
     (NS4B)
RNA-directed RNA polymerase NS5
     (EC 2.7.7.48)
     (EC 2.1.1.56)
     (Non-structural protein 5)

Gene name

None

From

Yellow fever virus (strain 17D vaccine) (YFV)

[TaxID: 11090]

Taxonomy

Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; Flavivirus; Yellow fever virus group.

Virus hosts

Aedes aegypti (Yellowfever mosquito) [TaxID: 7159]
Aedes luteocephalus [TaxID: 299629]
Aedes simpsoni [TaxID: 7161]
Homo sapiens (Human) [TaxID: 9606]
Simiiformes [TaxID: 314293]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. PubMed=4023707 [NCBI, ExPASy, EBI, Israel, Japan] Rice C.M., Lenches E.M., Eddy S.R., Shin S.J., Sheets R.L., Strauss J.H.; "Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution."; Science 229:726-733(1985).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. STRAIN=Isolate 17D-213 vaccine, and Isolate 17DD vaccine; DOI=10.1016/0168-1702(94)00076-O; PubMed=7754673 [NCBI, ExPASy, EBI, Israel, Japan] dos Santos C.N., Post P.R., Carvalho R., Ferreira I.I., Rice C.M., Galler R.; "Complete nucleotide sequence of yellow fever virus vaccine strains 17DD and 17D-213."; Virus Res. 35:35-41(1995).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. STRAIN=Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, and Isolate 17D-204-USA HONG3 vaccine; DOI=10.1016/S0168-1702(98)00036-7; PubMed=9712515 [NCBI, ExPASy, EBI, Israel, Japan] Xie H., Cass A.R., Barrett A.D.T.; "Yellow fever 17D vaccine virus isolated from healthy vaccinees accumulates very few mutations."; Virus Res. 55:93-99(1998).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. STRAIN=Isolate Pasteur 17D-204 vaccine; DOI=10.1093/nar/17.10.3989; PubMed=2734112 [NCBI, ExPASy, EBI, Israel, Japan] Dupuy A., Despres P., Cahour A., Girard M., Bouloy M.; "Nucleotide sequence comparison of the genome of two 17D-204 yellow fever vaccines."; Nucleic Acids Res. 17:3989-3989(1989).
[5]	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; PubMed=9714237 [NCBI, ExPASy, EBI, Israel, Japan] Xie H., Ryman K.D., Campbell G.A., Barrett A.D.T.; "Mutation in NS5 protein attenuates mouse neurovirulence of yellow fever 17D vaccine virus."; J. Gen. Virol. 79:1895-1899(1998).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. STRAIN=Isolate Spain/AVD2791-93F/2004 vaccine; DOI=10.1016/j.jcv.2006.02.005; PubMed=16597510 [NCBI, ExPASy, EBI, Israel, Japan] Doblas A., Domingo C., Bae H.G., Bohorquez C.L., de Ory F., Niedrig M., Mora D., Carrasco F.J., Tenorio A.; "Yellow fever vaccine-associated viscerotropic disease and death in Spain."; J. Clin. Virol. 36:156-158(2006).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. STRAIN=Isolate Brazil/YF-VAVD/1975 vaccine; DOI=10.1016/j.vaccine.2006.01.009; PubMed=16464518 [NCBI, ExPASy, EBI, Israel, Japan] Engel A.R., Vasconcelos P.F., McArthur M.A., Barrett A.D.; "Characterization of a viscerotropic yellow fever vaccine variant from a patient in Brazil."; Vaccine 24:2803-2809(2006).
[8]	PROTEIN SEQUENCE OF 779-798; 1485-1497 AND 2507-2510. DOI=10.1016/0042-6822(86)90098-X; PubMed=3008425 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Partial N-terminal amino acid sequences of three nonstructural proteins of two flaviviruses."; Virology 151:1-9(1986).
[9]	PROTEIN SEQUENCE OF 2257-2276. DOI=10.1016/0042-6822(89)90045-7; PubMed=2922923 [NCBI, ExPASy, EBI, Israel, Japan] Chambers T.J., McCourt D.W., Rice C.M.; "Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and partial N-terminal amino acid sequence analysis."; Virology 169:100-109(1989).
[10]	CHARACTERIZATION OF NS2B-NS3 PROTEASE, AND MUTAGENESIS OF HIS-1537; ASP-1561 AND SER-1622. PubMed=2147282 [NCBI, ExPASy, EBI, Israel, Japan] Chambers T.J., Weir R.C., Grakoui A., McCourt D.W., Bazan J.F., Fletterick R.J., Rice C.M.; "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."; Proc. Natl. Acad. Sci. U.S.A. 87:8898-8902(1990).
[11]	CHARACTERIZATION OF NS2B/NS3 PROTEASE. PubMed=7853494 [NCBI, ExPASy, EBI, Israel, Japan] Chambers T.J., Nestorowicz A., Rice C.M.; "Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants of cleavage site specificity and effects on polyprotein processing and viral replication."; J. Virol. 69:1600-1605(1995).
[12]	MUTAGENESIS OF ARG-2107; ARG-2505 AND ARG-2506. DOI=10.1006/viro.1993.1076; PubMed=8421901 [NCBI, ExPASy, EBI, Israel, Japan] Lin C., Chambers T.J., Rice C.M.; "Mutagenesis of conserved residues at the yellow fever virus 3/4A and 4B/5 dibasic cleavage sites: effects on cleavage efficiency and polyprotein processing."; Virology 192:596-604(1993).
[13]	CLEAVAGE OF NS4A/NS4B. PubMed=8445732 [NCBI, ExPASy, EBI, Israel, Japan] Lin C., Amberg S.M., Chambers T.J., Rice C.M.; "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."; J. Virol. 67:2327-2335(1993).
[14]	FUNCTION OF NS2B/NS3 PROTEASE. PubMed=8189517 [NCBI, ExPASy, EBI, Israel, Japan] Amberg S.M., Nestorowicz A., McCourt D.W., Rice C.M.; "NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies."; J. Virol. 68:3794-3802(1994).
[15]	MUTAGENESIS OF PHE-1351; GLY-1352; ARG-1353; ARG-1354 AND SER-1355. DOI=10.1006/viro.1994.1103; PubMed=8116234 [NCBI, ExPASy, EBI, Israel, Japan] Nestorowicz A., Chambers T.J., Rice C.M.; "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."; Virology 199:114-123(1994).
[16]	MUTAGENESIS OF ASN-908; SER-910; ASN-986 AND THR-988. DOI=10.1006/viro.1996.0406; PubMed=8806496 [NCBI, ExPASy, EBI, Israel, Japan] Muylaert I.R., Chambers T.J., Galler R., Rice C.M.; "Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence."; Virology 222:159-168(1996).
[17]	MUTAGENESIS OF ARG-1077. PubMed=8985349 [NCBI, ExPASy, EBI, Israel, Japan] Muylaert I.R., Galler R., Rice C.M.; "Genetic analysis of the yellow fever virus NS1 protein: identification of a temperature-sensitive mutation which blocks RNA accumulation."; J. Virol. 71:291-298(1997).
[18]	FUNCTION OF NS1. PubMed=9371625 [NCBI, ExPASy, EBI, Israel, Japan] Lindenbach B.D., Rice C.M.; "trans-Complementation of yellow fever virus NS1 reveals a role in early RNA replication."; J. Virol. 71:9608-9617(1997).
[19]	PHOSPHORYLATION OF NS5. PubMed=9621090 [NCBI, ExPASy, EBI, Israel, Japan] Reed K.E., Gorbalenya A.E., Rice C.M.; "The NS5A/NS5 proteins of viruses from three genera of the family flaviviridae are phosphorylated by associated serine/threonine kinases."; J. Virol. 72:6199-6206(1998).
[20]	INTERACTION OF NS1 WITH NS4A. PubMed=10233920 [NCBI, ExPASy, EBI, Israel, Japan] Lindenbach B.D., Rice C.M.; "Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function."; J. Virol. 73:4611-4621(1999).
[21]	MUTAGENESIS OF 99-ARG--ARG-101. PubMed=10482557 [NCBI, ExPASy, EBI, Israel, Japan] Amberg S.M., Rice C.M.; "Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus capsid protein demonstrates a requirement for coordinated processing."; J. Virol. 73:8083-8094(1999).
[22]	MUTAGENESIS OF 116-LEU--GLY-121. PubMed=10590087 [NCBI, ExPASy, EBI, Israel, Japan] Lee E., Stocks C.E., Amberg S.M., Rice C.M., Lobigs M.; "Mutagenesis of the signal sequence of yellow fever virus prM protein: enhancement of signalase cleavage In vitro is lethal for virus production."; J. Virol. 74:24-32(2000).
[23]	MUTAGENESIS OF 1406-GLU--LYS-1409. DOI=10.1006/viro.2000.0488; PubMed=10998334 [NCBI, ExPASy, EBI, Israel, Japan] Droll D.A., Krishna Murthy H.M., Chambers T.J.; "Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function."; Virology 275:335-347(2000).
[24]	MUTAGENESIS OF GLN-1319; LYS-1320 AND THR-1321. DOI=10.1128/JVI.76.10.4773-4784.2002; PubMed=11967294 [NCBI, ExPASy, EBI, Israel, Japan] Kummerer B.M., Rice C.M.; "Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles."; J. Virol. 76:4773-4784(2002).
[25]	SUBCELLULAR LOCATION OF SMALL ENVELOPE PROTEIN M AND ENVELOPE PROTEIN E. DOI=10.1128/JVI.78.22.12591-12602.2004; PubMed=15507646 [NCBI, ExPASy, EBI, Israel, Japan] Op De Beeck A., Rouille Y., Caron M., Duvet S., Dubuisson J.; "The transmembrane domains of the prM and E proteins of yellow fever virus are endoplasmic reticulum localization signals."; J. Virol. 78:12591-12602(2004).
[26]	STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) OF IMMATURE PARTICLES. DOI=10.1093/emboj/cdg270; PubMed=12773377 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Structures of immature flavivirus particles."; EMBO J. 22:2604-2613(2003).
[27]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1671-2107. DOI=10.1128/JVI.79.16.10268-10277.2005; PubMed=16051820 [NCBI, ExPASy, EBI, Israel, Japan] Wu J., Bera A.K., Kuhn R.J., Smith J.L.; "Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing."; J. Virol. 79:10268-10277(2005).

Comments

FUNCTION: Protein C packages viral RNA to form a viral nucleocapsid, and promotes virion budding.
FUNCTION: 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.
FUNCTION: 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.
FUNCTION: 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.
FUNCTION: Non-structural protein 2B is a required cofactor for the serine protease function of NS3.
FUNCTION: 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.
FUNCTION: Non-structural protein 4A plays a role in RNA replication.
FUNCTION: Non-structural protein 4B plays a role in RNA replication.
FUNCTION: 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.
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.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m₇G(5')pppR-RNA.
SUBUNIT: 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.
SUBCELLULAR LOCATION: Protein C: Virion.
SUBCELLULAR LOCATION: Peptide pr: Secreted.
SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane; Single-pass type I membrane protein.
SUBCELLULAR LOCATION: Envelope protein E: Virion membrane; Single-pass type I membrane protein.
SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Endoplasmic reticulum membrane.
SUBCELLULAR LOCATION: Non-structural protein 2A: Endoplasmic reticulum membrane.
SUBCELLULAR LOCATION: Serine protease subunit NS2B: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
SUBCELLULAR LOCATION: Serine protease subunit NS3: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
SUBCELLULAR LOCATION: Non-structural protein 4A: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
SUBCELLULAR LOCATION: Non-structural protein 4B: 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.
SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus.
DOMAIN: Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals.
PTM: 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.
PTM: RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.
PTM: 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.
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
SIMILARITY: Contains 1 peptidase S7 domain [view classification].
SIMILARITY: Contains 1 RdRp catalytic domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X03700; CAA27332.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15062; CAB37419.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17066; AAC54267.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17067; AAC54268.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052437; AAC35899.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052438; AAC35900.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052439; AAC35901.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052444; AAC35906.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052445; AAC35907.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052446; AAC35908.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ118157; AAZ31436.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ100292; AAZ07885.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A03914; GNWVY.
S07757; GNWVYP.

RefSeq

NP_041726.1; -.

3D structure databases

PDB

1NA4; EM; -; -.	[ExPASy / RCSB / EBI]
1YKS; X-ray; 1.80 A; A=1671-2107.	[ExPASy / RCSB / EBI]
1YMF; X-ray; 2.60 A; A=1671-2107.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1NA4; -.
1YKS; -.
1YMF; -.

ModBase

P03314.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0030529;	Cellular component: ribonucleoprotein complex (inferred from electronic annotation from UniProtKB-KW).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004482;	Molecular function: mRNA (guanine-N7-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0006410;	Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR014001; DEAD-like_N.
IPR011492; DEAD_Flavivir.
IPR001650; DNA/RNA_helicase_C.
IPR002464; DNA/RNA_helicase_DEAH_CS.
IPR013755; Flav_glyE_cen_1.
IPR013756; Flav_glyE_cen_2.
IPR011999; Flav_glyE_cen_dm.
IPR001122; Flavi_capsidC.
IPR000069; Flavi_M.
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; RrmJFtsJ_MeTrfase.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.387.10; Flav_glyE_cen_1; 1.
G3DSA:3.30.67.10; Flav_glyE_cen_2; 1.
G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1.

Pfam

PF01003; Flavi_capsid; 1.
PF07652; Flavi_DEAD; 1.
PF02832; Flavi_glycop_C; 1.
PF00869; Flavi_glycoprot; 1.
PF01004; Flavi_M; 1.
PF00948; Flavi_NS1; 1.
PF01005; Flavi_NS2A; 1.
PF01002; Flavi_NS2B; 1.
PF01350; Flavi_NS4A; 1.
PF01349; Flavi_NS4B; 1.
PF00972; Flavi_NS5; 1.
PF01570; Flavi_propep; 1.
PF01728; FtsJ; 1.
PF00271; Helicase_C; 1.
PF00949; Peptidase_S7; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF003817; Gen_Poly_FLV; 1.

ProDom

PD001496; Flavi_NS1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SMART graphical view of domain structure.

PROSITE

PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; FALSE_NEG.
PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; Capsid protein; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Envelope protein; Glycoprotein; Helicase; Hydrolase; Membrane; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Protease; Ribonucleoprotein; RNA replication; RNA-binding; RNA-directed RNA polymerase; Secreted; Serine protease; Transferase; Transmembrane; Viral nucleoprotein; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed; by host.`
`CHAIN`	`2 101`	`100`	`Protein C.`	`PRO_0000037754`
`PROPEP`	`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`
`TOPO_DOM`	`2 101`	`100`	`Cytoplasmic (Potential).`
`TRANSMEM`	`102 121`	`20`	`Potential.`
`TOPO_DOM`	`122 244`	`123`	`Extracellular (Potential).`
`TRANSMEM`	`245 265`	`21`	`Potential.`
`TOPO_DOM`	`266 269`	`4`	`Cytoplasmic (Potential).`
`TRANSMEM`	`270 287`	`18`	`Potential.`
`TOPO_DOM`	`288 730`	`443`	`Extracellular (Potential).`
`TRANSMEM`	`731 751`	`21`	`Potential.`
`TOPO_DOM`	`752 757`	`6`	`Cytoplasmic (Potential).`
`TRANSMEM`	`758 778`	`21`	`Potential.`
`TOPO_DOM`	`779 1130`	`352`	`Extracellular (Potential).`
`TRANSMEM`	`1131 1151`	`21`	`Potential.`
`TOPO_DOM`	`1152 1160`	`9`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1161 1181`	`21`	`Potential.`
`TOPO_DOM`	`1182 1201`	`20`	`Lumenal (Potential).`
`TRANSMEM`	`1202 1222`	`21`	`Potential.`
`TOPO_DOM`	`1223 1231`	`9`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1232 1252`	`21`	`Potential.`
`TOPO_DOM`	`1253 1262`	`10`	`Lumenal (Potential).`
`TRANSMEM`	`1263 1285`	`23`	`Potential.`
`TOPO_DOM`	`1286 1287`	`2`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1288 1308`	`21`	`Potential.`
`TOPO_DOM`	`1309 1321`	`13`	`Lumenal (Potential).`
`TRANSMEM`	`1322 1342`	`21`	`Potential.`
`TOPO_DOM`	`1343 2186`	`844`	`Cytoplasmic (Potential).`
`TRANSMEM`	`2187 2207`	`21`	`Potential.`
`TOPO_DOM`	`2208 2209`	`2`	`Lumenal (Potential).`
`TRANSMEM`	`2210 2230`	`21`	`Potential.`
`TOPO_DOM`	`2231 2233`	`3`	`Cytoplasmic (Potential).`
`TRANSMEM`	`2234 2256`	`23`	`Potential.`
`TOPO_DOM`	`2257 2359`	`103`	`Lumenal (Potential).`
`TRANSMEM`	`2360 2380`	`21`	`Potential.`
`TOPO_DOM`	`2381 2421`	`41`	`Cytoplasmic (Potential).`
`TRANSMEM`	`2422 2442`	`21`