Protein C
     (Core protein)
     (Capsid protein)
Small envelope protein M
     (Matrix protein)
Envelope protein E
Non-structural protein 1
     (NS1)
Non-structural protein 2A
     (NS2A)
Flavivirin protease NS2B regulatory subunit
Flavivirin protease NS3 catalytic subunit
     (EC 3.4.21.91)
Non-structural protein 4A
     (NS4A)
Non-structural protein 4B
     (NS4B)
RNA-directed RNA polymerase
     (EC 2.7.7.48)
     (NS5)

Gene name

None

From

Kunjin virus (strain MRM61C)

[TaxID: 11078]

Taxonomy

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

Virus hosts

Ciconiiformes [TaxID: 8920]
Culex annulirostris [TaxID: 162997]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. PubMed=2826659 [NCBI, ExPASy, EBI, Israel, Japan] Coia G., Parker M.D., Speight G., Byrne M.E., Westaway E.G.; "Nucleotide and complete amino acid sequences of Kunjin virus: definitive gene order and characteristics of the virus-specified proteins."; J. Gen. Virol. 69:1-21(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. STRAIN=Infectious clone FLSDX, and Infectious clone pAKUN; DOI=10.1128/JVI.77.14.7804-7813.2003; PubMed=12829820 [NCBI, ExPASy, EBI, Israel, Japan] Liu W.J., Chen H.B., Khromykh A.A.; "Molecular and functional analyses of Kunjin virus infectious cDNA clones demonstrate the essential role for NS2A in virus assembly and for a nonconservative residue in NS3 in RNA replication."; J. Virol. 77:7804-7813(2003).
[3]	FUNCTION OF NON-STRUCTURAL PROTEIN 2A, AND NON-STRUCTURAL PROTEIN 4A. DOI=10.1006/viro.1998.9156; PubMed=9636360 [NCBI, ExPASy, EBI, Israel, Japan] Mackenzie J.M., Khromykh A.A., Jones M.K., Westaway E.G.; "Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A."; Virology 245:203-215(1998).
[4]	X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-98. DOI=10.1016/j.str.2004.04.024; PubMed=15242592 [NCBI, ExPASy, EBI, Israel, Japan] Dokland T., Walsh M., Mackenzie J.M., Khromykh A.A., Ee K.H., Wang S.; "West Nile virus core protein; tetramer structure and ribbon formation."; Structure 12:1157-1163(2004).

Comments

FUNCTION: The small proteins NS2A, NS4A and NS4B are hydrophobic, suggesting a possible membrane-related function. NS5 may play a role in the viral RNA replication. The NS2B/NS3 protease complex processes the viral polyprotein.
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).
SUBUNIT: NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter (By similarity).
SUBCELLULAR LOCATION: Protein C: Virion (Potential). Membrane; Single-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Small envelope protein M: Virion (Potential). Membrane; Single-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Envelope protein E: Virion (Potential). Membrane; Multi-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Non-structural protein 4A: Membrane; Single-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Non-structural protein 4B: Membrane; Multi-pass membrane protein (Potential).
PTM: Specific enzymatic cleavages in vivo yield mature proteins (By similarity).
MISCELLANEOUS: The virion of this virus is a nucleocapsid covered by a lipoprotein envelope. The envelope contains two proteins: the protein M and glycoprotein E. The nucleocapsid is a complex of protein C and mRNA. 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 (By similarity).
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

D00246; BAA00176.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY274504; AAP78941.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY274505; AAP78942.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A28697; GNWVKV.

3D structure databases

PDB

1SFK; X-ray; 3.20 A; A/B/C/D/E/F/G/H=23-98.	[ExPASy / RCSB / EBI]
2HCN; X-ray; 2.35 A; A=2846-3433.	[ExPASy / RCSB / EBI]
2HCS; X-ray; 2.50 A; A=2846-3433.	[ExPASy / RCSB / EBI]
2HFZ; X-ray; 3.00 A; A=2802-3433.	[ExPASy / RCSB / EBI]
2OF6; EM; 24.00 A; A/B/C=291-690.	[ExPASy / RCSB / EBI]
2OY0; X-ray; 2.80 A; A/B=2534-2795.	[ExPASy / RCSB / EBI]
2QEQ; X-ray; 3.10 A; A/B=1691-2124.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1SFK; -.
2HCN; -.
2HCS; -.
2HFZ; -.
2OF6; -.
2OY0; -.
2QEQ; -.

SMR

P14335; 291-690, 1515-1683.

ModBase

P14335.

Protein family/group databases

MEROPS

S07.001; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0019031;	Cellular component: viral envelope (inferred from electronic annotation from InterPro).
GO:0019013;	Cellular component: viral nucleocapsid (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008026;	Molecular function: ATP-dependent helicase activity (inferred from electronic annotation from InterPro).
GO:0003725;	Molecular function: double-stranded RNA binding (inferred from electronic annotation from InterPro).
GO:0003724;	Molecular function: RNA helicase activity (inferred from electronic annotation from InterPro).
GO:0003968;	Molecular function: RNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0005198;	Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0016070;	Biological process: RNA metabolic process (inferred from electronic annotation from InterPro).
GO:0006410;	Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0019079;	Biological process: viral genome replication (inferred from electronic annotation from InterPro).
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.
IPR013756; Flav_glyE_cen_2.
IPR011999; Flav_glyE_cen_dm.
IPR013754; Flav_glyE_dim.
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:3.30.67.10; Flav_glyE_cen_2; 1.
G3DSA:2.60.98.10; Flav_glyE_dim; 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

PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; 1.
PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P14335.

Other

UniRef

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; Core protein; Envelope protein; Glycoprotein; Helicase; Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase; Transferase; Transmembrane; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed; by host.`
`CHAIN`	`2 123`	`122`	`Protein C.`	`PRO_0000037703`
`PROPEP`	`124 215`	`92`		`PRO_0000037704`
`CHAIN`	`216 290`	`75`	`Small envelope protein M.`	`PRO_0000037705`
`CHAIN`	`291 791`	`501`	`Envelope protein E.`	`PRO_0000037706`
`CHAIN`	`792 1143`	`352`	`Non-structural protein 1.`	`PRO_0000037707`
`CHAIN`	`1144 1374`	`231`	`Non-structural protein 2A.`	`PRO_0000037708`
`CHAIN`	`1375 1505`	`131`	`Flavivirin protease NS2B regulatory subunit.`	`PRO_0000037709`
`CHAIN`	`1506 2124`	`619`	`Flavivirin protease NS3 catalytic subunit.`	`PRO_0000037710`
`CHAIN`	`2125 2273`	`149`	`Non-structural protein 4A.`	`PRO_0000037711`
`CHAIN`	`2274 2528`	`255`	`Non-structural protein 4B.`	`PRO_0000037712`
`CHAIN`	`2529 3433`	`905`	`RNA-directed RNA polymerase.`	`PRO_0000037713`
`TRANSMEM`	`109 129`	`21`	`Potential.`
`TRANSMEM`	`249 269`	`21`	`Potential.`
`TRANSMEM`	`276 292`	`17`	`Potential.`
`TRANSMEM`	`744 764`	`21`	`Potential.`
`TRANSMEM`	`771 791`	`21`	`Potential.`
`TRANSMEM`	`1175 1195`	`21`	`Potential.`
`TRANSMEM`	`1217 1237`	`21`	`Potential.`
`TRANSMEM`	`1246 1268`	`23`	`Potential.`
`TRANSMEM`	`1289 1309`	`21`	`Potential.`
`TRANSMEM`	`1314 1331`	`18`	`Potential.`
`TRANSMEM`	`1346 1366`	`21`	`Potential.`
`TRANSMEM`	`1376 1396`	`21`	`Potential.`
`TRANSMEM`	`1400 1420`	`21`	`Potential.`
`TRANSMEM`	`1478 1498`	`21`	`Potential.`
`TRANSMEM`	`2175 2195`	`21`	`Potential.`
`TRANSMEM`	`2201 2221`	`21`	`Potential.`
`TRANSMEM`	`2223 2243`	`21`	`Potential.`
`TRANSMEM`	`2259 2279`	`21`	`Potential.`
`TRANSMEM`	`2313 2333`	`21`	`Potential.`
`TRANSMEM`	`2359 2379`	`21`	`Potential.`
`TRANSMEM`	`2381 2401`	`21`	`Potential.`
`TRANSMEM`	`2445 2465`	`21`	`Potential.`
`DOMAIN`	`1512 1683`	`172`	`Peptidase S7.`
`DOMAIN`	`1686 1842`	`157`	`Helicase ATP-binding.`
`DOMAIN`	`1853 2018`	`166`	`Helicase C-terminal.`
`DOMAIN`	`3058 3210`	`153`	`RdRp catalytic.`
`NP_BIND`	`1699 1706`	`8`	`ATP (Potential).`
`REGION`	`388 401`	`14`	`Involved in fusion.`
`MOTIF`	`1790 1793`	`4`	`DEAH box.`
`ACT_SITE`	`1556 1556`		`Charge relay system (By similarity).`
`ACT_SITE`	`1580 1580`		`Charge relay system (By similarity).`
`ACT_SITE`	`1640 1640`		`Charge relay system (By similarity).`
`CARBOHYD`	`138 138`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`921 921`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`966 966`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`998 998`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`293 320`		`By similarity.`
`DISULFID`	`350 406`		`By similarity.`
`DISULFID`	`364 395`		`By similarity.`
`DISULFID`	`382 411`		`By similarity.`
`DISULFID`	`480 578`		`By similarity.`
`DISULFID`	`595 626`		`By similarity.`
`VARIANT`	`150 150`	`1`	`P -> T (in strain: Infectious clone pAKUN and Infectious clone FLSDX).`
`VARIANT`	`820 820`	`1`	`I -> M (in strain: Infectious clone pAKUNa and Infectious clone FLSDX).`
`VARIANT`	`943 943`	`1`	`N -> S (in strain: Infectious clone pAKUN and Infectious clone FLSDX).`
`VARIANT`	`1041 1041`	`1`	`P -> L (in strain: Infectious clone pAKUN and Infectious clone FLSDX).`
`VARIANT`	`1202 1202`	`1`	`I -> N (in strain: Infectious clone pAKUN).`
`VARIANT`	`1318 1318`	`1`	`R -> K (in strain: Infectious clone pAKUN).`
`VARIANT`	`1967 1967`	`1`	`T -> I (in strain: Infectious clone pAKUN and Infectious clone FLSDX).`
`VARIANT`	`1974 1974`	`1`	`A -> V (in strain: Infectious clone pAKUN and Infectious clone FLSDX).`
`VARIANT`	`2023 2023`	`1`	`Y -> H (in strain: Infectious clone pAKUN).`
`VARIANT`	`2062 2062`	`1`	`S -> P (in strain: Infectious clone pAKUN).`
`VARIANT`	`2339 2339`	`1`	`T -> N (in strain: Infectious clone pAKUN and Infectious clone FLSDX).`
`HELIX`	`26 38`	`13`
`HELIX`	`44 56`	`13`
`HELIX`	`63 69`	`7`
`HELIX`	`74 95`	`22`
`STRAND`	`1694 1697`	`4`
`TURN`	`1703 1708`	`6`
`HELIX`	`1709 1719`	`11`
`STRAND`	`1724 1730`	`7`
`HELIX`	`1731 1740`	`10`
`STRAND`	`1763 1767`	`5`
`HELIX`	`1768 1776`	`9`
`STRAND`	`1777 1779`	`3`
`STRAND`	`1785 1791`	`7`
`HELIX`	`1797 1811`	`15`
`STRAND`	`1816 1820`	`5`
`STRAND`	`1839 1842`	`4`
`STRAND`	`1851 1853`	`3`
`HELIX`	`1855 1859`	`5`
`STRAND`	`1864 1867`	`4`
`HELIX`	`1871 1883`	`13`
`STRAND`	`1888 1891`	`4`
`STRAND`	`1909 1914`	`6`
`STRAND`	`1926 1930`	`5`
`STRAND`	`1937 1944`	`8`
`STRAND`	`1946 1949`	`4`
`HELIX`	`1957 1964`	`8`
`STRAND`	`1977 1980`	`4`
`HELIX`	`1992 2002`	`11`
`HELIX`	`2007 2009`	`3`
`HELIX`	`2016 2021`	`6`
`TURN`	`2026 2029`	`4`
`HELIX`	`2034 2044`	`11`
`HELIX`	`2050 2058`	`9`
`HELIX`	`2066 2069`	`4`
`HELIX`	`2074 2076`	`3`
`STRAND`	`2079 2084`	`6`
`STRAND`	`2086 2088`	`3`
`STRAND`	`2094 2096`	`3`
`STRAND`	`2100 2103`	`4`