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

Murray valley encephalitis virus (strain MVE-1-51) (MVEV)

[TaxID: 301478]

Taxonomy

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

Virus hosts

Culex annulirostris [TaxID: 162997]
Homo sapiens (Human) [TaxID: 9606]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE. PubMed=10567642 [NCBI, ExPASy, EBI, Israel, Japan] Hurrelbrink R.J., Nestorowicz A., McMinn P.C.; "Characterization of infectious Murray Valley encephalitis virus derived from a stably cloned genomic-length cDNA."; J. Gen. Virol. 80:3115-3125(1999).
[2]	NUCLEOTIDE SEQUENCE OF 1-1780. DOI=10.1016/0022-2836(86)90435-3; PubMed=3009829 [NCBI, ExPASy, EBI, Israel, Japan] Dalgarno L., Trent D.W., Strauss J.H., Rice C.M.; "Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins."; J. Mol. Biol. 187:309-323(1986).
[3]	NUCLEOTIDE SEQUENCE OF 1773-3434, AND PROTEIN SEQUENCE OF 794-807; 1504-1519 AND 2530-2537. DOI=10.1007/BF00265630; PubMed=1702914 [NCBI, ExPASy, EBI, Israel, Japan] Lee E., Fernon C., Simpson R., Weir R.C., Rice C.M., Dalgarno L.; "Sequence of the 3' half of the Murray Valley encephalitis virus genome and mapping of the nonstructural proteins NS1, NS3, and NS5."; Virus Genes 4:197-213(1990).
[4]	GLYCOSYLATION OF NS1, AND DISULFIDE BONDS. PubMed=11514736 [NCBI, ExPASy, EBI, Israel, Japan] Blitvich B.J., Scanlon D., Shiell B.J., Mackenzie J.S., Pham K., Hall R.A.; "Determination of the intramolecular disulfide bond arrangement and biochemical identification of the glycosylation sites of the nonstructural protein NS1 of Murray Valley encephalitis virus."; J. Gen. Virol. 82:2251-2256(2001).

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

AF161266; AAF05296.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03467; CAA27184.1; -; Unassigned_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24635; GNWVMV.

RefSeq

NP_051124.1; -.

3D structure databases

PDB

2PX2; X-ray; 2.00 A; A/B=2530-2798.	[ExPASy / RCSB / EBI]
2PX4; X-ray; 2.20 A; A=2530-2798.	[ExPASy / RCSB / EBI]
2PX5; X-ray; 2.30 A; A/B=2530-2798.	[ExPASy / RCSB / EBI]
2PX8; X-ray; 2.20 A; A/B=2530-2798.	[ExPASy / RCSB / EBI]
2PXA; X-ray; 2.30 A; A/B=2530-2798.	[ExPASy / RCSB / EBI]
2PXC; X-ray; 2.80 A; A=2530-2798.	[ExPASy / RCSB / EBI]
2V8O; X-ray; 1.90 A; A=1681-2122.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2PX2; -.
2PX4; -.
2PX5; -.
2PX8; -.
2PXA; -.
2PXC; -.
2V8O; -.

SMR

P05769; 27-97, 293-691, 1513-1679.

ModBase

P05769.

Protein family/group databases

MEROPS

S07.001; -.

Ontologies

GO:0019013;	Cellular component: viral nucleocapsid (inferred from electronic annotation from UniProtKB-KW).
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.
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).

Genome annotation databases

GeneID

1489715; -.

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; Direct protein sequencing; 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`	`2 121`	`120`	`Protein C.`	`PRO_0000037782`
`PROPEP`	`122 217`	`96`		`PRO_0000037783`
`CHAIN`	`218 292`	`75`	`Small envelope protein M.`	`PRO_0000037784`
`CHAIN`	`293 793`	`501`	`Envelope protein E.`	`PRO_0000037785`
`CHAIN`	`794 1207`	`414`	`Non-structural protein 1.`	`PRO_0000037786`
`CHAIN`	`1208 1372`	`165`	`Non-structural protein 2A.`	`PRO_0000037787`
`CHAIN`	`1373 1503`	`131`	`Flavivirin protease NS2B regulatory subunit.`	`PRO_0000037788`
`CHAIN`	`1504 2122`	`619`	`Flavivirin protease NS3 catalytic subunit.`	`PRO_0000037789`
`CHAIN`	`2123 2414`	`292`	`Non-structural protein 4A (By similarity).`	`PRO_0000037790`
`CHAIN`	`2415 2529`	`115`	`Non-structural protein 4B (By similarity).`	`PRO_0000037791`
`CHAIN`	`2530 3434`	`905`	`RNA-directed RNA polymerase.`	`PRO_0000037792`
`TRANSMEM`	`44 60`	`17`	`Potential.`
`TRANSMEM`	`112 128`	`17`	`Potential.`
`TRANSMEM`	`278 294`	`17`	`Potential.`
`TRANSMEM`	`773 789`	`17`	`Potential.`
`TRANSMEM`	`1178 1194`	`17`	`Potential.`
`TRANSMEM`	`1219 1235`	`17`	`Potential.`
`TRANSMEM`	`1250 1266`	`17`	`Potential.`
`TRANSMEM`	`1312 1328`	`17`	`Potential.`
`TRANSMEM`	`1378 1394`	`17`	`Potential.`
`TRANSMEM`	`1401 1417`	`17`	`Potential.`
`TRANSMEM`	`1476 1492`	`17`	`Potential.`
`DOMAIN`	`1510 1681`	`172`	`Peptidase S7.`
`DOMAIN`	`1684 1840`	`157`	`Helicase ATP-binding.`
`DOMAIN`	`1851 2016`	`166`	`Helicase C-terminal.`
`DOMAIN`	`3059 3211`	`153`	`RdRp catalytic.`
`NP_BIND`	`1697 1704`	`8`	`ATP (Potential).`
`MOTIF`	`1788 1791`	`4`	`DEAH box.`
`ACT_SITE`	`1554 1554`		`Charge relay system (By similarity).`
`ACT_SITE`	`1578 1578`		`Charge relay system (By similarity).`
`ACT_SITE`	`1638 1638`		`Charge relay system (By similarity).`
`CARBOHYD`	`73 73`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`140 140`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`446 446`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`923 923`		`N-linked (GlcNAc...).`
`CARBOHYD`	`968 968`		`N-linked (GlcNAc...).`
`CARBOHYD`	`1000 1000`		`N-linked (GlcNAc...) (high mannose).`
`CARBOHYD`	`2487 2487`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`2493 2493`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`2763 2763`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`295 322`		`By similarity.`
`DISULFID`	`352 408`		`By similarity.`
`DISULFID`	`366 397`		`By similarity.`
`DISULFID`	`384 413`		`By similarity.`
`DISULFID`	`482 580`		`By similarity.`
`DISULFID`	`597 628`		`By similarity.`
`DISULFID`	`797 808`
`DISULFID`	`848 936`
`DISULFID`	`972 1016`
`CONFLICT`	`115 115`		`L -> V (in Ref. 2; CAA27184).`
`CONFLICT`	`754 754`		`P -> Q (in Ref. 2; CAA27184).`
`CONFLICT`	`960 960`		`G -> V (in Ref. 2; CAA27184).`
`CONFLICT`	`1485 1485`		`R -> W (in Ref. 2; CAA27184).`
`CONFLICT`	`1779 1779`		`V -> G (in Ref. 2).`
`HELIX`	`1684 1687`	`4`
`STRAND`	`1692 1695`	`4`
`STRAND`	`1699 1701`	`3`
`TURN`	`1703 1706`	`4`
`HELIX`	`1707 1717`	`11`
`STRAND`	`1722 1728`	`7`
`HELIX`	`1729 1738`	`10`
`TURN`	`1739 1741`	`3`
`STRAND`	`1744 1746`	`3`
`STRAND`	`1761 1765`	`5`
`HELIX`	`1766 1773`	`8`
`STRAND`	`1775 1777`	`3`
`STRAND`	`1783 1789`	`7`
`HELIX`	`1795 1809`	`15`
`STRAND`	`1814 1818`	`5`
`STRAND`	`1836 1840`	`5`
`STRAND`	`1849 1851`	`3`
`HELIX`	`1853 1857`	`5`
`STRAND`	`1862 1865`	`4`
`HELIX`	`1869 1881`	`13`
`STRAND`	`1886 1889`	`4`
`TURN`	`1891 1893`	`3`
`HELIX`	`1894 1901`	`8`
`STRAND`	`1907 1911`	`5`
`HELIX`	`1913 1916`	`4`
`STRAND`	`1924 1928`	`5`
`STRAND`	`1935 1938`	`4`
`STRAND`	`1944 1947`	`4`
`HELIX`	`1955 1962`	`8`
`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`
`STRAND`	`2078 2081`	`4`
`STRAND`	`2098 2101`	`4`
`HELIX`	`2102 2104`	`3`
`HELIX`	`2108 2118`	`11`
`HELIX`	`2537 2546`	`10`
`HELIX`	`2550 2557`	`8`
`TURN`	`2558 2560`	`3`
`STRAND`	`2562 2564`	`3`
`HELIX`	`2566 2568`	`3`
`HELIX`	`2587 2596`	`10`
`STRAND`	`2604 2609`	`6`
`HELIX`	`2615 2620`	`6`
`STRAND`	`2626 2632`	`7`
`HELIX`	`2650 2652`	`3`
`STRAND`	`2653 2656`	`4`
`HELIX`	`2661 2663`	`3`
`STRAND`	`2670 2674`	`5`
`HELIX`	`2`