Q2YHF0 · POLG_DEN4T

Function

function

Capsid protein C

Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.

Capsid protein C

Inhibits RNA silencing by interfering with host Dicer.

Peptide pr

Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.

Protein prM

Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.

Small envelope protein M

May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.

Envelope protein E

Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.

Non-structural protein 1

Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).

Non-structural protein 1

Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.

Non-structural protein 2A

Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.

Serine protease subunit NS2B

Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (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.

Non-structural protein 4A

Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between RIGI and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity).

Peptide 2k

Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.

Non-structural protein 4B

Induces the formation of ER-derived membrane vesicles where the viral replication takes place. 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.

RNA-directed RNA polymerase NS5

Replicates the viral + and - RNA 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 RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).
May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity).

Catalytic activity

Features

Showing features for site, active site, binding site.

TypeIDPosition(s)Description
Site99-100Cleavage; by viral protease NS3
Site113-114Cleavage; by host signal peptidase
Site204-205Cleavage; by host furin
Site279-280Cleavage; by host signal peptidase
Site774-775Cleavage; by host signal peptidase
Site1126-1127Cleavage; by host
Site1344-1345Cleavage; by viral protease NS3
Site1474-1475Cleavage; by autolysis
Active site1525Charge relay system; for serine protease NS3 activity
Active site1549Charge relay system; for serine protease NS3 activity
Active site1609Charge relay system; for serine protease NS3 activity
Binding site1667-1674ATP (UniProtKB | ChEBI)
Site1931Involved in NS3 ATPase and RTPase activities
Site1934Involved in NS3 ATPase and RTPase activities
Site2092-2093Cleavage; by autolysis
Site2219-2220Cleavage; by viral protease NS3
Site2242-2243Cleavage; by host signal peptidase
Site2487-2488Cleavage; by viral protease NS3
Site2501mRNA cap binding
Site2504mRNA cap binding; via carbonyl oxygen
Site2505mRNA cap binding
Site2507mRNA cap binding; via carbonyl oxygen
Site2512mRNA cap binding
Site2516mRNA cap binding
Binding site2543S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2548For 2'-O-MTase activity
Site2548Essential for 2'-O-methyltransferase activity
Binding site2573S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2574S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2591S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2592S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2618S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2619S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2633For 2'-O-MTase activity
Site2633Essential for 2'-O-methyltransferase and N-7 methyltransferase activity
Binding site2634S-adenosyl-L-methionine (UniProtKB | ChEBI)
Site2637mRNA cap binding
Active site2668For 2'-O-MTase activity
Site2668Essential for 2'-O-methyltransferase activity
Site2699mRNA cap binding
Site2701mRNA cap binding
Active site2704For 2'-O-MTase activity
Site2704Essential for 2'-O-methyltransferase activity
Binding site2706S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2925Zn2+ 1 (UniProtKB | ChEBI)
Binding site2929Zn2+ 1 (UniProtKB | ChEBI)
Binding site2934Zn2+ 1 (UniProtKB | ChEBI)
Binding site2937Zn2+ 1 (UniProtKB | ChEBI)
Binding site3200Zn2+ 2 (UniProtKB | ChEBI)
Binding site3216Zn2+ 2 (UniProtKB | ChEBI)
Binding site3335Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell mitochondrion
Cellular Componenthost cell nucleus
Cellular Componenthost cell perinuclear region of cytoplasm
Cellular Componentmembrane
Cellular Componentviral capsid
Cellular Componentviral envelope
Cellular Componentvirion membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionchannel activity
Molecular Functiondouble-stranded RNA binding
Molecular Functionmetal ion binding
Molecular FunctionmRNA (nucleoside-2'-O-)-methyltransferase activity
Molecular FunctionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
Molecular Functionprotein dimerization activity
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionserine-type endopeptidase activity
Molecular Functionstructural molecule activity
Biological Processclathrin-dependent endocytosis of virus by host cell
Biological Processfusion of virus membrane with host endosome membrane
Biological Processinduction by virus of host autophagy
Biological Processmonoatomic ion transmembrane transport
Biological Processproteolysis
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity
Biological Processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
Biological Processviral RNA genome replication
Biological Processvirion attachment to host cell
Biological Processvirus-mediated perturbation of host defense response

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Organism names

Accessions

  • Primary accession
    Q2YHF0

Proteomes

Subcellular Location

Capsid protein C

Virion
Host nucleus
Host cytoplasm

Peptide pr

Secreted

Small envelope protein M

Virion membrane
; Multi-pass membrane protein
Host endoplasmic reticulum membrane
; Multi-pass membrane protein

Envelope protein E

Virion membrane
; Multi-pass membrane protein
Host endoplasmic reticulum membrane
; Multi-pass membrane protein

Non-structural protein 1

Secreted
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Note: Located in RE-derived vesicles hosting the replication complex.

Non-structural protein 2A

Host endoplasmic reticulum membrane
; Multi-pass membrane protein

Serine protease subunit NS2B

Host endoplasmic reticulum membrane ; Multi-pass membrane protein

Serine protease NS3

Host endoplasmic reticulum membrane
; Peripheral membrane protein
Note: Remains non-covalently associated to serine protease subunit NS2B.

Non-structural protein 4A

Host endoplasmic reticulum membrane
; Multi-pass membrane protein
Host mitochondrion
Note: Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes.

Non-structural protein 4B

Host endoplasmic reticulum membrane
; Multi-pass membrane protein
Note: Located in RE-derived vesicles hosting the replication complex.

RNA-directed RNA polymerase NS5

Host endoplasmic reticulum membrane ; Peripheral membrane protein
Host nucleus
Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes.

Features

Showing features for topological domain, transmembrane, intramembrane.

TypeIDPosition(s)Description
Topological domain1-100Cytoplasmic
Transmembrane101-117Helical
Topological domain118-237Extracellular
Transmembrane238-258Helical
Topological domain259-265Cytoplasmic
Transmembrane266-279Helical
Topological domain280-725Extracellular
Transmembrane726-746Helical
Topological domain747-753Cytoplasmic
Transmembrane754-774Helical
Topological domain775-1194Extracellular
Transmembrane1195-1218Helical
Topological domain1219-1224Lumenal
Transmembrane1225-1243Helical
Topological domain1244-1267Cytoplasmic
Transmembrane1268-1288Helical
Topological domain1289Lumenal
Transmembrane1290-1308Helical
Topological domain1309-1316Lumenal
Transmembrane1317-1337Helical
Topological domain1338-1345Cytoplasmic
Transmembrane1346-1366Helical
Topological domain1367-1369Lumenal
Transmembrane1370-1390Helical
Topological domain1391-1437Cytoplasmic
Intramembrane1438-1458Helical
Topological domain1459-2143Cytoplasmic
Transmembrane2144-2164Helical
Topological domain2165-2169Lumenal
Intramembrane2170-2190Helical
Topological domain2191Lumenal
Transmembrane2192-2212Helical
Topological domain2213-2225Cytoplasmic
Transmembrane2226-2246Helical; Note=Signal for NS4B
Topological domain2247-2270Lumenal
Intramembrane2271-2291Helical
Topological domain2292-2301Lumenal
Intramembrane2302-2322Helical
Topological domain2323-2343Lumenal
Transmembrane2344-2364Helical
Topological domain2365-2409Cytoplasmic
Transmembrane2410-2430Helical
Topological domain2431-2455Lumenal
Transmembrane2456-2476Helical
Topological domain2477-3387Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, propeptide, glycosylation, disulfide bond, modified residue, peptide.

TypeIDPosition(s)Description
ChainPRO_00002681311-99Capsid protein C
ChainPRO_00004052291-3387Genome polyprotein
PropeptidePRO_0000268132100-113ER anchor for the capsid protein C, removed in mature form by serine protease NS3
ChainPRO_0000268134114-204Peptide pr
ChainPRO_0000268133114-279Protein prM
Glycosylation182N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000268135205-279Small envelope protein M
ChainPRO_0000268136280-774Envelope protein E
Disulfide bond282↔309
Disulfide bond339↔400
Glycosylation346N-linked (GlcNAc...) asparagine; by host
Disulfide bond353↔384
Disulfide bond371↔395
Glycosylation432N-linked (GlcNAc...) asparagine; by host
Disulfide bond464↔564
Disulfide bond581↔612
ChainPRO_0000268137775-1126Non-structural protein 1
Disulfide bond778↔789
Disulfide bond829↔917
Glycosylation904N-linked (GlcNAc...) asparagine; by host
Disulfide bond953↔997
Glycosylation981N-linked (GlcNAc...) asparagine; by host
Disulfide bond1054↔1103
Disulfide bond1065↔1087
Disulfide bond1086↔1090
ChainPRO_00002681381127-1344Non-structural protein 2A
ChainPRO_00002681391345-1474Serine protease subunit NS2B
ChainPRO_00002681401475-2092Serine protease NS3
Modified residue1862N6-acetyllysine; by host
ChainPRO_00002681412093-2219Non-structural protein 4A
PeptidePRO_00002681422220-2242Peptide 2k
ChainPRO_00002681432243-2487Non-structural protein 4B
Glycosylation2297N-linked (GlcNAc...) asparagine; by host
Glycosylation2301N-linked (GlcNAc...) asparagine; by host
Glycosylation2453N-linked (GlcNAc...) asparagine; by host
ChainPRO_00002681442488-3387RNA-directed RNA polymerase NS5
Modified residue2543Phosphoserine

Post-translational modification

Genome polyprotein

Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.

Protein prM

Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.

Envelope protein E

N-glycosylated.

Non-structural protein 1

N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.

Serine protease NS3

Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication.

RNA-directed RNA polymerase NS5

Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication.

RNA-directed RNA polymerase NS5

Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.

Keywords

Interaction

Subunit

Capsid protein C

Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway.

Protein prM

Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi.

Envelope protein E

Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1.

Non-structural protein 1

Homodimer; Homohexamer when secreted. Interacts with envelope protein E.

Non-structural protein 2A

Interacts (via N-terminus) with serine protease NS3.

Serine protease subunit NS2B

Forms a heterodimer with serine protease NS3. May form homooligomers.

Serine protease NS3

Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Interacts with host SHFL.

Non-structural protein 4A

Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta. Interacts with host SHFL. Interacts with host AUP1; the interaction occurs in the presence of Dengue virus NS4B and induces lipophagy which facilitates production of virus progeny particles (By similarity).

Non-structural protein 4B

Interacts with serine protease NS3.

RNA-directed RNA polymerase NS5

Homodimer. Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with serine protease NS3 (By similarity).
Interacts with host PAF1 complex; the interaction may prevent the recruitment of the PAF1 complex to interferon-responsive genes, and thus reduces the immune response (By similarity).

Family & Domains

Features

Showing features for region, domain, motif.

TypeIDPosition(s)Description
Region36-71Hydrophobic; homodimerization of capsid protein C
Region377-390Fusion peptide
Region1397-1436Interacts with and activates NS3 protease
Domain1475-1652Peptidase S7
Domain1654-1810Helicase ATP-binding
Region1658-1661Important for RNA-binding
Motif1758-1761DEAH box
Domain1820-1987Helicase C-terminal
Domain2489-2751mRNA cap 0-1 NS5-type MT
Motif2564-2567SUMO-interacting motif
Domain3016-3166RdRp catalytic

Domain

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.

Sequence similarities

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    3,387
  • Mass (Da)
    378,438
  • Last updated
    2005-12-20 v1
  • Checksum
    1FEDC2D663A0F945
MNQRKKVARPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKILTGFRKEIGRMLNILNGRKRSTITLLCLIPTVMAFHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCEDTVTYKCPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWILRNPGFALLAGFMAYMIGQTGIQRTVFFILMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTLDFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDMVDRGWGNGCGLFGKGGVVTCAKFSCSGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKMKTKTWLVHKQWFLDLPLPWTAGADTLEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAGHLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGTGAPCKVPIEIRDVNKEKVVGRIISSTPFAENTNSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLLTSLGKAVHQVFGSVYTTMFGGVSWMVRILIGLLVLWIGTNSRNTSMAMSCIAVGGITLFLGFTVHADMGCAVSWSGKELKCGSGIFVIDNVHTWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAPPVNDLKYSWKTWGKAKIFTPETRNSTFLVDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSAAIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPISQHNYRQGYATQTVGPWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLNEKEENMVKSQVSAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVTTLCAIILGGLTWMDLLRALIMLGDTMSGRMGGQIHLAIMAVFKMSPGYVLGIFLRKLTSRETALMVIGMAMTTVLSIPHDLMEFIDGISLGLILLKMVTHFDNTQVGTLALSLTFIKSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASKRSWPLNEGIMAVGLVSLLGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMITLLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVFHTMWHVTRGSVICHESGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAVTLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPSIVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEAHFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIKAGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGPIPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLRNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLRGEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMALKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGKAYQHALNELPESLETLMLVALLGAMTAGIFLFFMQGKGIGKLSMGLIAIAVASGLLWVAEIQPQWIAASIILEFFLMVLLVPEPEKQRTPQDNQLIYVILTILTIIALVAANEMGLIEKTKTDFGFYQAKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKGWPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYDPKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIKNAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKYAVSRGTSKIRWIVERGMVKPKGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSNPTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVNTTSKMLLNRFTTRHRKPTYEKDADLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDHENPYRTWAYHGSYEAPSTGSASSMVNGVVKLLTKPWDVVPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRVVMTTTANWLWALLGRKKNPRLCTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLIYADDTAGWDTRITEDDLLNEELITEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITRDDMHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHHFHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSRTTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMIDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIQTAITQVRNLIGKEEYVDYMPVMKRYSAHFESEGVL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY618990
EMBL· GenBank· DDBJ
AAU89377.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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