Q9Q6P4 · POLG_WNV9

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 (PubMed:22925334).
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 2A

Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral 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/Helicase 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 (By similarity).
NS3 supports the separation of RNA daughter and template strands during viral replication. The helicase part is involved in the inhibition of phosphorylation of host STAT1, and thereby inhibition of host type-I IFN signaling (PubMed:29099073).
In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non-translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity).

Non-structural protein 4A

Facilitates host membrane remodelling necessary for viral replication by interacting with host RTN3. Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.

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 (PubMed:24465392).
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 (PubMed:15956546).
Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15956546).

RNA-directed RNA polymerase NS5

Replicates the viral + and - genome, and performs the capping of genomes in the cytoplasm (PubMed:19850911).
NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:19850911, PubMed:20685660).
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 (PubMed:20106931).
Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:15650160).

Catalytic activity

Features

Showing features for site, active site, binding site.

Type
IDPosition(s)Description
Site105-106Cleavage; by viral protease NS3
Site123-124Cleavage; by host signal peptidase
Site215-216Cleavage; by host furin
Site290-291Cleavage; by host signal peptidase
Site791-792Cleavage; by host signal peptidase
Site1143-1144Cleavage; by host
Site1374-1375Cleavage; by viral protease NS3
Site1505-1506Cleavage; by autolysis
Active site1556Charge relay system; for serine protease NS3 activity
Active site1580Charge relay system; for serine protease NS3 activity
Active site1640Charge relay system; for serine protease NS3 activity
Binding site1699-1706ATP (UniProtKB | ChEBI)
Site1754Inhibition of host STAT1 phosphorylation
Site1963Involved in NS3 ATPase and RTPase activities
Site1966Involved in NS3 ATPase and RTPase activities
Site1991Inhibition of host STAT1 phosphorylation
Site2124-2125Cleavage; by autolysis
Site2250-2251Cleavage; by viral protease NS3
Site2273-2274Cleavage; by host signal peptidase
Site2528-2529Cleavage; by viral protease NS3
Site2541mRNA cap binding
Site2544mRNA cap binding; via carbonyl oxygen
Site2545mRNA cap binding
Site2547mRNA cap binding; via carbonyl oxygen
Site2552mRNA cap binding
Site2556mRNA cap binding
Binding site2584S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2589For 2'-O-MTase activity
Site2589Essential for 2'-O-methyltransferase activity
Binding site2614S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2615S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2632S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2633S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2639S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2659S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2660S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2674For 2'-O-MTase activity
Binding site2674S-adenosyl-L-methionine (UniProtKB | ChEBI)
Site2674Essential for 2'-O-methyltransferase and N-7 methyltransferase activity
Binding site2675S-adenosyl-L-methionine (UniProtKB | ChEBI)
Site2678mRNA cap binding
Active site2710For 2'-O-MTase activity
Site2710Essential for 2'-O-methyltransferase activity
Site2741mRNA cap binding
Site2743mRNA cap binding
Active site2746For 2'-O-MTase activity
Site2746Essential for 2'-O-methyltransferase activity
Binding site2748S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2968Zn2+ 1 (UniProtKB | ChEBI)
Binding site2972Zn2+ 1 (UniProtKB | ChEBI)
Binding site2977Zn2+ 1 (UniProtKB | ChEBI)
Binding site2980Zn2+ 1 (UniProtKB | ChEBI)
Binding site3245Zn2+ 2 (UniProtKB | ChEBI)
Binding site3261Zn2+ 2 (UniProtKB | ChEBI)
Binding site3380Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell nucleus
Cellular Componenthost cell perinuclear region of cytoplasm
Cellular Componentmembrane
Cellular Componentviral capsid
Cellular Componentvirion membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent H2AZ histone chaperone activity
Molecular FunctionATP-dependent H3-H4 histone complex chaperone activity
Molecular Functionchromatin extrusion motor activity
Molecular Functioncohesin loader activity
Molecular FunctionDNA clamp loader 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 Processfusion of virus membrane with host endosome membrane
Biological Processinduction by virus of host autophagy
Biological Processproteolysis
Biological Processsymbiont entry into host cell
Biological Processsymbiont-mediated suppression of host innate immune response
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 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

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      GP1
    • ORF names
      MZ11_60484gpGP1
      , MZ11_60553gpGP1

Organism names

Accessions

  • Primary accession
    Q9Q6P4

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
Note: ER membrane retention is mediated by the transmembrane domains.

Envelope protein E

Virion membrane
; Multi-pass membrane protein
Host endoplasmic reticulum membrane
; Multi-pass membrane protein
Note: ER membrane retention is mediated by the transmembrane domains.

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/Helicase 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
Note: Located in RE-derived vesicles hosting the replication complex.

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
Host cytoplasm
Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles (By similarity).
Shuttles between the cytoplasm and nucleus (By similarity).

Features

Showing features for topological domain, transmembrane, intramembrane.

Type
IDPosition(s)Description
Topological domain2-108Cytoplasmic
Transmembrane109-129Helical
Topological domain130-248Extracellular
Transmembrane249-269Helical
Topological domain270-275Cytoplasmic
Transmembrane276-290Helical
Topological domain291-743Extracellular
Transmembrane744-764Helical
Topological domain765-770Cytoplasmic
Transmembrane771-791Helical
Topological domain792-1216Extracellular
Transmembrane1217-1237Helical
Topological domain1238-1245Cytoplasmic
Transmembrane1246-1268Helical
Topological domain1269-1288Lumenal
Transmembrane1289-1309Helical
Topological domain1310-1313Cytoplasmic
Transmembrane1314-1331Helical
Topological domain1332-1345Lumenal
Transmembrane1346-1366Helical
Topological domain1367-1375Cytoplasmic
Transmembrane1376-1396Helical
Topological domain1397-1399Lumenal
Transmembrane1400-1420Helical
Topological domain1421-1477Cytoplasmic
Intramembrane1478-1498Helical
Topological domain1499-2174Cytoplasmic
Transmembrane2175-2195Helical
Topological domain2196-2200Lumenal
Intramembrane2201-2221Helical
Topological domain2222Lumenal
Transmembrane2223-2243Helical
Topological domain2244-2258Cytoplasmic
Transmembrane2259-2279Helical; Note=Signal for NS4B
Topological domain2280-2312Lumenal
Intramembrane2313-2333Helical
Topological domain2334-2380Lumenal
Transmembrane2381-2401Helical
Topological domain2402-2444Cytoplasmic
Transmembrane2445-2465Helical
Topological domain2466-2470Lumenal
Transmembrane2471-2491Helical
Topological domain2492-3433Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis444Complete loss of glycosylation. Attenuated phenotype.
Mutagenesis446Complete loss of glycosylation.
Mutagenesis446Complete loss of glycosylation. Attenuated phenotype.
Mutagenesis446No effect on glycosylation. No effect on avian virulence properties as NYS, but enhanced host oral infectivity.
Mutagenesis968No effect on TL3 signaling inhibition by NS1.
Mutagenesis982No effect on TL3 signaling inhibition by NS1.
Mutagenesis1029No effect on TL3 signaling inhibition by NS1.
Mutagenesis1046Complete loss of TL3 signaling inhibition by NS1.
Mutagenesis1086Almost no effect on TL3 signaling inhibition by NS1.
Mutagenesis1108Complete loss of TL3 signaling inhibition by NS1.
Mutagenesis1111About 50% loss of TL3 signaling inhibition by NS1.
Mutagenesis1124About 50% loss of TL3 signaling inhibition by NS1.
Mutagenesis2169-2173Complete loss of regulation of the ATPase activity of NS3 helicase by NS4A.
Mutagenesis255785% loss of NS5-GMP formation.
Mutagenesis2589Complete loss of 2'-O-methyltransferase activity.
Mutagenesis2674Complete loss of 2'-O-methyltransferase activity.
Mutagenesis267686% loss of N7 guanine methyltransferase activity; 60% loss of 2'-O-methyltransferase activity.
Mutagenesis268878% loss of N7 guanine methyltransferase activity; no effect 2'-O-methyltransferase activity.
Mutagenesis269150% loss of N7 guanine methyltransferase activity; no effect 2'-O-methyltransferase activity.
Mutagenesis269210% loss of N7 guanine methyltransferase activity; 50% loss of 2'-O-methyltransferase activity.
Mutagenesis2710Complete loss of 2'-O-methyltransferase activity.
Mutagenesis271220% loss of N7 guanine methyltransferase activity7; 74% loss of 2'-O-methyltransferase activity.
Mutagenesis2746Complete loss of 2'-O-methyltransferase activity.

PTM/Processing

Features

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

Type
IDPosition(s)Description
ChainPRO_00004415771-105Capsid protein C
ChainPRO_00004415761-3433Genome polyprotein
PropeptidePRO_0000441578106-123ER anchor for the capsid protein C, removed in mature form by serine protease NS3
ChainPRO_0000441580124-215Peptide pr
ChainPRO_0000441579124-290Protein prM
Glycosylation138N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000441581216-290Small envelope protein M
ChainPRO_0000441582291-791Envelope protein E
Disulfide bond293↔320
Disulfide bond350↔406
Disulfide bond350↔411
Disulfide bond364↔395
Disulfide bond382↔406
Disulfide bond382↔411
Glycosylation444N-linked (GlcNAc...) asparagine; by host
Disulfide bond480↔578
Disulfide bond595↔626
ChainPRO_0000441583792-1143Non-structural protein 1
Disulfide bond795↔806
Disulfide bond846↔934
Glycosylation921N-linked (GlcNAc...) asparagine; by host
Glycosylation966N-linked (GlcNAc...) asparagine; by host
Disulfide bond970↔1014
Glycosylation998N-linked (GlcNAc...) asparagine; by host
Disulfide bond1071↔1120
Disulfide bond1082↔1103
Disulfide bond1104↔1107
ChainPRO_00004415841144-1374Non-structural protein 2A
ChainPRO_00004415851375-1505Serine protease subunit NS2B
ChainPRO_00004415861506-2124Serine protease/Helicase NS3
Modified residue1894N6-acetyllysine; by host
ChainPRO_00004415872125-2250Non-structural protein 4A
PeptidePRO_00004415882251-2273Peptide 2k
ChainPRO_00004415892274-2528Non-structural protein 4B
ChainPRO_00004415902529-3433RNA-directed RNA polymerase NS5
Modified residue2584Phosphoserine

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 (PubMed:24505133).
The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells (By similarity).

Serine protease/Helicase 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

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

Keywords

PTM databases

Interaction

Subunit

Capsid protein C

Homodimer (By similarity).
Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity).
Interacts with host DDX56; this interaction plays an important role in genomic RNA encapsidation (PubMed:22925334).

Protein prM

Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity).

Envelope protein E

Homodimer; in the endoplasmic reticulum and Golgi (PubMed:20956322).

Non-structural protein 1

Homodimer; Homohexamer when secreted (PubMed:24505133, PubMed:24594604).
NS1 interacts with NS4B (PubMed:22553322).
Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (PubMed:17132743).

Serine protease subunit NS2B

Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity).
Interacts with human SPCS1 (PubMed:29593046).

Serine protease/Helicase NS3

Forms a heterodimer with NS2B (By similarity).
Interacts with NS4B (By similarity).
Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity).

Non-structural protein 4A

Interacts with host RTN3; this interaction is important to remodel host cell membranes (PubMed:29117567).

Non-structural protein 4B

Interacts with Serine protease/Helicase NS3 (By similarity).
Interacts with NS1 (PubMed:22553322).

RNA-directed RNA polymerase NS5

Homodimer (By similarity).
Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity).

Structure

Family & Domains

Features

Showing features for region, domain, motif.

Type
IDPosition(s)Description
Region2-15Interaction with host EXOC1
Region37-72Hydrophobic; homodimerization of capsid protein C
Region388-401Fusion peptide
Region1428-1467Interacts with and activates NS3 protease
Domain1506-1683Peptidase S7
Domain1686-1842Helicase ATP-binding
Region1690-1693Important for RNA-binding
Motif1790-1793DEAH box
Domain1853-2018Helicase C-terminal
Region2169-2173Regulates the ATPase activity of NS3 helicase
Domain2529-2794mRNA cap 0-1 NS5-type MT
Motif2917-2919Nuclear localization signal
Domain3058-3210RdRp catalytic
Motif3431-3433PDZ-binding

Domain

Small envelope protein M

The transmembrane domains contain an endoplasmic reticulum retention signal.

Envelope protein E

The transmembrane domains contain an endoplasmic reticulum retention signal.

RNA-directed RNA polymerase NS5

Contains a PDZ-binding motif that binds to several PDZ-containing cellular proteins. These interactions seem necessary for an optimal viral replication.

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
    3,433
  • Mass (Da)
    381,176
  • Last updated
    2001-03-01 v2
  • MD5 Checksum
    EFF65EEF6616F54D651EDCB674659A4C
MSKKPGGPGKSRAVNMLKRGMPRVLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAVMIGLIASVGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYMCDDTITYECPVLSAGNDPEDIDCWCTKSAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFVVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSDLSTKAACPTMGEAHNDKRADPAFVCRQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKAIGRTILKENIKYEVAIFVHGPTTVESHGNYSTQVGATQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTNAYYVMTVGTKTFLVHREWFMDLNLPWSSAGSTVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFLGTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGRLVTVNPFVSVATANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWMDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSVVVEKQEGMYKSAPKRLTATTEKLEIGWKAWGKSILFAPELANNTFVVDGPETKECPTQNRAWNSLEVEDFGFGLTSTRMFLKVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRLNDTWKLERAVLGEVKSCTWPETHTLWGDGILESDLIIPVTLAGPRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDSGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAVFFQMAYHDARQILLWEIPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGLFNPMILAAGLIACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWESDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMVCLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKKGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPIPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVPREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTKVELGEAAAIFMTATPPGTSDPFPESNSPISDLQTEIPDRAWNSGYEWITEYTGKTVWFVPSVKMGNEIALCLQRAGKKVVQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKAFKDFASGKRSQIGLIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGAVLGVATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVMTLVSAVAANEMGWLDKTKSDISSLFGQRIEVKENFSMGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTAATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQIMLILVSLAAVVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFTRYRKEAIIEVDRSAAKHARKEGNVTGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTIRVLEMVEDWLHRGPREFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKRTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYDVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGKIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLFENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRAIIGDEKYVDYMSSLKRYEDTTLVEDTVL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF196835
EMBL· GenBank· DDBJ
AAF20092.2
EMBL· GenBank· DDBJ
Genomic RNA
AF404755
EMBL· GenBank· DDBJ
AAM81751.1
EMBL· GenBank· DDBJ
Genomic RNA
HM488125
EMBL· GenBank· DDBJ
ADL27936.1
EMBL· GenBank· DDBJ
Genomic RNA
HM488126
EMBL· GenBank· DDBJ
ADL27937.1
EMBL· GenBank· DDBJ
Genomic RNA
HM488127
EMBL· GenBank· DDBJ
ADL27938.1
EMBL· GenBank· DDBJ
Genomic RNA
HM488128
EMBL· GenBank· DDBJ
ADL27939.1
EMBL· GenBank· DDBJ
Genomic RNA
KC407666
EMBL· GenBank· DDBJ
AGI15883.1
EMBL· GenBank· DDBJ
Genomic RNA
KM083619
EMBL· GenBank· DDBJ
AIO10814.1
EMBL· GenBank· DDBJ
Genomic RNA
KX547386
EMBL· GenBank· DDBJ
ANW69091.1
EMBL· GenBank· DDBJ
Genomic RNA
KX547393
EMBL· GenBank· DDBJ
ANW69112.1
EMBL· GenBank· DDBJ
Genomic RNA
AB185914
EMBL· GenBank· DDBJ
BAD34488.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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