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{
"metadata": {
"accession": "A0A0S2VEI3",
"id": "A0A0S2VEI3_LIV",
"source_organism": {
"taxId": "11086",
"scientificName": "Louping ill virus",
"fullName": "Louping ill virus (LIV)"
},
"name": "Genome polyprotein",
"description": [
"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",
"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",
"Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response",
"Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter",
"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. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment",
"Inhibits RNA silencing by interfering with host Dicer",
"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)",
"May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity",
"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",
"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",
"Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding",
"Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins"
],
"length": 3414,
"sequence": "MGRKTILKGKGSGPPRRVSKETATKTRQSRVQMPNGLVLMRMMGILWHAVAGTARNPVLKAFWNSVPLRQATAALRKIKRTVSALMVGLQRRGKRRSVTNWMNWLLVIALLGMTLAATVRKERDGTTVIRAEGRDAATQVRVESGTCVILATDMGSWCDDSLSYECVTIEQGEEPVDVDCFCRNVDGVYLEYGRCGKQEGSRTRRSVLIPTHAQGELTGRGRKWLEGDSLRTHLTRVEGWVWKNKLLALAMVAVVWLALESVVTRVAVLVMLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPSVDVWLDAIYQESPAKTREYCLHAKLSETKVAARCPTMGPAVLTEEHQIGTVCKRDQSDRGWGNHCGLFGKGSIVACVKAACEAKKKATGYVYDANKIVYTVKVEPHTGDYVAANETHKGRKTATFTVSSEKTILTLGEYGDVSLLCRVASGVDLAQTIILELDKTAEHLPTAWQVHRDWFNDLALPWKHDGNPHWNNAERLVEFGVPHAVKMDVYNLGDQTGVLLKALAGVPVAHIEGNKYHLKSGHVTCEVGLENLKMKGLTYTMCDKSKFAWKRTPTDSGHDTVVMEVTFSGSKPCRIPVRAVAHGSPDVNVAMLITPNPTIENDGGGFIEMQLPPGDNIIYVGELSHQWFQTGSSIGRVFQTTRKGIERLTVIGEHAWDFGSAGGFFSSIGKAVHTVLGGAFNSIFGGVGFLPKLLMGVALAWLGLNTRNPTMSMSFLLAGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWREVSEWYDNYAYYPETPGALASAIKEAFEEGSCGIVPQNRLEMAMWRSSVTELNLALAEGDANLTVVVDKNDPTDYRGGVPGMLKKGKDMEVSWRSWGHSMIWSIPEAPRRFMVGTEGQSECPLERRKTGVFTVAEFGVGLRTKVFLDFRQEPTHECDTGVMGAAVKNGMAVHTDQSLWMKSTRNDTGTYIVELLVTDLRNCSWPASHTIDNADVVNSELFLPASLAGPRSWYNRIPGYSEQVKGPWKHTPLRVIREECPGTTVTINAKCEKRGASVRSTTESGKVIPEWCCRACTMPPVTFRTGTDCWYAMEIRPVHAQGGFVRSMVVADNGELLSEGGVPGIVALFVVLECIIRRRPSTGVTVAWGGVVVLALLVTGMVRIESLVRYVVAVGIAFHLELGPETVALMLLQAVFELRVGLLSAFALRRGFTVREMVTTYFLLLVLEMGLPSASLGDLWKWSDALAMGALIFRACTAEGKTGTGLLLIALMTQRDVVIVHHGLVCFLAAAAACSVWRLLRGHREQKGLTWIIPLARLLGGEGSGIRLLAFWELAAHKGRRSFSEPLTVVGVMLTLASGMMRHTSQEALCALAVASFFLLMLVLGTRKMQLVAEWSGCVEWHPELVNEGGEISLRVRQDSMGNFHLTELEKEERMMAFWLLAGLVASALHWSGILGVMGLWTLTEIMRSSRRSDLVYSGQGGQERGDRPFEVKDGVYRIFSPGLFWGQRQVGVGYGHKGVLHTMWHVTRGAALSIDDALAGPYWADVKEDVVCYGGAWSLEEKWKGEMVQVHAFPPGKAHEVHQCQPGELILDTGKRLGAIPIDLAKGTSGSPILNAQGAVVGLYGNGLKTNESYVSSIAQGEAEKSRPNLPQAVVGTGWTSKGQITVLDMHPGSGKTHRVLPELIRQCIDRRLRTLVLAPTRVVLKEMERALSGKRVRFHSPAVSDQQVGGAIVDVMCHATYVNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYTLAKENKCALVLMTATPPGKSEPFPESNGAITSEERQIPDGEWRDGFDWITEYEGRTAWFVPSIAKGGVIARTLRQKGKSVICLNSKTFEKDYSRVREEKPDFVVTTDISEMGANLDVSRVIDGRTNIKPEEVDGKVEFTGTRRVTTASAAQRRGRVGRQGGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTLRGPVATFYGPEQDKMPEVAGHFRLTEEKRKHFRHLLTHCDFTPWLAWHVAANVSSVTDRSWTWEGPEANAVDEASGDLVTFRSPNGAERTLRPVWRDARMFREGHDIKEFVAYASGRRSFGDVLTGMSGVPELLRHRCVSALDVFYTLMHEEPGSRAMKMAERDAPEAFLTVAEMMVLGLATLGVVWCFVVRTSISRMTLGTLVLLASLLLLWAGGVSYGNMAGVALIFYTLLTVLQPETGKQRSSDDNKLAYFLLTLCSLAGLVAANEMGFLEKTKADLSAVLWSEHEEHRQWSEWTNVDIQPARSWGTYVLVVSLFTPYIIHQLQTKIQQLVNSAVASGAQAMRDLGGGAPFFGVAGHVITLGVVSLVGATPTSLIVGIGLAAFHLAIVVSGLEAELTQRAHKVFFSAMVRNPMVDGDVINPFREGEAKPALYERKMSLALAIVLCLVSVVMNRTVASMTEAAAVGLAAIGQFLRPEADTLWTMPVACGMSSVVRGSLWGFLPLGHRLWLRASGGRRGGSDGDTLGDLWKRRLNNCTKEEFFVYRRTGILETERDKARELLRRGETNMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMGVRAYTIGGRGHEVPKMVTSLGWNLIKFRAGMDVFSMQPHRADTIMCDIGESNPDAAVEGERTRKVILLMEQWKIRNPAAACVFKVLAPYRPEVIEALHRFQLQWGGGLVRTPFSRNSTHEMYYSTAVTGNIVNSVNIQSRKLLARFGDQRGPTKVPELDLGVGTRCVVLAEDKVKEQDVQERIRALREQYNETWHKDEEHPYRTWQYWGSYRTAPTGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEPQPGTRVIMRAVNDWILERLAQKSKPRMCSREEFIAKVRSNAALGAWSDEQNRWASAREAVEDPVFWALVDEERERHLVGRCAHCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNEDHWASRESSGGGVEGISLNYLGWHLKKLSTLNGGLFYADDTAGWDTKVTNADLEDEEQILRYMEGEHKRLAATIMQKAYHAKVVKVARPSRDGGCIMDVITRRDQRGSGQVVTYALNTLTNIKVQLIRMMEGEGVIEAEDAHNPRLLRVERWLKEHGEERLGRMLVSGDDCVVRPMDDRFGKALYFLNDMAKTRKDIGEWEPSTGFSSWEEVPFCSHHFHELVMKDGRTLVVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFHRRDLRTLGFAISSAVPVDWVPTGRTTWSIHASGAWMTTEDMLDVWNRVWILDNPFMQNKERIMEWRDVPYLPKTQDMICSSLVGRKERAEWAKNIWGAVEKVRKMIGPERFKDYLSCMDRHDLHWELKLESSII",
"proteome": null,
"gene": null,
"go_terms": [
{
"identifier": "GO:0046983",
"name": "protein dimerization activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0004252",
"name": "serine-type endopeptidase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0044423",
"name": "virion component",
"category": {
"code": "C",
"name": "cellular_component"
}
},
{
"identifier": "GO:0003723",
"name": "RNA binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0003724",
"name": "RNA helicase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0005524",
"name": "ATP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0004386",
"name": "helicase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0004482",
"name": "mRNA 5'-cap (guanine-N7-)-methyltransferase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0004483",
"name": "methyltransferase cap1 activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0003968",
"name": "RNA-directed RNA polymerase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0039694",
"name": "viral RNA genome replication",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0005198",
"name": "structural molecule activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0019028",
"name": "viral capsid",
"category": {
"code": "C",
"name": "cellular_component"
}
},
{
"identifier": "GO:0016817",
"name": "hydrolase activity, acting on acid anhydrides",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0017111",
"name": "ribonucleoside triphosphate phosphatase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0019058",
"name": "viral life cycle",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0003725",
"name": "double-stranded RNA binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0016032",
"name": "viral process",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0016070",
"name": "RNA metabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0008168",
"name": "methyltransferase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0032259",
"name": "methylation",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"protein_evidence": 4,
"source_database": "unreviewed",
"is_fragment": false,
"in_alphafold": false,
"in_bfvd": false,
"ida_accession": "d798a6f37980000b45969b8b3fddcd909e454b3b",
"counters": {
"domain_architectures": 338,
"entries": 85,
"isoforms": 0,
"proteomes": 0,
"sets": 11,
"structures": 0,
"taxa": 1,
"dbEntries": {
"cathgene3d": 12,
"cdd": 5,
"pfam": 16,
"ssf": 6,
"profile": 6,
"smart": 2,
"pirsf": 1,
"ncbifam": 1,
"interpro": 36
},
"proteome": 0,
"taxonomy": 1,
"similar_proteins": 338
}
}
}
