HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "S6DZ58",
"id": "S6DZ58_9ENTO",
"source_organism": {
"taxId": "47502",
"scientificName": "Echovirus E14",
"fullName": "Echovirus E14"
},
"name": "Genome polyprotein",
"description": [
"Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. During genome replication, the VPg-RNA linkage is removed by the host TDP2, thereby accelerating replication. During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions",
"Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step",
"Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome",
"Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3",
"Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm",
"Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface. Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place",
"Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity"
],
"length": 1381,
"sequence": "NDPEQAIDRALARVADTIRSGPSNSEQIPALTAVETGHTSQVVPSDTMQTRHVKNYHSRSESTIENFLCRSACVHIATYKARGGAGDTNRYDSWDINIKELVQLRRKCEMFTYLRFDMEVTFVITSIQEQGTALTQDMPVLTHQIMYVPPGGAVPSDAESFAWQSSTNPSVFWTEGNAPARMSIPFISIGNAYSNFYDGWSHFTQDGGYGYNTLNKMGKIYVRHVNKQTPTDVTSTIRIYFKPKHVRAWIPRPPRLCPYKNKANVNFEVTSVTTARTSLNDVPTPNHSSSVHLQLRTHGAFGQQSGAVYVGNYRVINRHLATFADWQNCVWEDYNRDLLVSTTTAQGCDVIARCQCTTGVYFCQSRNKHYPVSFEGPGLVEVQESEYYPRRFQSHVLLAAGFSEPGDCGGILRCEHGTIGIVTMGGDGVVGFADVRDLLWLEDDAMEQGVRDYVEQLGNAFGSGFTNQICEQVNLLKESLVGQDSILEKSLKALVKIISALVIVVRNHDDLITVTATLALVGCTSSPWRWLKQKVSQYYGIPMAERQNNGWLKKFTEMTNACKGMEWIAIKIQKFIEWLKVKILPEVKEKHEFLSRLKQLPLLESQIATIEQSAPSQSDQEQLFSNVQYFAHYCRKYAPLYAAEAKRVFALEKKMSNYIQFKSKCRIEPVCLLLHGSPGAGKSVATNLIGRSLAEKLNSSVYSLPPDPDHFDGYKQQAVVIMDDLCQNPDGKDVSLFCQMVSSVDFVPPMAALEEKGILFTSPFVLASTNAGSINAPTVSDSRALARRFHFDMNIEVISMYSQNGKINMPLSVKTCDEECCPVNFKKCCPLLCGKAIQFIDRRTQVRYSLDMLVTEMFREYNHRHSVGATLEALFQGPPVYREIKISVAPETPPPPAIADLLKSVDSEAVREYCKEKGWLVPEVNATLQIEKHVSRAFICLQALTTFVSVAGIIYIIYKLFAGFQGAYTGMPNQKPKVPTLRQAKVQGPIFEFAVAMMKRNSSTVKTEYGEFTMIGIYDRWAVLPRHAKPGPTILMNDQEVGVLDAKELVDKDGTNLELTLLKLNRNEKFRDIRGFLAREEVEVNEAVLAINTSKFPNMYIPVGQVTDYGFLNLGGTPTKRMLMYNFPTRAGQCGGVLMSTGKVLGIHVGGNGHQGFSAALLRHYFNEEQGEIEFIESSKEAGFPVINTPSKTKLEPSVFHHVFEGNKEPSVLRNGDPRLKVNFEEAIFSKYIGNVNTHVDEYMQEAVDHYAGQLATLDISTEPMKLEDAVYGTEGLEALDLTTSAGYPYVALGIKKRDILSKKTKDLTKLKECMDKYGLNLPMVTYVKDELRSADKVAKGKSRLIEASSLNDSVAMRQTFGNLYKAFHLNPGIVTGSAVG",
"proteome": null,
"gene": null,
"go_terms": [
{
"identifier": "GO:0005198",
"name": "structural molecule activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0008233",
"name": "peptidase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006508",
"name": "proteolysis",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0016032",
"name": "viral process",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"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:0003968",
"name": "RNA-directed RNA polymerase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0004197",
"name": "cysteine-type endopeptidase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0017111",
"name": "ribonucleoside triphosphate phosphatase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006351",
"name": "DNA-templated transcription",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"protein_evidence": 3,
"source_database": "unreviewed",
"is_fragment": true,
"in_alphafold": false,
"in_bfvd": false,
"ida_accession": "de7685794ebdc5d44bb538b6b8acbb23aebdb3a9",
"counters": {
"domain_architectures": 89,
"entries": 36,
"isoforms": 0,
"proteomes": 0,
"sets": 5,
"structures": 0,
"taxa": 1,
"dbEntries": {
"cathgene3d": 4,
"ssf": 5,
"pfam": 7,
"cdd": 1,
"profile": 2,
"smart": 1,
"interpro": 16
},
"proteome": 0,
"taxonomy": 1,
"similar_proteins": 89
}
}
}
