{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P13901","secondaryAccessions":["Q81083","Q81084","Q81085","Q81086","Q81087","Q81088","Q81089","Q81090","Q81091","Q81092","Q81093"],"uniProtkbId":"POLG_HAVMB","entryAudit":{"firstPublicDate":"1990-01-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1990-01-01","entryVersion":178,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Human hepatitis A virus genotype IB (isolate MBB)","commonName":"HHAV","synonyms":["Human hepatitis A virus (isolate Human/Northern Africa/MBB/1978)"],"taxonId":12100,"lineage":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Picornavirales","Picornaviridae","Heptrevirinae","Hepatovirus","Hepatovirus fejalco","Hepatovirus ahepa","Hepatovirus A"]},"organismHosts":[{"scientificName":"Cercopithecus hamlyni","commonName":"Owl-faced monkey","synonyms":["Hamlyn's monkey"],"taxonId":9536},{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606},{"scientificName":"Macaca","commonName":"macaques","taxonId":9539},{"scientificName":"Pan troglodytes","commonName":"Chimpanzee","taxonId":9598}],"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Genome polyprotein"}},"contains":[{"recommendedName":{"fullName":{"value":"Capsid protein VP0"}},"alternativeNames":[{"fullName":{"value":"VP4-VP2"}}]},{"recommendedName":{"fullName":{"value":"Capsid protein VP4"}},"alternativeNames":[{"fullName":{"value":"P1A"}},{"fullName":{"value":"Virion protein 4"}}]},{"recommendedName":{"fullName":{"value":"Capsid protein VP2"}},"alternativeNames":[{"fullName":{"value":"P1B"}},{"fullName":{"value":"Virion protein 2"}}]},{"recommendedName":{"fullName":{"value":"Capsid protein VP3"}},"alternativeNames":[{"fullName":{"value":"P1C"}},{"fullName":{"value":"Virion protein 3"}}]},{"recommendedName":{"fullName":{"value":"Protein VP1-2A"}},"alternativeNames":[{"fullName":{"value":"VPX"}}]},{"recommendedName":{"fullName":{"value":"Capsid protein VP1"}},"alternativeNames":[{"fullName":{"value":"P1D"}},{"fullName":{"value":"Virion protein 1"}}]},{"recommendedName":{"fullName":{"value":"Assembly signal 2A"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"pX"}}]},{"recommendedName":{"fullName":{"value":"Protein 2BC"}}},{"recommendedName":{"fullName":{"value":"Protein 2B"},"shortNames":[{"value":"P2B"}]}},{"recommendedName":{"fullName":{"value":"Protein 2C"},"shortNames":[{"value":"P2C"}],"ecNumbers":[{"value":"3.6.1.15"}]}},{"recommendedName":{"fullName":{"value":"Protein 3ABCD"},"shortNames":[{"value":"P3"}]}},{"recommendedName":{"fullName":{"value":"Protein 3ABC"}}},{"recommendedName":{"fullName":{"value":"Protein 3AB"}}},{"recommendedName":{"fullName":{"value":"Protein 3A"},"shortNames":[{"value":"P3A"}]}},{"recommendedName":{"fullName":{"value":"Viral protein genome-linked"},"shortNames":[{"value":"VPg"}]},"alternativeNames":[{"fullName":{"value":"Protein 3B"},"shortNames":[{"value":"P3B"}]}]},{"recommendedName":{"fullName":{"value":"Protein 3CD"}}},{"recommendedName":{"fullName":{"value":"Protease 3C"},"shortNames":[{"value":"P3C"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"3.4.22.28"}]},"alternativeNames":[{"fullName":{"value":"Picornain 3C"}}]},{"recommendedName":{"fullName":{"value":"RNA-directed RNA polymerase"},"shortNames":[{"value":"P3D-POL"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"2.7.7.48"}]}}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell"}],"commentType":"FUNCTION","molecule":"Capsid protein VP1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell"}],"commentType":"FUNCTION","molecule":"Capsid protein VP2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell"}],"commentType":"FUNCTION","molecule":"Capsid protein VP3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"VP0 precursor is a component of the immature procapsids"}],"commentType":"FUNCTION","molecule":"Capsid protein VP0"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size"}],"commentType":"FUNCTION","molecule":"Capsid protein VP4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein"}],"commentType":"FUNCTION","molecule":"Protein VP1-2A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway"}],"commentType":"FUNCTION","molecule":"Protein 2B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Affects membrane integrity and causes an increase in membrane permeability"}],"commentType":"FUNCTION","molecule":"Protein 2BC"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity"}],"commentType":"FUNCTION","molecule":"Protein 2C"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin"}],"commentType":"FUNCTION","molecule":"Protein 3ABC"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs"}],"commentType":"FUNCTION","molecule":"Protein 3AB"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA"}],"commentType":"FUNCTION","molecule":"Protein 3A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P03300"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"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 VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome"}],"commentType":"FUNCTION","molecule":"Viral protein genome-linked"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis"}],"commentType":"FUNCTION","molecule":"Protease 3C"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF"}],"commentType":"FUNCTION","molecule":"Protein 3CD"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Replicates genomic and antigenomic RNA by recognizing replications specific signals"}],"commentType":"FUNCTION","molecule":"RNA-directed RNA polymerase"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.48","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00539"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23680"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57930"},{"database":"ChEBI","id":"CHEBI:61557"}],"ecNumber":"3.6.1.15","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.","ecNumber":"3.4.22.28","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01222"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Homodimer. Homomultimer; probably interacts with membranes in a multimeric form. Seems to assemble into amyloid-like fibers"}],"commentType":"SUBUNIT","molecule":"Protein 2B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Homodimer. Monomer. Interacts with protein 3CD"}],"commentType":"SUBUNIT","molecule":"Protein 3AB"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with host ACBD3 (By similarity)"}],"commentType":"SUBUNIT","molecule":"Protein 3A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with protein 3AB"}],"commentType":"SUBUNIT","molecule":"Protein 3CD"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with human MAVS"}],"commentType":"SUBUNIT","molecule":"Protein 3ABC"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Homodimer; disulfide-linked"}],"commentType":"SUBUNIT","molecule":"Protease 3C"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Homopentamer. Homooligomer"}],"commentType":"SUBUNIT","molecule":"Protein VP1-2A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with capsid protein VP2. Interacts with capsid protein VP3"}],"commentType":"SUBUNIT","molecule":"Capsid protein VP1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with capsid protein VP1. Interacts with capsid protein VP3"}],"commentType":"SUBUNIT","molecule":"Capsid protein VP2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with capsid protein VP1. Interacts with capsid protein VP2"}],"commentType":"SUBUNIT","molecule":"Capsid protein VP3"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Capsid protein VP2","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Virion","id":"SL-0274"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host endosome, host multivesicular body","id":"SL-0453"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Capsid protein VP3","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Virion","id":"SL-0274"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host endosome, host multivesicular body","id":"SL-0453"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Capsid protein VP1","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Virion","id":"SL-0274"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host endosome, host multivesicular body","id":"SL-0453"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Capsid protein VP4","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Virion","id":"SL-0274"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Protein 2B","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Protein 2C","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. May associate with membranes through a N-terminal amphipathic helix"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Protein 3ABC","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass membrane protein","id":"SL-9904"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host mitochondrion outer membrane","id":"SL-0411"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Protein 3AB","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Protein 3A","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Viral protein genome-linked","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Virion","id":"SL-0274"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Protease 3C","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"RNA-directed RNA polymerase","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Interacts with membranes in a complex with viral protein 3AB. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Host cytoplasmic vesicle membrane","id":"SL-0387"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The assembly signal 2A region mediates pentamerization of P1-2A"}],"commentType":"DOMAIN","molecule":"Protein VP1-2A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. The genome polyprotein contains two L domains: a tandem of (L)YPX(n)L domain which is known to bind the PDCD6IP/ALIX adaptater protein"}],"commentType":"DOMAIN","molecule":"Genome polyprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Capsid protein VP2 contains two L domains: a tandem of (L)YPX(n)L domain which is known to bind the Alix adaptater protein"}],"commentType":"DOMAIN","molecule":"Capsid protein VP2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The C-terminus displays a membrane-penetrating ability"}],"commentType":"DOMAIN","molecule":"Protein 2B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini"}],"commentType":"PTM","molecule":"Genome polyprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P03303"}],"value":"During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle"}],"commentType":"PTM","molecule":"Capsid protein VP0"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in naked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini"}],"commentType":"PTM","molecule":"Protein VP1-2A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P03300"}],"value":"VPg is uridylylated prior to priming replication into VPg-pUpU"}],"commentType":"PTM","molecule":"Viral protein genome-linked"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"Unlike other picornaviruses, does not seem to be myristoylated"}],"commentType":"PTM","molecule":"Capsid protein VP4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"The need for an intact eIF4G factor for the initiation of translation of HAV results in an inability to shut off host protein synthesis by a mechanism similar to that of other picornaviruses"}],"commentType":"MISCELLANEOUS","molecule":"Genome polyprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"During infection, enveloped virions (eHAV) are released from cells. These eHAV are cloaked in host-derived membranes and resemble exosomes. The membrane of eHAV is devoid of viral proteins and thus prevents their neutralization by antibodies. eHAV budding is dependent on ESCRT-associated proteins VPS4B and PDCD6IP/ALIX. eHAV are produced and released in the serum and plasma, but not in bile and feces which only contain the naked, nonenveloped virions. It is likely that eHAV also use HAVCR1 as a functional receptor to infect cells, an evolutionary trait that may enhance HAV infectivity"}],"commentType":"MISCELLANEOUS","molecule":"Genome polyprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the picornaviridae polyprotein family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}],"value":"It is uncertain whether Met-1 or Met-3 is the initiator"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":2227,"modifier":"EXACT"}},"description":"Genome polyprotein","featureId":"PRO_0000311015"},{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Capsid protein VP0","featureId":"PRO_0000311016"},{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Capsid protein VP4","featureId":"PRO_0000039968"},{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Capsid protein VP2","featureId":"PRO_0000039969"},{"type":"Chain","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"Capsid protein VP3","featureId":"PRO_0000039970"},{"type":"Chain","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":836,"modifier":"EXACT"}},"description":"Protein VP1-2A","featureId":"PRO_0000039971"},{"type":"Chain","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":764,"modifier":"EXACT"}},"description":"Capsid protein VP1","featureId":"PRO_0000311017"},{"type":"Chain","location":{"start":{"value":765,"modifier":"EXACT"},"end":{"value":836,"modifier":"EXACT"}},"description":"Assembly signal 2A","featureId":"PRO_0000039972"},{"type":"Chain","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":1422,"modifier":"EXACT"}},"description":"Protein 2BC","featureId":"PRO_0000311018"},{"type":"Chain","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":1087,"modifier":"EXACT"}},"description":"Protein 2B","featureId":"PRO_0000039973"},{"type":"Chain","location":{"start":{"value":1088,"modifier":"EXACT"},"end":{"value":1422,"modifier":"EXACT"}},"description":"Protein 2C","featureId":"PRO_0000039974"},{"type":"Chain","location":{"start":{"value":1423,"modifier":"EXACT"},"end":{"value":2227,"modifier":"EXACT"}},"description":"Protein 3ABCD","featureId":"PRO_0000311019"},{"type":"Chain","location":{"start":{"value":1423,"modifier":"EXACT"},"end":{"value":1738,"modifier":"EXACT"}},"description":"Protein 3ABC","featureId":"PRO_0000311020"},{"type":"Chain","location":{"start":{"value":1423,"modifier":"EXACT"},"end":{"value":1519,"modifier":"EXACT"}},"description":"Protein 3AB","featureId":"PRO_0000311021"},{"type":"Chain","location":{"start":{"value":1423,"modifier":"EXACT"},"end":{"value":1496,"modifier":"EXACT"}},"description":"Protein 3A","featureId":"PRO_0000039975"},{"type":"Chain","location":{"start":{"value":1497,"modifier":"EXACT"},"end":{"value":1519,"modifier":"EXACT"}},"description":"Viral protein genome-linked","featureId":"PRO_0000039976"},{"type":"Chain","location":{"start":{"value":1520,"modifier":"EXACT"},"end":{"value":2227,"modifier":"EXACT"}},"description":"Protein 3CD","featureId":"PRO_0000311022"},{"type":"Chain","location":{"start":{"value":1520,"modifier":"EXACT"},"end":{"value":1738,"modifier":"EXACT"}},"description":"Protease 3C","featureId":"PRO_0000039977"},{"type":"Chain","location":{"start":{"value":1739,"modifier":"EXACT"},"end":{"value":2227,"modifier":"EXACT"}},"description":"RNA-directed RNA polymerase","featureId":"PRO_0000039978"},{"type":"Transmembrane","location":{"start":{"value":1010,"modifier":"EXACT"},"end":{"value":1030,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":1462,"modifier":"EXACT"},"end":{"value":1482,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Domain","location":{"start":{"value":1204,"modifier":"EXACT"},"end":{"value":1366,"modifier":"EXACT"}},"description":"SF3 helicase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00551"}]},{"type":"Domain","location":{"start":{"value":1514,"modifier":"EXACT"},"end":{"value":1728,"modifier":"EXACT"}},"description":"Peptidase C3","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01222"}]},{"type":"Domain","location":{"start":{"value":1976,"modifier":"EXACT"},"end":{"value":2097,"modifier":"EXACT"}},"description":"RdRp catalytic","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00539"}]},{"type":"Region","location":{"start":{"value":766,"modifier":"EXACT"},"end":{"value":836,"modifier":"EXACT"}},"description":"Involved in P1-2A pentamerization","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Region","location":{"start":{"value":1043,"modifier":"EXACT"},"end":{"value":1070,"modifier":"EXACT"}},"description":"Membrane-penetrating ability","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Coiled coil","location":{"start":{"value":1127,"modifier":"EXACT"},"end":{"value":1152,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Motif","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"(L)YPX(n)L motif","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Motif","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"(L)YPX(n)L motif","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Active site","location":{"start":{"value":1563,"modifier":"EXACT"},"end":{"value":1563,"modifier":"EXACT"}},"description":"For protease 3C activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01222"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16288920"}]},{"type":"Active site","location":{"start":{"value":1603,"modifier":"EXACT"},"end":{"value":1603,"modifier":"EXACT"}},"description":"For protease 3C activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01222"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16288920"}]},{"type":"Active site","location":{"start":{"value":1691,"modifier":"EXACT"},"end":{"value":1691,"modifier":"EXACT"}},"description":"For protease 3C activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01222"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16288920"}]},{"type":"Binding site","location":{"start":{"value":1230,"modifier":"EXACT"},"end":{"value":1237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00551"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Cleavage","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":491,"modifier":"EXACT"},"end":{"value":492,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":764,"modifier":"EXACT"},"end":{"value":765,"modifier":"EXACT"}},"description":"Cleavage; partial; by host","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":769,"modifier":"EXACT"},"end":{"value":769,"modifier":"EXACT"}},"description":"Important for VP1 folding and capsid assembly","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":836,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":1087,"modifier":"EXACT"},"end":{"value":1088,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":1422,"modifier":"EXACT"},"end":{"value":1423,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":1496,"modifier":"EXACT"},"end":{"value":1497,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":1519,"modifier":"EXACT"},"end":{"value":1520,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Site","location":{"start":{"value":1738,"modifier":"EXACT"},"end":{"value":1739,"modifier":"EXACT"}},"description":"Cleavage; by protease 3C","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Modified residue","location":{"start":{"value":1499,"modifier":"EXACT"},"end":{"value":1499,"modifier":"EXACT"}},"description":"O-(5'-phospho-RNA)-tyrosine","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Disulfide bond","location":{"start":{"value":1543,"modifier":"EXACT"},"end":{"value":1543,"modifier":"EXACT"}},"description":"Interchain","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08617"}]},{"type":"Helix","location":{"start":{"value":1521,"modifier":"EXACT"},"end":{"value":1531,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1532,"modifier":"EXACT"},"end":{"value":1538,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1545,"modifier":"EXACT"},"end":{"value":1555,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1557,"modifier":"EXACT"},"end":{"value":1561,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Helix","location":{"start":{"value":1562,"modifier":"EXACT"},"end":{"value":1564,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Turn","location":{"start":{"value":1565,"modifier":"EXACT"},"end":{"value":1567,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Helix","location":{"start":{"value":1571,"modifier":"EXACT"},"end":{"value":1573,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1574,"modifier":"EXACT"},"end":{"value":1580,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1583,"modifier":"EXACT"},"end":{"value":1588,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Helix","location":{"start":{"value":1589,"modifier":"EXACT"},"end":{"value":1591,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1592,"modifier":"EXACT"},"end":{"value":1600,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1603,"modifier":"EXACT"},"end":{"value":1608,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Helix","location":{"start":{"value":1619,"modifier":"EXACT"},"end":{"value":1621,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Helix","location":{"start":{"value":1625,"modifier":"EXACT"},"end":{"value":1631,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1636,"modifier":"EXACT"},"end":{"value":1642,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1645,"modifier":"EXACT"},"end":{"value":1651,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1655,"modifier":"EXACT"},"end":{"value":1665,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1671,"modifier":"EXACT"},"end":{"value":1683,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1694,"modifier":"EXACT"},"end":{"value":1698,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Helix","location":{"start":{"value":1700,"modifier":"EXACT"},"end":{"value":1702,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1706,"modifier":"EXACT"},"end":{"value":1714,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Beta strand","location":{"start":{"value":1717,"modifier":"EXACT"},"end":{"value":1722,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]},{"type":"Helix","location":{"start":{"value":1725,"modifier":"EXACT"},"end":{"value":1730,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2CXV"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0167","category":"Cellular component","name":"Capsid protein"},{"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"id":"KW-0191","category":"PTM","name":"Covalent protein-RNA linkage"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"id":"KW-1035","category":"Cellular component","name":"Host cytoplasm"},{"id":"KW-1036","category":"Cellular component","name":"Host cytoplasmic vesicle"},{"id":"KW-1039","category":"Cellular component","name":"Host endosome"},{"id":"KW-1043","category":"Cellular component","name":"Host membrane"},{"id":"KW-1045","category":"Cellular component","name":"Host mitochondrion"},{"id":"KW-1047","category":"Cellular component","name":"Host mitochondrion outer membrane"},{"id":"KW-0945","category":"Biological process","name":"Host-virus interaction"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-1090","category":"Biological process","name":"Inhibition of host innate immune response by virus"},{"id":"KW-1097","category":"Biological process","name":"Inhibition of host MAVS by virus"},{"id":"KW-1113","category":"Biological process","name":"Inhibition of host RLR pathway by virus"},{"id":"KW-0922","category":"Biological process","name":"Interferon antiviral system evasion"},{"id":"KW-0407","category":"Molecular function","name":"Ion channel"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0696","category":"Molecular function","name":"RNA-directed RNA polymerase"},{"id":"KW-1143","category":"Cellular component","name":"T=pseudo3 icosahedral capsid protein"},{"id":"KW-0788","category":"Molecular function","name":"Thiol protease"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"},{"id":"KW-1161","category":"Biological process","name":"Viral attachment to host cell"},{"id":"KW-0899","category":"Biological process","name":"Viral immunoevasion"},{"id":"KW-1182","category":"Molecular function","name":"Viral ion channel"},{"id":"KW-0693","category":"Biological process","name":"Viral RNA replication"},{"id":"KW-0946","category":"Cellular component","name":"Virion"},{"id":"KW-1160","category":"Biological process","name":"Virus entry into host cell"}],"references":[{"referenceNumber":1,"citation":{"id":"2823500","citationType":"journal article","authors":["Paul A.V.","Tada H.","der Helm K.","Wissel T.","Kiehn R.","Wimmer E.","Deinhardt F."],"citationCrossReferences":[{"database":"PubMed","id":"2823500"},{"database":"DOI","id":"10.1016/0168-1702(87)90026-8"}],"title":"The entire nucleotide sequence of the genome of human hepatitis A virus (isolate MBB).","publicationDate":"1987","journal":"Virus Res.","firstPage":"153","lastPage":"171","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC RNA]"]},{"referenceNumber":2,"citation":{"id":"16288920","citationType":"journal article","authors":["Yin J.","Bergmann E.M.","Cherney M.M.","Lall M.S.","Jain R.P.","Vederas J.C.","James M.N.G."],"citationCrossReferences":[{"database":"PubMed","id":"16288920"},{"database":"DOI","id":"10.1016/j.jmb.2005.09.074"}],"title":"Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site.","publicationDate":"2005","journal":"J. Mol. Biol.","firstPage":"854","lastPage":"871","volume":"354"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1520-1738 IN COMPLEX WITH THE INHIBITOR N-CBZ-L-SERINE B-LACTONE","ACTIVE SITE (PROTEASE 3C)"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M20273","properties":[{"key":"ProteinId","value":"AAA45474.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_RNA"}]},{"database":"PDB","id":"2A4O","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A=1520-1738"}]},{"database":"PDB","id":"2CXV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A=1520-1738"}]},{"database":"PDBsum","id":"2A4O","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"2CXV","properties":[{"key":"Description","value":"-"}]},{"database":"BMRB","id":"P13901","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P13901","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB04634","properties":[{"key":"GenericName","value":"N-BENZYLOXYCARBONYL-L-SERINE-BETALACTONE"}]},{"database":"DrugBank","id":"DB04029","properties":[{"key":"GenericName","value":"Phenylalanylamide"}]},{"database":"MEROPS","id":"C03.005","properties":[{"key":"Description","value":"-"}]},{"database":"EvolutionaryTrace","id":"P13901","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0030430","properties":[{"key":"GoTerm","value":"C:host cell cytoplasm"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0044162","properties":[{"key":"GoTerm","value":"C:host cell cytoplasmic vesicle membrane"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0033644","properties":[{"key":"GoTerm","value":"C:host cell membrane"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0044193","properties":[{"key":"GoTerm","value":"C:host cell mitochondrial outer membrane"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0072494","properties":[{"key":"GoTerm","value":"C:host multivesicular body"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0039618","properties":[{"key":"GoTerm","value":"C:T=pseudo3 icosahedral viral capsid"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0034062","properties":[{"key":"GoTerm","value":"F:5'-3' RNA polymerase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0015267","properties":[{"key":"GoTerm","value":"F:channel activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0004197","properties":[{"key":"GoTerm","value":"F:cysteine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0017111","properties":[{"key":"GoTerm","value":"F:ribonucleoside triphosphate phosphatase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0003724","properties":[{"key":"GoTerm","value":"F:RNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003968","properties":[{"key":"GoTerm","value":"F:RNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0005198","properties":[{"key":"GoTerm","value":"F:structural molecule activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0034220","properties":[{"key":"GoTerm","value":"P:monoatomic ion transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0046718","properties":[{"key":"GoTerm","value":"P:symbiont entry into host cell"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0039545","properties":[{"key":"GoTerm","value":"P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0039694","properties":[{"key":"GoTerm","value":"P:viral RNA genome replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019062","properties":[{"key":"GoTerm","value":"P:virion attachment to host cell"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"CDD","id":"cd23215","properties":[{"key":"EntryName","value":"Hepatovirus_RdRp"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00205","properties":[{"key":"EntryName","value":"rhv_like"},{"key":"MatchStatus","value":"2"}]},{"database":"FunFam","id":"2.60.120.20:FF:000016","properties":[{"key":"EntryName","value":"Genome polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.120.20:FF:000017","properties":[{"key":"EntryName","value":"Genome polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.270:FF:000111","properties":[{"key":"EntryName","value":"Genome polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.960.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"3.30.70.270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR049133","properties":[{"key":"EntryName","value":"2B_soluble"}]},{"database":"InterPro","id":"IPR043502","properties":[{"key":"EntryName","value":"DNA/RNA_pol_sf"}]},{"database":"InterPro","id":"IPR004004","properties":[{"key":"EntryName","value":"Helic/Pol/Pept_Calicivir-typ"}]},{"database":"InterPro","id":"IPR000605","properties":[{"key":"EntryName","value":"Helicase_SF3_ssDNA/RNA_vir"}]},{"database":"InterPro","id":"IPR014759","properties":[{"key":"EntryName","value":"Helicase_SF3_ssRNA_vir"}]},{"database":"InterPro","id":"IPR024354","properties":[{"key":"EntryName","value":"Hepatitis_A_VP1-2A"}]},{"database":"InterPro","id":"IPR044067","properties":[{"key":"EntryName","value":"PCV_3C_PRO"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001676","properties":[{"key":"EntryName","value":"Picornavirus_capsid"}]},{"database":"InterPro","id":"IPR043128","properties":[{"key":"EntryName","value":"Rev_trsase/Diguanyl_cyclase"}]},{"database":"InterPro","id":"IPR033703","properties":[{"key":"EntryName","value":"Rhv-like"}]},{"database":"InterPro","id":"IPR001205","properties":[{"key":"EntryName","value":"RNA-dir_pol_C"}]},{"database":"InterPro","id":"IPR007094","properties":[{"key":"EntryName","value":"RNA-dir_pol_PSvirus"}]},{"database":"InterPro","id":"IPR029053","properties":[{"key":"EntryName","value":"Viral_coat"}]},{"database":"Pfam","id":"PF20758","properties":[{"key":"EntryName","value":"2B_soluble"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12944","properties":[{"key":"EntryName","value":"HAV_VP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00680","properties":[{"key":"EntryName","value":"RdRP_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00073","properties":[{"key":"EntryName","value":"Rhv"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00910","properties":[{"key":"EntryName","value":"RNA_helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00918","properties":[{"key":"EntryName","value":"CALICVIRUSNS"}]},{"database":"SUPFAM","id":"SSF56672","properties":[{"key":"EntryName","value":"DNA/RNA polymerases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88633","properties":[{"key":"EntryName","value":"Positive stranded ssRNA viruses"},{"key":"MatchStatus","value":"3"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51874","properties":[{"key":"EntryName","value":"PCV_3C_PRO"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50507","properties":[{"key":"EntryName","value":"RDRP_SSRNA_POS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51218","properties":[{"key":"EntryName","value":"SF3_HELICASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNMSRQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQVEPLRTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVSGITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMKDLKGKANRGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIIIGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDKRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKKKGLFSQAKISLFYTEEHEIMKFSWRGVTADTRALRRFGFSLAAGRSVWTLEMDAGVLTGRLIRLNDEKWTEMKDDKIVSLIEKFTSNKYWSKVNFPHGMLDLEEIAANSKDFPNMSETDLCFLLHWLNPKKINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLKSMMFGFHHSVTVEIINTVLCFVKSGILLYVMQQLNQDEHSHIIGLLRVMNYVDIGCSVISCGKVFSKMLETVFNWQMDSRMMELRTQSFSNWLRDICSGITIFKNFKDAIYWLYTKLNDFYEVNYGKKKDILNILKDNQQKIEKAIEEADKFSILQIQDVEKFEQYQKGVDLIQKLRTVHSMAQVDPNLMVHLSPLRDCIARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPLRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVNPASFSKNPHNDMLNVNLAKTNDAIKDMSCVDLIMDGHNVSLMDLLSSLVMTVEIRKQNMTAFMELWSQGISDDDNDSAMAEFFQSFPSGEPSNSKLSGFFQSVTNHKWVAVGAAVGILGVLVGGWFVYKHFSRKEEEPIPAEGVYHGVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGVKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITQHFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAWRGKGEGLPGMCGGALVSSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIESQRIMKVEFTQCSMNVVSKTLFRKSPIHHHIDKTMINFPAAMPFSKAEIDPMAMMLSKYSLPIVEEPEDYKEASIFYQNKIVGKTQLVDDFLDLDMAITGAPGIDAINMDSSPGFPYVQERLTKRDLIWLDENGLLLGVHPRLAQRILFNTVMMENCSDLDVVFTTCPKDELRPLEKVLESKTRAIDACPLDYTILCRMYWGPAISYFHLNPGFHTGVAIGIDPDCQWDELFKTMIRFGDVGLDLDFSAFDASLSPFMIREAGRIMSELSGTPSHFGTALMNTIIYSKHLLYNCCYHVCGSMPSGSPCTALLNSIINNVNLYYVFSKIFGKSPVFFCQALKILCYGDDVLIVFSRDVQIDNLDLIGQKIVDEFKKLGMTATSADKNVPQLKPVSELTFLKRSFNLVEDRIRPAISEKTIWSLIAWQRSNAEFEQNLENAQWFAFMHGYEFYQKFYYFVQSCLEKEMIEYRLKSYDWWRMRFYDQCFICDLS","length":2227,"molWeight":251427,"crc64":"EC983ED2A7C86349","md5":"CABB87B6FEABFB5BA0ECF5EAA74D8BC3"},"extraAttributes":{"countByCommentType":{"FUNCTION":16,"CATALYTIC ACTIVITY":3,"SUBUNIT":10,"SUBCELLULAR LOCATION":12,"DOMAIN":4,"PTM":5,"MISCELLANEOUS":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":19,"Transmembrane":2,"Domain":3,"Region":2,"Coiled coil":1,"Motif":2,"Active site":3,"Binding site":1,"Site":11,"Modified residue":1,"Disulfide bond":1,"Helix":8,"Beta strand":14,"Turn":1},"uniParcId":"UPI0000131E36"}}