viHumans
Reviewed
Homo Sapiens (Human) [TaxID: 9606]
Not Available
♦Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2)
♦ Protein VP4 (P1A) (Virion protein 4)
♦ Protein VP2 (P1B) (Virion protein 2)
♦ Protein VP3 (P1C) (Virion protein 3)
♦ Protein VP1-2A (PX)
♦ Protein VP1 (P1D) (Virion protein 1)
♦ Protein 2A (P2A)
♦ Protein 2BC
♦ Protein 2B (P2B)
♦ Protein 2C (P2C) (EC 3.6.1.15)
♦ Protein 3ABCD (P3)
♦ Protein 3ABC
♦ Protein 3AB
♦ Protein 3A (P3A)
♦ Protein 3B (P3B) (VPg)
♦ Protein 3CD
♦ Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C)
♦ RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
Human Hepatitis A Virus Genotype IA (isolate H2) (HHAV) (Human Hepatitis A Virus (isolate Human/China/H2/1982))
Viruses> SsRNA Viruses> SsRNA Positive-strand Viruses> No DNA Stage> Picornavirales> Picornaviridae> Hepatovirus> Hepatovirus A> Human Hepatitis A Virus> Human Hepatitis A Virus Genotype IA (isolate H2) (HHAV) (Human Hepatitis A Virus (isolate Human/China/H2/1982))
Not Available
Various pathway(s) in which protein is involved
Not Available
Not Available
MNMSKQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQIEPLKTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHE
VAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQY
PVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDPEDWKSDPSQGGGIKITHFTTWT
SIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVTGITLKQATTA
PCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFS
TTVSTEQNVPDPQVGITTMRDLKGKANRGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTF
PITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLY
AVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDRRFESHIECRKPY
KELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKISLFYTEEHEIMKFSWRGVTADTRALRRFGFSMAAGRSVWTLEMDAGVLTGRLVRLNDEKWT
EMKDDKIVSLIEKFTSNKYWSKVSFPHGMLDLEEIAANSTDFPNMSETDLCFLLHWLNPKKINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLK
SMMFGFHHSVTVEIINTVLCFVKSGILLYVIQQLNQDEHSHIIGLLRVMNYADIGCSVISCGKVFSKMLETVFNWQMDSRMMELRTQSFSNWLRDICSGI
TIFKSFKDAIYWLYTKLKDFYEVNYGKKKDILNILKDNQQKIEKAIEEADNFCILQIQDVEKFDQYQKGVDLIQKLRTVHSMAQVDPNLGVHLSPLRDCI
ARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVS
GCPMRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDMLNVNLAKTNDAIKDMSCVDLIMDGHNISLMDLLS
SLVMTVEIRKQNMSEFMELWSQGISDDDNDSAVAEFFQSFPSGEPSNSKLSSFFQSVTNHKWVAVGAAVGILGVLVGGWFVYKHFSRKEEEPIPAEGVYH
GVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGVKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVG
FQDVVLMKVPTIPKFRDITQHFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAWRGKGEGLPGMCGGALVSSNQ
SIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIESQRIMKVEFTQCSMNVVSKTLFRKSPIHHHIDKTMINFPAVMPFSKAEVDPMAVMLSKYSLPIV
EEPEDYKEASIFYQNKIVGKTQLVDDFLDLDMAITGAPGIDAINMDSSPGFPYVQEKLTKRDLIWLDENGLLLGVHPRLAQRILFNTVMMENCSDLDVVF
TTCPKDELRPLEKVLESKTRAIDACPLDYTILCRMYWGPAISYFHLNPGFHTGVAIGIDPDRQWDELFKTMIRFGDVGLDLDFSAFDASLSPFMIREAGR
IMSELSGTPSHFGTALINTIIYSKHLLYNCCYHVCGSMPSGSPCTALLNSIINNINLYYVFSKIFGKSPVFFCQALRILCYGDDVLIVFSRDVQIDNLDL
IGQKIVDEFKKLGMTATSADKNVPQLKPVSELTFLKRSFNLVEDRIRPAISEKTIWSLIAWQRSNAEFEQNLENAQWFAFMHGYEFYQKFYYFVQSCLEK
EMIEYRLKSYDWWRMRFYDQCFICDLS
2227
Not Available
Not Available
20-03-2007
Inferred from homology
Amino Acid Count % Frequency Amino Acid Count % Frequency
Alanine (A) Leucine (L)
Arginine (R) Lysine (K)
Asparagine (N) Methionine (M)
Aspartic Acid (D) Phenylalanine (F)
Cysteine (C) Proline (P)
Glutamine (Q) Serine (S)
Glutamic Acid (E) Threonine (T)
Glycine (G) Tryptophan (W)
Histidine (H) Tyrosine (Y)
Isoleucine (I) Valine (V)
% Number of Residues in Helices % Number of Residues in Strands % Number of Residues in Coils
♦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 capsid interacts with HAVCR1 to provide virion attachment to target cell (By similarity).
♦ Protein VP0: VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, HAV VP4 does not seem to be myristoylated and has not been detected in mature virions, supposedly owing to its small size (By similarity).
♦ VP1-2A precursor is a component of immature procapsids and corresponds to an extended form of the structural protein VP1. The C-terminal domain of VP1-2A, protein 2A, acts as an assembly signal that allows multimerization of VP1-2A and formation of pentamers of VP1-VP2-VP3 trimers. It is proteolytically removed from the precursor by a host protease and does not seem to be found in mature particles (By similarity).
♦ Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability.
♦ Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
♦ Protein 3A, via its hydrophobic domain, serves as membrane anchor to the 3AB and 3ABC precursors.
♦ The 3AB precursor 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 (By similarity).
♦ The 3ABC precursor 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 (By similarity).
♦ Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer (By similarity).
♦ Protease 3C: 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. Also cleaves host proteins such as PCBP2 (By similarity).
♦ RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.
3.6.1.15  ,   3.4.22.28  ,   2.7.7.48  
GO:0003723  ;   GO:0003724  ;   GO:0003968  ;   GO:0004197  ;   GO:0005198  ;  
GO:0005216  ;   GO:0005524  ;   GO:0006351  ;   GO:0016020  ;   GO:0018144  ;  
GO:0019028  ;   GO:0019062  ;   GO:0039545  ;   GO:0039657  ;   GO:0039694  ;  
GO:0039707  ;   GO:0044162  ;   GO:0044193  ;   GO:0044385  ;   GO:0046718  ;  
GO:0051259  
♦ Protein VP2: Virion . Host cytoplasm .
♦ Protein VP3: Virion . Host cytoplasm .
♦ Protein VP1: Virion . Host cytoplasm .
♦ Protein VP1-2A: Virion . Host cytoplasm .
♦ Protein 2B: Host cytoplasmic vesicle membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Note=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 (By similarity). .
♦ Protein 2C: Host cytoplasmic vesicle membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Note=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. May associate with membranes through a N-terminal amphipathic helix (By similarity). .
♦ Protein 3ABC: Host cytoplasmic vesicle membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Host mitochondrion outer membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Note=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 (By similarity). .
♦ Protein 3AB: Host cytoplasmic vesicle membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Note=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 (By similarity). .
♦ Protein 3A: Host cytoplasmic vesicle membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Note=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 (By similarity). .
♦ Protein 3B: Virion .
♦ Protease 3C: Host cytoplasm .
♦ RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Note=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 (By similarity). .
♦DOMAIN 1204 1366 SF3 helicase.
♦ DOMAIN 1520 1716 Peptidase C3.
♦ DOMAIN 1976 2097 RdRp catalytic.
Not Available
Predicted/Modelled
Not Available
♦ACT_SITE 1563 1563 For protease 3C activity.
♦ ACT_SITE 1603 1603 For protease 3C activity.
♦ ACT_SITE 1691 1691 For protease 3C activity.
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.
Not Available
Virtual screening has been performed using RASPD
  • Million Molecules

Best 20 Hit molecules

    Not Available