Reviewed
Homo Sapiens (Human) [TaxID: 9606]
Not Available
♦Genome polyprotein [Cleaved into: P3
♦ Protein 3AB
♦ P2
♦ P1
♦ Capsid protein VP0 (VP4-VP2)
♦ Capsid protein VP4 (P1A) (Virion protein 4)
♦ Capsid protein VP2 (P1B) (Virion protein 2)
♦ Capsid protein VP3 (P1C) (Virion protein 3)
♦ Capsid protein VP1 (P1D) (Virion protein 1)
♦ Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A)
♦ Protein 2B (P2B)
♦ Protein 2C (P2C) (EC 3.6.1.15)
♦ Protein 3A (P3A)
♦ Viral protein genome-linked (VPg) (Protein 3B) (P3B)
♦ Protein 3CD (EC 3.4.22.28)
♦ Protease 3C (P3C) (EC 3.4.22.28)
♦ RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
♦ Protein 3AB
♦ P2
♦ P1
♦ Capsid protein VP0 (VP4-VP2)
♦ Capsid protein VP4 (P1A) (Virion protein 4)
♦ Capsid protein VP2 (P1B) (Virion protein 2)
♦ Capsid protein VP3 (P1C) (Virion protein 3)
♦ Capsid protein VP1 (P1D) (Virion protein 1)
♦ Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A)
♦ Protein 2B (P2B)
♦ Protein 2C (P2C) (EC 3.6.1.15)
♦ Protein 3A (P3A)
♦ Viral protein genome-linked (VPg) (Protein 3B) (P3B)
♦ Protein 3CD (EC 3.4.22.28)
♦ Protease 3C (P3C) (EC 3.4.22.28)
♦ RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
Human Rhinovirus 2 (HRV-2)
Viruses> SsRNA Viruses> SsRNA Positive-strand Viruses> No DNA Stage> Picornavirales> Picornaviridae> Enterovirus> Rhinovirus A> Human Rhinovirus 2 (HRV-2)
Not Available
Various pathway(s) in which protein is involved
Not Available
Not Available
MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASNGASKLEFTQDPSKFTDPVKDVLEKGIPTLQSPTVEACGYSDRIIQITRGDSTITSQDVANA
IVAYGVWPHYLSSKDASAIDKPSQPDTSSNRFYTLRSVTWSSSSKGWWWKLPDALKDMGIFGENMFYHYLGRSGYTIHVQCNASKFHQGTLIVALIPEHQ
IASALHGNVNVGYNYTHPGETGREVKAETRLNPDLQPTEEYWLNFDGTLLGNITIFPHQFINLRSNNSATIIAPYVNAVPMDSMRSHNNWSLVIIPICPL
ETSSAINTIPITISISPMCAEFSGARAKRQGLPVFITPGSGQFLTTDDFQSPCALPWYHPTKEISIPGEVKNLVEICQVDSLVPINNTDTYINSENMYSV
VLQSSINAPDKIFSIRTDVASQPLATTLIGEISSYFTHWTGSLRFSFMFCGTANTTVKLLLAYTPPGIAEPTTRKDAMLGTHVIWDVGLQSTISMVVPWI
SASHYRNTSPGRSTSGYITCWYQTRLVIPPQTPPTARLLCFVSGCKDFCLRMARDTNLHLQSGAIAQNPVENYIDEVLNEVLVVPNINSSNPTTSNSAPA
LDAAETGHTSSVQPEDVIETRYVQTSQTRDEMSLESFLGRSGCIHESKLEVTLANYNKENFTVWAINLQEMAQIRRKFELFTYTRFDSEITLVPCISALS
QDIGHITMQYMYVPPGAPVPNSRDDYAWQSGTNASVFWQHGQAYPRFSLPFLSVASAYYMFYDGYDEQDQNYGTANTNNMGSLCSRIVTEKHIHKVHIMT
RIYHKAKHVKAWCPRPPRALEYTRAHRTNFKIEDRSIQTAIVTRPIITTAGPSDMYVHVGNLIYRNLHLFNSEMHESILVSYSSDLIIYRTNTVGDDYIP
SCDCTQATYYCKHKNRYFPITVTSHDWYEIQESEYYPKHIQYNLLIGEGPCEPGDCGGKLLCKHGVIGIVTAGGDNHVAFIDLRHFHCAEEQGVTDYIHM
LGEAFGNGFVDSVKEHIHAINPVGNISKKIIKWMLRIISAMVIIIRNSSDPQTILATLTLIGCSGSPWRFLKEKFCKWTQLNYIHKESDSWLKKFTEACN
AARGLEWIGNKISKFIEWMKSMLPQAQLKVKYLNELKKLNLYEKQVESLRVADMKTQEKIKMEIDTLHDLSRKFLPLYASEAKRIKTLYIKCDNIIKQKK
RCEPVAIVIHGPPGAGKSITTNFLAKMITNDSDIYSLPPDPKYFDGYDQQSVVIMDDIMQNPAGDDMTLFCQMVSSVTFIPPMADLPDKGKAFDSRFVLC
STNHSLLTPPTITSLPAMNRRFFLDLDIIVHDNFKDPQGKLNVAAAFRPCDVDNRIGNARCCPFVCGKAVSFKDRNSCNKYSLAQVYNIMIEEDRRRRQV
VDVMTAIFQGPIDMKNPPPPAITDLLQSVRTPEVIKYCEGNRWIIPAECKIEKELNLANTIITIIANVIGMARIIYVIYKLFCTLQGPYSGEPKPKTKIP
ERRVVTQGPEEEFGMSLIKHNSCVITTENGKFTGLGVYDRFVVVPTHADPGKEIQVDGITTKVIDSYDLYNKNGIKLEITVLKLDRNEKFRDIRRYIPNN
EDDYPNCNLALLANQPEPTIINVGDVVSYGNILLSGNQTARMLKYSYPTKSGYCGGVLYKIGQVLGIHVGGNGRDGFSAMLLRSYFTDVQGQITLSKKTS
ECNLPSIHTPCKTKLQPSVFYDVFPGSKEPAVLSEKDARLQVDFNEALFSKYKGNTDCSINDHIRIASSHYAAQLITLDIDPKPITLEDSVFGTDGLEAL
DLNTSAGFPYIAMGVKKRDLINNKTKDISKLKEAIDKYGVDLPMVTFLKDELRKHEKVIKGKTRVIEASSVNDTLLFRTTFGNLFSKFHLNPGIVTGSAV
GCDPEVFWSKIPAMLDDKCIMAFDYTNYDGSIHPIWFEALKQVLVDLSFNPTLIDRLCKSKHIFKNTYYEVEGGVPSGCSGTSIFNTMINNIIIRTLVLD
AYKNIDLDKLKIIAYGDDVIFSYIHELDMEAIAIEGVKYGLTITPADKSNTFVKLDYSNVTFLKRGFKQDEKYNFLIHPTFPEDEIFESIRWTKKPSQMH
EHVLSLCHLMWHNGRDAYKKFVEKIRSVSAGRALYIPPYDLLLHEWYEKF
IVAYGVWPHYLSSKDASAIDKPSQPDTSSNRFYTLRSVTWSSSSKGWWWKLPDALKDMGIFGENMFYHYLGRSGYTIHVQCNASKFHQGTLIVALIPEHQ
IASALHGNVNVGYNYTHPGETGREVKAETRLNPDLQPTEEYWLNFDGTLLGNITIFPHQFINLRSNNSATIIAPYVNAVPMDSMRSHNNWSLVIIPICPL
ETSSAINTIPITISISPMCAEFSGARAKRQGLPVFITPGSGQFLTTDDFQSPCALPWYHPTKEISIPGEVKNLVEICQVDSLVPINNTDTYINSENMYSV
VLQSSINAPDKIFSIRTDVASQPLATTLIGEISSYFTHWTGSLRFSFMFCGTANTTVKLLLAYTPPGIAEPTTRKDAMLGTHVIWDVGLQSTISMVVPWI
SASHYRNTSPGRSTSGYITCWYQTRLVIPPQTPPTARLLCFVSGCKDFCLRMARDTNLHLQSGAIAQNPVENYIDEVLNEVLVVPNINSSNPTTSNSAPA
LDAAETGHTSSVQPEDVIETRYVQTSQTRDEMSLESFLGRSGCIHESKLEVTLANYNKENFTVWAINLQEMAQIRRKFELFTYTRFDSEITLVPCISALS
QDIGHITMQYMYVPPGAPVPNSRDDYAWQSGTNASVFWQHGQAYPRFSLPFLSVASAYYMFYDGYDEQDQNYGTANTNNMGSLCSRIVTEKHIHKVHIMT
RIYHKAKHVKAWCPRPPRALEYTRAHRTNFKIEDRSIQTAIVTRPIITTAGPSDMYVHVGNLIYRNLHLFNSEMHESILVSYSSDLIIYRTNTVGDDYIP
SCDCTQATYYCKHKNRYFPITVTSHDWYEIQESEYYPKHIQYNLLIGEGPCEPGDCGGKLLCKHGVIGIVTAGGDNHVAFIDLRHFHCAEEQGVTDYIHM
LGEAFGNGFVDSVKEHIHAINPVGNISKKIIKWMLRIISAMVIIIRNSSDPQTILATLTLIGCSGSPWRFLKEKFCKWTQLNYIHKESDSWLKKFTEACN
AARGLEWIGNKISKFIEWMKSMLPQAQLKVKYLNELKKLNLYEKQVESLRVADMKTQEKIKMEIDTLHDLSRKFLPLYASEAKRIKTLYIKCDNIIKQKK
RCEPVAIVIHGPPGAGKSITTNFLAKMITNDSDIYSLPPDPKYFDGYDQQSVVIMDDIMQNPAGDDMTLFCQMVSSVTFIPPMADLPDKGKAFDSRFVLC
STNHSLLTPPTITSLPAMNRRFFLDLDIIVHDNFKDPQGKLNVAAAFRPCDVDNRIGNARCCPFVCGKAVSFKDRNSCNKYSLAQVYNIMIEEDRRRRQV
VDVMTAIFQGPIDMKNPPPPAITDLLQSVRTPEVIKYCEGNRWIIPAECKIEKELNLANTIITIIANVIGMARIIYVIYKLFCTLQGPYSGEPKPKTKIP
ERRVVTQGPEEEFGMSLIKHNSCVITTENGKFTGLGVYDRFVVVPTHADPGKEIQVDGITTKVIDSYDLYNKNGIKLEITVLKLDRNEKFRDIRRYIPNN
EDDYPNCNLALLANQPEPTIINVGDVVSYGNILLSGNQTARMLKYSYPTKSGYCGGVLYKIGQVLGIHVGGNGRDGFSAMLLRSYFTDVQGQITLSKKTS
ECNLPSIHTPCKTKLQPSVFYDVFPGSKEPAVLSEKDARLQVDFNEALFSKYKGNTDCSINDHIRIASSHYAAQLITLDIDPKPITLEDSVFGTDGLEAL
DLNTSAGFPYIAMGVKKRDLINNKTKDISKLKEAIDKYGVDLPMVTFLKDELRKHEKVIKGKTRVIEASSVNDTLLFRTTFGNLFSKFHLNPGIVTGSAV
GCDPEVFWSKIPAMLDDKCIMAFDYTNYDGSIHPIWFEALKQVLVDLSFNPTLIDRLCKSKHIFKNTYYEVEGGVPSGCSGTSIFNTMINNIIIRTLVLD
AYKNIDLDKLKIIAYGDDVIFSYIHELDMEAIAIEGVKYGLTITPADKSNTFVKLDYSNVTFLKRGFKQDEKYNFLIHPTFPEDEIFESIRWTKKPSQMH
EHVLSLCHLMWHNGRDAYKKFVEKIRSVSAGRALYIPPYDLLLHEWYEKF
2150
Not Available
Not Available
23-01-2007
Evidence at protein level
| 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 protein VP1: 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. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host VLDLR to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).
♦ Capsid protein VP2: 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 (By similarity).
♦ Capsid protein VP3: 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 (By similarity).
♦ Capsid protein VP4: 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. After genome has been released, the channel shrinks (By similarity).
♦ Capsid protein VP0: 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 (By similarity).
♦ Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).
♦ Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).
♦ Protein 2C: 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 (By similarity).
♦ Protein 3AB: 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 (By similarity).
♦ Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly 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 (By similarity).
♦ Viral protein genome-linked: 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. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).
♦ Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).
♦ Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).
♦ RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated (By similarity).
♦ Capsid protein VP2: 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 (By similarity).
♦ Capsid protein VP3: 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 (By similarity).
♦ Capsid protein VP4: 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. After genome has been released, the channel shrinks (By similarity).
♦ Capsid protein VP0: 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 (By similarity).
♦ Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).
♦ Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).
♦ Protein 2C: 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 (By similarity).
♦ Protein 3AB: 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 (By similarity).
♦ Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly 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 (By similarity).
♦ Viral protein genome-linked: 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. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).
♦ Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).
♦ Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).
♦ RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated (By similarity).
3.4.22.29 , 3.6.1.15 , 3.4.22.28 , 3.4.22.28 , 2.7.7.48
GO:0003723 ; GO:0003724 ; GO:0003968 ; GO:0004197 ; GO:0005198 ;
GO:0005216 ; GO:0005524 ; GO:0006260 ; GO:0006351 ; GO:0016020 ;
GO:0018144 ; GO:0019062 ; GO:0039520 ; GO:0039522 ; GO:0039540 ;
GO:0039611 ; GO:0039618 ; GO:0039657 ; GO:0039690 ; GO:0039694 ;
GO:0039707 ; GO:0044162 ; GO:0044385 ; GO:0044694 ; GO:0051259 ;
GO:0075509
GO:0005216 ; GO:0005524 ; GO:0006260 ; GO:0006351 ; GO:0016020 ;
GO:0018144 ; GO:0019062 ; GO:0039520 ; GO:0039522 ; GO:0039540 ;
GO:0039611 ; GO:0039618 ; GO:0039657 ; GO:0039690 ; GO:0039694 ;
GO:0039707 ; GO:0044162 ; GO:0044385 ; GO:0044694 ; GO:0051259 ;
GO:0075509
♦ Capsid protein VP0: Virion . Host cytoplasm .
♦ Capsid protein VP4: Virion .
♦ Capsid protein VP2: Virion . Host cytoplasm .
♦ Capsid protein VP3: Virion . Host cytoplasm .
♦ Capsid protein VP1: 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.
♦ 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.
♦ 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.
♦ 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.
♦ Viral protein genome-linked: Virion . Host cytoplasm .
♦ Protease 3C: Host cytoplasm .
♦ Protein 3CD: 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.
♦ RNA-directed RNA polymerase: 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.
♦ Capsid protein VP4: Virion .
♦ Capsid protein VP2: Virion . Host cytoplasm .
♦ Capsid protein VP3: Virion . Host cytoplasm .
♦ Capsid protein VP1: 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.
♦ 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.
♦ 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.
♦ 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.
♦ Viral protein genome-linked: Virion . Host cytoplasm .
♦ Protease 3C: Host cytoplasm .
♦ Protein 3CD: 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.
♦ RNA-directed RNA polymerase: 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.
♦DOMAIN 1181 1343 SF3 helicase.
♦ DOMAIN 1508 1673 Peptidase C3.
♦ DOMAIN 1918 2031 RdRp catalytic.
♦ DOMAIN 1508 1673 Peptidase C3.
♦ DOMAIN 1918 2031 RdRp catalytic.
Not Available
X-ray crystallography (14)
♦ACT_SITE 868 868 For Protease 2A activity.
♦ ACT_SITE 885 885 For Protease 2A activity.
♦ ACT_SITE 956 956 For Protease 2A activity.
♦ ACT_SITE 1547 1547 For Protease 3C activity.
♦ ACT_SITE 1578 1578 For Protease 3C activity.
♦ ACT_SITE 1654 1654 For Protease 3C activity.
♦ ACT_SITE 2017 2017 For RdRp activity.
♦ ACT_SITE 885 885 For Protease 2A activity.
♦ ACT_SITE 956 956 For Protease 2A activity.
♦ ACT_SITE 1547 1547 For Protease 3C activity.
♦ ACT_SITE 1578 1578 For Protease 3C activity.
♦ ACT_SITE 1654 1654 For Protease 3C activity.
♦ ACT_SITE 2017 2017 For RdRp activity.
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.