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Genome polyprotein [Cleaved into: 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); P2; Protease 2A (P2A) (EC 3 4 22 29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3 6 1 15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3 4 22 28); Protease 3C (EC 3 4 22 28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2 7 7 48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

 POLG_HRV14              Reviewed;        2179 AA.
P03303; Q82083; Q82123; Q84736; Q84737; Q84738; Q84739; Q84740; Q84741;
Q84774; Q84775; Q84776; Q84777; Q84778; Q84779; Q89441; Q89649; Q89763;
Q89883;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
17-JUN-2020, entry version 209.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P1;
Contains:
RecName: Full=Capsid protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Capsid protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Capsid protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Capsid protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Capsid protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=P2;
Contains:
RecName: Full=Protease 2A;
Short=P2A;
EC=3.4.22.29 {ECO:0000250|UniProtKB:P03300};
AltName: Full=Picornain 2A;
AltName: Full=Protein 2A;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15 {ECO:0000250|UniProtKB:P03300};
Contains:
RecName: Full=P3;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Viral protein genome-linked;
Short=VPg;
AltName: Full=Protein 3B;
Short=P3B;
Contains:
RecName: Full=Protein 3CD;
EC=3.4.22.28;
Contains:
RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
Contains:
RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
Short=RdRp;
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=3D polymerase;
Short=3Dpol;
AltName: Full=Protein 3D;
Short=3D;
Human rhinovirus 14 (HRV-14).
Viruses; Riboviria; Picornavirales; Picornaviridae; Enterovirus.
NCBI_TaxID=12131;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6093056; DOI=10.1093/nar/12.20.7859;
Stanway G., Hughes P.J., Mountford R.C., Minor P.D., Almond J.W.;
"The complete nucleotide sequence of a common cold virus: human rhinovirus
14.";
Nucleic Acids Res. 12:7859-7875(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEOLYTIC CLEAVAGE (CAPSID PROTEIN
VP0).
PubMed=8383233;
Lee W.M., Monroe S., Rueckert R.R.;
"Role of maturation cleavage in infectivity of picornaviruses: activation
of an infectosome.";
J. Virol. 67:2110-2122(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2983312; DOI=10.1073/pnas.82.3.732;
Callahan P.L., Mizutani S., Colonno R.J.;
"Molecular cloning and complete sequence determination of RNA genome of
human rhinovirus type 14.";
Proc. Natl. Acad. Sci. U.S.A. 82:732-736(1985).
[4]
FUNCTION (PROTEIN 3A), AND INTERACTION WITH HOST GBF1 (PROTEIN 3A).
PubMed=17005635; DOI=10.1128/jvi.01225-06;
Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L.,
Melchers W.J., van Kuppeveld F.J.;
"Effects of picornavirus 3A Proteins on Protein Transport and GBF1-
dependent COP-I recruitment.";
J. Virol. 80:11852-11860(2006).
[5]
FUNCTION (PROTEASE 3C).
PubMed=18572216; DOI=10.1016/j.virol.2008.05.019;
de Breyne S., Bonderoff J.M., Chumakov K.M., Lloyd R.E., Hellen C.U.;
"Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C
proteases.";
Virology 378:118-122(2008).
[6]
REVIEW.
PubMed=20629045; DOI=10.1002/rmv.654;
Fuchs R., Blaas D.;
"Uncoating of human rhinoviruses.";
Rev. Med. Virol. 20:281-297(2010).
[7]
REVIEW.
PubMed=23227049; DOI=10.1155/2012/826301;
Fuchs R., Blaas D.;
"Productive entry pathways of human rhinoviruses.";
Adv. Virol. 2012:826301-826301(2012).
[8]
FUNCTION (PROTEIN 3A).
PubMed=30755512; DOI=10.1128/mbio.02742-18;
Lyoo H., van der Schaar H.M., Dorobantu C.M., Rabouw H.H.,
Strating J.R.P.M., van Kuppeveld F.J.M.;
"ACBD3 is an essential pan-enterovirus host factor that mediates the
interaction between viral 3A protein and cellular protein PI4KB.";
MBio 10:0-0(2019).
[9]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=2993920; DOI=10.1038/317145a0;
Rossman M.G., Arnold E., Erickson J.W., Frankenberger E.A., Griffith J.P.,
Hecht H.-J., Johnson J.E., Kamer G., Luo M., Mosser A.G., Rueckert R.R.,
Sherry B., Vriend G.;
"Structure of a human common cold virus and functional relationship to
other picornaviruses.";
Nature 317:145-153(1985).
[10]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=2856083; DOI=10.1107/s0108767387011875;
Arnold E., Rossman M.G.;
"The use of molecular-replacement phases for the refinement of the human
rhinovirus 14 structure.";
Acta Crystallogr. A 44:270-282(1988).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=2156077; DOI=10.1016/0022-2836(90)90076-x;
Arnold E., Rossman M.G.;
"Analysis of the structure of a common cold virus, human rhinovirus 14,
refined at a resolution of 3.0 A.";
J. Mol. Biol. 211:763-801(1990).
[12]
STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH
ICAM1, FUNCTION (CAPSID PROTEIN VP1), AND INTERACTION WITH HOST ICAM1
(CAPSID PROTEIN VP1).
PubMed=10562537; DOI=10.1093/emboj/18.22.6249;
Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.;
"Structural studies of two rhinovirus serotypes complexed with fragments of
their cellular receptor.";
EMBO J. 18:6249-6259(1999).
[13]
FUNCTION (PROTEASE 2A).
PubMed=12163599; DOI=10.1128/jvi.76.17.8787-8796.2002;
Gustin K.E., Sarnow P.;
"Inhibition of nuclear import and alteration of nuclear pore complex
composition by rhinovirus.";
J. Virol. 76:8787-8796(2002).
[14] {ECO:0000244|PDB:5W3E, ECO:0000244|PDB:5W3L, ECO:0000244|PDB:5W3M, ECO:0000244|PDB:5W3O}
STRUCTURE BY ELECTRON MICROSCOPY (2.26 ANGSTROMS) OF 2-856, AND FUNCTION
(CAPSID PROTEIN VP1).
PubMed=28696310; DOI=10.1073/pnas.1707369114;
Dong Y., Liu Y., Jiang W., Smith T.J., Xu Z., Rossmann M.G.;
"Antibody-induced uncoating of human rhinovirus B14.";
Proc. Natl. Acad. Sci. U.S.A. 114:8017-8022(2017).
[15] {ECO:0000244|PDB:6HLT}
X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 1430-1485, INTERACTION WITH HOST
ACBD3 (PROTEIN 3A), AND FUNCTION (PROTEIN 3A).
PubMed=31381608; DOI=10.1371/journal.ppat.1007962;
Horova V., Lyoo H., Rozycki B., Chalupska D., Smola M., Humpolickova J.,
Strating J.R.P.M., van Kuppeveld F.J.M., Boura E., Klima M.;
"Convergent evolution in the mechanisms of ACBD3 recruitment to
picornavirus replication sites.";
PLoS Pathog. 15:E1007962-E1007962(2019).
-!- FUNCTION: [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 (By similarity). Capsid
protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1
interacts with host ICAM1 to provide virion attachment to target host
cells (PubMed:10562537). This attachment induces virion internalization
(By similarity). Tyrosine kinases are probably involved in the entry
process. After binding to its receptor, the capsid undergoes
conformational changes (By similarity). Capsid protein VP1 N-terminus
(that contains an amphipathic alpha-helix) and capsid protein VP4 are
externalized (Probable). Together, they shape a pore in the host
membrane through which viral genome is translocated to host cell
cytoplasm (PubMed:28696310). After genome has been released, the
channel shrinks. {ECO:0000250|UniProtKB:P03300,
ECO:0000269|PubMed:10562537, ECO:0000269|PubMed:28696310,
ECO:0000305|PubMed:28696310}.
-!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). 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). {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). 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). {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
shell (By similarity). After binding to the host receptor, the capsid
undergoes conformational changes (By similarity). 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 (By similarity).
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
is cleaved into capsid proteins VP4 and VP2 after maturation (By
similarity). Allows the capsid to remain inactive before the maturation
step (By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral
polyprotein and specific host proteins (By similarity). It is
responsible for the autocatalytic cleavage between the P1 and P2
regions, which is the first cleavage occurring in the polyprotein (By
similarity). Cleaves also the host translation initiation factor
EIF4G1, in order to shut down the capped cellular mRNA translation (By
similarity). Inhibits the host nucleus-cytoplasm protein and RNA
trafficking by cleaving host members of the nuclear pores including
NUP62 and NUP153 (Probable). Counteracts stress granule formation
probably by antagonizing its assembly or promoting its dissassembly (By
similarity). {ECO:0000250|UniProtKB:P03300,
ECO:0000250|UniProtKB:P03301, ECO:0000305|PubMed:12163599}.
-!- FUNCTION: [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 cytoplasmic calcium
may trigger membrane trafficking and transport of viral ER-associated
proteins to viroplasms, sites of viral genome replication.
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [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. {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [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.
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protein 3A]: Localizes the viral replication complex to the
surface of membranous vesicles (By similarity). It inhibits host cell
endoplasmic reticulum-to-Golgi apparatus transport and causes the
disassembly of the Golgi complex, possibly through GBF1 interaction
(PubMed:17005635). This would result in depletion of MHC, trail
receptors and IFN receptors at the host cell surface (PubMed:17005635).
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 (Probable). {ECO:0000250|UniProtKB:P03300,
ECO:0000269|PubMed:17005635, ECO:0000305|PubMed:30755512,
ECO:0000305|PubMed:31381608}.
-!- FUNCTION: [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 (By
similarity). 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 (By
similarity). Following genome release from the infecting virion in the
cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
similarity). 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 (By similarity).
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protein 3CD]: 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. Protein 3CD binds to the
5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
processing of the polyprotein (By similarity). Cleaves host EIF5B,
contributing to host translation shutoff (PubMed:18572216). Cleaves
also host PABPC1, contributing to host translation shutoff (By
similarity). {ECO:0000250|UniProtKB:P03300,
ECO:0000269|PubMed:18572216}.
-!- FUNCTION: [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. {ECO:0000250|UniProtKB:P03300}.
-!- CATALYTIC ACTIVITY: [Protein 2C]:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Evidence={ECO:0000250|UniProtKB:P03300};
-!- CATALYTIC ACTIVITY: [Protease 2A]:
Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300};
-!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
-!- CATALYTIC ACTIVITY: [Protease 3C]:
Reaction=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.; EC=3.4.22.28;
Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
-!- COFACTOR: [RNA-directed RNA polymerase]:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P03300};
Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
center (By similarity). The magnesium ions are not prebound but only
present for catalysis (By similarity). Requires the presence of 3CDpro
or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300,
ECO:0000250|UniProtKB:P03313};
-!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Replication or
transcription is subject to high level of random mutations by the
nucleotide analog ribavirin. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
capsid protein VP3 to form heterotrimeric protomers.
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
capsid protein VP3 to form heterotrimeric protomers (By similarity).
Five protomers subsequently associate to form pentamers which serve as
building blocks for the capsid (By similarity). Interacts with capsid
protein VP2, capsid protein VP3 and capsid protein VP4 following
cleavage of capsid protein VP0 (By similarity). Interacts with host
ICAM1 (PubMed:10562537). {ECO:0000250|UniProtKB:P03300,
ECO:0000269|PubMed:10562537}.
-!- SUBUNIT: [Capsid protein VP2]: Interacts with capsid protein VP1 and
capsid protein VP3 in the mature capsid.
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
capsid protein VP1 to form heterotrimeric protomers (By similarity).
Five protomers subsequently associate to form pentamers which serve as
building blocks for the capsid (By similarity). Interacts with capsid
protein VP4 in the mature capsid (By similarity). Interacts with
protein 2C; this interaction may be important for virion morphogenesis
(By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP4]: Interacts with capsid protein VP1 and
capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protease 2A]: Homodimer. {ECO:0000250|UniProtKB:P04936}.
-!- SUBUNIT: [Protein 2C]: Homohexamer; forms a hexameric ring structure
with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).
Interacts (via N-terminus) with host RTN3 (via reticulon domain); this
interaction is important for viral replication (By similarity).
Interacts with capsid protein VP3; this interaction may be important
for virion morphogenesis (By similarity).
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protein 3AB]: Interacts with protein 3CD.
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
GBF1 (PubMed:17005635). Interacts (via GOLD domain) with host ACBD3
(via GOLD domain); this interaction allows the formation of a viral
protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will
stimulate the recruitment of host PI4KB in order to synthesize PI4P at
the viral RNA replication sites (PubMed:31381608).
{ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:17005635,
ECO:0000269|PubMed:31381608}.
-!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
polymerase. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protein 3CD]: Interacts with protein 3AB and with RNA-
directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with Viral protein
genome-linked and with protein 3CD. {ECO:0000250|UniProtKB:P03300}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.
-!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm
{ECO:0000250|UniProtKB:Q66478}.
-!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.
-!- SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm
{ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
vesicle membrane {ECO:0000305}; Peripheral membrane protein
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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: [Protein 2C]: The N-terminus has membrane-binding (By
similarity). The N-terminus also displays RNA-binding properties (By
similarity). The N-terminus is involved in oligomerization (By
similarity). The central part contains an ATPase domain and a C4-type
zinc-finger (By similarity). The C-terminus is involved in RNA-binding
(By similarity). The extreme C-terminus contains a region involved in
oligomerization (By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
viral proteases yield processing intermediates and the mature proteins.
{ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
of pentamers during virus assembly. Further assembly of 12 pentamers
and a molecule of genomic RNA generates the provirion.
{ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Capsid protein VP0]: 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 it is followed by a conformational
change infectious virion. {ECO:0000269|PubMed:8383233}.
-!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
encapsidation and formation of the mature virus particle.
{ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Viral protein genome-linked]: VPg is uridylylated by the
polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for
the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-!- CAUTION: The PDB data bank contains the 3D-structure coordinates of
proteins VP1, VP2, VP3 and VP4. {ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=4rhv";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2r04";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2r06";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2r07";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2rm2";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2rmu";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2rr1";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2rs1";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2rs3";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2rs5";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2hwb";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2hwc";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1vrh";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1rmu";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ruc";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1rud";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1rue";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ruf";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1rug";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ruh";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1rui";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ruj";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1rvf";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1r08";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1r09";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ncq";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1na1";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1k5m";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1d3i";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure complexed with antiviral compound SCH 38057;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1hri";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure complexed with antiviral compound SDZ 35-682;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1hrv";
---------------------------------------------------------------------------
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EMBL; X01087; CAA25565.1; -; Genomic_RNA.
EMBL; L05355; AAA45758.1; -; Genomic_RNA.
EMBL; K02121; AAA45756.1; -; Genomic_RNA.
PIR; A03901; GNNYH4.
RefSeq; NP_041009.1; NC_001490.1.
PDB; 1D3I; EM; 26.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1HRI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1HRV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1K5M; X-ray; 2.70 A; A=568-856, B=70-331, C=332-567, D=2-69.
PDB; 1NA1; X-ray; 3.30 A; A=568-856, B=70-331, C=332-567, D=2-69.
PDB; 1NCQ; X-ray; 2.50 A; A=568-856, B=70-331, C=332-567, D=2-69.
PDB; 1R08; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1R09; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUC; X-ray; 3.10 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUD; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUE; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUF; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUG; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RUJ; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1RVF; X-ray; 4.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1VRH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 1XR5; X-ray; 2.80 A; A=1720-2179.
PDB; 2B0F; NMR; -; A=1538-1719.
PDB; 2HWB; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2HWC; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2IN2; NMR; -; A=1538-1719.
PDB; 2R04; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2R06; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2R07; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2RM2; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2RR1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2RS1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2RS3; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 2RS5; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 4PDW; X-ray; 3.00 A; A=568-856, B=70-331, C=332-567.
PDB; 4RHV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
PDB; 5W3E; EM; 2.53 A; A=568-856, B=332-567, C=70-331, D=2-69.
PDB; 5W3L; EM; 2.71 A; A=568-856, B=332-567, C=70-331, D=2-69.
PDB; 5W3M; EM; 2.26 A; A=568-856, B=332-567, C=70-331, D=2-69.
PDB; 5W3O; EM; 3.01 A; A=568-856, B=332-567, C=70-331.
PDB; 6HLT; X-ray; 2.81 A; B/D=1430-1485.
PDBsum; 1D3I; -.
PDBsum; 1HRI; -.
PDBsum; 1HRV; -.
PDBsum; 1K5M; -.
PDBsum; 1NA1; -.
PDBsum; 1NCQ; -.
PDBsum; 1R08; -.
PDBsum; 1R09; -.
PDBsum; 1RMU; -.
PDBsum; 1RUC; -.
PDBsum; 1RUD; -.
PDBsum; 1RUE; -.
PDBsum; 1RUF; -.
PDBsum; 1RUG; -.
PDBsum; 1RUH; -.
PDBsum; 1RUI; -.
PDBsum; 1RUJ; -.
PDBsum; 1RVF; -.
PDBsum; 1VRH; -.
PDBsum; 1XR5; -.
PDBsum; 2B0F; -.
PDBsum; 2HWB; -.
PDBsum; 2HWC; -.
PDBsum; 2IN2; -.
PDBsum; 2R04; -.
PDBsum; 2R06; -.
PDBsum; 2R07; -.
PDBsum; 2RM2; -.
PDBsum; 2RMU; -.
PDBsum; 2RR1; -.
PDBsum; 2RS1; -.
PDBsum; 2RS3; -.
PDBsum; 2RS5; -.
PDBsum; 4PDW; -.
PDBsum; 4RHV; -.
PDBsum; 5W3E; -.
PDBsum; 5W3L; -.
PDBsum; 5W3M; -.
PDBsum; 5W3O; -.
PDBsum; 6HLT; -.
SMR; P03303; -.
IntAct; P03303; 1.
ChEMBL; CHEMBL4295564; -.
DrugBank; DB08725; (S)-5-(7-(4-(4-Ethyl-4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methylisoxazole.
DrugBank; DB08543; 1-[2-HYDROXY-3-(4-CYCLOHEXYL-PHENOXY)-PROPYL]-4-(2-PYRIDYL)-PIPERAZINE.
DrugBank; DB08509; 1-[6-(2-CHLORO-4-METHYXYPHENOXY)-HEXYL]-IMIDAZOLE.
DrugBank; DB08540; 2-[4-(2H-1,4-BENZOTHIAZINE-3-YL)-PIPERAZINE-1-LY]-1,3-THIAZOLE-4-CARBOXYLIC ACID ETHYLESTER.
DrugBank; DB08017; 3-METHOXY-6-[4-(3-METHYLPHENYL)-1-PIPERAZINYL]PYRIDAZINE.
DrugBank; DB08727; 3-Methyl-5-(7-{4-[(4R)-4-methyl-4,5-dihydro-1,3-oxazol-2-yl]phenoxy}heptyl)-1,2-oxazole.
DrugBank; DB08728; 5-(3-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)propyl)-3-methyl isoxazole.
DrugBank; DB08723; 5-(5-(2,6-DICHLORO-4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE.
DrugBank; DB08721; 5-(5-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)pentyl)-3-(hydroxyethyl oxymethyleneoxymethyl) isoxazole.
DrugBank; DB08720; 5-(5-(4-(4,5-dihydro-2-oxazoly)phenoxy)pentyl)-3-methyl osoxazole.
DrugBank; DB08724; 5-(5-(4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)pentyl)-3-methyl isoxazole.
DrugBank; DB08719; 5-(5-(6-CHLORO-4-(4,5-DIHYDRO-2-OXAZOLYL)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE.
DrugBank; DB08726; 5-(7-(4-(4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DrugBank; DB08722; 5-(7-(6-chloro-4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DrugBank; DB05102; Rupintrivir.
DrugBank; DB03203; Sphingosine.
MEROPS; C03.013; -.
PRIDE; P03303; -.
ABCD; P03303; 3 sequenced antibodies.
GeneID; 1461213; -.
KEGG; vg:1461213; -.
EvolutionaryTrace; P03303; -.
Proteomes; UP000007679; Genome.
Proteomes; UP000118299; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
GO; GO:0039664; P:lysis of host organelle involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; ISS:UniProtKB.
GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 1.10.10.870; -; 1.
Gene3D; 2.60.120.20; -; 3.
Gene3D; 3.30.70.270; -; 1.
Gene3D; 4.10.80.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014838; P3A.
InterPro; IPR036203; P3A_soluble_dom.
InterPro; IPR000081; Peptidase_C3.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR003138; Pico_P1A.
InterPro; IPR036988; Pico_P1A_sf.
InterPro; IPR002527; Pico_P2B.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
Pfam; PF08727; P3A; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF02226; Pico_P1A; 1.
Pfam; PF00947; Pico_P2A; 1.
Pfam; PF01552; Pico_P2B; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF89043; SSF89043; 1.
PROSITE; PS51874; PCV_3C_PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Autocatalytic cleavage; Capsid protein; Covalent protein-RNA linkage;
DNA replication; Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
Host cytoplasmic vesicle; Host gene expression shutoff by virus;
Host membrane; Host mRNA suppression by virus; Host nucleus;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host mRNA nuclear export by virus;
Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
Ion channel; Ion transport; Lipoprotein; Magnesium; Membrane;
Metal-binding; Myristate; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Pore-mediated penetration of viral genome into host cell;
Protease; Repeat; RNA-binding; RNA-directed RNA polymerase;
T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
Transport; Viral attachment to host cell; Viral immunoevasion;
Viral ion channel; Viral penetration into host cytoplasm;
Viral penetration via lysis of host organellar membrane;
Viral RNA replication; Virion; Virus endocytosis by host;
Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1
/note="Removed; by host"
/evidence="ECO:0000250|UniProtKB:P03300"
CHAIN 2..2179
/note="Genome polyprotein"
/id="PRO_0000426536"
CHAIN 2..856
/note="P1"
/id="PRO_0000426537"
CHAIN 2..331
/note="Capsid protein VP0"
/id="PRO_0000426538"
CHAIN 2..69
/note="Capsid protein VP4"
/id="PRO_0000426539"
CHAIN 70..331
/note="Capsid protein VP2"
/id="PRO_0000426540"
CHAIN 332..563
/note="Capsid protein VP3"
/id="PRO_0000426541"
CHAIN 564..856
/note="Capsid protein VP1"
/id="PRO_0000426542"
CHAIN 857..1429
/note="P2"
/id="PRO_0000426543"
CHAIN 857..1002
/note="Protease 2A"
/id="PRO_0000040029"
CHAIN 1003..1099
/note="Protein 2B"
/id="PRO_0000040030"
CHAIN 1100..1429
/note="Protein 2C"
/id="PRO_0000426544"
CHAIN 1430..2179
/note="P3"
/id="PRO_0000426545"
CHAIN 1430..1537
/note="Protein 3AB"
/id="PRO_0000426546"
CHAIN 1430..1514
/note="Protein 3A"
/id="PRO_0000040032"
CHAIN 1515..1537
/note="Viral protein genome-linked"
/id="PRO_0000426547"
CHAIN 1538..2179
/note="Protein 3CD"
/id="PRO_0000426548"
CHAIN 1538..1719
/note="Protease 3C"
/id="PRO_0000426549"
CHAIN 1720..2179
/note="RNA-directed RNA polymerase"
/id="PRO_0000426550"
TOPO_DOM 2..1491
/note="Cytoplasmic"
/evidence="ECO:0000255"
INTRAMEM 1492..1507
/evidence="ECO:0000255"
TOPO_DOM 1508..2179
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 1205..1361
/note="SF3 helicase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
DOMAIN 1538..1715
/note="Peptidase C3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
DOMAIN 1946..2060
/note="RdRp catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
ZN_FING 1369..1386
/note="C4-type"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 564..584
/note="Amphipatic alpha-helix"
/evidence="ECO:0000255"
REGION 1101..1239
/note="Oligomerization"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1101..1173
/note="Membrane-binding"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1122..1126
/note="RNA-binding"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1413..1420
/note="RNA-binding"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1424..1429
/note="Oligomerization"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1430..1451
/note="Disordered"
/evidence="ECO:0000250"
ACT_SITE 876
/note="For protease 2A activity"
/evidence="ECO:0000250|UniProtKB:P03300"
ACT_SITE 894
/note="For protease 2A activity"
/evidence="ECO:0000250|UniProtKB:P03300"
ACT_SITE 965
/note="For protease 2A activity"
/evidence="ECO:0000250|UniProtKB:P03300"
ACT_SITE 1577
/note="For protease 3C activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
ACT_SITE 1608
/note="For protease 3C activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
ACT_SITE 1683
/note="For protease 3C activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
METAL 911
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 913
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 971
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 973
/note="Zinc; via pros nitrogen; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 1369
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1372
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1381
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1386
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1952
/note="Magnesium 1; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1952
/note="Magnesium 2; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 2046
/note="Magnesium 1; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 2046
/note="Magnesium 2; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
SITE 69..70
/note="Cleavage; by autolysis"
/evidence="ECO:0000305|PubMed:8383233"
SITE 331..332
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 856..857
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1002..1003
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1099..1100
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1125
/note="Involved in the interaction with host RTN3"
/evidence="ECO:0000250|UniProtKB:Q66478"
SITE 1429..1430
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1514..1515
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1537..1538
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1719..1720
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
MOD_RES 1517
/note="O-(5'-phospho-RNA)-tyrosine"
/evidence="ECO:0000250|UniProtKB:P03300"
LIPID 2
/note="N-myristoyl glycine; by host"
/evidence="ECO:0000250|UniProtKB:P03300"
CONFLICT 368
/note="P -> L (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 459
/note="I -> T (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 722
/note="P -> H (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 726..727
/note="NP -> KS (in Ref. 3)"
/evidence="ECO:0000305"
CONFLICT 729..731
/note="EWD -> RVG (in Ref. 3)"
/evidence="ECO:0000305"
CONFLICT 913
/note="C -> R (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 942
/note="N -> S (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 962
/note="P -> L (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 982
/note="G -> E (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 1193
/note="L -> F (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 1193
/note="L -> H (in Ref. 2; AAA45758)"
/evidence="ECO:0000305"
CONFLICT 1220
/note="I -> T (in Ref. 2 and 3)"
/evidence="ECO:0000305"
CONFLICT 1399
/note="I -> V (in Ref. 2 and 3)"
/evidence="ECO:0000305"
CONFLICT 1446
/note="P -> S (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
CONFLICT 1739
/note="P -> A (in Ref. 3; AAA45756)"
/evidence="ECO:0000305"
STRAND 33..35
/evidence="ECO:0000244|PDB:1NCQ"
HELIX 36..38
/evidence="ECO:0000244|PDB:5W3M"
HELIX 51..54
/evidence="ECO:0000244|PDB:5W3M"
STRAND 57..59
/evidence="ECO:0000244|PDB:5W3M"
STRAND 83..87
/evidence="ECO:0000244|PDB:5W3M"
STRAND 90..96
/evidence="ECO:0000244|PDB:5W3M"
STRAND 100..102
/evidence="ECO:0000244|PDB:5W3O"
HELIX 103..105
/evidence="ECO:0000244|PDB:5W3M"
TURN 113..115
/evidence="ECO:0000244|PDB:5W3M"
HELIX 126..129
/evidence="ECO:0000244|PDB:5W3M"
STRAND 138..140
/evidence="ECO:0000244|PDB:5W3M"
STRAND 147..151
/evidence="ECO:0000244|PDB:5W3M"
HELIX 153..155
/evidence="ECO:0000244|PDB:5W3M"
HELIX 159..167
/evidence="ECO:0000244|PDB:5W3M"
STRAND 168..180
/evidence="ECO:0000244|PDB:5W3M"
STRAND 188..197
/evidence="ECO:0000244|PDB:5W3M"
STRAND 203..205
/evidence="ECO:0000244|PDB:5W3M"
HELIX 213..216
/evidence="ECO:0000244|PDB:5W3M"
HELIX 219..221
/evidence="ECO:0000244|PDB:5W3M"
HELIX 225..227
/evidence="ECO:0000244|PDB:1K5M"
HELIX 238..240
/evidence="ECO:0000244|PDB:5W3M"
TURN 241..243
/evidence="ECO:0000244|PDB:5W3M"
HELIX 247..252
/evidence="ECO:0000244|PDB:5W3M"
STRAND 253..259
/evidence="ECO:0000244|PDB:5W3M"
TURN 260..262
/evidence="ECO:0000244|PDB:5W3M"
STRAND 264..270
/evidence="ECO:0000244|PDB:5W3M"
STRAND 275..279
/evidence="ECO:0000244|PDB:5W3M"
STRAND 281..284
/evidence="ECO:0000244|PDB:5W3M"
STRAND 287..298
/evidence="ECO:0000244|PDB:5W3M"
STRAND 307..323
/evidence="ECO:0000244|PDB:5W3M"
TURN 339..342
/evidence="ECO:0000244|PDB:5W3M"
STRAND 354..356
/evidence="ECO:0000244|PDB:5W3M"
STRAND 368..373
/evidence="ECO:0000244|PDB:5W3E"
HELIX 374..377
/evidence="ECO:0000244|PDB:5W3M"
TURN 386..389
/evidence="ECO:0000244|PDB:1R09"
STRAND 390..392
/evidence="ECO:0000244|PDB:5W3M"
HELIX 395..398
/evidence="ECO:0000244|PDB:5W3M"
STRAND 399..402
/evidence="ECO:0000244|PDB:5W3M"
STRAND 410..415
/evidence="ECO:0000244|PDB:5W3M"
HELIX 421..423
/evidence="ECO:0000244|PDB:5W3M"
HELIX 427..432
/evidence="ECO:0000244|PDB:5W3M"
STRAND 435..440
/evidence="ECO:0000244|PDB:5W3M"
STRAND 442..448
/evidence="ECO:0000244|PDB:5W3M"
STRAND 455..463
/evidence="ECO:0000244|PDB:5W3M"
STRAND 471..473
/evidence="ECO:0000244|PDB:5W3M"
HELIX 474..477
/evidence="ECO:0000244|PDB:5W3M"
STRAND 479..485
/evidence="ECO:0000244|PDB:5W3M"
STRAND 487..489
/evidence="ECO:0000244|PDB:5W3M"
STRAND 491..496
/evidence="ECO:0000244|PDB:5W3M"
STRAND 501..503
/evidence="ECO:0000244|PDB:5W3M"
STRAND 505..508
/evidence="ECO:0000244|PDB:5W3M"
STRAND 509..512
/evidence="ECO:0000244|PDB:1K5M"
STRAND 517..527
/evidence="ECO:0000244|PDB:5W3M"
STRAND 536..544
/evidence="ECO:0000244|PDB:5W3M"
STRAND 549..553
/evidence="ECO:0000244|PDB:5W3M"
STRAND 557..559
/evidence="ECO:0000244|PDB:5W3M"
HELIX 580..582
/evidence="ECO:0000244|PDB:1K5M"
STRAND 585..587
/evidence="ECO:0000244|PDB:5W3M"
HELIX 604..606
/evidence="ECO:0000244|PDB:5W3M"
HELIX 614..616
/evidence="ECO:0000244|PDB:5W3M"
HELIX 630..632
/evidence="ECO:0000244|PDB:5W3M"
HELIX 634..637
/evidence="ECO:0000244|PDB:5W3M"
STRAND 642..651
/evidence="ECO:0000244|PDB:5W3M"
TURN 660..664
/evidence="ECO:0000244|PDB:5W3M"
STRAND 665..670
/evidence="ECO:0000244|PDB:5W3M"
STRAND 673..676
/evidence="ECO:0000244|PDB:5W3M"
HELIX 677..683
/evidence="ECO:0000244|PDB:5W3M"
STRAND 686..702
/evidence="ECO:0000244|PDB:5W3M"
STRAND 714..719
/evidence="ECO:0000244|PDB:5W3M"
STRAND 722..724
/evidence="ECO:0000244|PDB:2RM2"
STRAND 729..731
/evidence="ECO:0000244|PDB:2HWB"
HELIX 733..736
/evidence="ECO:0000244|PDB:5W3M"
STRAND 738..740
/evidence="ECO:0000244|PDB:5W3M"
STRAND 742..746
/evidence="ECO:0000244|PDB:5W3M"
STRAND 749..755
/evidence="ECO:0000244|PDB:5W3M"
STRAND 760..766
/evidence="ECO:0000244|PDB:5W3M"
STRAND 772..774
/evidence="ECO:0000244|PDB:5W3M"
STRAND 776..778
/evidence="ECO:0000244|PDB:5W3M"
STRAND 780..782
/evidence="ECO:0000244|PDB:1RUE"
HELIX 784..786
/evidence="ECO:0000244|PDB:5W3M"
STRAND 790..795
/evidence="ECO:0000244|PDB:5W3M"
STRAND 804..822
/evidence="ECO:0000244|PDB:5W3M"
STRAND 832..834
/evidence="ECO:0000244|PDB:1NCQ"
HELIX 1446..1455
/evidence="ECO:0000244|PDB:6HLT"
HELIX 1459..1467
/evidence="ECO:0000244|PDB:6HLT"
STRAND 1470..1473
/evidence="ECO:0000244|PDB:6HLT"
STRAND 1479..1482
/evidence="ECO:0000244|PDB:6HLT"
HELIX 1539..1551
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1552..1557
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1560..1569
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1571..1576
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1582..1586
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1589..1592
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1594..1601
/evidence="ECO:0000244|PDB:2B0F"
TURN 1602..1604
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1605..1613
/evidence="ECO:0000244|PDB:2B0F"
HELIX 1623..1625
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1634..1644
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1646..1663
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1666..1676
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1686..1689
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1692..1701
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1704..1709
/evidence="ECO:0000244|PDB:2B0F"
HELIX 1712..1716
/evidence="ECO:0000244|PDB:2B0F"
STRAND 1721..1726
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1728..1731
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1748..1750
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1773..1778
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1791..1805
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1816..1821
/evidence="ECO:0000244|PDB:1XR5"
STRAND 1824..1826
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1839..1842
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1846..1849
/evidence="ECO:0000244|PDB:1XR5"
TURN 1852..1855
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1858..1867
/evidence="ECO:0000244|PDB:1XR5"
STRAND 1873..1877
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1884..1888
/evidence="ECO:0000244|PDB:1XR5"
STRAND 1894..1897
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1900..1906
/evidence="ECO:0000244|PDB:1XR5"
TURN 1907..1909
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1911..1919
/evidence="ECO:0000244|PDB:1XR5"
TURN 1923..1926
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1933..1936
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1937..1939
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1940..1943
/evidence="ECO:0000244|PDB:1XR5"
STRAND 1949..1955
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1957..1959
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1962..1975
/evidence="ECO:0000244|PDB:1XR5"
TURN 1978..1981
/evidence="ECO:0000244|PDB:1XR5"
HELIX 1982..1987
/evidence="ECO:0000244|PDB:1XR5"
STRAND 1988..1992
/evidence="ECO:0000244|PDB:1XR5"
STRAND 1994..2002
/evidence="ECO:0000244|PDB:1XR5"
STRAND 2008..2010
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2011..2030
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2036..2038
/evidence="ECO:0000244|PDB:1XR5"
STRAND 2040..2044
/evidence="ECO:0000244|PDB:1XR5"
STRAND 2047..2051
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2058..2065
/evidence="ECO:0000244|PDB:1XR5"
TURN 2066..2069
/evidence="ECO:0000244|PDB:1XR5"
TURN 2086..2088
/evidence="ECO:0000244|PDB:1XR5"
STRAND 2094..2098
/evidence="ECO:0000244|PDB:1XR5"
STRAND 2100..2102
/evidence="ECO:0000244|PDB:1XR5"
STRAND 2105..2109
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2112..2119
/evidence="ECO:0000244|PDB:1XR5"
STRAND 2121..2124
/evidence="ECO:0000244|PDB:1XR5"
TURN 2125..2127
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2128..2139
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2140..2142
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2144..2154
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2158..2162
/evidence="ECO:0000244|PDB:1XR5"
HELIX 2168..2177
/evidence="ECO:0000244|PDB:1XR5"
SEQUENCE 2179 AA; 242991 MW; 827201A3032F0285 CRC64;
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP SKFTEPVKDL
MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA VVCYAEWPEY LPDVDASDVN
KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ
CNATKFHSGC LLVVVIPEHQ LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY
NMNGTLLGNL LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP
TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPNYE
PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI PLNANRQNEQ VFGTNLFIGD
GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG PALSSAKLIL AYTPPGARGP QDRREAMLGT
HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS
FISACPDFKL RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI
LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ NKDATGIDNH
REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPDSANYS SNLVVQAMYV
PPGAPNPKEW DDYTWQSASN PSVFFKVGDT SRFSVPYVGL ASAYNCFYDG YSHDDAETQY
GITVLNHMGS MAFRIVNEHD EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK
NTEPVIKKRK GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST
GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ AGVMKGVGPA
EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE EQGLSDYITG LGRAFGVGFT
DQISTKVTEL QEVAKDFLTT KVLSKVVKMV SALVIICRNH DDLVTVTATL ALLGCDGSPW
RFLKMYISKH FQVPYIERQA NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA
KEKLEFCSKL KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR
IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF NSAVYSLPPD
PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL PPMASLDNKG MLFTSNFVLA
STNSNTLSPP TILNPEALVR RFGFDLDICL HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK
CCPLVCGKAI SLVDRTTNIR YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV
CNTPPPECIN DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL
GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK NIMTITTSKG
EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV DPENINLELT VLTLDRNEKF
RDIRGFISED LEGVDATLVV HSNNFTNTIL EVGPVTMAGL INLSSTPTNR MIRYDYATKT
GQCGGVLCAT GKIFGIHVGG NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT
KSKLHPSVFY DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY
AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL NKETQDTEKM
KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL NDSVNMRMKL GNLYKAFHQN
PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA FDYSNFDASL SPVWFVCLEK VLTKLGFAGS
SLIQSICNTH HIFRDEIYVV EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK
ILAYGDDLIV SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ
QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF IQKIRTTDIG
KCLILPEYSV LRRRWLDLF


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orb81838 Rubella RSVP (TM) Antigen (HPV77) protein Rubella RSVP (TM) (Strain HPV77) >90 percent Viral Protein, Capsid-Free is an infectious disease antigen_toxin. For research use only. 1 mg
EIAAB35746 A34.5,Antisense to ERCC-1 protein,ASE1,ASE-1,CAST,CAST,CD3EAP,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Homo sapiens,Human,PAF49,RNA polymerase
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
AB2A242 Polyclonal Antibodies: Anti-Capsid protein VP1(Middle residues) Polyclonal Antibody; Specificity: Anti-Capsid protein VP1(Middle residues) Polyclonal Antibody ; Application: IHC 0.1mg
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
orb82441 Rubella Virus Capsid, recombinant protein Rubella Capsid (C), Recombinant is an infectious disease antigen_toxin. For research use only. 1 mg
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
EIAAB45903 ERVK6,HERV-K(C7) Pro protein,HERV-K(HML-2.HOM) Pro protein,HERV-K_7p22.1 provirus ancestral Pro protein,HERV-K108 Pro protein,Homo sapiens,Human,PR,Protease,Proteinase
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
Pathways :
WP1663: Homologous recombination
WP1694: Pyrimidine metabolism
WP2199: Seed Development
WP1672: Mismatch repair
WP1693: Purine metabolism
WP1438: Influenza A virus infection
WP1644: DNA replication
WP2203: TSLP Signaling Pathway
WP1049: G Protein Signaling Pathways
WP1657: Glycerolipid metabolism
WP2292: Chemokine signaling pathway
WP1371: G Protein Signaling Pathways
WP1714: Tyrosine metabolism
WP1502: Mitochondrial biogenesis
WP1892: Protein folding
WP1673: Naphthalene and anthracene degradation
WP2371: Parkinsons Disease Pathway
WP1678: Nucleotide excision repair
WP1613: 1,4-Dichlorobenzene degradation
WP1909: Signal regulatory protein (SIRP) family interactions
WP1625: Base excision repair
WP210: Cytoplasmic Ribosomal Proteins
WP1690: Propanoate metabolism
WP73: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways

Related Genes :

Bibliography :
[30443749] Structural disorder in the proteome and interactome of Alkhurma virus (ALKV).
[29541253] Toll-like receptor 9 activation by CpG oligodeoxynucleotide 7909 enhances the radiosensitivity of A549 lung cancer cells via the p53 signaling pathway.
[27273223] First isolation of West Nile virus from a dromedary camel.
[18807167] Role of genetic recombination in the molecular architecture of Papaya ringspot virus.
[14698672] An adenine-to-guanine nucleotide change in the IRES SL-IV domain of picornavirus/hepatitis C chimeric viruses leads to a nonviable phenotype.
[7503676] Evaluation of complete genome sequences and sequences of individual gene products for the classification of hepatitis C viruses.