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 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.
22-NOV-2017, entry version 191.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P3;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=P2;
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=Protease 2A;
Short=P2A;
EC=3.4.22.29;
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;
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;
Short=P3C;
EC=3.4.22.28;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=3D polymerase;
Short=3Dpol;
AltName: Full=Protein 3D;
Short=3D;
Human rhinovirus 14 (HRV-14).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
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].
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 OF 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).
[5]
REVIEW.
PubMed=20629045; DOI=10.1002/rmv.654;
Fuchs R., Blaas D.;
"Uncoating of human rhinoviruses.";
Rev. Med. Virol. 20:281-297(2010).
[6]
REVIEW.
PubMed=23227049; DOI=10.1155/2012/826301;
Fuchs R., Blaas D.;
"Productive entry pathways of human rhinoviruses.";
Adv. Virol. 2012:826301-826301(2012).
[7]
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).
[8]
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).
[9]
STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX
WITH ICAM1.
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).
[10]
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).
-!- 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. 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. 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- 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
cyctoplasmic calcium may trigger membrane trafficking and
transport of viral ER-associated proteins to viroplasms, sites of
viral genome replication (By similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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
(By similarity). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- 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.
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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: Protease 3C: cleaves host DDX58/RIG-I and thus
contributes to the inhibition of type I interferon production.
Cleaves also host PABPC1 (By similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000255|PROSITE-
ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the
picornavirus polyprotein.
-!- CATALYTIC ACTIVITY: 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.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- ENZYME REGULATION: RNA-directed RNA polymerase: replication or
transcription is subject to high level of random mutations by the
nucleotide analog ribavirin.
-!- SUBUNIT: Capsid protein VP1: Interacts with capsid protein VP0,
and capsid protein VP3 to form heterotrimeric protomers. Five
protomers subsequently associate to form pentamers which serve as
building blocks for the capsid. Interacts with capsid protein VP4
in the mature capsid (By similarity). Interacts with host ICAM1.
Capsid protein VP0: interacts with capsid protein VP1 and capsid
protein VP3 to form heterotrimeric protomers. Five protomers
subsequently associate to form pentamers which serve as building
blocks for the capsid. Capsid protein VP2: Interacts with capsid
protein VP1 and capsid protein VP3 in the mature capsid (By
similarity). Capsid protein VP3: interacts with capsid protein VP0
and capsid protein VP1 to form heterotrimeric protomers. Five
protomers subsequently associate to form pentamers which serve as
building blocks for the capsid. Interacts with capsid protein VP4
in the mature capsid (By similarity). Capsid protein VP4:
Interacts with capsid protein VP1 and capsid protein VP3 (By
similarity). Protein 2C: interacts with capsid protein VP3; this
interaction may be important for virion morphogenesis (By
similarity). Protein 3AB: interacts with protein 3CD (By
similarity). Viral protein genome-linked: interacts with RNA-
directed RNA polymerase (By similarity). Protein 3CD: interacts
with protein 3AB and with RNA-directed RNA polymerase. RNA-
directed RNA polymerase: interacts with viral protein genome-
linked and with protein 3CD (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP0: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP4: Virion {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP1: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- 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}. Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3CD: 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.
-!- PTM: Specific enzymatic cleavages in vivo by the viral proteases
yield a variety of precursors and mature proteins. Polyprotein
processing intermediates such as VP0 which is a VP4-VP2 precursor
are produced. During virion maturation, non-infectious particles
are rendered infectious following cleavage of VP0. This maturation
cleavage is followed by a conformational change of the particle
(By similarity). {ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
linked to the 5'-end of genomic RNA. This uridylylated form acts
as a nucleotide-peptide primer for the polymerase (By similarity).
{ECO:0000250}.
-!- PTM: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {ECO:0000250}.
-!- 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
(By similarity). {ECO:0000250}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo by
the viral proteases yield processing intermediates and the mature
proteins. {ECO:0000250}.
-!- 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 (By similarity).
{ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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.
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; -.
ProteinModelPortal; P03303; -.
SMR; P03303; -.
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; DB08017; 3-METHOXY-6-[4-(3-METHYLPHENYL)-1-PIPERAZINYL]PYRIDAZINE.
DrugBank; DB08724; 5-(5-(4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)pentyl)-3-methyl isoxazole.
DrugBank; DB08725; 5-(7-(5-hydro-4-ethyl-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DrugBank; DB08727; 5-(7-(5-hydro-4-methyl-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; AG7088.
DrugBank; DB03203; Sphingosine.
MEROPS; C03.013; -.
GeneID; 1461213; -.
KEGG; vg:1461213; -.
OrthoDB; VOG0900001E; -.
EvolutionaryTrace; P03303; -.
Proteomes; UP000007679; Genome.
Proteomes; UP000118299; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; 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: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 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; 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; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
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.
ProDom; PD001306; Peptidase_C3; 1.
ProDom; PD649346; Pico_P2B; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF89043; SSF89043; 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;
Capsid protein; Complete proteome; 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-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; Membrane; 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.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 2179 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426536.
CHAIN 2 856 P1. {ECO:0000250}.
/FTId=PRO_0000426537.
CHAIN 2 331 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426538.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426539.
CHAIN 70 331 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426540.
CHAIN 332 563 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426541.
CHAIN 564 858 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426542.
CHAIN 859 1429 P2. {ECO:0000250}.
/FTId=PRO_0000426543.
CHAIN 859 1002 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000040029.
CHAIN 1003 1099 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000040030.
CHAIN 1101 1429 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000426544.
CHAIN 1430 2179 P3. {ECO:0000250}.
/FTId=PRO_0000426545.
CHAIN 1430 1537 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426546.
CHAIN 1430 1514 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000040032.
CHAIN 1515 1537 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426547.
CHAIN 1538 2179 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426548.
CHAIN 1538 1718 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426549.
CHAIN 1719 2179 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426550.
TOPO_DOM 2 1491 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1492 1507 {ECO:0000255}.
TOPO_DOM 1508 2179 Cytoplasmic. {ECO:0000255}.
DOMAIN 1205 1361 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1538 1702 Peptidase C3.
DOMAIN 1946 2060 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 564 584 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1430 1451 Disordered. {ECO:0000250}.
ACT_SITE 876 876 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 894 894 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 965 965 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1577 1577 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1608 1608 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1683 1683 For Protease 3C activity. {ECO:0000250}.
ACT_SITE 2046 2046 For RdRp activity. {ECO:0000250}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 331 332 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 858 859 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 1002 1003 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1429 1430 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1514 1515 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1537 1538 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1719 1720 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1517 1517 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
CONFLICT 368 368 P -> L (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 459 459 I -> T (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 722 722 P -> H (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 726 727 NP -> KS (in Ref. 3). {ECO:0000305}.
CONFLICT 729 731 EWD -> RVG (in Ref. 3). {ECO:0000305}.
CONFLICT 913 913 C -> R (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 942 942 N -> S (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 962 962 P -> L (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 982 982 G -> E (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 1193 1193 L -> F (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 1193 1193 L -> H (in Ref. 2; AAA45758).
{ECO:0000305}.
CONFLICT 1220 1220 I -> T (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 1399 1399 I -> V (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 1446 1446 P -> S (in Ref. 3; AAA45756).
{ECO:0000305}.
CONFLICT 1739 1739 P -> A (in Ref. 3; AAA45756).
{ECO:0000305}.
STRAND 33 35 {ECO:0000244|PDB:1NCQ}.
HELIX 36 38 {ECO:0000244|PDB:1NCQ}.
HELIX 51 54 {ECO:0000244|PDB:1NCQ}.
STRAND 57 59 {ECO:0000244|PDB:1NCQ}.
STRAND 83 87 {ECO:0000244|PDB:1NCQ}.
STRAND 90 96 {ECO:0000244|PDB:1NCQ}.
HELIX 103 105 {ECO:0000244|PDB:1NCQ}.
HELIX 113 115 {ECO:0000244|PDB:1NCQ}.
HELIX 126 128 {ECO:0000244|PDB:1NCQ}.
STRAND 138 141 {ECO:0000244|PDB:1NCQ}.
STRAND 147 151 {ECO:0000244|PDB:1NCQ}.
HELIX 153 155 {ECO:0000244|PDB:1NCQ}.
HELIX 159 167 {ECO:0000244|PDB:1NCQ}.
STRAND 168 180 {ECO:0000244|PDB:1NCQ}.
STRAND 188 197 {ECO:0000244|PDB:1NCQ}.
HELIX 213 216 {ECO:0000244|PDB:1NCQ}.
HELIX 219 221 {ECO:0000244|PDB:1NCQ}.
HELIX 238 240 {ECO:0000244|PDB:1NCQ}.
TURN 241 243 {ECO:0000244|PDB:1NCQ}.
HELIX 247 252 {ECO:0000244|PDB:1NCQ}.
STRAND 253 259 {ECO:0000244|PDB:1NCQ}.
TURN 260 262 {ECO:0000244|PDB:1NCQ}.
STRAND 264 270 {ECO:0000244|PDB:1NCQ}.
STRAND 275 279 {ECO:0000244|PDB:1NCQ}.
STRAND 281 284 {ECO:0000244|PDB:1NCQ}.
STRAND 287 298 {ECO:0000244|PDB:1NCQ}.
STRAND 305 323 {ECO:0000244|PDB:1NCQ}.
TURN 339 342 {ECO:0000244|PDB:1NCQ}.
STRAND 354 356 {ECO:0000244|PDB:1NCQ}.
HELIX 374 377 {ECO:0000244|PDB:1NCQ}.
TURN 386 389 {ECO:0000244|PDB:1R09}.
STRAND 390 392 {ECO:0000244|PDB:1NCQ}.
HELIX 395 398 {ECO:0000244|PDB:1NCQ}.
STRAND 399 402 {ECO:0000244|PDB:1NCQ}.
STRAND 410 415 {ECO:0000244|PDB:1NCQ}.
HELIX 421 425 {ECO:0000244|PDB:1NCQ}.
HELIX 427 432 {ECO:0000244|PDB:1NCQ}.
STRAND 435 440 {ECO:0000244|PDB:1NCQ}.
STRAND 442 448 {ECO:0000244|PDB:1NCQ}.
STRAND 457 463 {ECO:0000244|PDB:1NCQ}.
HELIX 473 477 {ECO:0000244|PDB:1NCQ}.
STRAND 479 485 {ECO:0000244|PDB:1NCQ}.
STRAND 487 489 {ECO:0000244|PDB:1NCQ}.
STRAND 491 496 {ECO:0000244|PDB:1NCQ}.
STRAND 501 503 {ECO:0000244|PDB:1NCQ}.
STRAND 505 508 {ECO:0000244|PDB:1NCQ}.
STRAND 517 524 {ECO:0000244|PDB:1NCQ}.
STRAND 536 544 {ECO:0000244|PDB:1NCQ}.
STRAND 549 553 {ECO:0000244|PDB:1NCQ}.
STRAND 585 587 {ECO:0000244|PDB:1NCQ}.
HELIX 604 606 {ECO:0000244|PDB:1NCQ}.
HELIX 614 616 {ECO:0000244|PDB:1NCQ}.
HELIX 630 632 {ECO:0000244|PDB:1NCQ}.
HELIX 634 637 {ECO:0000244|PDB:1NCQ}.
STRAND 642 651 {ECO:0000244|PDB:1NCQ}.
TURN 660 664 {ECO:0000244|PDB:1NCQ}.
STRAND 665 670 {ECO:0000244|PDB:1NCQ}.
STRAND 673 676 {ECO:0000244|PDB:1R09}.
HELIX 677 683 {ECO:0000244|PDB:1NCQ}.
STRAND 686 702 {ECO:0000244|PDB:1NCQ}.
STRAND 714 720 {ECO:0000244|PDB:1NCQ}.
STRAND 722 724 {ECO:0000244|PDB:2RM2}.
STRAND 729 731 {ECO:0000244|PDB:2HWB}.
HELIX 733 736 {ECO:0000244|PDB:1NCQ}.
STRAND 738 740 {ECO:0000244|PDB:1NCQ}.
STRAND 742 746 {ECO:0000244|PDB:1NCQ}.
STRAND 749 755 {ECO:0000244|PDB:1NCQ}.
STRAND 760 766 {ECO:0000244|PDB:1NCQ}.
STRAND 772 774 {ECO:0000244|PDB:1NCQ}.
STRAND 776 778 {ECO:0000244|PDB:1NCQ}.
HELIX 782 784 {ECO:0000244|PDB:1NCQ}.
STRAND 790 795 {ECO:0000244|PDB:1NCQ}.
STRAND 804 822 {ECO:0000244|PDB:1NCQ}.
STRAND 832 834 {ECO:0000244|PDB:1NCQ}.
HELIX 1539 1551 {ECO:0000244|PDB:2B0F}.
STRAND 1552 1557 {ECO:0000244|PDB:2B0F}.
STRAND 1560 1569 {ECO:0000244|PDB:2B0F}.
STRAND 1571 1576 {ECO:0000244|PDB:2B0F}.
STRAND 1582 1586 {ECO:0000244|PDB:2B0F}.
STRAND 1589 1592 {ECO:0000244|PDB:2B0F}.
STRAND 1594 1601 {ECO:0000244|PDB:2B0F}.
TURN 1602 1604 {ECO:0000244|PDB:2B0F}.
STRAND 1605 1613 {ECO:0000244|PDB:2B0F}.
HELIX 1623 1625 {ECO:0000244|PDB:2B0F}.
STRAND 1634 1644 {ECO:0000244|PDB:2B0F}.
STRAND 1646 1663 {ECO:0000244|PDB:2B0F}.
STRAND 1666 1676 {ECO:0000244|PDB:2B0F}.
STRAND 1686 1689 {ECO:0000244|PDB:2B0F}.
STRAND 1692 1701 {ECO:0000244|PDB:2B0F}.
STRAND 1704 1709 {ECO:0000244|PDB:2B0F}.
HELIX 1712 1716 {ECO:0000244|PDB:2B0F}.
STRAND 1721 1726 {ECO:0000244|PDB:1XR5}.
HELIX 1728 1731 {ECO:0000244|PDB:1XR5}.
HELIX 1748 1750 {ECO:0000244|PDB:1XR5}.
HELIX 1773 1778 {ECO:0000244|PDB:1XR5}.
HELIX 1791 1805 {ECO:0000244|PDB:1XR5}.
HELIX 1816 1821 {ECO:0000244|PDB:1XR5}.
STRAND 1824 1826 {ECO:0000244|PDB:1XR5}.
HELIX 1839 1842 {ECO:0000244|PDB:1XR5}.
HELIX 1846 1849 {ECO:0000244|PDB:1XR5}.
TURN 1852 1855 {ECO:0000244|PDB:1XR5}.
HELIX 1858 1867 {ECO:0000244|PDB:1XR5}.
STRAND 1873 1877 {ECO:0000244|PDB:1XR5}.
HELIX 1884 1888 {ECO:0000244|PDB:1XR5}.
STRAND 1894 1897 {ECO:0000244|PDB:1XR5}.
HELIX 1900 1906 {ECO:0000244|PDB:1XR5}.
TURN 1907 1909 {ECO:0000244|PDB:1XR5}.
HELIX 1911 1919 {ECO:0000244|PDB:1XR5}.
TURN 1923 1926 {ECO:0000244|PDB:1XR5}.
HELIX 1933 1936 {ECO:0000244|PDB:1XR5}.
HELIX 1937 1939 {ECO:0000244|PDB:1XR5}.
HELIX 1940 1943 {ECO:0000244|PDB:1XR5}.
STRAND 1949 1955 {ECO:0000244|PDB:1XR5}.
HELIX 1957 1959 {ECO:0000244|PDB:1XR5}.
HELIX 1962 1975 {ECO:0000244|PDB:1XR5}.
TURN 1978 1981 {ECO:0000244|PDB:1XR5}.
HELIX 1982 1987 {ECO:0000244|PDB:1XR5}.
STRAND 1988 1992 {ECO:0000244|PDB:1XR5}.
STRAND 1994 2002 {ECO:0000244|PDB:1XR5}.
STRAND 2008 2010 {ECO:0000244|PDB:1XR5}.
HELIX 2011 2030 {ECO:0000244|PDB:1XR5}.
HELIX 2036 2038 {ECO:0000244|PDB:1XR5}.
STRAND 2040 2044 {ECO:0000244|PDB:1XR5}.
STRAND 2047 2051 {ECO:0000244|PDB:1XR5}.
HELIX 2058 2065 {ECO:0000244|PDB:1XR5}.
TURN 2066 2069 {ECO:0000244|PDB:1XR5}.
TURN 2086 2088 {ECO:0000244|PDB:1XR5}.
STRAND 2094 2098 {ECO:0000244|PDB:1XR5}.
STRAND 2100 2102 {ECO:0000244|PDB:1XR5}.
STRAND 2105 2109 {ECO:0000244|PDB:1XR5}.
HELIX 2112 2119 {ECO:0000244|PDB:1XR5}.
STRAND 2121 2124 {ECO:0000244|PDB:1XR5}.
TURN 2125 2127 {ECO:0000244|PDB:1XR5}.
HELIX 2128 2139 {ECO:0000244|PDB:1XR5}.
HELIX 2140 2142 {ECO:0000244|PDB:1XR5}.
HELIX 2144 2154 {ECO:0000244|PDB:1XR5}.
HELIX 2158 2162 {ECO:0000244|PDB:1XR5}.
HELIX 2168 2177 {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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