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 POLG_BOVEV              Reviewed;        2175 AA.
P12915;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 171.
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;
Bovine enterovirus (strain VG-5-27) (BEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus.
NCBI_TaxID=12065;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2828511; DOI=10.1099/0022-1317-69-2-253;
Earle J.A.P., Skuce R.A., Fleming C.S., Hoey E.M., Martin S.J.;
"The complete nucleotide sequence of a bovine enterovirus.";
J. Gen. Virol. 69:253-263(1988).
[2]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-840.
PubMed=7773791; DOI=10.1038/nsb0395-224;
Smyth M., Tate J., Hoey E.M., Lyons C., Martin S.J., Stuart D.;
"Implications for viral uncoating from the structure of bovine
enterovirus.";
Nat. Struct. Biol. 2:224-231(1995).
-!- 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 cell receptor 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). 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 uridylated 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}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1bev";
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EMBL; D00214; BAA24003.1; ALT_SEQ; Genomic_RNA.
PIR; A29824; GNNYBE.
RefSeq; NP_045756.1; NC_001859.1.
PDB; 1BEV; X-ray; 3.00 A; 1=560-840, 2=70-317, 3=318-559, 4=2-69.
PDBsum; 1BEV; -.
ProteinModelPortal; P12915; -.
SMR; P12915; -.
DrugBank; DB08231; MYRISTIC ACID.
MEROPS; C03.014; -.
PRIDE; P12915; -.
GeneID; 1493914; -.
KEGG; vg:1493914; -.
OrthoDB; VOG0900001E; -.
EvolutionaryTrace; P12915; -.
Proteomes; UP000006566; 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: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; 1.10.10.870; -; 1.
Gene3D; 2.60.120.20; -; 3.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
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; IPR002527; Pico_P2B.
InterPro; IPR001676; Picornavirus_capsid.
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.
PRINTS; PR00918; CALICVIRUSNS.
ProDom; PD001306; Peptidase_C3; 1.
ProDom; PD649346; Pico_P2B; 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 RNA replication; Virion; Virus endocytosis by host;
Virus entry into host cell.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 2175 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426107.
CHAIN 2 840 P1. {ECO:0000250}.
/FTId=PRO_0000426108.
CHAIN 2 317 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426109.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426110.
CHAIN 70 317 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426111.
CHAIN 318 557 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426112.
CHAIN 557 840 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426113.
CHAIN 841 1419 P2. {ECO:0000250}.
/FTId=PRO_0000426114.
CHAIN 841 990 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000039463.
CHAIN 991 1089 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000039464.
CHAIN 1090 1419 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039465.
CHAIN 1420 2175 P3. {ECO:0000250}.
/FTId=PRO_0000426115.
CHAIN 1420 1531 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426116.
CHAIN 1420 1508 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039466.
CHAIN 1509 1531 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426117.
CHAIN 1532 2175 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426118.
CHAIN 1532 1713 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426119.
CHAIN 1714 2175 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426120.
TOPO_DOM 2 1485 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1486 1501 {ECO:0000255}.
TOPO_DOM 1502 2175 Cytoplasmic. {ECO:0000255}.
DOMAIN 1194 1352 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1532 1697 Peptidase C3.
DOMAIN 1941 2056 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 557 574 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1420 1443 Disordered. {ECO:0000250}.
ACT_SITE 861 861 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 879 879 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 950 950 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1571 1571 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1602 1602 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1678 1678 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 2042 2042 For RdRp activity. {ECO:0000250}.
SITE 317 318 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 840 841 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 990 991 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1419 1420 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1508 1509 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1531 1532 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1714 1715 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1511 1511 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 33 35 {ECO:0000244|PDB:1BEV}.
HELIX 36 38 {ECO:0000244|PDB:1BEV}.
HELIX 51 54 {ECO:0000244|PDB:1BEV}.
STRAND 57 59 {ECO:0000244|PDB:1BEV}.
STRAND 78 81 {ECO:0000244|PDB:1BEV}.
STRAND 83 87 {ECO:0000244|PDB:1BEV}.
STRAND 90 96 {ECO:0000244|PDB:1BEV}.
HELIX 103 105 {ECO:0000244|PDB:1BEV}.
TURN 113 115 {ECO:0000244|PDB:1BEV}.
HELIX 126 128 {ECO:0000244|PDB:1BEV}.
STRAND 147 151 {ECO:0000244|PDB:1BEV}.
HELIX 153 155 {ECO:0000244|PDB:1BEV}.
HELIX 159 167 {ECO:0000244|PDB:1BEV}.
STRAND 168 180 {ECO:0000244|PDB:1BEV}.
STRAND 187 197 {ECO:0000244|PDB:1BEV}.
STRAND 203 205 {ECO:0000244|PDB:1BEV}.
HELIX 209 212 {ECO:0000244|PDB:1BEV}.
HELIX 215 217 {ECO:0000244|PDB:1BEV}.
HELIX 224 226 {ECO:0000244|PDB:1BEV}.
TURN 227 230 {ECO:0000244|PDB:1BEV}.
HELIX 234 238 {ECO:0000244|PDB:1BEV}.
STRAND 239 245 {ECO:0000244|PDB:1BEV}.
TURN 246 248 {ECO:0000244|PDB:1BEV}.
STRAND 250 256 {ECO:0000244|PDB:1BEV}.
STRAND 261 263 {ECO:0000244|PDB:1BEV}.
TURN 267 269 {ECO:0000244|PDB:1BEV}.
STRAND 273 289 {ECO:0000244|PDB:1BEV}.
STRAND 294 309 {ECO:0000244|PDB:1BEV}.
TURN 325 328 {ECO:0000244|PDB:1BEV}.
STRAND 340 342 {ECO:0000244|PDB:1BEV}.
STRAND 356 359 {ECO:0000244|PDB:1BEV}.
HELIX 361 364 {ECO:0000244|PDB:1BEV}.
HELIX 382 384 {ECO:0000244|PDB:1BEV}.
STRAND 386 389 {ECO:0000244|PDB:1BEV}.
STRAND 397 402 {ECO:0000244|PDB:1BEV}.
HELIX 410 413 {ECO:0000244|PDB:1BEV}.
HELIX 415 420 {ECO:0000244|PDB:1BEV}.
STRAND 423 428 {ECO:0000244|PDB:1BEV}.
STRAND 430 436 {ECO:0000244|PDB:1BEV}.
STRAND 445 451 {ECO:0000244|PDB:1BEV}.
STRAND 453 455 {ECO:0000244|PDB:1BEV}.
HELIX 461 464 {ECO:0000244|PDB:1BEV}.
STRAND 467 473 {ECO:0000244|PDB:1BEV}.
STRAND 475 477 {ECO:0000244|PDB:1BEV}.
STRAND 479 484 {ECO:0000244|PDB:1BEV}.
STRAND 489 491 {ECO:0000244|PDB:1BEV}.
STRAND 493 495 {ECO:0000244|PDB:1BEV}.
TURN 499 502 {ECO:0000244|PDB:1BEV}.
HELIX 503 506 {ECO:0000244|PDB:1BEV}.
STRAND 510 517 {ECO:0000244|PDB:1BEV}.
STRAND 527 537 {ECO:0000244|PDB:1BEV}.
STRAND 542 546 {ECO:0000244|PDB:1BEV}.
HELIX 600 602 {ECO:0000244|PDB:1BEV}.
HELIX 610 613 {ECO:0000244|PDB:1BEV}.
HELIX 626 628 {ECO:0000244|PDB:1BEV}.
HELIX 630 634 {ECO:0000244|PDB:1BEV}.
STRAND 638 641 {ECO:0000244|PDB:1BEV}.
TURN 647 649 {ECO:0000244|PDB:1BEV}.
STRAND 651 655 {ECO:0000244|PDB:1BEV}.
HELIX 662 668 {ECO:0000244|PDB:1BEV}.
STRAND 671 685 {ECO:0000244|PDB:1BEV}.
STRAND 699 705 {ECO:0000244|PDB:1BEV}.
STRAND 714 716 {ECO:0000244|PDB:1BEV}.
HELIX 718 721 {ECO:0000244|PDB:1BEV}.
STRAND 723 725 {ECO:0000244|PDB:1BEV}.
STRAND 727 731 {ECO:0000244|PDB:1BEV}.
STRAND 737 741 {ECO:0000244|PDB:1BEV}.
STRAND 746 752 {ECO:0000244|PDB:1BEV}.
STRAND 756 759 {ECO:0000244|PDB:1BEV}.
HELIX 765 767 {ECO:0000244|PDB:1BEV}.
HELIX 772 774 {ECO:0000244|PDB:1BEV}.
STRAND 778 785 {ECO:0000244|PDB:1BEV}.
STRAND 792 807 {ECO:0000244|PDB:1BEV}.
STRAND 818 820 {ECO:0000244|PDB:1BEV}.
SEQUENCE 2175 AA; 242504 MW; 44FCADE8704E48FD CRC64;
MGAQLSRNTA GSHTTGTYAT GGSTINYNNI NYYSHAASAA QNKQDFTQDP SKFTQPIADV
IKETAVPLKS PSAEACGYSD RVAQLTLGNS TITTQEAANI CVAYGCWPAK LSDTDATSVD
KPTEPGVSAD AFYTLRSKPW QADSKGWYWK LPDALNNTGM FGQNAQFHYI YRGGWAVHVQ
CNATKFHQGT LLVLAIPEHQ IATQEQPAFD RTMPGSEGGT FQEPFWLEDG TSLGNSLIYP
HQWINLRTNN SATLILPYVN AIPMDSAIRH SNWTLAIIPV APLKYAAETT PLVPITVTIA
PMETEYNGLR RAIASNQGLP TKPGPGSYQF MTTDEDCSPC ILPDFQPTLE IFIPGKVNNL
LEIAQVESIL EANNREGVEG VERYVIPVSV QDALDAQIYA LRLELGGSGP LSSSLLGTLA
KHYTQWSGSV EITCMFTGTF MTTGKVLLAY TPPGGDMPRN REEAMLGTHV VWDFGLQSSI
TLVIPWISAS HFRGVSNDDV LNYQYYAAGH VTIWYQTNMV IPPGFPNTAG IIMMIAAQPN
FSFRIQKDRE DMTQTAILQN DPGKMLKDAI DKQVAGALVA GTTTSTHSVA TDSTPALQAA
ETGATSTARD ESMIETRTIV PTHGIHETSV ESFFGRSSLV GMPLLATGTS ITNWRIDFRE
FVQLRAKMSW FTYMRFDVEF TIIATSSTGQ NVTTEQHTTY QVMYVPPGAP VPSNQDSFQW
QSGCNPSVFA DTDGPPAQFS VPFMSSANAY STVYDGYARF MDTDPDRYGI LPSNFLGFMY
FRTLEDAAHQ VRFRICAKIK HTSCWIPRAP RQAPYKKRYN LVFSGDSDRI CSNRASLTSY
GPFGQQQGAA YVGSYKILNR HLATYADWEN EVWQSYQRDL LVTRVDAHGC DTIARCNCRS
GIYYCKSTAK HYPIVVTPPS IYKIEANDYY PERMQTHILL GIGFAEPGDC GGLLRCEHGV
MGILTVGGGD HVGFADVRDL LWIEDDAMEQ GITDYVQQLG NAFGAGFTAE IANYTNQLRD
MLMGSDSVVE KIIRSLVRLV SALVIVVRNH QDLITVGATL ALLGCEGSPW KWLKRKVCQI
LGINMAERQS DNWMKKFTEM CNAFRGLDWI AAKISKFIDW LKQKILPELK ERAEFVKKLK
QLPLLEAQVN TLEHSSASQE RQEQLFGNVQ YLAHHCRKNA PLYAAEAKRV YHLEKRVLGA
MQFKTKNRIE PVCALIHGSP GTGQSLATMI VGRKLAEYEG SDVYSLPPDP DHFDGYQQQA
VVVMDDLLQN PDGKDMTLFC QMVSTAPFTV PMAALEDKGK LFTSKFVLAS TNAGQVTPPT
VADYKALQRR FFFDCDIEVQ KEYKRDGVTL DVAKATETCE DCSPANFKKC MPLICGKALQ
LKSRKGDGMR YSLDTLISEL RRESNRRYNI GNVLEALFQG PVCYKPLRIE VHEEEPAPSA
ISDLLQAVDS EEVREYCRSK GWIVEERVTE LKLERNVNRA LAVIQSVSLI AAVAGTIYIV
YRLFSGMQGP YSGIGTNYAT KKPVVRQVQT QGPLFDFGVS LLKKNIRTVK TGAGEFTALG
VYDTVVVLPR HAMPGKTIEM NGKDIEVLDA YDLNDKTDTS LELTIVKLKM NEKFRDIRAM
VPDQITDYNE AVVVVNTSYY PQLFTCVGRV KDYGFLNLAG RPTHRVLMYE FPTKAGQCGG
VVISMGKIVG VHVGGNGAQG FAASLLRRYF TAEQGQIEYI EKSKDAGYPV INAPTQTKLE
PSVFFDVFPG VKEPAVLHKK DKRLETNFEE ALFSKYIGNV QRDMPEELLI AIDHYSEQLK
MLNIDPRPIS MEDAIYGTEG LEALDLGTSA SYPYVAMGIK KRDILNKETR DVTKMQECID
KYGLNLPMVT YVKDELRAPD KIRKGKSRLI EASSLNDSVA MRCYFGNLYK VFHTNPGTIS
GCAVGCDPET FWSKIPVMMD GELFGFDYTA YDASLSPMWF HALAEVLRRI GFVECKHFID
QLCCSHHLYM DKHYYVVGGM PSGCSGTSIF NSMINNLIIR TLVLTVYKNI DLDDLKIIAY
GDDVLASYPY EIDASLLAEA GKSFGLIMTP PDKSAEFVKL TWDNVTFLKR KFVRDARYPF
LVHPVMDMSN IHESIRWTKD PRHTEDHVRS LCLLAWHCGE EEYNEFVTKI RSVPVGRALH
LPSFKALERK WYDSF


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