Protein VP0
     (VP4-VP2)
Protein VP4
     (Virion protein 4)
     (P1A)
Protein VP2
     (Virion protein 2)
     (P1B)
Protein VP3
     (Virion protein 3)
     (P1C)
Protein VP1
     (Virion protein 1)
     (P1D)
Picornain 2A
     (Protein 2A)
     (P2A)
     (EC 3.4.22.29)
Protein 2B
     (P2B)
Protein 2C
     (P2C)
     (EC 3.6.1.15)
Protein 3A
     (P3A)
Protein 3B
     (P3B)
     (VPg)
Picornain 3C
     (EC 3.4.22.28)
     (Protease 3C)
     (P3C)
RNA-directed RNA polymerase 3D-POL
     (P3D-POL)
     (EC 2.7.7.48)

Gene name

None

From

Human rhinovirus 14 (HRV-14)

[TaxID: 12131]

Taxonomy

Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; Picornaviridae; Rhinovirus.

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. DOI=10.1093/nar/12.20.7859; PubMed=6093056 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1038/317145a0; PubMed=2993920 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1107/S0108767387011875; PubMed=2856083 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH ICAM1. DOI=10.1093/emboj/18.22.6249; PubMed=10562537 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1016/0022-2836(90)90076-X; PubMed=2156077 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell.
FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
FUNCTION: Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity).
FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).
FUNCTION: Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).
FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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 + H₂O = NDP + phosphate.
SUBUNIT: Capsid proteins interact with host ICAM1.
SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
SUBCELLULAR LOCATION: Protein 2B: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
SUBCELLULAR LOCATION: Protein 2C: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
SUBCELLULAR LOCATION: Protein 3A: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
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).
PTM: VPg is covalently linked to the genomic RNA (By similarity).
PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
SIMILARITY: Belongs to the picornaviruses polyprotein family.
SIMILARITY: Contains 2 peptidase C3 domains [view classification].
SIMILARITY: Contains 1 RdRp catalytic domain.
SIMILARITY: Contains 1 SF3 helicase domain.
CAUTION: The PDB data bank contains the 3D-structure coordinates of proteins VP1, VP2, VP3 and VP4.
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";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X01087; CAA25565.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L05355; AAA45758.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K02121; AAA45756.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A03901; GNNYH4.

3D structure databases

PDB

1D3I; EM; 26.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1HRI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1HRV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1K5M; X-ray; 2.70 A; A=568-856, B=70-331, C=332-567, D=1-69.	[ExPASy / RCSB / EBI]
1NA1; X-ray; 3.30 A; A=568-856, B=70-331, C=332-567, D=1-69.	[ExPASy / RCSB / EBI]
1NCQ; X-ray; 2.50 A; A=568-856, B=70-331, C=332-567, D=1-69.	[ExPASy / RCSB / EBI]
1R08; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1R09; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUC; X-ray; 3.10 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUD; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUE; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUF; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUG; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RUJ; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1RVF; X-ray; 4.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1VRH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
1XR5; X-ray; 2.80 A; A=1720-2179.	[ExPASy / RCSB / EBI]
2B0F; NMR; -; A=1538-1719.	[ExPASy / RCSB / EBI]
2HWB; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2HWC; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2IN2; NMR; -; A=1538-1719.	[ExPASy / RCSB / EBI]
2R04; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2R06; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2R07; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2RM2; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2RR1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2RS1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2RS3; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
2RS5; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]
4RHV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=1-69.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1D3I; -.
1HRI; -.
1HRV; -.
1K5M; -.
1NA1; -.
1NCQ; -.
1R08; -.
1R09; -.
1RMU; -.
1RUC; -.
1RUD; -.
1RUE; -.
1RUF; -.
1RUG; -.
1RUH; -.
1RUI; -.
1RUJ; -.
1RVF; -.
1VRH; -.
1XR5; -.
2B0F; -.
2HWB; -.
2HWC; -.
2IN2; -.
2R04; -.
2R06; -.
2R07; -.
2RM2; -.
2RMU; -.
2RR1; -.
2RS1; -.
2RS3; -.
2RS5; -.
4RHV; -.

ModBase

P03303.

Protein family/group databases

MEROPS

C03.013; -.
C03.020; -.

Ontologies

GO:0031410;	Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003593; AAA+_ATPase_core.
IPR004004; Helicase/Pol/Pept_Calicivir.
IPR000605; Helicase_SF3_ssDNA/RNA_vir.
IPR014759; Helicase_SF3_ssRNA_vir.
IPR014838; P3A.
IPR000199; Pept_C3_picorn.
IPR000081; Peptidase_C3.
IPR003138; Pico_P1A.
IPR002527; Pico_P2B.
IPR001676; Picornavirus_capsid.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.

Pfam

PF08727; P3A; 1.
PF00548; Peptidase_C3; 1.
PF02226; Pico_P1A; 1.
PF00947; Pico_P2A; 1.
PF01552; Pico_P2B; 1.
PF00680; RdRP_1; 1.
PF00073; Rhv; 3.
PF00910; RNA_helicase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00918; CALICVIRUSNS.

ProDom

PD001125; Pept_C3_picorn; 1.
PD001306; Peptidase_C3_2; 1.
PD001274; Pico_P2B; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00382; AAA; 1.
SMART graphical view of domain structure.

PROSITE

PS50507; RDRP_SSRNA_POS; 1.
PS51218; SF3_HELICASE_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

P03303; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Cytoplasm; Cytoplasmic vesicle; Helicase; Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; RNA replication; RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed; by host (By similarity).`
`CHAIN`	`2 331`	`330`	`Protein VP0 (Potential).`	`PRO_0000311074`
`CHAIN`	`2 69`	`68`	`Protein VP4 (Potential).`	`PRO_0000040025`
`CHAIN`	`70 331`	`262`	`Protein VP2 (Potential).`	`PRO_0000040026`
`CHAIN`	`332 567`	`236`	`Protein VP3 (Potential).`	`PRO_0000040027`
`CHAIN`	`568 856`	`289`	`Protein VP1 (Potential).`	`PRO_0000040028`
`CHAIN`	`857 1002`	`146`	`Picornain 2A (Potential).`	`PRO_0000040029`
`CHAIN`	`1003 1099`	`97`	`Protein 2B (Potential).`	`PRO_0000040030`
`CHAIN`	`1100 1429`	`330`	`Protein 2C (Potential).`	`PRO_0000040031`
`CHAIN`	`1430 1514`	`85`	`Protein 3A (Potential).`	`PRO_0000040032`
`CHAIN`	`1515 1537`	`23`	`Protein 3B (Potential).`	`PRO_0000040033`
`CHAIN`	`1538 1719`	`182`	`Picornain 3C (Potential).`	`PRO_0000040034`
`CHAIN`	`1720 2179`	`460`	`RNA-directed RNA polymerase 3D-POL (Potential).`	`PRO_0000040035`
`TOPO_DOM`	`2 1491`	`1490`	`Cytoplasmic (Potential).`
`TOPO_DOM`	`1492 1507`	`16`	`In membrane (Potential).`
`TOPO_DOM`	`1508 2179`	`672`	`Cytoplasmic (Potential).`
`DOMAIN`	`1205 1361`	`157`	`SF3 helicase.`
`DOMAIN`	`1946 2060`	`115`	`RdRp catalytic.`
`NP_BIND`	`1229 1236`	`8`	`ATP (Potential).`
`ACT_SITE`	`876 876`		`For picornain 2A activity (By similarity).`
`ACT_SITE`	`894 894`		`For picornain 2A activity (By similarity).`
`ACT_SITE`	`965 965`		`For picornain 2A activity (By similarity).`
`ACT_SITE`	`1577 1577`		`For picornain 3C activity (Potential).`
`ACT_SITE`	`1608 1608`		`For picornain 3C activity (Potential).`
`ACT_SITE`	`1683 1683`		`For picornain 3C activity (By similarity).`
`SITE`	`69 70`	`2`	`Cleavage (Potential).`
`SITE`	`331 332`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`856 857`	`2`	`Cleavage; by picornain 2A (Potential).`
`SITE`	`1002 1003`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1099 1100`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1429 1430`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1514 1515`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1537 1538`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1719 1720`	`2`	`Cleavage; by picornain 3C (Potential).`
`MOD_RES`	`1517 1517`		`O-(5'-phospho-RNA)-tyrosine (By similarity).`
`LIPID`	`2 2`		`N-myristoyl glycine; by host (By similarity).`
`CONFLICT`	`368 368`		`P -> L (in Ref. 3; AAA45756).`
`CONFLICT`	`459 459`		`I -> T (in Ref. 3; AAA45756).`
`CONFLICT`	`722 722`		`P -> H (in Ref. 3; AAA45756).`
`CONFLICT`	`726 727`		`NP -> KS (in Ref. 3).`
`CONFLICT`	`729 731`		`EWD -> RVG (in Ref. 3).`
`CONFLICT`	`913 913`		`C -> R (in Ref. 3; AAA45756).`
`CONFLICT`	`942 942`		`N -> S (in Ref. 3; AAA45756).`
`CONFLICT`	`962 962`		`P -> L (in Ref. 3; AAA45756).`
`CONFLICT`	`982 982`		`G -> E (in Ref. 3; AAA45756).`
`CONFLICT`	`1193 1193`		`L -> F (in Ref. 3; AAA45756).`
`CONFLICT`	`1193 1193`		`L -> H (in Ref. 2; AAA45758).`
`CONFLICT`	`1220 1220`		`I -> T (in Ref. 2 and 3).`
`CONFLICT`	`1399 1399`		`I -> V (in Ref. 2 and 3).`
`CONFLICT`	`1446 1446`		`P -> S (in Ref. 3; AAA45756).`