DB code: M00217

RLCP classification 1.13.30000.42 : Hydrolysis
1.13.30000.41 : Hydrolysis
CATH domain 4.10.80.- : Rhinovirus 14, subunit 4
2.60.120.- : Jelly Rolls
2.60.120.- : Jelly Rolls
2.60.120.- : Jelly Rolls
2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
-.-.-.- :
-.-.-.- :
1.-.-.- :
-.-.-.- :
2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
3.-.-.- :
3.30.70.- : Alpha-Beta Plaits
1.20.960.- : Mitochondrial Import Receptor Subunit Tom20; Chain A
E.C. 3.4.22.29 3.6.1.15 3.4.22.28 2.7.7.48
CSA 1cqq
M-CSA 1cqq
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00216 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains RefSeq MEROPS Pfam
P03300 Genome polyprotein
None Protein VP0 VP4-VP2
Protein VP4 P1A Virion protein 4
Protein VP2 P1B Virion protein 2
Protein VP3 P1C Virion protein 3
Protein VP1 P1D Virion protein 1
Picornain 2A
(P2A)
(Protein 2A)
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
NP_041277.1 (Protein)
NC_002058.3 (DNA/RNA sequence)
C03.001 (Cysteine)
PF08727 (P3A)
PF00548 (Peptidase_C3)
PF02226 (Pico_P1A)
PF00947 (Pico_P2A)
PF01552 (Pico_P2B)
PF00680 (RdRP_1)
PF00073 (Rhv)
PF00910 (RNA_helicase)
[Graphical View]
P04936 Genome polyprotein
None Protein VP0 VP4-VP2
Protein VP4 P1A Virion protein 4
Protein VP2 P1B Virion protein 2
Protein VP3 P1C Virion protein 3
Protein VP1 P1D Virion protein 1
Protease 2A
(P2A)
EC 3.4.22.29
Protein 2A
Protein 2B
(P2B)
Protein 2C
(P2C)
EC 3.6.1.15
Protein 3A
(P3A)
Protein 3B
(P3B)
VPg
Protease 3C
(P3C)
EC 3.4.22.28
Picornain 3C
RNA-directed RNA polymerase 3D-POL
(P3D-POL)
EC 2.7.7.48
C03.021 (Cysteine)
PF08727 (P3A)
PF00548 (Peptidase_C3)
PF02226 (Pico_P1A)
PF00947 (Pico_P2A)
PF01552 (Pico_P2B)
PF00680 (RdRP_1)
PF00073 (Rhv)
PF00910 (RNA_helicase)
[Graphical View]
P08292 Genome polyprotein
None Protein VP0 VP4-VP2
Protein VP4 P1A Virion protein 4
Protein VP2 P1B Virion protein 2
Protein VP3 P1C Virion protein 3
Protein VP1 P1D Virion protein 1
Protease 2A
(P2A)
EC 3.4.22.29
Protein 2A
Protein 2B
(P2B)
Protein 2C
(P2C)
EC 3.6.1.15
Protein 3A
(P3A)
Protein 3B
(P3B)
VPg
Protease 3C
(P3C)
EC 3.4.22.28
Picornain 3C
RNA-directed RNA polymerase 3D-POL
(P3D-POL)
EC 2.7.7.48
C03.011 (Cysteine)
PF08727 (P3A)
PF00548 (Peptidase_C3)
PF02226 (Pico_P1A)
PF00947 (Pico_P2A)
PF01552 (Pico_P2B)
PF00680 (RdRP_1)
PF00073 (Rhv)
PF00910 (RNA_helicase)
[Graphical View]

KEGG enzyme name
picornain 2A
(EC 3.4.22.29 )
picornavirus endopeptidase 2A
(EC 3.4.22.29 )
poliovirus protease 2A
(EC 3.4.22.29 )
rhinovirus protease 2A
(EC 3.4.22.29 )
2A protease
(EC 3.4.22.29 )
2A proteinase
(EC 3.4.22.29 )
protease 2A
(EC 3.4.22.29 )
proteinase 2Apro
(EC 3.4.22.29 )
picornaviral 2A proteinase
(EC 3.4.22.29 )
Y-G proteinase 2A
(EC 3.4.22.29 )
poliovirus proteinase 2A
(EC 3.4.22.29 )
poliovirus protease 2Apro
(EC 3.4.22.29 )
picornaviral 2A proteinase
(EC 3.4.22.29 )
nucleoside-triphosphatase
(EC 3.6.1.15 )
nucleoside triphosphate phosphohydrolase
(EC 3.6.1.15 )
nucleoside-5-triphosphate phosphohydrolase
(EC 3.6.1.15 )
nucleoside 5-triphosphatase
(EC 3.6.1.15 )
picornain 3C
(EC 3.4.22.28 )
picornavirus endopeptidase 3C
(EC 3.4.22.28 )
poliovirus protease 3C
(EC 3.4.22.28 )
rhinovirus protease 3C
(EC 3.4.22.28 )
foot-and-mouth protease 3C
(EC 3.4.22.28 )
poliovirus proteinase 3C
(EC 3.4.22.28 )
rhinovirus proteinase 3C
(EC 3.4.22.28 )
coxsackievirus 3C proteinase
(EC 3.4.22.28 )
foot-and-mouth-disease virus proteinase 3C
(EC 3.4.22.28 )
3C protease
(EC 3.4.22.28 )
3C proteinase
(EC 3.4.22.28 )
cysteine proteinase 3C
(EC 3.4.22.28 )
hepatitis A virus 3C proteinase
(EC 3.4.22.28 )
protease 3C
(EC 3.4.22.28 )
tomato ringspot nepovirus 3C-related protease
(EC 3.4.22.28 )
RNA-directed RNA polymerase
(EC 2.7.7.48 )
RNA nucleotidyltransferase (RNA-directed)
(EC 2.7.7.48 )
RNA nucleotidyltransferase (RNA-directed)
(EC 2.7.7.48 )
RNA-dependent ribonucleate nucleotidyltransferase
(EC 2.7.7.48 )
3D polymerase
(EC 2.7.7.48 )
PB1 proteins
(EC 2.7.7.48 )
PB2 proteins
(EC 2.7.7.48 )
phage f2 replicase
(EC 2.7.7.48 )
polymerase L
(EC 2.7.7.48 )
Q-beta replicase
(EC 2.7.7.48 )
phage f2 replicase
(EC 2.7.7.48 )
ribonucleic acid replicase
(EC 2.7.7.48 )
ribonucleic acid-dependent ribonucleate nucleotidyltransferase
(EC 2.7.7.48 )
ribonucleic acid-dependent ribonucleic acid polymerase
(EC 2.7.7.48 )
ribonucleic replicase
(EC 2.7.7.48 )
ribonucleic synthetase
(EC 2.7.7.48 )
RNA replicase
(EC 2.7.7.48 )
RNA synthetase
(EC 2.7.7.48 )
RNA transcriptase
(EC 2.7.7.48 )
RNA-dependent ribonucleate nucleotidyltransferase
(EC 2.7.7.48 )
RDRP
(EC 2.7.7.48 )
RNA-dependent RNA polymerase
(EC 2.7.7.48 )
RNA-dependent RNA replicase
(EC 2.7.7.48 )
transcriptase
(EC 2.7.7.48 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P03300 POLG_POL1M Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. 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. NTP + H(2)O = NDP + phosphate. P2C N-terminus interacts with human RTN3. This interaction is important for viral replication (By similarity). Interacts with human PVR. Protein VP2: Virion. Cytoplasm (Potential). Protein VP3: Virion. Cytoplasm (Potential). Protein VP1: Virion. Cytoplasm (Potential). 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). 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). 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). Protein 3B: Virion (Potential). Picornain 3C: Cytoplasm (Potential). 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).
P04936 POLG_HRV2 Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. 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. NTP + H(2)O = NDP + phosphate. Capsid proteins interact with host ICAM1 (By similarity). Protein VP2: Virion. Cytoplasm (Potential). Protein VP3: Virion. Cytoplasm (Potential). Protein VP1: Virion. Cytoplasm (Potential). 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). 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). 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). Protein 3B: Virion (Potential). Picornain 3C: Cytoplasm (Potential). 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).
P08292 POLG_CXB4J Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. 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. NTP + H(2)O = NDP + phosphate. Capsid proteins interact with host CXADR. 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). Protein 3B: Virion (Potential). Picornain 3C: Cytoplasm (Potential). 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). Protein VP2: Virion. Cytoplasm (Potential). Protein VP3: Virion. Cytoplasm (Potential). Protein VP1: Virion. Cytoplasm (Potential). 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). 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).

KEGG Pathways
Map code Pathways E.C.
MAP00730 Thiamine metabolism 3.6.1.15
MAP00230 Purine metabolism 3.6.1.15 2.7.7.48

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00305 C00017 C00001 C00201 C00046 C00017 C00012 C00454 C00009 C00046 C00013 I00153 I00154 I00155
E.C. 3.4.22.29
2.7.7.48
3.4.22.28
3.4.22.29
3.4.22.28
3.4.22.29
3.6.1.15
3.6.1.15
2.7.7.48
2.7.7.48
3.4.22.28
3.4.22.29
3.4.22.28
3.4.22.29
3.6.1.15
3.6.1.15
2.7.7.48
2.7.7.48
3.4.22.28
3.4.22.28
3.4.22.28
Compound Zinc Magnesium Protein H2O Nucleoside triphosphate RNA(n) Protein Peptide Nucleoside diphosphate Phosphate RNA(n+1) Diphosphate Peptidyl-Cys-tetrahedral-intermediate (with previous peptide) Acyl-enzyme(Peptidyl-Cys-acyl group) Peptidyl-Cys-tetrahedral-intermediate
Type heavy metal divalent metal (Ca2+, Mg2+) peptide/protein H2O nucleotide nucleic acids peptide/protein peptide/protein nucleotide phosphate group/phosphate ion nucleic acids phosphate group/phosphate ion
ChEBI 29105
18420
15377
26078
29888
PubChem 32051
888
22247451
962
1004
22486802
1023
21961011
2hrvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hrvB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1z8rA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hrvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hrvB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1z8rA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1l1nA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1l1nB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cqqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1l1nA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1l1nB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cqqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:AG7 Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P03300, P04936 & literature [7], [11]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2hrvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 18;ASP 35
2hrvB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 18;ASP 35
1z8rA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 21;ASP 39
2hrvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 106 CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding) GLY 104;CYS 106
2hrvB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 106 CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding) GLY 104;CYS 106
1z8rA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 56;CYS 58;CYS 116;HIS 118(Zinc binding) GLY 108; mutant C110A
1l1nA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 40;GLU 71
1l1nB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 40;GLU 71
1cqqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 40;GLU 71
1l1nA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 147 GLY 145;CYS 147
1l1nB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 147 GLY 145;CYS 147
1cqqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 147 GLY 145;CYS 147

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.110
[4]
p.623-624
[9]
p.763-765, p.767-769
[12]
p.1440-1441
[17]
p.210
[19]
p.11000-11001
[21]
p.5468-5469
[30]

References
[1]
Resource
Comments
Medline ID
PubMed ID 3186696
Journal Proc Natl Acad Sci U S A
Year 1988
Volume 85
Pages 7872-6
Authors Bazan JF, Fletterick RJ
Title Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2645167
Journal FEBS Lett
Year 1989
Volume 243
Pages 103-14
Authors Gorbalenya AE, Donchenko AP, Blinov VM, Koonin EV
Title Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1849679
Journal Virology
Year 1991
Volume 181
Pages 609-19
Authors Kean KM, Teterina NL, Marc D, Girard M
Title Analysis of putative active site residues of the poliovirus 3C protease.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1850921
Journal Virology
Year 1991
Volume 182
Pages 615-25
Authors Yu SF, Lloyd RE
Title Identification of essential amino acid residues in the functional activity of poliovirus 2A protease.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1331062
Journal J Biol Chem
Year 1992
Volume 267
Pages 22639-44
Authors Sommergruber W, Ahorn H, Zophel A, Maurer-Fogy I, Fessl F, Schnorrenberg G, Liebig HD, Blaas D, Kuechler E, Skern T
Title Cleavage specificity on synthetic peptide substrates of human rhinovirus 2 proteinase 2A.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8320292
Journal J Chem Inf Comput Sci
Year 1993
Volume 33
Pages 345-9
Authors Arad D, Kreisberg R, Shokhen M
Title Structural and mechanistic aspects of 3C proteases from the Picornavirus family.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8386363
Journal Protein Eng
Year 1993
Volume 6
Pages 189-93
Authors Miyashita K, Kusumi M, Utsumi R, Katayama S, Noda M, Komano T, Satoh N
Title Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: evidence of a functional relationship with trypsin-like serine proteinases.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8097606
Journal Virology
Year 1993
Volume 194
Pages 360-4
Authors Kean KM, Howell MT, Grunert S, Girard M, Jackson RJ
Title Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7515772
Journal Cell
Year 1994
Volume 77
Pages 761-71
Authors Matthews DA, Smith WW, Ferre RA, Condon B, Budahazi G, Sisson W, Villafranca JE, Janson CA, McElroy HE, Gribskov CL, et al
Title Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8164744
Journal Nature
Year 1994
Volume 369
Pages 72-6
Authors Allaire M, Chernaia MM, Malcolm BA, James MN
Title Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8112306
Journal EMBO J
Year 1994
Volume 13
Pages 924-7
Authors Macadam AJ, Ferguson G, Fleming T, Stone DM, Almond JW, Minor PD
Title Role for poliovirus protease 2A in cap independent translation.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8520469
Journal Protein Sci
Year 1995
Volume 4
Pages 1439-45
Authors Malcolm BA
Title The picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8580843
Journal Protein Sci
Year 1995
Volume 4
Pages 2526-31
Authors Voss T, Meyer R, Sommergruber W
Title Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 8615011
Journal Virology
Year 1996
Volume 218
Pages 1-13
Authors Blair WS, Nguyen JH, Parsley TB, Semler BL
Title Mutations in the poliovirus 3CD proteinase S1-specificity pocket affect substrate recognition and RNA binding.
Related PDB
Related UniProtKB
[15]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9367789
Journal J Mol Biol
Year 1997
Volume 273
Pages 1032-47
Authors Mosimann SC, Cherney MM, Sia S, Plotch S, James MN
Title Refined X-ray crystallographic structure of the poliovirus 3C gene product.
Related PDB 1l1n
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9139725
Journal J Biol Chem
Year 1997
Volume 272
Pages 12683-91
Authors Barco A, Ventoso I, Carrasco L
Title The yeast Saccharomyces cerevisiae as a genetic system for obtaining variants of poliovirus protease 2A.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9268151
Journal Virology
Year 1997
Volume 234
Pages 203-14
Authors Sommergruber W, Seipelt J, Fessl F, Skern T, Liebig HD, Casari G
Title Mutational analyses support a model for the HRV2 2A proteinase.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 10400760
Journal J Virol
Year 1999
Volume 73
Pages 6626-33
Authors Sosnovtseva SA, Sosnovtsev SV, Green KY
Title Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1507-1686.
Medline ID
PubMed ID 10500114
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 11000-7
Authors Matthews DA, Dragovich PS, Webber SE, Fuhrman SA, Patick AK, Zalman LS, Hendrickson TF, Love RA, Prins TJ, Marakovits JT, Zhou R, Tikhe J, Ford CE, Meador JW, Ferre RA, Brown EL, Binford SL, Brothers MA, DeLisle DM, Worland ST
Title Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes.
Related PDB 1cqq
Related UniProtKB P04936
[20]
Resource
Comments
Medline ID
PubMed ID 10507325
Journal Virus Res
Year 1999
Volume 62
Pages 159-68
Authors Seipelt J, Guarne A, Bergmann E, James M, Sommergruber W, Fita I, Skern T
Title The structures of picornaviral proteinases.
Related PDB
Related UniProtKB
[21]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 850-991.
Medline ID
PubMed ID 10523291
Journal EMBO J
Year 1999
Volume 18
Pages 5463-75
Authors Petersen JF, Cherney MM, Liebig HD, Skern T, Kuechler E, James MN
Title The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis.
Related PDB 2hrv
Related UniProtKB P04936
[22]
Resource
Comments
Medline ID
PubMed ID 11056105
Journal Circulation
Year 2000
Volume 102
Pages 2276-81
Authors Badorff C, Fichtlscherer B, Rhoads RE, Zeiher AM, Muelsch A, Dimmeler S, Knowlton KU
Title Nitric oxide inhibits dystrophin proteolysis by coxsackieviral protease 2A through S-nitrosylation: A protective mechanism against enteroviral cardiomyopathy.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 11007981
Journal FEBS Lett
Year 2000
Volume 481
Pages 289-92
Authors Sarkany Z, Skern T, Polgar L
Title Characterization of the active site thiol group of rhinovirus 2A proteinase.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 10769080
Journal J Gen Virol
Year 2000
Volume 81
Pages 1361-72
Authors Santti J, Harvala H, Kinnunen L, Hyypia T
Title Molecular epidemiology and evolution of coxsackievirus A9.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 11162821
Journal Virology
Year 2001
Volume 280
Pages 80-6
Authors Wang QM, Johnson RB
Title Activation of human rhinovirus-14 3C protease.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 11161279
Journal J Gen Virol
Year 2001
Volume 82
Pages 397-408
Authors Li X, Lu HH, Mueller S, Wimmer E
Title The C-terminal residues of poliovirus proteinase 2A(pro) are critical for viral RNA replication but not for cis- or trans-proteolytic cleavage.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 12525179
Journal Biochemistry
Year 2003
Volume 42
Pages 516-22
Authors Sarkany Z, Polgar L
Title The unusual catalytic triad of poliovirus protease 3C.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 14966374
Journal J Biomed Sci
Year 2004
Volume 11
Pages 239-48
Authors Shih SR, Chiang C, Chen TC, Wu CN, Hsu JT, Lee JC, Hwang MJ, Li ML, Chen GW, Ho MS
Title Mutations at KFRDI and VGK domains of enterovirus 71 3C protease affect its RNA binding and proteolytic activities.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 16227288
Journal J Virol
Year 2005
Volume 79
Pages 13685-93
Authors Nakamura K, Someya Y, Kumasaka T, Ueno G, Yamamoto M, Sato T, Takeda N, Miyamura T, Tanaka N
Title A norovirus protease structure provides insights into active and substrate binding site integrity.
Related PDB
Related UniProtKB
[30]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 16415022
Journal J Virol
Year 2006
Volume 80
Pages 1451-62
Authors Baxter NJ, Roetzer A, Liebig HD, Sedelnikova SE, Hounslow AM, Skern T, Waltho JP
Title Structure and dynamics of coxsackievirus B4 2A proteinase, an enyzme involved in the etiology of heart disease.
Related PDB 1z8r
Related UniProtKB

Comments
This protein is a genome polyprotein from picornavirus, which is composed of 4 coat proteins, 3 core proteins, 2 proteases (picornain 2A, picornain 3C), genome-linked protein, 3D polymerase.
###
One of the protease enzymes in this entry is picornain 2A (E.C. 3.4.22.29), which cleaves TYR-|-GLY bond in virus polyprotein.
Although zinc is included as cofactor, it is not involved in catalysis (see [13], [21]).
This enzyme belongs to the peptidase family-C3, to which the other protease, picornain 3C (E.C. 3.4.22.28;M00209, M00216 in EzCatDB, and described below) belongs.
The catalytic mechanism of this enzyme seems to be similar to that of trypsin (D00197 in EzCatDB), which is its homologous enzyme, although its catalytic site is composed of Cys/His/Asp and mainchain amide groups.
###
The other protease enzyme in this entry is picornain 3C (EC 3.4.22.28) from poliovirus or rhinovirus, whitch cleaves GLN/GLU-|-GLY/SER/THR bonds in its polyprotein.
This enzyme belongs to the peptidase family-C3, to which picornain 3C from other viruses (M00209, M00216 in EzCatDB) and picornain 2A (EC 3.4.22.29; described above) belong.
The catalytic mechanism of this enzyme seems to be similar to that of trypsin (D00197 in EzCatDB), which is its homologous enzyme, although its catalytic site is composed of Cys/His/Glu and mainchain amide groups.

Created Updated
2006-07-21 2012-10-22