DB code: M00217
| RLCP classification | 1.13.30000.41 : Hydrolysis | |
|---|---|---|
| 1.13.30000.42 : 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 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 |
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 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 |
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 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 |
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 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). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00230 | Purine metabolism | 3.6.1.15 2.7.7.48 |
| MAP00730 | Thiamine metabolism | 3.6.1.15 |
| 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 29105 |
18420 18420 |
15377 15377 |
26078 26078 |
29888 29888 |
|||||||||||||||
| PubChem |
32051 32051 |
888 888 |
22247451 962 22247451 962 |
1004 22486802 1004 22486802 |
1023 21961011 1023 21961011 |
|||||||||||||||
| 2hrvA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hrvB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1z8rA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hrvA02 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hrvB02 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1z8rA02 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1l1nA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1l1nB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1cqqA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1l1nA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1l1nB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1cqqA02 |
|
|
|
|
|
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 |
|
|
|
|
|
HIS 18;ASP 35 | ||||
| 2hrvB01 |
|
|
|
|
|
HIS 18;ASP 35 | ||||
| 1z8rA01 |
|
|
|
|
|
HIS 21;ASP 39 | ||||
| 2hrvA02 |
|
|
|
|
|
CYS 106 | CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding) | GLY 104;CYS 106 | ||
| 2hrvB02 |
|
|
|
|
|
CYS 106 | CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding) | GLY 104;CYS 106 | ||
| 1z8rA02 |
|
|
|
|
|
CYS 56;CYS 58;CYS 116;HIS 118(Zinc binding) | GLY 108; | mutant C110A | ||
| 1l1nA01 |
|
|
|
|
|
HIS 40;GLU 71 | ||||
| 1l1nB01 |
|
|
|
|
|
HIS 40;GLU 71 | ||||
| 1cqqA01 |
|
|
|
|
|
HIS 40;GLU 71 | ||||
| 1l1nA02 |
|
|
|
|
|
CYS 147 | GLY 145;CYS 147 | |||
| 1l1nB02 |
|
|
|
|
|
CYS 147 | GLY 145;CYS 147 | |||
| 1cqqA02 |
|
|
|
|
|
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. |
| 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, |
| 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, |
| Related PDB | 1z8r |
| Related UniProtKB | |
| Comments |
|---|
|
This protein is a genome polyprotein from picornavirus, ### One of the protease enzymes in this entry is picornain 2A (E.C. Although zinc is included as cofactor, This enzyme belongs to the peptidase family-C3, The catalytic mechanism of this enzyme seems to be similar to that of trypsin (D00197 in EzCatDB), ### The other protease enzyme in this entry is picornain 3C (EC 3.4.22.28) from poliovirus or rhinovirus, This enzyme belongs to the peptidase family-C3, The catalytic mechanism of this enzyme seems to be similar to that of trypsin (D00197 in EzCatDB), |
| Created | Updated |
|---|---|
| 2006-07-21 | 2012-10-22 |