| IED ID | IndEnz0002010274 |
| Enzyme Type ID | protease010274 |
| Protein Name |
Genome polyprotein Cleaved into: Protein p28; NTPase EC 3.6.1.15 p35 ; Protein p32; Viral genome-linked protein VPg p14 ; Protease-polymerase p70 Pro-Pol EC 2.7.7.48 EC 3.4.22.66 ; Capsid protein CP VP1 p60 Fragment |
| Gene Name | ORF1 |
| Organism | Sapporo virus (strain Human/United Kingdom/Manchester/1993) (Hu/SV/Man/1993/UK) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Caliciviridae Sapovirus Sapporo virus Sapovirus GI Sapporo virus (strain Human/United Kingdom/Manchester/1993) (Hu/SV/Man/1993/UK) |
| Enzyme Sequence | MFGTKAPDSVQEGTLFRELFGVDQTEQFPLSLADLARLQGELVDATRTPGHALRQKYTMTTIQDLINKITKVVPVQATLNEMHARRQFERERADLFHELPLVDEDAVAQPKTYFYTMWRQVVKKGKAYFCPLVKTSAWRTKISAITEPIKDFLIAFWQAVQQEMGVNPQYLQLAWLQKLKPTTLTIILQQHKHTVSGWLATMTALVEVYSNLFDDLRKSSVTIVSSIGAFFDICKDFVSQVVELVKTTFTAQGPTDLGWAAVLAGAAMILLKMSGCPGVIGMWTKVLKICGGITTITAAARGVRWLKDLYEEAEGRRLPKMYMARGAALIELAASREVTGVDELKGLLDCFTILIEEGTELIHKFGTSPLAGLVRTYVSELETQANNIRSTIKLDTPRRVPVVIILTGAPGIGKTRLAQYIGQRFGKTSNFSVAVDHHDGYTGNTVCIWDEFDVDSKGAFVETMIGIANTAPFPLNCDRVENKGRVFTSDYVICTSNYPTSVIPDNPRAAAFYRRVLTVDVSAPDLEEWKKRNPGKRPTPDLYQDDFSHLKLMLRPYLGYNPDGDTLEGPRVAPTQISIAGLITLMERRFKEQAGPLQNLWLQVPKTLVEQSTNMVKAFMYANRAVCDVIPNPATRDITETALSKVFVCGTAPPPEFVGKHIVITGIEVGDASIANSLLSMFTTTTRLSAAAQREYMYRVWSPLIHIQDRSMNTQNLPYINRVIPVTSHWDFLRGLRHHLGFTSIPGMWKAFQGWRTSQGIVDFVAHHMADVTFPSNPECTIFRTPDADVVFYTFGSYVCFATPARVPYVGTPPTTIHSNTPRCMTWGETLALLCEVVAEFVLHFGPVILSAANIAYLMTRGSRTEEAKGKTKHGRGMRHGHRAGVSLSDDEYDEWRDLMRDWRRDMSVNDFLMLRERSALGMDDEDVARYRAWLEIRAMRMAGGAYTHATIIGRGGVRDEIIRTSPRRAPTRPQQHYEEEGPTAIVEFTQGGDHIGYGVHIGNGNVITVTHVASTSDEVNGSAFKITRTVGETTWVQGPFSQLPHMQIGSGSPVYFTTRLHPVFTISEGTFETPNITVNGFHVRIMNGYPTKKGDCGLPYFNSNRQLVALHAGTDTQGETKVAQRVVKEVTTQDEFQWKGLPVVKSGLDVGGMPTGTRYHRSPAWPEEQPGETHAPAPFGSGDKRYTFSQTEMLVNGLKPYTEPTAGVPPQLLSRAVTHVRSYIETIIGTHRSPVLTYHQACELLERTTSCGPFVQGLKGDYWDEEQQQYTGVLANHLEQAWDKANKGIAPRNAYKLALKDELRPIEKNKAGKRRLLWGCDAATTLIATAAFKAVATRLQVVTPMTPVAVGINMDSVQMQVMNDSLKGGVLYCLDYSKWDSTQNPAVTAASLAILERFAEPHPIVSCAIEALSSPAEGYVNDIKFVTRGGLPSGMPFTSVVNSINHMIYVAAAILQAYESHNVPYTGNVFQVETIHTYGDDCMYSVCPATASIFHTVLANLTSYGLKPTAADKSDAIKPTNTPVFLKRTFTQTPHGIRALLDITSITRQFYWLKANRTSDPSSPPAFDRQARSAQLENALAYASQHGPVMFDTVRQIAIKTAQGEGLVLVNTNYDQALATYNAWFIGGTVPDPVGHTEGTHKIVFEMEGNGSNPEPKQSNNPMVVDPPGTTGPTTSHVVVANPEQPNGAAQRLELAVATGAIQSNVPEAIRNCFAVFRTFAWNDRMPTGTFLGSISLHPNINPYTSHLSGMWAGWGGSFEVRLSISGSGVFAGRIIASVIPPGVDPSSIRDPGVLPHAFVDARITEPVSFMIPDVRAVDYHRMDGAEPTCSLGFWVYQPLLNPFSTTAVSTCWVSVETKPGGDFDFCLLRPPGQQMENGVSPEGLLPRRLGYSRGNRVGGLVVGMILVAEHKQVNRHFNSNSVTFGWSTAPVNPMAAEIVTNQAHSTSRHAWLSIGAQNKGPLFPGIPNHFPDSCASTVVGAMDTSLGGRPSTGVCGPAISFQNNGDVYENDTPSVMFATYDPLTSGTGVALTNSINPASLALVRISNNDFDTSGFANDKNVVVQMSWEMYTGTNQIRGQVTPMSGTNYTFTSTGANTLVLWQERMLSYDGHQAILYSSQLERTAEYFQNDIVNIPENSMAVFNVETNSASFQIGIRPDGYMVTGGSIGVNVPLEPETRFQYVGILPLSAALSGPSGNMGRARRVFQ |
| Enzyme Length | 2208 |
| Uniprot Accession Number | Q69014 |
| Absorption | |
| Active Site | ACT_SITE 1012; /note=For 3CLpro activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01242; ACT_SITE 1033; /note=For 3CLpro activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01242; ACT_SITE 1097; /note=For 3CLpro activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01242 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-ProRule:PRU01242}; |
| DNA Binding | |
| EC Number | 3.6.1.15; 2.7.7.48; 3.4.22.66 |
| Enzyme Function | FUNCTION: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity (By similarity). {ECO:0000250}.; FUNCTION: Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation (By similarity). {ECO:0000250}.; FUNCTION: Protease-polymerase processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved. {ECO:0000250}.; FUNCTION: Protease-polymerase is an RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Catalyzes the covalent attachment VPg with viral RNAs (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 408..415; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (3); Alternative sequence (1); Beta strand (21); Chain (7); Compositional bias (1); Domain (3); Helix (21); Modified residue (1); Non-terminal residue (1); Nucleotide binding (1); Region (1); Site (5); Turn (5) |
| Keywords | 3D-structure;ATP-binding;Alternative initiation;Alternative promoter usage;Capsid protein;Covalent protein-RNA linkage;DNA replication;Host cytoplasm;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed RNA polymerase;Thiol protease;Transferase;Viral RNA replication;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein]: Virion. Host cytoplasm. |
| Modified Residue | MOD_RES 893; /note=O-(5'-phospho-RNA)-tyrosine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein.; PTM: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 2CKW; 2UUT; 2UUW; 2WK4; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 242,737 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23680; RHEA:21248 |
| Cross Reference Brenda |