| IED ID | IndEnz0002000437 |
| Enzyme Type ID | protease000437 |
| Protein Name |
Genome polyprotein Cleaved into: Protein p34; NTPase EC 3.6.1.15 p37 ; Protein p30; Viral genome-linked protein VPg p8 ; 3C-like protease 3CLpro EC 3.4.22.66 p20 ; RNA-directed RNA polymerase RdRp EC 2.7.7.48 p53 ; Capsid protein VP1 |
| Gene Name | ORF1 |
| Organism | Bovine enteric calicivirus Newbury agent-1 (isolate Bovine/UK/Newbury1/1976) (BEC) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Caliciviridae Nebovirus Newbury 1 virus Bovine enteric calicivirus Newbury agent-1 (isolate Bovine/UK/Newbury1/1976) (BEC) |
| Enzyme Sequence | MAPVVSRDRHRHKIPKPHQPAPPHRCTVWCPEDCGWYVGRCSCPKSCQREGWDDFFVADKVKPPSYVASKTSVADVVDWLLEEDPATDGPSEFDLTQFFQAYTDKSHQIHRDYAPDQLAQALDMAYILSVDPPDIKLPEYEATRFTHDTSYKGKLPRWLRVYGFKSRELAKKAITNIKGGAHWAKGLFKQAWDTLPGWSEVEAYFKAFFAGIITGVEDALSKSPSSVWTSLKLTPLLYIWRNINECSDIPVILGAFWATLELYNIPSKVYDLVSTALGPMVQDLARRVINIIKGDGNGPKQEGGRPSFSIPGVLLATFLSAIILGSMPSDGIIKKVLRGCATAAGLVGGFNAVKSIITTVQGASACKDVKKLASQLMCVTTMAATVSTRGERQVLASMLNDLNESVRERLVDPAFAALVPQLSAMSSKIMELSTINAAALSAARKRVPAKIVVLCGPPGHGKSVAAHKLAKMLNPNEPSIWNPFSDHHDEYTAEDVVIIDETPAEPGQWVEDLIAMGSNSPFVPNYDRVENKTRCFDSKYVLITTNHNPLINPTHSRAAALARRLTWVYVNSPDVADFLRQHPGVAPPATLFKADCSHLNFDIHPYNSIGTTAVVGHNGTTPLPRAKRTSLEGLCKHIKDLPDREGPPDGVPERMVLVAPDKGTARFVEAVINTYHNSGLVAQPAAWDTTPQKYQLAVTWQGSTSSVVGQRWDCNPQTPFVAPHFTRNMFKRVLGTEVPEYHLLAYACRITSSSLGDKSLPVPNPTVVINDPSPTRLALALMRHLKNPIASGLRVVWDLFRGCATGPKRLFTWALSQEWNPMPVTTAFTFPAGTVILHTAGGVRVVVLPPGPQFGLTEVTHLADHSGQDDPVVPDMFGQTWTELLWRLLKVIGTFLANYGVAIAGLTLSIAAFKTANKSTRNDRQGWLSGSGVALSDEEYDEWMKYSKKKGKKINADEFLQLRHRAAMGNDDDDARDYRSFYTAYQLGREGNNCEDLPLHPAVGPTTGGGYYVHIGNGVGITLKHVASGEDVIKELGNDLVKIRARHHKMGDPAMVVGEGAPVKFVTGHLVVDARNESVVFDQTRLSVVRVKVPGLETQRGYCGLPYVNSAGHVVGLHQGSYGVGDKVFTPITDAPAASPDTIMWRGLECTRSDIVTHLPHGTKYSISPGMREEAHKCTHQPASLGRNDPRCNQTQVAMVVKALTPYTSAPAIEKLDPCMVAAITEVRTAIQSLTPKGGFRPLTFAAAWQSLDLSTSAGALAPGKTKRDLCDPDTGMPAGKYREMLLAAWSRAGTGTPLDHTYIVALKDELRPVEKVAEGKRRLIWGADARVALIASAALTPVANALKTVTNLLPIQVGVDPSSANCVSSWVGRLQRHDHCLELDYSKWDSTMSPVIINIAIDILCNTCGSDSLRMAVAQTLKSRPTALVEGVSVPTKSGLPSGMPFTSQINSIVHWILWSATVRKCSLPLHIGSVNELAPFLTYGDDGLYTIPSHLTKSIDEIISTLKGYGLSPTAPDKGANVEIKRTSFTYLSGPVFLKRRIVLTPGGHRALLDLTSLARQPVWVNGPRRSVWNHEAQPIEIDAETRTIQLQNVLIELAWHQPQDFDHVLALVVKSAEASGLTIPRYSQEEARAIYDGRYYGIQHVSLPNNSDLIREGNMSDNKSTPEQQHESSRAMDAGATGAAAAAPAPPVAAAPASGLVGALVAEPQSGPSAEQWRTAYTLFGTVSWNANAGPGTILTVGRLGPGMNPYTQHIAAMYGGWAGGMDIRITIAGSGFIGGTLAVAAIPPGVDPESVNVLRMPHVLIDARGGVPLEVTLEDIRTSLYHPMGDTNTASLVIAVMTGLINPLGTDTLSVTVQLETRPGRDWVFFSLLPPTAGVASADPSQLLTRVALATSPEVRFGTGVLGILGLPSNPSVNRVYDVQSRTRGWSFPIPSSSVFMGDARNVEHNRRVMVQSSAPNNPLSDVFPDGFPDFVPQSDTEPDGGAVIAGQVLPHPGDNDNFWRLTPVVRGNTTAAINTIPERFNQVYFINLADEEAVSAATEELRFNGIQGIFGQRTNARAVQVMQGYVPRAEHIIRPAGFAGVGPQGPNVPIGFAGTMPNFNATASGADDLVPVWGPTLVHTASLLAGTTYELAENSMYVFSVSTSTSTFELGMLANGTWLGPAQLAGTGITWTEVLSVTYMGMRFAYNPLSGQGIGGESRRL |
| Enzyme Length | 2210 |
| Uniprot Accession Number | Q288N7 |
| Absorption | |
| Active Site | ACT_SITE 1025; /note=For 3CLpro activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01242; ACT_SITE 1039; /note=For 3CLpro activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01242; ACT_SITE 1103; /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; 3.4.22.66; 2.7.7.48 |
| Enzyme Function | FUNCTION: NTPase presumably plays a role in replication. {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: 3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. {ECO:0000250}.; FUNCTION: RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.; FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. 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 456..463; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (3); Chain (8); Compositional bias (1); Domain (3); Modified residue (1); Nucleotide binding (1); Region (2); Site (6) |
| Keywords | ATP-binding;Capsid protein;Covalent protein-RNA linkage;Helicase;Host cytoplasm;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed RNA polymerase;Reference proteome;Thiol protease;Transferase;Viral RNA replication;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein]: Virion. Host cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 940; /note=O-(5'-phospho-RNA)-tyrosine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Specific enzymatic cleavages by its own cysteine protease yield mature proteins. The protease cleaves itself from the nascent polyprotein autocatalytically (By similarity). {ECO:0000250}.; 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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 239,021 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23680; RHEA:21248 |
| Cross Reference Brenda |