| IED ID | IndEnz0002012793 |
| Enzyme Type ID | protease012793 |
| Protein Name |
Genome polyprotein p254 Cleaved into: Protein p16; Protein p23; NTPase EC 3.6.1.15 2C-like protein P2C p37 ; Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein VPg p13 ; 3C-like protease 3CLpro EC 3.4.22.66 Calicivirin Thiol protease P3C p15 ; RNA-directed RNA polymerase EC 2.7.7.48 3Dpol p58 ; Capsid protein VP60 |
| Gene Name | ORF1 |
| Organism | Rabbit hemorrhagic disease virus (strain V-351) (Ra/LV/RHDV/V351/1991/CK) (RHDV-V351) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Caliciviridae Lagovirus Rabbit hemorrhagic disease virus (RHDV) Rabbit hemorrhagic disease virus (strain V-351) (Ra/LV/RHDV/V351/1991/CK) (RHDV-V351) |
| Enzyme Sequence | MAAMSRLTGMTTAILPEKKPLSFFLDLRDKTPPCCIRATGRLAWPVFPGQNGKEGPLETCNMCGKWLNGFGNFGLEDLGDVCLRSIAQQKHKFGPVCLCNRVYLHDCGRWRRRSRFLKHYKALNKVIPCAYQFVESFPTPIFEGEVDDLFVELGAPTSMGFMDKKLLKKGKKLMDKFVDVDEPCLTSRDASLLDSIASDNTIRAKLEEEYGVEMVQAARDRKDFMKNLRLALDNWPANPVTWYRKLGNITKKGKQWAKKVVYGARKVTDPLKTLASILLVGLHNVIAVDTTVMLSTFNPVNLLAILMDWNNDLTGFFATLVRLLELYGVVQATVNLIIEGVKSFWDKVVCATDRCFDLLKRLFDTFEDSVPTGPTAGCLIFMAFVFSTVVGYLPNNSVITTFMKGAGKLTTFAGVVGAIRTLWITINQHMVAKDLTSVQQKVMTVVKMANEAATLDQLEIVSCLCSDLETTLTNRCTLPSYNQHLGILNASQKVISDLHTMVLGKINTSKQRPQPVAVIFKGAPGIGKTYLVHRIARDLGCQHPSTINFGLDHFDSYTGEEVAIADESNTCGDGESWVELFIQMVNTNPCPLNCDKAENKNKVFNSKYLLCTTNSNMILNATHPRAGAFYRRVMIVEARNKAVESWQATRHGSKPGKSCYNKDMSHLTFQVYPHNMPAPGFVFVGDKLVKSQVTPREYKYSELLDLIKSEHPDVASFEGANKFNFVYPDAQYDQALLMWKQYFVMYGCVARLAKNFVDDIPYNQVHISRASDPKIEGCVEYQCKFQHLWRMVPQFVLGCVNMTNQLGTPLTQQQLDRITNGVEGVTVTTVNNILPFHSQTTLINPSFIKLIWAVRKHLKGLSGVTKVAQFIWRVMTNPVDAYGTLVRTLTGAATFSDDPVSTTIICSNCTIQLHSCGGLLVRYSRDPVPVASDNVDRGDQGVDVFTDPNLISGFSWRQIAHLFVEVISHLCANHLVNLATMAALGAVATKAFQGVKGKTKRGRGARVNLGNDEYDEWQAARREFVNAHDMTAEEYLAMKNKAAMGSDDQDSIMFRSWWTRRQLRPDEDQVTIVGRSGVRNEVIRTRVRQTPRGPKTLDDGGFYDNDYEGLPGFMRHNGSGRMIHIGNGLYISNTHTARSSCSEIVTCSPTTDLCLVKGEAIRSVAQIAEGTPVCDWKKSPISTYGIKKTLSDSTKIDVLAYDGCTQTTHGDCGLPLYDSSGKIVAIHTGKLLGFSKMCTLIDLTITKGVYETSNFFCGEPIDYRGITAHRLVGAEPRPPVSGTRYAKVPGVPDEYKTGYRPANLGRSDPDSDKSLMNIAVKNLQVYQQEPKLDKVDEFIERAAADVLGYLRFLTKGERQANLNFKAAFNTLDLSTSCGPFAPGKKIDHVKDGVMDQVLAKHLYKCWSVANSGKALHHIYACGLKDELRPLDKVKEGKKRLLWGCDVGVAVCAAAVFHNICYELKMVARFGPIAVGVDMTSRDVDVIINNLTSKASDFLCLDYSKWDSTMSPCVVRLAIDILADCCEQTELTKSVVLTLKSHPMTILDAMIVQTKRGLPSGMPFTSVINSICHWLLWSAAVYKSCAEIGLHCSNLYEDAPFYTYGDDGVYAMTPMMVSLLPAIIENLRDYGLSPTAADKTEFIDVCPLNKISFLKRTFELTDIGWVSKLDKSSILRQLEWSKTTSRHMVIEETYDLAKEERGVQLEELQVAAAAHGQEFFNFVCGELVRQQAYTQFSVYSYDAARKILADRKRVVSVVPDDEFVNVMEGKARAAPQGEAARTATTASVPGTTTDGMDPGVVATTSVITAENSSASIATAGIGGPPQQVDQQETWRTNFYYNDVFTWSVADAPGSILYTVQHSPQNNPFTAVLSQMYAGWAGGMQFRFIVAGSGVFGGRLVRAVIPPGIEIGPGLEVRQFPHVVIDARSLEPVTITMPDLRPNMYHPTGDPGLVPTLVLSVYNNLINPFGGSTSAIQVTVETRPSEDFEFVMIRAPSSKTVDSISPAGLLTTPDLTGVGNDNRWNGQIVGLQPVPGGFSTCNRHWNLNGSTYGWSSPRFADIDHRKGSASYPGSNATNVLQFWYANAGSAIDNPISQVAPDGLPDMSFVPFNGPGIPAAGWVGFGAIWNSNSGAPNVTTVQAYELGFATGAPGNLQPTTNTSGAQTVAKSIYAVVTGTAQNPAGLFVMASGIISTPNASAITYTPQPDRIVTTPGTPAAAPVGKNTPIMFASVVRRTGDVNATAGSANGTQYGTGSQPLPVTIGLSLNNYSSALMPGQFFVWQLTFASGFMEIGLSVDGYFYAGTGASTTLIDLTELIDVRPVGPRPSKSTLVFNLGGTANGFSYV |
| Enzyme Length | 2344 |
| Uniprot Accession Number | P27411 |
| Absorption | |
| Active Site | ACT_SITE 1135; /note=For 3CLpro activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01242; ACT_SITE 1152; /note=For 3CLpro activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01242; ACT_SITE 1212; /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 (p72) 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 VP60 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 by binding histo-blood group antigens, 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 522..529; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (3); Alternative sequence (1); Chain (12); Disulfide bond (1); Domain (3); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (1); Site (8) |
| Keywords | ATP-binding;Alternative promoter usage;Capsid protein;Covalent protein-RNA linkage;Disulfide bond;Helicase;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 VP60]: Virion. Host cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 1014; /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. Precursor p41 can be cleaved by viral 3CLpro into protein p19 and VPg, or cleaved by host protease into protein p23/2 and protein p18 (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 | 256,908 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23680; RHEA:21248 |
| Cross Reference Brenda | 2.7.7.48; |