| IED ID | IndEnz0002000922 |
| Enzyme Type ID | protease000922 |
| Protein Name |
Genome polyprotein Cleaved into: Capsid protein VP0 VP4-VP2 ; Capsid protein VP4 P1A Virion protein 4 ; Capsid protein VP2 P1B Virion protein 2 ; Capsid protein VP3 P1C Virion protein 3 ; Capsid protein VP1 P1D Virion protein 1 ; Protein 2A P2A ; 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 |
| Gene Name | |
| Organism | Avian encephalomyelitis virus (strain L2Z) (AEV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Picornaviridae Tremovirus Tremovirus A Avian encephalomyelitis virus (strain L2Z) (AEV) |
| Enzyme Sequence | MSKLFSTVGRTVDEVLSVLNDEDTESYAGPDRTAVVGGGFLTTVDQSSVSTATMGSLQDVQYRTAVDIPGSRVTQGERFFLIDQREWNSTQSEWQLLGKIDIVKELLDQSYAVDGLLKYHSYARFGLDVIVQINPTSFQAGGLIAALVPYDQVDIESIVAMTTYCHGKVNCNINYVVRMKVPYIYSRGCYNLRNSAYSIWMLVIRVWSRLQLGSGTSTQITITTLARFVDLELHGLSPLVAQMMRNEFRLSSSSNIVNLANYDDARAKVSLALGQEEFSRDSSSTGGELVHHFSQWTSIPCLAFTFTFPGTVGPGTHIWSTTVDPFSCNLRASSTVHPTNLSSIAGMFCFWRGDIVFEFQVFCTKYHSGRLMFVYVPGDENTKISTLTAKQASTGLTAVFDINGVNSTLVFRCPFISDTPYRVNPTTHKSLWPYATGKLVCYVYNILNAPASVSPSVSINVYKSAADLELYAPVYGVSPTNTSIFAQGKEDEGGFFSVPEVEQHVVEDKEPQGPLHVTPFGAVKAMEDPQLARKTPGTFPELAPGKPRHTVDHMDLYKFMGRAHYLWGHEFTKTDMQYTFQIPLSPIKEGFVTGTLRWFLSLFQLYRGSLDITMTFAGKTNVDGIVYFVPEGVAIETEREEQTPLLTLNYKTSVGAIRFNTGQTTNVQFRIPFYTPLEHIATHSKNAMDSVLGAITTQITNYSAQDEYLQVTYYISFNEDSQFSVPRAVPVVSSFTDTSSKTVMNTYWLDDDELVEESSHSSFDEIEEAQCSKCKMDLGDIVICSGEKAKHFGVYVGDGVVHVDPEGNATNWFMKRKATVKKSKNLDKWCFALSPRIDRTLICETANLMVGREVEYDIFVKNCETYARGIASGDYGTKEGEKWKTLLSAVGVAAMTTTMMAMRHQLLDTSLTKLPQKVGEVTNEVRKILEDTSAGVREFKEKVSSILRKTWPGKTSIKIMKWTFRIVKMCVGVGLCYAHGWDSKPVTAVVTMFSMDFLDLVIDGIEIGRMIIHELTTPKAQGLSEINQVLSIAKNAKDVIKMLIEIFCKVIERITGEHGKKIQWAQDKKEEIMNVLERAEKWITTSDDHSEGIECLKLVRSIQSVIRGEESLKELAGELRAVGTHVLNKLGRLDKPNAPILVRAEPTVLYLYGNRGGGKSLASMAIAVKLCKELGISHVEGIYTKPIMSDFWDGYAGQPVVIMDDLGQSTSDEDWTNFCQLVSSCPLRLNMANLEKKGTQFNSPFIIASSNLSHPCPKTVYCTDAIARRLHIKVKVSPKEEFSTHAMLDVAKAKKAGAYCNLDCLDFQKISDLASTPVSVQDIVLALLHTNVDKQTVMGNIIQYWAQSNPREVFDTMAEGKNSGKYLWLFEKIKTSKWYILGCVGAALSVSVLGVFAYHMIKNHFRDQQHDQSAYSAAIKPLRVVRLEQSDAQSVVDISNVVHGNLVRVGVGPNEARIHWLNNGWGVYNTYILMPYHGIKDADVDDDLYIERAGTIYSTNMKMVQVLFLESREGDLVLINVPRLPKFRDIRNHFSTEENIRRAEGMPGTLCTLDHERFTLVTESDLKMVEAATYVCEDDKGVRTDISVGRSWKAKACTVAGMCGGALVTSNNKMQNAIVGIHVAGGAPAISRVITKEMIEEMLKTRAQCSRIWKTEFVEKKISVGSKTKYHKSPLYDFCPQKVIKCPTKLFYQGEIDVMQVMLAKYSSPIVSEPLGYATVVEAYTNRMVSFFSEPRQLTYDECINGIEGLDAIDLKTSAGFPYNTLSLKKSDLIINGKKAQRLQQDVEKMEEDLHMNRSIQVVFTTCAKDELRPLSKGMLGKTRAIKACPVSFTILFRKYLGYALAQIQSHPGFHTGIAVGVDPDQDWHCMWYSIVTQCDLVVGLDFSNYDASLSPFMIYHAGRVLGQICGLDPRLVDRIMEPIVNSVHQLGSMRYYVDGSMPSGTPATSVLNSIINVVNISHVLCALEKISVFEVFKLSKILTYGDDVLFCIKKESLDQKSFPLSSFVQGLKELGMSPTGADKMEVKVTPVHKMSFLKRTFYVDEWSICHPRISEETVYSMLAWKSDNASMKHVIETSIWFMFHHGPRKYVIFCTCLRGVLCRVGIGLYIPTYKELEVRYDRLVKDRVIDDSF |
| Enzyme Length | 2134 |
| Uniprot Accession Number | Q6WQ42 |
| Absorption | |
| Active Site | ACT_SITE 791; /evidence=ECO:0000255|PROSITE-ProRule:PRU01283; ACT_SITE 802; /evidence=ECO:0000255|PROSITE-ProRule:PRU01283; ACT_SITE 863; /note=Acyl-thioester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU01283; ACT_SITE 1477; /note=For protease 3C activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1515; /note=For protease 3C activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1603; /note=For protease 3C activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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=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=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.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; |
| DNA Binding | |
| EC Number | 3.6.1.15; 3.4.22.28; 2.7.7.48 |
| Enzyme Function | FUNCTION: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). {ECO:0000250}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, AEV VP4 may not be myristoylated (By similarity). {ECO:0000250}.; FUNCTION: Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability. {ECO:0000250}.; FUNCTION: [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). {ECO:0000250}.; FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor. {ECO:0000250}.; FUNCTION: Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer (By similarity). {ECO:0000250}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity). {ECO:0000250}.; FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. {ECO:0000255|PROSITE-ProRule:PRU00539}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 1153..1160; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (6); Chain (13); Domain (4); Intramembrane (1); Modified residue (1); Nucleotide binding (1); Site (10); Topological domain (2) |
| Keywords | ATP-binding;Capsid protein;Covalent protein-RNA linkage;Helicase;Host cytoplasm;Host cytoplasmic vesicle;Host membrane;Host-virus interaction;Hydrolase;Ion channel;Ion transport;Membrane;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-binding;RNA-directed RNA polymerase;Thiol protease;Transferase;Transport;Viral RNA replication;Viral attachment to host cell;Viral ion channel;Virion;Virus entry into host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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. May associate with membranes through a N-terminal amphipathic helix (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.; SUBCELLULAR LOCATION: [Protein 3B]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Interacts with membranes in a complex with viral protein 3AB. 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). {ECO:0000250}. |
| Modified Residue | MOD_RES 1415; /note=O-(5'-phospho-RNA)-tyrosine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity). {ECO:0000250}.; PTM: VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. 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 | 238,653 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21248; RHEA:23680 |
| Cross Reference Brenda |