| IED ID | IndEnz0002011333 |
| Enzyme Type ID | protease011333 |
| Protein Name |
Transposon Ty3-G Gag-Pol polyprotein Gag3-Pol3 Transposon Ty3-1 TYA-TYB polyprotein Cleaved into: Capsid protein CA p24 ; Spacer peptide p3; Nucleocapsid protein p11 NC ; Ty3 protease PR EC 3.4.23.- p16 ; Spacer peptide J; Reverse transcriptase/ribonuclease H RT RT-RH EC 2.7.7.49 EC 2.7.7.7 EC 3.1.26.4 p55 ; Integrase p61 IN ; Integrase p58 IN |
| Gene Name | TY3B-G YGRWTy3-1 POL YGR109W-B G5984 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSFMDQIPGGGNYPKLPVECLPNFPIQPSLTFRGRNDSHKLKNFISEIMLNMSMISWPNDASRIVYCRRHLLNPAAQWANDFVQEQGILEITFDTFIQGLYQHFYKPPDINKIFNAITQLSEAKLGIERLNQRFRKIWDRMPPDFMTEKAAIMTYTRLLTKETYNIVRMHKPETLKDAMEEAYQTTALTERFFPGFELDADGDTIIGATTHLQEEYDSDYDSEDNLTQNGYVHTVRTRRSYNKPMSNHRNRRNNNPSREECIKNRLCFYCKKEGHRLNECRARKAVLTDLELESKDQQTPFIKTLPIVHYIAIPEMDNTAEKTIKIQNTKVKTLFDSGSPTSFIRRDIVELLKYEIYETPPLRFRGFVATKSAVTSEAVTIDLKINDLHITLAAYILDNMDYQLLIGNPILRRYPKILHTVLNTRESPDSLKPKTYRSETVNNVRTYSAGNRGNPRNIKLSFAPTILEATDPKSAGNRGDSRTKTLSLATTTPAAIDPLTTLDNPGSTQSTFAQFPIPEEASILEEDGKYSNVVSTIQSVEPNATDHSNKDTFCTLPVWLQQKYREIIRNDLPPRPADINNIPVKHDIEIKPGARLPRLQPYHVTEKNEQEINKIVQKLLDNKFIVPSKSPCSSPVVLVPKKDGTFRLCVDYRTLNKATISDPFPLPRIDNLLSRIGNAQIFTTLDLHSGYHQIPMEPKDRYKTAFVTPSGKYEYTVMPFGLVNAPSTFARYMADTFRDLRFVNVYLDDILIFSESPEEHWKHLDTVLERLKNENLIVKKKKCKFASEETEFLGYSIGIQKIAPLQHKCAAIRDFPTPKTVKQAQRFLGMINYYRRFIPNCSKIAQPIQLFICDKSQWTEKQDKAIDKLKDALCNSPVLVPFNNKANYRLTTDASKDGIGAVLEEVDNKNKLVGVVGYFSKSLESAQKNYPAGELELLGIIKALHHFRYMLHGKHFTLRTDHISLLSLQNKNEPARRVQRWLDDLATYDFTLEYLAGPKNVVADAISRAVYTITPETSRPIDTESWKSYYKSDPLCSAVLIHMKELTQHNVTPEDMSAFRSYQKKLELSETFRKNYSLEDEMIYYQDRLVVPIKQQNAVMRLYHDHTLFGGHFGVTVTLAKISPIYYWPKLQHSIIQYIRTCVQCQLIKSHRPRLHGLLQPLPIAEGRWLDISMDFVTGLPPTSNNLNMILVVVDRFSKRAHFIATRKTLDATQLIDLLFRYIFSYHGFPRTITSDRDVRMTADKYQELTKRLGIKSTMSSANHPQTDGQSERTIQTLNRLLRAYASTNIQNWHVYLPQIEFVYNSTPTRTLGKSPFEIDLGYLPNTPAIKSDDEVNARSFTAVELAKHLKALTIQTKEQLEHAQIEMETNNNQRRKPLLLNIGDHVLVHRDAYFKKGAYMKVQQIYVGPFRVVKKINDNAYELDLNSHKKKHRVINVQFLKKFVYRPDAYPKNKPISSTERIKRAHEVTALIGIDTTHKTYLCHMQDVDPTLSVEYSEAEFCQIPERTRRSILANFRQLYETQDNPEREEDVVSQNEICQYDNTSP |
| Enzyme Length | 1547 |
| Uniprot Accession Number | Q99315 |
| Absorption | |
| Active Site | ACT_SITE 336; /note=For protease activity; shared with dimeric partner; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; |
| DNA Binding | |
| EC Number | 3.4.23.-; 2.7.7.49; 2.7.7.7; 3.1.26.4 |
| Enzyme Function | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the genomic RNA-nucleocapsid complex.; FUNCTION: Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription. {ECO:0000250, ECO:0000269|PubMed:10593967, ECO:0000269|PubMed:1371165, ECO:0000269|PubMed:2159534, ECO:0000269|PubMed:7515969}.; FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.; FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends.; FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (16); Chain (7); Domain (3); Erroneous gene model prediction (4); Helix (19); Initiator methionine (1); Metal binding (8); Modified residue (1); Mutagenesis (2); Peptide (2); Region (1); Site (7); Turn (5); Zinc finger (1) |
| Keywords | 3D-structure;ATP-binding;Acetylation;Aspartyl protease;Cytoplasm;DNA integration;DNA recombination;DNA-binding;DNA-directed DNA polymerase;Endonuclease;Hydrolase;Magnesium;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotide-binding;Nucleotidyltransferase;Nucleus;Protease;RNA-binding;RNA-directed DNA polymerase;Reference proteome;Ribosomal frameshifting;Transferase;Transposable element;Viral release from host cell;Virion maturation;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1371165}. Nucleus {ECO:0000269|PubMed:1371165}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000269|PubMed:15956549 |
| Post Translational Modification | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs. {ECO:0000269|PubMed:15956549, ECO:0000269|PubMed:7677953}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4OL8; |
| Mapped Pubmed ID | 11604517; 11604518; 11861848; 11994277; 15647500; 15944162; 19759143; 20444245; 21189452; 22998189; 23226439; 24603646; 24608367; 27141325; 34848735; 9448009; |
| Motif | |
| Gene Encoded By | |
| Mass | 178,307 |
| Kinetics | |
| Metal Binding | METAL 686; /note=Magnesium 1; catalytic; for reverse transcriptase activity; /evidence=ECO:0000250; METAL 748; /note=Magnesium 1; catalytic; for reverse transcriptase activity; /evidence=ECO:0000250; METAL 749; /note=Magnesium 1; catalytic; for reverse transcriptase activity; /evidence=ECO:0000250; METAL 893; /note=Magnesium 2; catalytic; for RNase H activity; /evidence=ECO:0000250; METAL 936; /note=Magnesium 2; catalytic; for RNase H activity; /evidence=ECO:0000250; METAL 961; /note=Magnesium 2; catalytic; for RNase H activity; /evidence=ECO:0000250; METAL 1175; /note=Magnesium 3; catalytic; for integrase activity; /evidence=ECO:0000250; METAL 1236; /note=Magnesium 3; catalytic; for integrase activity; /evidence=ECO:0000250 |
| Rhea ID | RHEA:22508 |
| Cross Reference Brenda |