Detail Information for IndEnz0002011514
IED ID IndEnz0002011514
Enzyme Type ID protease011514
Protein Name Truncated transposon Ty1-A Gag-Pol polyprotein
TY1B
Transposon Ty1 TYB polyprotein

Cleaved into: Integrase
IN
Pol-p71
p84
p90
; Reverse transcriptase/ribonuclease H
RT
RT-RH
EC 2.7.7.49
EC 2.7.7.7
EC 3.1.26.4
Pol-p63
p60
Gene Name TY1B-A YARCTy1-1 POL YAR009C
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 METFTGYLKSTCFHQISPYPPSIMSIQVKVHANILILSFIECLRMPMHRQIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKLRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Enzyme Length 1196
Uniprot Accession Number O13527
Absorption
Active Site
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; 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; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
DNA Binding
EC Number 2.7.7.49; 2.7.7.7; 3.1.26.4
Enzyme Function 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 (By similarity). {ECO:0000250}.; 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 (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (3); Compositional bias (7); Domain (3); Metal binding (8); Motif (1); Region (3); Site (1)
Keywords Cytoplasm;DNA integration;DNA recombination;DNA-binding;DNA-directed DNA polymerase;Endonuclease;Hydrolase;Magnesium;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotidyltransferase;Nucleus;RNA-binding;RNA-directed DNA polymerase;Reference proteome;Transferase;Transposable element;Transposition
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
Modified Residue
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 yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 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 (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10861903; 11413300; 11743162; 11805837; 14504219; 14690591; 18167548; 19536198; 20419146; 21179020; 22842922; 23226439; 9448008; 9448009;
Motif MOTIF 619..653; /note=Bipartite nuclear localization signal; /evidence=ECO:0000250
Gene Encoded By
Mass 136,732
Kinetics
Metal Binding METAL 112; /note=Magnesium 1; catalytic; for integrase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 177; /note=Magnesium 1; catalytic; for integrase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 787; /note=Magnesium 2; catalytic; for reverse transcriptase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 868; /note=Magnesium 2; catalytic; for reverse transcriptase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 869; /note=Magnesium 2; catalytic; for reverse transcriptase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 1051; /note=Magnesium 3; catalytic; for RNase H activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 1093; /note=Magnesium 3; catalytic; for RNase H activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 1126; /note=Magnesium 3; catalytic; for RNase H activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457
Rhea ID RHEA:22508
Cross Reference Brenda