Detail Information for IndEnz0002011245
IED ID IndEnz0002011245
Enzyme Type ID protease011245
Protein Name Gag-Pol polyprotein
Cleaved into: Protease
EC 3.4.23.-
; Reverse transcriptase/ribonuclease H
RT
EC 2.7.7.49
EC 2.7.7.7
EC 3.1.26.4
; Integrase
IN
EC 2.7.7.-
EC 3.1.-.-

Fragment
Gene Name pol
Organism Avian reticuloendotheliosis virus
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Gammaretrovirus Avian reticuloendotheliosis virus
Enzyme Sequence MSKESVAIIGATGNIRNYPKSEGRLVDLGRGLVTHSFLVIPECPDPLLGRDLLQKLRATISFTGEGPPEIRTEGKLLVTAPLEEEYRLFLEAPIQNVTLLEQWKREIPKVWAEINPPGLASTQAPIHVQLLSTALPVRVRQYPITLEAKRSLRETIRKFRAAGILRPVHSPWNTPLLPVRKSGTSEYRMVQDLREVNKRVETIHPTVPNPYTLLSLLPPDRIWYSVLDLKDAFFCIPLAPESQLIFAFEWADAEEGESGQLTWTRLPQGFKNSPTLFDEALNRDLQGFRLDHPSVSLLQYVDDLLIAADTQAACLSATRDLLMTLAELGYRVSGKKAQLCQEEVTYLGFKIHKGSRSLSNSRTQAILQIPVPKTKRQVREFLGTIGYCRLWIPGFAELAQPLYAATRGGNDPLVWGEKEEEAFQSLKLALTQPPALALPSLDKPFQLFVEETSGAAKGVLTQALGPWKRPVAYLSKRLDPVAAGWPRCLRAIAAAALLTREASKLTFGQDIEITSSHNLESLLRSPPDKWLTNARITQYQVLLLDPPRVRFKQTAALNPATLLPETDDTLPIHHCLDTLDSLTSTRPDLTDQPLAQAEATLFTDGSSYIRDGKRYAGAAVVTLDSVIWAEPLPIGTSAQKAELIALTKALEWSKDKSVNIYTDSRYAFATLHVHGMIYRERGLLTAGGKAIKNAPEILALLTAVWLPKRVAVMHCKGHQKDDAPTSTGNRRADEVAREVAIRPLSTQATISDAPDMPDTETPQYSNVEEALGHRLRGTKDPAGWWHLPDGRLLLPRAVGRKVLEQTHRATHLGESKLTELVRKHYLICGIYRAARDITTRCVACAQVNPGAAPVEKGLNSRIRGAAPGEHWEVDFTEMITAKGGYKYLLVLVDTFSGWVEAYPAKRETSQVVIKHLIHDIIPRFGLPVQIGSDNGPAFVAKVTQQLCEALNVSWKLHCAYRPQSSGQVERMNRTLKETIAKLRIETGGDWVSLLPQALLRARCTPGREGLSPFEILYGLKPPVVPRVGCDKLASITNQTLLKSLQALQATRSLARATLRDQLPQKEAQQDRTPLFQPGDLVFVKKHDFQQLGPRWDGPYTVVLSTPTAVKVAGKTPWIHYSRLKKAPDNQEEWTVSPTSDPLRVKLTRRAKP
Enzyme Length 1152
Uniprot Accession Number P03360
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; 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
DNA Binding
EC Number 3.4.23.-; 2.7.7.49; 2.7.7.7; 3.1.26.4; 2.7.7.-; 3.1.-.-
Enzyme Function FUNCTION: [Protease]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This 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 in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perfom a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000255|PROSITE-ProRule:PRU00405}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. {ECO:0000305|PubMed:24124581}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (4); Domain (4); Frameshift (1); Metal binding (9); Natural variant (7); Non-terminal residue (1); Region (1); Sequence conflict (1); Site (2)
Keywords DNA integration;DNA recombination;DNA-binding;DNA-directed DNA polymerase;Endonuclease;Hydrolase;Magnesium;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotidyltransferase;RNA-binding;RNA-directed DNA polymerase;Transferase;Viral genome integration;Virus entry into host cell
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000305}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 128,060
Kinetics
Metal Binding METAL 228; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 302; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 303; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 604; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 642; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 663; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 733; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 874; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 933; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457
Rhea ID RHEA:22508
Cross Reference Brenda