Detail Information for IndEnz0002008247
IED ID IndEnz0002008247
Enzyme Type ID protease008247
Protein Name Pol polyprotein
Cleaved into: Protease
Retropepsin
EC 3.4.23.-
; Reverse transcriptase/ribonuclease H
RT
EC 2.7.7.49
EC 3.1.26.13
Exoribonuclease H
EC 3.1.13.2
; Integrase
IN
EC 2.7.7.-
EC 3.1.-.-
Gene Name pol
Organism Caprine arthritis encephalitis virus (strain Cork) (CAEV-Co)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Caprine arthritis encephalitis virus (CAEV) Caprine arthritis encephalitis virus (strain Cork) (CAEV-Co)
Enzyme Sequence TRNHMSQLWKERTYAKRMQRKERHKGKTAGKREEGDTCGAVRSSYGITSAPPMVQVRIGSQQRNLLFDTGADRTIVRWHEGSGNPAGRIKLQGIGGIVEGEKWNNVELEYKGETRKGTIVVLPQSPVEVLGRDNMARFGIKIIMANLEEKRIPITKVKLKEGCTGPHVPQWPLTEEKLKGLTEIIDKLVEEGKLGKAPPHWTCNTPIFCIKKKSGKWRMLIDFRELNKQTEDLTEAQLGLPHPGGLQKKKHVTILDIGDAYFTIPLYEPYREYTCFTLLSPNNLGPCKRYYWKVLPQGWKLSPSVYQFTMQEILEDWIQQHPEIQFGIYMDDIYIGSDLEIKKHREIVKDLANYIAQYGFTLPEEKRQKGYPAKWLGFELHPQTWKFQKHTLPELTKGTITLNKLQKLVGELVWRQSIIGKSIPNILKLMEGDRELQSERKIEEVHVKEWEACRKKLEEMEGNYYNKDKDVYGQLAWGDKAIEYIVYQEKGKPLWVNVVHNIKNLSIPQQVIKAAQKLTQEVIIRTGKIPWILLPGKEEDWRLELQLGNITWMPKFWSCYRGHTRWRKRNIIEEVVEGPTYYTDGGKKNKVGSLGFIVSTGEKFRKHEEGTNQQLELRAIEEALKQGPQTMNLVTDSRYAFEFLLRNWDEEVIKNPIQARIMEIAHKKDRIGVHWVPGHKGIPQNEEIDKYISEIFLAKEGEGILPKREEDAGYDLICPEEVTIEPGQVKCIPIELRLNLKKSQWAMIATKSSMAAKGVFTQGGIIDSGYQGQIQVIMYNSNKIAVVIPQGRKFAQLILMDKKHGKLEPWGESRKTERGEKGFGSTGMYWIENIPLAEEDHTKWHQDARSLHLEFEIPRTAAEDIVNQCEICKEARTPAVIRGGNKRGVNHWQVDYTHYENIILLVWVETNSGLIYAEKVKGESGQEFRIKVMHWYALFGPESLQSDNGPAFAAEPTQLLMQYLGVKHTTGIPWNPQSQAIVERAHQLLKSTLKKFQPQFVAVESAIAAALVAINIKRKGGLGTSPMDIFIYNKEQKRINNKYNKNSQKIQFCYYRIRKRGHQESGKDQPRYCGKGKEPIVVKDIESEKYLVIPYKDAKFIPPPTKEKE
Enzyme Length 1109
Uniprot Accession Number P33459
Absorption
Active Site ACT_SITE 68; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; 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};
DNA Binding DNA_BIND 1051..1103; /note=Integrase-type; /evidence=ECO:0000255|PROSITE-ProRule:PRU00506
EC Number 3.4.23.-; 2.7.7.49; 3.1.26.13; 3.1.13.2; 2.7.7.-; 3.1.-.-
Enzyme Function FUNCTION: During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (3); DNA binding (1); Domain (4); Erroneous initiation (1); Metal binding (4); Region (1); Zinc finger (1)
Keywords Aspartyl protease;DNA integration;DNA recombination;DNA-binding;Endonuclease;Hydrolase;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotidyltransferase;Protease;RNA-directed DNA polymerase;Transferase;Viral genome integration;Virus entry into host cell;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 127,678
Kinetics
Metal Binding METAL 841; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 845; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 869; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 872; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450
Rhea ID RHEA:22508
Cross Reference Brenda