Detail Information for IndEnz0002006488
IED ID IndEnz0002006488
Enzyme Type ID protease006488
Protein Name Pol polyprotein
Cleaved into: Protease
EC 3.4.23.-
Retropepsin
; Reverse transcriptase/ribonuclease H
RT
EC 2.7.7.49
EC 3.1.26.13
Exoribonuclease H
EC 3.1.13.2
; Deoxyuridine 5'-triphosphate nucleotidohydrolase
dUTPase
EC 3.6.1.23
; Integrase
IN
EC 2.7.7.-
EC 3.1.-.-
Gene Name pol
Organism Ovine maedi visna related virus (strain South Africa) (SA-OMVV) (Ovine lentivirus)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Visna-maedi virus Visna/maedi virus SA-OMVV Ovine maedi visna related virus (strain South Africa) (SA-OMVV) (Ovine lentivirus)
Enzyme Sequence SNITAGKQQEGATCGAVRAPYVVTEAPPKIDIKVGTNWKKVLVDTGADRTIVRYHDNSGIPTGRIKLQGIGGIIEGEKWDKVVIQYKEKRIEGTIVVLPSSPVEVLGRDNMAKLDIGIIMANLEEKKIPITQVKLKEGCKGPHIAQWPLTQEKLEGLKEIVDKLEKEGKVGRAPPHWTCNTPIFCIKKKSGKWRMLIDFRELNKQTEDLAEAQLGLPHPGGLQKKKHVTILDIGDAYFTIPLYEPYRPYTCFTMLSPNNLGPCTRYYWKVLPQGWKLSPSVYQFTMQEILRDWIAKHPMIQFGIYMDDIYIGSDLDIMKHREIVEELASYIAQYGFMLPEEKRQEGYPAKWLGFELHPEKWRFQKHTLPEIKEGTITLNKLQKLVGDLVWRQSLIGKSIPNILKLMEGDRALQSERRIELRHVKEWEECRRKLAEMEGNYYDEEKDVYGQIDWGDKAIEYIVFQERGKPLWVNVVHNIKNLSQSQQIIKAAQKLTQEVIIRIGKIPWILLPGKEEDWILELQIGNITWMPSFWSCYRGSIRWKKRNVITEVVEGPTYYTDGGKKNGKGSLGFIASTGVKFRKHEEGTNQQLELRAIEEACKQGPEKMNIVTDSRYAYEFMRRNWDEEVIKNPIQARIMKLVHDKEQIGVHWVPGHKGIPQNEEIDKYISEIFLAREGSGILPKRAEDAGYDLICPQEVCIPAGQVRKIPINLRINLKEDQWAMVGTKSSFASKGVFVQGGIIDSGYQGIIQVVVYNSNDKEVIIPQGRKFAQLILMPLIHEDLEAWGETRRTERGNQGFGSTGAYWIENIPLAEEDHSKWHQDAGSLHLDFGIPRTAAEDIVQQCEVCQENKMPSTIRGSNRRGIDHWQVDYTHYEDKIILVWVETNSGLIYAERVKGETGQEFRIMTIRWYGLFAPKSLQSDNGPAFVAEPTQLLMKYLGITHTTGIPWNPQSQALVERTHQTLKNTIEKFVSMFASFDSAIAAALITLNIKRKGGLGTSPMDIFIFNKEQQRIQQQSTRNQSKFRFCYYRVRKRGHPGEWLGPTQVLWEGEGAIVIKDKNLEKYLVIAKKDVKFIPQPKEIQTE
Enzyme Length 1086
Uniprot Accession Number P16901
Absorption
Active Site ACT_SITE 44; /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=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; 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 1027..1079; /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; 3.6.1.23; 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 (4); DNA binding (1); Domain (4); Metal binding (4); Zinc finger (1)
Keywords Aspartyl protease;DNA integration;DNA recombination;DNA-binding;Endonuclease;Hydrolase;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotide metabolism;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: Cleavage sites that yield the mature proteins remain to be determined.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 124,515
Kinetics
Metal Binding METAL 817; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 821; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 845; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 848; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450
Rhea ID RHEA:10248; RHEA:22508
Cross Reference Brenda