Detail Information for IndEnz0002010495
IED ID IndEnz0002010495
Enzyme Type ID protease010495
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
; Deoxyuridine 5'-triphosphate nucleotidohydrolase
dUTPase
EC 3.6.1.23
; Integrase
IN
EC 2.7.7.-
EC 3.1.-.-
Gene Name pol
Organism Feline immunodeficiency virus (isolate Petaluma) (FIV)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Feline immunodeficiency virus Feline immunodeficiency virus (isolate Petaluma) (FIV)
Enzyme Sequence KEFGKLEGGASCSPSESNAASSNAICTSNGGETIGFVNYNKVGTTTTLEKRPEILIFVNGYPIKFLLDTGADITILNRRDFQVKNSIENGRQNMIGVGGGKRGTNYINVHLEIRDENYKTQCIFGNVCVLEDNSLIQPLLGRDNMIKFNIRLVMAQISDKIPVVKVKMKDPNKGPQIKQWPLTNEKIEALTEIVERLEKEGKVKRADSNNPWNTPVFAIKKKSGKWRMLIDFRELNKLTEKGAEVQLGLPHPAGLQIKKQVTVLDIGDAYFTIPLDPDYAPYTAFTLPRKNNAGPGRRFVWCSLPQGWILSPLIYQSTLDNIIQPFIRQNPQLDIYQYMDDIYIGSNLSKKEHKEKVEELRKLLLWWGFETPEDKLQEEPPYTWMGYELHPLTWTIQQKQLDIPEQPTLNELQKLAGKINWASQAIPDLSIKALTNMMRGNQNLNSTRQWTKEARLEVQKAKKAIEEQVQLGYYDPSKELYAKLSLVGPHQISYQVYQKDPEKILWYGKMSRQKKKAENTCDIALRACYKIREESIIRIGKEPRYEIPTSREAWESNLINSPYLKAPPPEVEYIHAALNIKRALSMIKDAPIPGAETWYIDGGRKLGKAAKAAYWTDTGKWRVMDLEGSNQKAEIQALLLALKAGSEEMNIITDSQYVINIILQQPDMMEGIWQEVLEELEKKTAIFIDWVPGHKGIPGNEEVDKLCQTMMIIEGDGILDKRSEDAGYDLLAAKEIHLLPGEVKVIPTGVKLMLPKGYWGLIIGKSSIGSKGLDVLGGVIDEGYRGEIGVIMINVSRKSITLMERQKIAQLIILPCKHEVLEQGKVVMDSERGDNGYGSTGVFSSWVDRIEEAEINHEKFHSDPQYLRTEFNLPKMVAEEIRRKCPVCRIIGEQVGGQLKIGPGIWQMDCTHFDGKIILVGIHVESGYIWAQIISQETADCTVKAVLQLLSAHNVTELQTDNGPNFKNQKMEGVLNYMGVKHKFGIPGNPQSQALVENVNHTLKVWIQKFLPETTSLDNALSLAVHSLNFKRRGRIGGMAPYELLAQQESLRIQDYFSAIPQKLQAQWIYYKDQKDKKWKGPMRVEYWGQGSVLLKDEEKGYFLIPRRHIRRVPEPCALPEGDE
Enzyme Length 1124
Uniprot Accession Number P16088
Absorption
Active Site ACT_SITE 68; /note=For protease activity
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 1067..1115; /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); Beta strand (29); Chain (4); DNA binding (1); Domain (4); Helix (9); Metal binding (9); Turn (6); Zinc finger (1)
Keywords 3D-structure;Aspartyl protease;DNA integration;DNA recombination;DNA-binding;Endonuclease;Hydrolase;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotide metabolism;Nucleotidyltransferase;Protease;RNA-directed DNA polymerase;Reference proteome;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 X-ray crystallography (20)
Cross Reference PDB 1B11; 1DUT; 1F7D; 1F7K; 1F7N; 1F7O; 1F7P; 1F7Q; 1F7R; 1FIV; 2FIV; 2HAH; 3FIV; 3OGP; 3OGQ; 4FIV; 4MQ3; 4PA1; 5FIV; 6FIV;
Mapped Pubmed ID 10651036; 10957629; 17212810; 21636894; 25199694; 9827997;
Motif
Gene Encoded By
Mass 127,494
Kinetics
Metal Binding METAL 601; /note=Magnesium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 601; /note=Magnesium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 634; /note=Magnesium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 654; /note=Magnesium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 704; /note=Magnesium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 857; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 861; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 885; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 888; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450
Rhea ID RHEA:10248; RHEA:22508
Cross Reference Brenda 3.4.23.B4;