Detail Information for IndEnz0002011629
IED ID IndEnz0002011629
Enzyme Type ID protease011629
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 Equine infectious anemia virus (isolate 1369) (EIAV)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Equine infectious anemia virus Equine infectious anemia virus (isolate 1369) (EIAV)
Enzyme Sequence TAWTFLKAMQKCSKKREARGSREAPETNFPDTTEESAQQICCTRDSSDSKSVPRSERNKKGIQCQGEGSSRGSQPGQFVGVTYNLEKRPTTIVLINDTPLNVLLDTGADTSVLTTAHYNRLKYRGRKYQGTGIIGVGGNVETFSTPVTIKKKGRHIKTRMLVADIPVTILGRDILQDLGAKLVLAQLSKEIKFRKIELKEGTMGPKIPQWPLTKEKLEGAKEIVQRLLSEGKISEASDNNPYNSPIFVIKKRSGKWRLLQDLRELNKTVQVGTEISRGLPHPGGLIKCKHMTVLDIGDAYFTIPLDPEFRPYTAFTIPSINHQEPDKRYVWNCLPQGFVLSPYIYQKTLQEILQPFRERYPEVQLYQYMDDLFVGSNGSKKQHKELIIELRAILLEEGFETPDDKLQEVPPYSWLGYQLCPENWKVQKMQLDMVKNPTLNDVQKLMGNITWMSSGVPGLTVKHIAATTKGCLELNQKVIWTEEAQKELEENNEKIKNAQGLQYYNPEEEMLCEVEITKNYEATYVIKQSQGILWAGKKIMKANKGWSTVKNLMLLLQHVATESITRVGKCPTFKVPFTKEQVMWEMQKGWYYSWLPEIVYTHQVVHDDWRMKLVEEPTSGITIYTDGGKQNGEGIAAYVTSNGRTKQKRLGPVTHQVAERMAIQMALEDTRDKQVNIVTDSYYCWKNITEGLGLEGPQSPWWPIIQNIREKEIVYFAWVPGHKGICGNQLADEAAKIKEEIMLAYQGTQIKEKRDEDAGFDLCVPYDIMIPVSDTKIIPTDVKIQVPPNSFGWVTGKSSMAKQGLLINGGIIDEGYTGEIQVICTNIGKSNIKLIEGQKFAQLIILQHHSNSRQPWDENKISQRGDKGFGSTGVFWVENIQEAQDEHENWHTSPKILARNYKIPLTVAKQITQECPHCTKQGSGPAGCVMRSPNHWQADCTHLDNKIILTFVESNSGYIHATLLSKENALCTSLAILEWARLFSPKSLHTDNGTNFVAEPVVNLLKFLKIAHTTGIPYHPESQGIVERANRTLKEKIQSHRDNTQTLEAALQLALITCNKGRESMGGQTPWEVFITNQAQVIHEKLLLQQAQSSKKFCFYKIPGEHDWKGPTRVLWKGDGAVVVNDEGKGIIAVPLTRTKLLIKPN
Enzyme Length 1146
Uniprot Accession Number P11204
Absorption
Active Site ACT_SITE 105; /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 1096..1144; /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); Beta strand (13); Chain (3); Compositional bias (2); DNA binding (1); Domain (4); Erroneous initiation (1); Helix (1); Metal binding (4); Region (1); Zinc finger (1)
Keywords 3D-structure;Aspartyl protease;Cleavage on pair of basic residues;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 X-ray crystallography (2)
Cross Reference PDB 1DUC; 1DUN;
Mapped Pubmed ID 9878436;
Motif
Gene Encoded By
Mass 129,510
Kinetics
Metal Binding METAL 887; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 891; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 915; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 918; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450
Rhea ID RHEA:22508
Cross Reference Brenda