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 |