| IED ID | IndEnz0002007584 |
| Enzyme Type ID | protease007584 |
| Protein Name |
Gag-Pol polyprotein Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide SP p3 ; Nucleocapsid protein p12; Protease p15 EC 3.4.23.- ; Reverse transcriptase beta-subunit RT-beta ; Reverse transcriptase alpha-subunit RT-alpha EC 2.7.7.49 EC 2.7.7.7 EC 3.1.26.4 ; Integrase IN EC 2.7.7.- EC 3.1.-.- pp32 ; p4 |
| Gene Name | gag-pol |
| Organism | Rous sarcoma virus (strain Prague C) (RSV-PrC) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Alpharetrovirus Rous sarcoma virus Rous sarcoma virus (strain Prague C) (RSV-PrC) |
| Enzyme Sequence | MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLNRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQKTAPLTDQGIAAAMSSAIQPLIMAVVNRERDGQTGSGGRARGLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCNGMGHNAKQCRKRDGNQGQRPGKGLSSGPWPGPEPPAVSLAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNLIGRATVLTVALHLAIPLKWKPDHTPVWIDQWPLPEGKLVALTQLVEKELQLGHIEPSLSCWNTPVFVIRKASGSYRLLHDLRAVNAKLVPFGAVQQGAPVLSALPRGWPLMVLDLKDCFFSIPLAEQDREAFAFTLPSVNNQAPARRFQWKVLPQGMTCSPTICQLVVGQVLEPLRLKHPSLCMLHYMDDLLLAASSHDGLEAAGEEVISTLERAGFTISPDKVQREPGVQYLGYKLGSTYVAPVGLVAEPRIATLWDVQKLVGSLQWLRPALGIPPRLMGPFYEQLRGSDPNEAREWNLDMKMAWREIVRLSTTAALERWDPALPLEGAVARCEQGAIGVLGQGLSTHPRPCLWLFSTQPTKAFTAWLEVLTLLITKLRASAVRTFGKEVDILLLPACFREDLPLPEGILLALKGFAGKIRSSDTPSIFDIARPLHVSLKVRVTDHPVPGPTVFTDASSSTHKGVVVWREGPRWEIKEIADLGASVQQLEARAVAMALLLWPTTPTNVVTDSAFVAKMLLKMGQEGVPSTAAAFILEDALSQRSAMAAVLHVRSHSEVPGFFTEGNDVADSQATFQAYPLREAKDLHTALHIGPRALSKACNISMQQAREVVQTCPHCNSAPALEAGVNPRGLGPLQIWQTDFTLEPRMAPRSWLAVTVDTASSAIVVTQHGRVTSVAVQHHWATAIAVLGRPKAIKTDNGSCFTSKSTREWLARWGIAHTTGIPGNSQGQAMVERANRLLKDRIRVLAEGDGFMKRIPTSKQGELLAKAMYALNHFERGENTKTPIQKHWRPTVLTEGPPVKIRIETGEWEKGWNVLVWGRGYAAVKNRDTDKVIWVPSRKVKPDITQKDEVTKKDEASPLFAGISDWIPWEDEQEGLQGETASNKQERPGEDTLAANES |
| Enzyme Length | 1603 |
| Uniprot Accession Number | P03354 |
| Absorption | |
| Active Site | ACT_SITE 614; /note=For protease activity; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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}; 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=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; |
| DNA Binding | DNA_BIND 1502..1550; /note=Integrase-type; /evidence=ECO:0000255|PROSITE-ProRule:PRU00506 |
| EC Number | 3.4.23.-; 2.7.7.49; 2.7.7.7; 3.1.26.4; 2.7.7.-; 3.1.-.- |
| Enzyme Function | FUNCTION: Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. {ECO:0000250|UniProtKB:P03322}.; FUNCTION: [Spacer peptide]: Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle. Essential layering element during tube assembly. {ECO:0000250|UniProtKB:P03322}.; FUNCTION: [Nucleocapsid protein p12]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.; FUNCTION: [Protease p15]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This recombination event is an essential step in the viral replication cycle. Has a strong preference for using the 3'-OH at the viral DNA end as a nucleophile. {ECO:0000269|PubMed:11024025}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Chain (13); Compositional bias (1); DNA binding (1); Domain (4); Erroneous initiation (1); Helix (17); Metal binding (14); Motif (4); Mutagenesis (4); Natural variant (10); Peptide (1); Region (8); Sequence conflict (4); Site (13); Turn (2); Zinc finger (3) |
| Keywords | 3D-structure;Aspartyl protease;Capsid protein;DNA integration;DNA recombination;DNA-binding;DNA-directed DNA polymerase;Endonuclease;Hydrolase;Magnesium;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed DNA polymerase;Repeat;Ribosomal frameshifting;Transferase;Viral genome integration;Viral nucleoprotein;Virion;Virus entry into host cell;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:15102858, ECO:0000269|PubMed:8636100}.; PTM: Capsid protein p27: The cleavage at the C-terminus is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1. {ECO:0000250|UniProtKB:P03322}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (5); Electron microscopy (3); X-ray crystallography (10) |
| Cross Reference PDB | 1BAI; 1C0M; 1C1A; 3TIR; 4FW1; 4FW2; 5EJK; 5KZ9; 5KZA; 5KZB; 6CCJ; 6CE5; 6CUS; 6CV8; 6CW4; 7JN3; 7KU7; 7KUI; |
| Mapped Pubmed ID | 29117524; 30309983; 33712691; |
| Motif | MOTIF 172..175; /note=PPXY motif; /evidence=ECO:0000269|PubMed:20392845; MOTIF 180..184; /note=LYPX(n)L motif; /evidence=ECO:0000269|PubMed:20392845; MOTIF 219..229; /note=Nuclear export signal; /evidence=ECO:0000250|UniProtKB:P03322; MOTIF 524..527; /note=Nuclear/nucleolar localization signal; /evidence=ECO:0000250|UniProtKB:P03322 |
| Gene Encoded By | |
| Mass | 173,881 |
| Kinetics | |
| Metal Binding | METAL 815; /note="Magnesium 1; catalytic; for reverse transcriptase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"; METAL 890; /note="Magnesium 1; catalytic; for reverse transcriptase activity"; /evidence="ECO:0000269|PubMed:10708441"; METAL 891; /note="Magnesium 1; catalytic; for reverse transcriptase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"; METAL 1158; /note="Magnesium 2; catalytic; for RNase H activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"; METAL 1192; /note="Magnesium 2; catalytic; for RNase H activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"; METAL 1213; /note="Magnesium 2; catalytic; for RNase H activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:10708441"; METAL 1272; /note="Magnesium 2; catalytic; for RNase H activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"; METAL 1289; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"; METAL 1293; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"; METAL 1317; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"; METAL 1320; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"; METAL 1344; /note="Magnesium 3; catalytic; for integrase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:10669607"; METAL 1401; /note="Magnesium 3; catalytic; for integrase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:10669607"; METAL 1437; /note="Magnesium 3; catalytic; for integrase activity"; /evidence="ECO:0000269|PubMed:10669607" |
| Rhea ID | RHEA:22508 |
| Cross Reference Brenda |