Q1A249 · POL_SIVEK
- ProteinGag-Pol polyprotein
- Genegag-pol
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1448 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Miscellaneous
Catalytic activity
- 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.
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Cofactor
Activity regulation
Features
Showing features for site, active site, binding site, dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 135-136 | Cleavage; by viral protease | ||||
Sequence: YP | ||||||
Site | 224-225 | Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA | ||||
Sequence: GP | ||||||
Site | 366-367 | Cleavage; by viral protease | ||||
Sequence: LA | ||||||
Site | 380-381 | Cleavage; by viral protease | ||||
Sequence: FM | ||||||
Site | 435-436 | Cleavage; by viral protease | ||||
Sequence: QF | ||||||
Site | 497-498 | Cleavage; by viral protease | ||||
Sequence: FP | ||||||
Active site | 522 | For protease activity; shared with dimeric partner | ||||
Sequence: D | ||||||
Site | 596-597 | Cleavage; by viral protease | ||||
Sequence: FP | ||||||
Binding site | 706 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 781 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 782 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Site | 997 | Essential for RT p66/p51 heterodimerization | ||||
Sequence: W | ||||||
Site | 1010 | Essential for RT p66/p51 heterodimerization | ||||
Sequence: W | ||||||
Site | 1036-1037 | Cleavage; by viral protease | ||||
Sequence: YY | ||||||
Binding site | 1039 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: D | ||||||
Binding site | 1074 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: E | ||||||
Binding site | 1094 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: D | ||||||
Binding site | 1145 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: D | ||||||
Site | 1156-1157 | Cleavage; by viral protease | ||||
Sequence: LF | ||||||
Binding site | 1168 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1172 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1196 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1199 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1220 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for integrase activity | ||||
Sequence: D | ||||||
Binding site | 1272 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for integrase activity | ||||
Sequence: D | ||||||
DNA binding | 1379-1426 | Integrase-type | ||||
Sequence: FRVYYRDSREPTWKGPAKLLWKGEGAVVIQDNGDIKVVPRRKAKIIRD |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGag-Pol polyprotein
- Alternative names
- Cleaved into 10 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Ortervirales > Retroviridae > Orthoretrovirinae > Lentivirus > Simian immunodeficiency virus
- Virus hosts
Accessions
- Primary accessionQ1A249
Proteomes
Subcellular Location
Matrix protein p17
Capsid protein p24
Nucleocapsid protein p7
Reverse transcriptase/ribonuclease H
Integrase
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; by host | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine; by host | ||||
Sequence: G | ||||||
Chain | PRO_0000249374 | 2-135 | Matrix protein p17 | |||
Sequence: GARASVLTGGKLDQWEKIYLRPGGKKKYMMKHLVWASRELERFACNPGLMDTAEGCAQLLRQLEPALKTGSEGLRSLFNTLAVLYCVHNNIKVQNTQEALEKLREKMKAEQKEPEPEQAAGAAAAPESSISRNY | ||||||
Chain | PRO_0000261302 | 2-1448 | Gag-Pol polyprotein | |||
Sequence: GARASVLTGGKLDQWEKIYLRPGGKKKYMMKHLVWASRELERFACNPGLMDTAEGCAQLLRQLEPALKTGSEGLRSLFNTLAVLYCVHNNIKVQNTQEALEKLREKMKAEQKEPEPEQAAGAAAAPESSISRNYPLVQNAQGQMVHQPLSPRTLNAWVKVVEEKAFNPEVIPMFMALSEGATPQDLNTMLNTVGGHQAAMQMLKEVINEEAAEWDRGHPVHMGPIPPGQVREPRGSDIAGTTSTLAEQVAWMTANPPVPVGDIYRRWIVLGLNKIVRMYSPASILDIKQGPKETFRDYVDRFYKTLRAEQATQEVKNWMTETLLVQNANPDCKNILRALGPGASLEEMMTACQGVGGPAHKARVLAEAMTQAQTATSVFMQRGNFKGIRKTIKCFNCGKEGHLARNCKAPRKKGCWKCGQEGHQMKDCRSGERQFFREGLASLQREARKFPPDNNKERANSPSNRELWVSGGEDHTGDREGRKGEDRELSVPTLNFPQITLWQRPILTVKIGGEIKEALLDTGADDTVIEEIQLEGKWKPKMIGGIGGFIKVKQYDNVIIEIQGKKAVGTVLVGPTPVNIIGRNFLTQIGCTLNFPISPIETIPVKLKPGMDGPRVKQWPLTEEKIKALTEICTEMEKEGKISRIGPENPYNTPIFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSCPLDENFRKYTAFTIPSVNNETPGIRYQYNVLPQGWKGSPAIFQSTMTKILEPFRKNNPELVIYQYMDDLYVGSDLEITQHREAVERLRSHLLTWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQTIQLPEKDTWTVNDIQQLVGKLNWASQIYPGIKVKQLCKLIRGAKALTEVVTLTREAELELAENREILKEPVHGAYYNPDKELIAEIQKQGQGQWTYQIYQDLHKNLKTGKYAKMRSTHTNDIRQLTEVVQKVALESIVIWGKTPKFRLPVQKEVWETWWTEYWQATWIPDWEFVNTPPLVKLWYQLETEPISGAETYYVDGAANRETKLGKAGFVTDRGRQKVTSISETTNQQAELQAVLMALQDAGQEVNIVTDSQYVLGIIHSQPDKSESELVNQIIEELIKKERIYLSWVPAHKGIGGNEQIDKLVSTGIRKVLFLDGIDKAQEEHERYHSNWKAMASDFNLPPIVAKEIVASCDKCQLKGEAIHGQINCSPGVWQLDCTHLEGKIILVAVHVASGYLEAEVIPAETGQETAYFILKLAGRWPVKVIHTDNGSNFTSATVKAACWWANIQQEFGIPYNPQSQGAVESMNKELKKIIGQIRDQAEHLKTAVQMAVFIHNFKRKGGIGGYTAGERIIDIIATDIQTTKLQTQILKVQNFRVYYRDSREPTWKGPAKLLWKGEGAVVIQDNGDIKVVPRRKAKIIRDYGKQMAGDGCVASGQDESQDME | ||||||
Modified residue | 135 | Phosphotyrosine; by host | ||||
Sequence: Y | ||||||
Chain | PRO_0000249375 | 136-366 | Capsid protein p24 | |||
Sequence: PLVQNAQGQMVHQPLSPRTLNAWVKVVEEKAFNPEVIPMFMALSEGATPQDLNTMLNTVGGHQAAMQMLKEVINEEAAEWDRGHPVHMGPIPPGQVREPRGSDIAGTTSTLAEQVAWMTANPPVPVGDIYRRWIVLGLNKIVRMYSPASILDIKQGPKETFRDYVDRFYKTLRAEQATQEVKNWMTETLLVQNANPDCKNILRALGPGASLEEMMTACQGVGGPAHKARVL | ||||||
Peptide | PRO_0000249376 | 367-380 | Spacer peptide p2 | |||
Sequence: AEAMTQAQTATSVF | ||||||
Chain | PRO_0000249377 | 381-435 | Nucleocapsid protein p7 | |||
Sequence: MQRGNFKGIRKTIKCFNCGKEGHLARNCKAPRKKGCWKCGQEGHQMKDCRSGERQ | ||||||
Chain | PRO_0000249379 | 436-497 | p6-pol | |||
Sequence: FFREGLASLQREARKFPPDNNKERANSPSNRELWVSGGEDHTGDREGRKGEDRELSVPTLNF | ||||||
Chain | PRO_0000249380 | 498-596 | Protease | |||
Sequence: PQITLWQRPILTVKIGGEIKEALLDTGADDTVIEEIQLEGKWKPKMIGGIGGFIKVKQYDNVIIEIQGKKAVGTVLVGPTPVNIIGRNFLTQIGCTLNF | ||||||
Chain | PRO_0000249382 | 597-1036 | p51 RT | |||
Sequence: PISPIETIPVKLKPGMDGPRVKQWPLTEEKIKALTEICTEMEKEGKISRIGPENPYNTPIFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSCPLDENFRKYTAFTIPSVNNETPGIRYQYNVLPQGWKGSPAIFQSTMTKILEPFRKNNPELVIYQYMDDLYVGSDLEITQHREAVERLRSHLLTWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQTIQLPEKDTWTVNDIQQLVGKLNWASQIYPGIKVKQLCKLIRGAKALTEVVTLTREAELELAENREILKEPVHGAYYNPDKELIAEIQKQGQGQWTYQIYQDLHKNLKTGKYAKMRSTHTNDIRQLTEVVQKVALESIVIWGKTPKFRLPVQKEVWETWWTEYWQATWIPDWEFVNTPPLVKLWYQLETEPISGAETY | ||||||
Chain | PRO_0000249381 | 597-1156 | Reverse transcriptase/ribonuclease H | |||
Sequence: PISPIETIPVKLKPGMDGPRVKQWPLTEEKIKALTEICTEMEKEGKISRIGPENPYNTPIFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSCPLDENFRKYTAFTIPSVNNETPGIRYQYNVLPQGWKGSPAIFQSTMTKILEPFRKNNPELVIYQYMDDLYVGSDLEITQHREAVERLRSHLLTWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQTIQLPEKDTWTVNDIQQLVGKLNWASQIYPGIKVKQLCKLIRGAKALTEVVTLTREAELELAENREILKEPVHGAYYNPDKELIAEIQKQGQGQWTYQIYQDLHKNLKTGKYAKMRSTHTNDIRQLTEVVQKVALESIVIWGKTPKFRLPVQKEVWETWWTEYWQATWIPDWEFVNTPPLVKLWYQLETEPISGAETYYVDGAANRETKLGKAGFVTDRGRQKVTSISETTNQQAELQAVLMALQDAGQEVNIVTDSQYVLGIIHSQPDKSESELVNQIIEELIKKERIYLSWVPAHKGIGGNEQIDKLVSTGIRKVL | ||||||
Chain | PRO_0000249383 | 1037-1156 | p15 | |||
Sequence: YVDGAANRETKLGKAGFVTDRGRQKVTSISETTNQQAELQAVLMALQDAGQEVNIVTDSQYVLGIIHSQPDKSESELVNQIIEELIKKERIYLSWVPAHKGIGGNEQIDKLVSTGIRKVL | ||||||
Chain | PRO_0000249384 | 1157-1448 | Integrase | |||
Sequence: FLDGIDKAQEEHERYHSNWKAMASDFNLPPIVAKEIVASCDKCQLKGEAIHGQINCSPGVWQLDCTHLEGKIILVAVHVASGYLEAEVIPAETGQETAYFILKLAGRWPVKVIHTDNGSNFTSATVKAACWWANIQQEFGIPYNPQSQGAVESMNKELKKIIGQIRDQAEHLKTAVQMAVFIHNFKRKGGIGGYTAGERIIDIIATDIQTTKLQTQILKVQNFRVYYRDSREPTWKGPAKLLWKGEGAVVIQDNGDIKVVPRRKAKIIRDYGKQMAGDGCVASGQDESQDME |
Post-translational modification
Keywords
- PTM
Interaction
Subunit
Matrix protein p17
Protease
Reverse transcriptase/ribonuclease H
Integrase
Family & Domains
Features
Showing features for motif, region, zinc finger, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 16-22 | Nuclear export signal | ||||
Sequence: WEKIYLR | ||||||
Motif | 26-32 | Nuclear localization signal | ||||
Sequence: KKKYMMK | ||||||
Region | 107-129 | Disordered | ||||
Sequence: KMKAEQKEPEPEQAAGAAAAPES | ||||||
Zinc finger | 393-410 | CCHC-type 1 | ||||
Sequence: IKCFNCGKEGHLARNCKA | ||||||
Zinc finger | 414-431 | CCHC-type 2 | ||||
Sequence: KGCWKCGQEGHQMKDCRS | ||||||
Region | 446-490 | Disordered | ||||
Sequence: REARKFPPDNNKERANSPSNRELWVSGGEDHTGDREGRKGEDREL | ||||||
Compositional bias | 472-490 | Basic and acidic residues | ||||
Sequence: GGEDHTGDREGRKGEDREL | ||||||
Domain | 517-586 | Peptidase A2 | ||||
Sequence: KEALLDTGADDTVIEEIQLEGKWKPKMIGGIGGFIKVKQYDNVIIEIQGKKAVGTVLVGPTPVNIIGRNF | ||||||
Domain | 640-830 | Reverse transcriptase | ||||
Sequence: EGKISRIGPENPYNTPIFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSCPLDENFRKYTAFTIPSVNNETPGIRYQYNVLPQGWKGSPAIFQSTMTKILEPFRKNNPELVIYQYMDDLYVGSDLEITQHREAVERLRSHLLTWGFTTPDKKHQKEPPFLWMGYEL | ||||||
Region | 823-831 | RT 'primer grip' | ||||
Sequence: FLWMGYELH | ||||||
Motif | 994-1010 | Tryptophan repeat motif | ||||
Sequence: WETWWTEYWQATWIPDW | ||||||
Domain | 1030-1153 | RNase H type-1 | ||||
Sequence: ISGAETYYVDGAANRETKLGKAGFVTDRGRQKVTSISETTNQQAELQAVLMALQDAGQEVNIVTDSQYVLGIIHSQPDKSESELVNQIIEELIKKERIYLSWVPAHKGIGGNEQIDKLVSTGIR | ||||||
Zinc finger | 1159-1200 | Integrase-type | ||||
Sequence: DGIDKAQEEHERYHSNWKAMASDFNLPPIVAKEIVASCDKCQ | ||||||
Domain | 1210-1360 | Integrase catalytic | ||||
Sequence: INCSPGVWQLDCTHLEGKIILVAVHVASGYLEAEVIPAETGQETAYFILKLAGRWPVKVIHTDNGSNFTSATVKAACWWANIQQEFGIPYNPQSQGAVESMNKELKKIIGQIRDQAEHLKTAVQMAVFIHNFKRKGGIGGYTAGERIIDII |
Domain
Keywords
- Domain
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Ribosomal frameshifting. Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
Q1A249-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameGag-Pol polyprotein
- NoteProduced by -1 ribosomal frameshifting.
- Length1,448
- Mass (Da)163,246
- Last updated2007-01-23 v3
- Checksum0147967C358DBB01
Q1A250-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameGag polyprotein
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 472-490 | Basic and acidic residues | ||||
Sequence: GGEDHTGDREGRKGEDREL |
Keywords
- Coding sequence diversity
- Technical term