UniProtKB - Q1A267 (POL_SIVMB)
Gag-Pol polyprotein
gag-pol
Functioni
Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).
By similarityMatrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristointegration complex. The myristoylation signal and the NLS exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).
By similarityCapsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with host PPIA/CYPA protects the virus from restriction by host TRIM5-alpha and from an unknown antiviral activity in host cells. This capsid restriction by TRIM5 is one of the factors which restricts SIV to the simian species (By similarity).
By similarityNucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).
By similarityThe 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. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
PROSITE-ProRule annotationReverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H can probably proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).
By similarityIntegrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the SIV genome, a 5 bp duplication of host DNA is produced at the ends of SIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).
By similarityMiscellaneous
Catalytic activityi
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)PROSITE-ProRule annotationEC:2.7.7.49PROSITE-ProRule annotation EC:2.7.7.7PROSITE-ProRule annotation
- Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.PROSITE-ProRule annotation EC:3.4.23.16
- 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
- 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. EC:3.1.13.2
Cofactori
Protein has several cofactor binding sites:- Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
- Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.By similarity
- Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.By similarity
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 219 – 220 | Cis/trans isomerization of proline peptide bond; by human PPIA/CYPABy similarity | 2 | |
Active sitei | 512 | For protease activity; shared with dimeric partnerPROSITE-ProRule annotation | 1 | |
Metal bindingi | 696 | Magnesium 1; catalytic; for reverse transcriptase activityBy similarity | 1 | |
Metal bindingi | 771 | Magnesium 1; catalytic; for reverse transcriptase activityBy similarity | 1 | |
Metal bindingi | 772 | Magnesium 1; catalytic; for reverse transcriptase activityBy similarity | 1 | |
Sitei | 987 | Essential for RT p66/p51 heterodimerizationBy similarity | 1 | |
Sitei | 1000 | Essential for RT p66/p51 heterodimerizationBy similarity | 1 | |
Metal bindingi | 1029 | Magnesium 2; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1064 | Magnesium 2; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1084 | Magnesium 2; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1135 | Magnesium 2; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1158 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1162 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1186 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1189 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1210 | Magnesium 3; catalytic; for integrase activityBy similarity | 1 | |
Metal bindingi | 1262 | Magnesium 3; catalytic; for integrase activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 385 – 402 | CCHC-type 1PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 406 – 423 | CCHC-type 2PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 1149 – 1190 | Integrase-typePROSITE-ProRule annotationAdd BLAST | 42 | |
DNA bindingi | 1369 – 1416 | Integrase-typePROSITE-ProRule annotationAdd BLAST | 48 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB-KW
- DNA binding Source: UniProtKB-KW
- DNA-directed DNA polymerase activity Source: UniProtKB-KW
- exoribonuclease H activity Source: UniProtKB-EC
- RNA binding Source: UniProtKB-KW
- RNA-directed DNA polymerase activity Source: UniProtKB-KW
- RNA-DNA hybrid ribonuclease activity Source: InterPro
- structural molecule activity Source: InterPro
- zinc ion binding Source: InterPro
GO - Biological processi
- DNA integration Source: UniProtKB-KW
- DNA recombination Source: UniProtKB-KW
- establishment of integrated proviral latency Source: UniProtKB-KW
- suppression by virus of host gene expression Source: UniProtKB-KW
- viral entry into host cell Source: UniProtKB-KW
- viral genome integration into host DNA Source: UniProtKB-KW
- viral penetration into host nucleus Source: UniProtKB-KW
Keywordsi
Names & Taxonomyi
Protein namesi | Recommended name: Gag-Pol polyproteinAlternative name(s): Pr160Gag-Pol Cleaved into the following 9 chains: Alternative name(s): PR Retropepsin Reverse transcriptase/ribonuclease H (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.13) Alternative name(s): Exoribonuclease H (EC:3.1.13.2) p66 RT |
Gene namesi | Name:gag-pol |
Organismi | Simian immunodeficiency virus (isolate MB66) (SIV-cpz) (Chimpanzee immunodeficiency virus) |
Taxonomic identifieri | 388911 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Pararnavirae › Artverviricota › Revtraviricetes › Ortervirales › Retroviridae › Orthoretrovirinae › Lentivirus › |
Virus hosti | Pan troglodytes (Chimpanzee) [TaxID: 9598] |
Proteomesi |
|
Subcellular locationi
- Virion Curated
- Host nucleus By similarity
- Host cytoplasm By similarity
- Host cell membrane Curated; Lipid-anchor Curated Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity).By similarity
- Virion Curated
- Virion Curated
- Virion Curated
- Host nucleus Curated
- Host cytoplasm Curated Note: Nuclear at initial phase, cytoplasmic at assembly.Curated
Keywords - Cellular componenti
Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Host nucleus, Membrane, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostBy similarity | |||
ChainiPRO_0000261303 | 2 – 1438 | Gag-Pol polyproteinAdd BLAST | 1437 | |
ChainiPRO_0000249385 | 2 – 130 | Matrix protein p17By similarityAdd BLAST | 129 | |
ChainiPRO_0000249386 | 131 – 361 | Capsid protein p24By similarityAdd BLAST | 231 | |
ChainiPRO_0000249387 | 362 – 428 | Nucleocapsid protein p7By similarityAdd BLAST | 67 | |
ChainiPRO_0000249389 | 429 – 487 | p6-polSequence analysisAdd BLAST | 59 | |
ChainiPRO_0000249390 | 488 – 586 | ProteaseBy similarityAdd BLAST | 99 | |
ChainiPRO_0000249391 | 587 – 1146 | Reverse transcriptase/ribonuclease HBy similarityAdd BLAST | 560 | |
ChainiPRO_0000249392 | 587 – 1026 | p51 RTBy similarityAdd BLAST | 440 | |
ChainiPRO_0000249393 | 1027 – 1146 | p15By similarityAdd BLAST | 120 | |
ChainiPRO_0000249394 | 1147 – 1438 | IntegraseBy similarityAdd BLAST | 292 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 130 – 131 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 361 – 362 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 428 – 429 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 487 – 488 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 586 – 587 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 1026 – 1027 | Cleavage; by viral protease; partialBy similarity | 2 | |
Sitei | 1146 – 1147 | Cleavage; by viral proteaseBy similarity | 2 |
Keywords - PTMi
Lipoprotein, Myristate, PhosphoproteinInteractioni
Subunit structurei
Heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding.
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 507 – 576 | Peptidase A2PROSITE-ProRule annotationAdd BLAST | 70 | |
Domaini | 630 – 820 | Reverse transcriptasePROSITE-ProRule annotationAdd BLAST | 191 | |
Domaini | 1020 – 1143 | RNase H type-1PROSITE-ProRule annotationAdd BLAST | 124 | |
Domaini | 1200 – 1350 | Integrase catalyticPROSITE-ProRule annotationAdd BLAST | 151 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 439 – 481 | DisorderedSequence analysisAdd BLAST | 43 | |
Regioni | 813 – 821 | RT 'primer grip'By similarity | 9 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 16 – 22 | Nuclear export signalBy similarity | 7 | |
Motifi | 26 – 32 | Nuclear localization signalBy similarity | 7 | |
Motifi | 984 – 1000 | Tryptophan repeat motifBy similarityAdd BLAST | 17 |
Domaini
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 385 – 402 | CCHC-type 1PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 406 – 423 | CCHC-type 2PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 1149 – 1190 | Integrase-typePROSITE-ProRule annotationAdd BLAST | 42 |
Keywords - Domaini
Repeat, Zinc-fingerFamily and domain databases
CDDi | cd05482, HIV_retropepsin_like, 1 hit |
Gene3Di | 1.10.10.200, 1 hit 1.10.1200.30, 1 hit 1.10.150.90, 1 hit 1.10.375.10, 1 hit 2.30.30.10, 1 hit 2.40.70.10, 1 hit 3.30.420.10, 2 hits 3.30.70.270, 3 hits |
InterProi | View protein in InterPro IPR001969, Aspartic_peptidase_AS IPR043502, DNA/RNA_pol_sf IPR045345, Gag_p24_C IPR017856, Integrase-like_N IPR036862, Integrase_C_dom_sf_retrovir IPR001037, Integrase_C_retrovir IPR001584, Integrase_cat-core IPR003308, Integrase_Zn-bd_dom_N IPR000071, Lentvrl_matrix_N IPR012344, Matrix_HIV/RSV_N IPR001995, Peptidase_A2_cat IPR021109, Peptidase_aspartic_dom_sf IPR034170, Retropepsin-like_cat_dom IPR018061, Retropepsins IPR008916, Retrov_capsid_C IPR008919, Retrov_capsid_N IPR010999, Retrovr_matrix IPR043128, Rev_trsase/Diguanyl_cyclase IPR012337, RNaseH-like_sf IPR002156, RNaseH_domain IPR036397, RNaseH_sf IPR000477, RT_dom IPR010659, RVT_connect IPR010661, RVT_thumb IPR001878, Znf_CCHC IPR036875, Znf_CCHC_sf |
Pfami | View protein in Pfam PF00540, Gag_p17, 1 hit PF19317, Gag_p24_C, 1 hit PF00552, IN_DBD_C, 1 hit PF02022, Integrase_Zn, 1 hit PF00075, RNase_H, 1 hit PF00665, rve, 1 hit PF00077, RVP, 1 hit PF00078, RVT_1, 1 hit PF06815, RVT_connect, 1 hit PF06817, RVT_thumb, 1 hit PF00098, zf-CCHC, 2 hits |
PRINTSi | PR00234, HIV1MATRIX |
SMARTi | View protein in SMART SM00343, ZnF_C2HC, 2 hits |
SUPFAMi | SSF46919, SSF46919, 1 hit SSF47836, SSF47836, 1 hit SSF47943, SSF47943, 1 hit SSF50122, SSF50122, 1 hit SSF50630, SSF50630, 1 hit SSF53098, SSF53098, 2 hits SSF56672, SSF56672, 1 hit SSF57756, SSF57756, 1 hit |
PROSITEi | View protein in PROSITE PS50175, ASP_PROT_RETROV, 1 hit PS00141, ASP_PROTEASE, 1 hit PS50994, INTEGRASE, 1 hit PS51027, INTEGRASE_DBD, 1 hit PS50879, RNASE_H_1, 1 hit PS50878, RT_POL, 1 hit PS50158, ZF_CCHC, 2 hits PS50876, ZF_INTEGRASE, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MGARASVLTG GKLDRWEKIY LRPGGKKKYM MKHLVWASRE LERFACNPSL
60 70 80 90 100
METTEGCKQL LQQLEPALKT GSEGLRSLFN TIVVLWCVHQ GIPVKDTKEA
110 120 130 140 150
LDQLQEAQQK GKQEVAAATA DGTSTVSRNF PIVANAQGQM VHQPISPRTL
160 170 180 190 200
NAWVKVVEEK AFSPEVIPMF MALSEGATPQ DLNTMLNTVG GHQAAMQMLK
210 220 230 240 250
EVINEEAAEW DRLHPVHAGP VPPGQMREPR GSDIAGTTST IQEQVGWMTS
260 270 280 290 300
NPPIPVGDIY KRWIILGLNK IVKMYCPVSI LDIKQGPKES FRDYVDRFYK
310 320 330 340 350
TLRAEQATQE VKNWMTDTLL VQNANPDCKS ILRALGPGAT LEGDEPAFQG
360 370 380 390 400
VGGPSHKARV LAEAMSQAQH SNDAKRQFKG PKRIVKCFNC GKEGHIARNC
410 420 430 440 450
KAPRRKGCWK CGQEGHQMRN CTNERQANFF RETLAFQQGK AREFPSEETR
460 470 480 490 500
TNSSTNRELR VQGGGTCPEG GSEERGDREQ AVSSANFPQI SLWQRPVVTV
510 520 530 540 550
RIEGQLKEAL LDTGADDTVL EEIELGGRWK PKMIGGIGGF IKVRQYDNVT
560 570 580 590 600
IDICGKRAVG TVLVGPTPVN IIGRNILTQI GCTLNFPISP IETVPVSLKP
610 620 630 640 650
GMDGPRVKQW PLTEEKIRAL TEICTEMEKE GKISRVGPEN PYNTPIFAIK
660 670 680 690 700
KKDSTKWRKL VDFRELNKRT QDFWEVQLGI PHPAGLKQKK SVTVLDVGDA
710 720 730 740 750
YFSCPLDENF RKYTAFTIPS VNNETPGIRY QYNVLPQGWK GSPAIFQSSM
760 770 780 790 800
TKILEPFRKQ NPEIIIYQYM DDLYVGSDLK IELHREKVEE LRAHLLKWGF
810 820 830 840 850
TTPDKKHQKE PPFLWMGYEL HPDKWTVQPI QLPEKESWTV NDIQKLIGKL
860 870 880 890 900
NWACQIYPGI RVKQLCKLIR GTKALTEVVT FTTEAELELA ENREILKEPV
910 920 930 940 950
HGAYYDPSKE LIAEIQKQGQ GQWTYQIFQE QYKNLKTGKY ARMRSAHTND
960 970 980 990 1000
VKQLTEVVQK VALESIVIWG KVPRFRLPIQ KETWEAWWTD YWQATWIPEW
1010 1020 1030 1040 1050
EYVNTPPLVK LWYQLEQDPI PGAETFYVDG AANRETKLGK AGYVTDKGRQ
1060 1070 1080 1090 1100
KIISLTETTN QKAELQAIQL ALQDSEVEVN IVTDSQYALG IIQGQPDTSE
1110 1120 1130 1140 1150
SEIVNQIIEE LIKKEKVYLS WVPAHKGIGG NEQIDKLVSS GIRKVLFLDG
1160 1170 1180 1190 1200
IDKAQEEHEK YHNNWRAMAS DFNLPPIVAK EIVANCDKCQ LKGEAIHGQV
1210 1220 1230 1240 1250
DCSPGIWQLD CTHLEGKIIL VAVHVASGYM EAEVIPAETG QETAYFILKL
1260 1270 1280 1290 1300
AGRWPVKVIH TDNGSNFTSS TVKAACWWAG IQQEFGIPYN PQSQGVVESM
1310 1320 1330 1340 1350
NKELKKIIGQ IRDQAEHLKT AVQMAVFIHN FKRKGGIGGY SAGERIIDIL
1360 1370 1380 1390 1400
ATDIQTTKLQ QQISNIQKFR VYYRDSRDPI WKGPAKLLWK GEGAVVLQDQ
1410 1420 1430
EEIKVVPRRK AKIIRDYGKQ MAGDDCVASR QDENQNME
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ373063 Genomic RNA Translation: ABD19475.1 Sequence problems. |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ373063 Genomic RNA Translation: ABD19475.1 Sequence problems. |
3D structure databases
SMRi | Q1A267 |
ModBasei | Search... |
Miscellaneous databases
PROi | PR:Q1A267 |
Family and domain databases
CDDi | cd05482, HIV_retropepsin_like, 1 hit |
Gene3Di | 1.10.10.200, 1 hit 1.10.1200.30, 1 hit 1.10.150.90, 1 hit 1.10.375.10, 1 hit 2.30.30.10, 1 hit 2.40.70.10, 1 hit 3.30.420.10, 2 hits 3.30.70.270, 3 hits |
InterProi | View protein in InterPro IPR001969, Aspartic_peptidase_AS IPR043502, DNA/RNA_pol_sf IPR045345, Gag_p24_C IPR017856, Integrase-like_N IPR036862, Integrase_C_dom_sf_retrovir IPR001037, Integrase_C_retrovir IPR001584, Integrase_cat-core IPR003308, Integrase_Zn-bd_dom_N IPR000071, Lentvrl_matrix_N IPR012344, Matrix_HIV/RSV_N IPR001995, Peptidase_A2_cat IPR021109, Peptidase_aspartic_dom_sf IPR034170, Retropepsin-like_cat_dom IPR018061, Retropepsins IPR008916, Retrov_capsid_C IPR008919, Retrov_capsid_N IPR010999, Retrovr_matrix IPR043128, Rev_trsase/Diguanyl_cyclase IPR012337, RNaseH-like_sf IPR002156, RNaseH_domain IPR036397, RNaseH_sf IPR000477, RT_dom IPR010659, RVT_connect IPR010661, RVT_thumb IPR001878, Znf_CCHC IPR036875, Znf_CCHC_sf |
Pfami | View protein in Pfam PF00540, Gag_p17, 1 hit PF19317, Gag_p24_C, 1 hit PF00552, IN_DBD_C, 1 hit PF02022, Integrase_Zn, 1 hit PF00075, RNase_H, 1 hit PF00665, rve, 1 hit PF00077, RVP, 1 hit PF00078, RVT_1, 1 hit PF06815, RVT_connect, 1 hit PF06817, RVT_thumb, 1 hit PF00098, zf-CCHC, 2 hits |
PRINTSi | PR00234, HIV1MATRIX |
SMARTi | View protein in SMART SM00343, ZnF_C2HC, 2 hits |
SUPFAMi | SSF46919, SSF46919, 1 hit SSF47836, SSF47836, 1 hit SSF47943, SSF47943, 1 hit SSF50122, SSF50122, 1 hit SSF50630, SSF50630, 1 hit SSF53098, SSF53098, 2 hits SSF56672, SSF56672, 1 hit SSF57756, SSF57756, 1 hit |
PROSITEi | View protein in PROSITE PS50175, ASP_PROT_RETROV, 1 hit PS00141, ASP_PROTEASE, 1 hit PS50994, INTEGRASE, 1 hit PS51027, INTEGRASE_DBD, 1 hit PS50879, RNASE_H_1, 1 hit PS50878, RT_POL, 1 hit PS50158, ZF_CCHC, 2 hits PS50876, ZF_INTEGRASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | POL_SIVMB | |
Accessioni | Q1A267Primary (citable) accession number: Q1A267 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 5, 2006 |
Last sequence update: | October 2, 2007 | |
Last modified: | February 23, 2022 | |
This is version 109 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |