ID POL_HV1N5 Reviewed; 1435 AA. AC P12497; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 02-SEP-2026, entry version 249. DE RecName: Full=Gag-Pol polyprotein; DE AltName: Full=Pr160Gag-Pol; DE Contains: DE RecName: Full=Matrix protein p17; DE Short=MA; DE Contains: DE RecName: Full=Capsid protein p24; DE Short=CA; DE Contains: DE RecName: Full=Spacer peptide 1 {ECO:0000303|PubMed:22334652}; DE Short=SP1; DE AltName: Full=p2; DE Contains: DE RecName: Full=Nucleocapsid protein p7; DE Short=NC; DE Contains: DE RecName: Full=Transframe peptide; DE Short=TF; DE Contains: DE RecName: Full=p6-pol; DE Short=p6*; DE Contains: DE RecName: Full=Protease; DE EC=3.4.23.16; DE AltName: Full=PR; DE AltName: Full=Retropepsin; DE Contains: DE RecName: Full=Reverse transcriptase/ribonuclease H; DE EC=2.7.7.49; DE EC=2.7.7.7; DE EC=3.1.26.13; DE AltName: Full=Exoribonuclease H; DE EC=3.1.13.2; DE AltName: Full=p66 RT; DE Contains: DE RecName: Full=p51 RT; DE Contains: DE RecName: Full=p15; DE Contains: DE RecName: Full=Integrase; DE Short=IN; DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585}; DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585}; GN Name=gag-pol; OS Human immunodeficiency virus type 1 group M subtype B (isolate NY5) OS (HIV-1). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus; OC Lentivirus humimdef1; Human immunodeficiency virus type 1. OX NCBI_TaxID=11698; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Clone pNL4-3; RA Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.; RL Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE REVISION TO 545. RA Strebel K.J., Martin M.A.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [3] RP INTERACTION WITH HOST GP41 (MATRIX PROTEIN P17). RX PubMed=8918455; DOI=10.1002/j.1460-2075.1996.tb00964.x; RA Cosson P.; RT "Direct interaction between the envelope and matrix proteins of HIV-1."; RL EMBO J. 15:5783-5788(1996). RN [4] RP INTERACTION WITH HUMAN AP3D1 (MATRIX PROTEIN P17). RX PubMed=15766529; DOI=10.1016/j.cell.2004.12.023; RA Dong X., Li H., Derdowski A., Ding L., Burnett A., Chen X., Peters T.R., RA Dermody T.S., Woodruff E., Wang J.J., Spearman P.; RT "AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a key RT role in particle assembly."; RL Cell 120:663-674(2005). RN [5] RP INTERACTION WITH HUMAN NUP153 (INTEGRASE). RC STRAIN=Clone pNL4-3; RX PubMed=19369352; DOI=10.1128/jvi.02061-08; RA Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.; RT "Integrase interacts with nucleoporin NUP153 to mediate the nuclear import RT of human immunodeficiency virus type 1."; RL J. Virol. 83:6522-6533(2009). RN [6] RP MUTAGENESIS OF SER-9; SER-67; SER-72 AND SER-77. RX PubMed=19059618; DOI=10.1016/j.virol.2008.10.047; RA Bhatia A.K., Kaushik R., Campbell N.A., Pontow S.E., Ratner L.; RT "Mutation of critical serine residues in HIV-1 matrix result in an envelope RT incorporation defect which can be rescued by truncation of the gp41 RT cytoplasmic tail."; RL Virology 384:233-241(2009). RN [7] RP SUBCELLULAR LOCATION (GAG-POL POLYPROTEIN). RX PubMed=19297499; DOI=10.1128/jvi.00109-09; RA Joshi A., Ablan S.D., Soheilian F., Nagashima K., Freed E.O.; RT "Evidence that productive human immunodeficiency virus type 1 assembly can RT occur in an intracellular compartment."; RL J. Virol. 83:5375-5387(2009). RN [8] RP INTERACTION WITH RAT CALM1 (MATRIX PROTEIN P17). RX PubMed=21799007; DOI=10.1074/jbc.m111.273623; RA Samal A.B., Ghanam R.H., Fernandez T.F., Monroe E.B., Saad J.S.; RT "NMR, biophysical, and biochemical studies reveal the minimal Calmodulin RT binding domain of the HIV-1 matrix protein."; RL J. Biol. Chem. 286:33533-33543(2011). RN [9] RP PROTEOLYTIC PROCESSING (GAG-POL POLYPROTEIN). RX PubMed=22334652; DOI=10.1074/jbc.m112.339374; RA Lee S.K., Potempa M., Kolli M., Ozen A., Schiffer C.A., Swanstrom R.; RT "Context surrounding processing sites is crucial in determining cleavage RT rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol RT polyprotein precursors by viral protease."; RL J. Biol. Chem. 287:13279-13290(2012). RN [10] RP INTERACTION WITH HUMAN NUP153 (CAPSID PROTEIN P24). RC STRAIN=Clone pNL4-3; RX PubMed=24130490; DOI=10.1371/journal.ppat.1003693; RA Matreyek K.A., Yucel S.S., Li X., Engelman A.; RT "Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding RT pocket within the HIV-1 capsid protein to mediate lentiviral infectivity."; RL PLoS Pathog. 9:E1003693-E1003693(2013). RN [11] RP SUBUNIT (CAPSID PROTEIN P24). RX PubMed=24066695; DOI=10.1021/ja406246z; RA Deshmukh L., Schwieters C.D., Grishaev A., Ghirlando R., Baber J.L., RA Clore G.M.; RT "Structure and dynamics of full-length HIV-1 capsid protein in solution."; RL J. Am. Chem. Soc. 135:16133-16147(2013). RN [12] RP RNA-BINDING (MATRIX PROTEIN P17). RX PubMed=23552424; DOI=10.1128/jvi.00075-13; RA Chukkapalli V., Inlora J., Todd G.C., Ono A.; RT "Evidence in support of RNA-mediated inhibition of phosphatidylserine- RT dependent HIV-1 Gag membrane binding in cells."; RL J. Virol. 87:7155-7159(2013). RN [13] RP PHOSPHORYLATION AT SER-148 (CAPSID PROTEIN P24). RX PubMed=24509437; DOI=10.1099/vir.0.060053-0; RA Dochi T., Nakano T., Inoue M., Takamune N., Shoji S., Sano K., Misumi S.; RT "Phosphorylation of human immunodeficiency virus type 1 capsid protein at RT serine 16, required for peptidyl-prolyl isomerase-dependent uncoating, is RT mediated by virion-incorporated extracellular signal-regulated kinase 2."; RL J. Gen. Virol. 95:1156-1166(2014). RN [14] RP REVIEW. RX PubMed=8791726; DOI=10.1007/978-3-642-80145-7_4; RA Vogt V.M.; RT "Proteolytic processing and particle maturation."; RL Curr. Top. Microbiol. Immunol. 214:95-131(1996). RN [15] RP REVIEW. RX PubMed=9878383; DOI=10.1006/jmbi.1998.2354; RA Turner B.G., Summers M.F.; RT "Structural biology of HIV."; RL J. Mol. Biol. 285:1-32(1999). RN [16] RP REVIEW. RX PubMed=11700285; DOI=10.1146/annurev.genet.35.102401.090551; RA Negroni M., Buc H.; RT "Mechanisms of retroviral recombination."; RL Annu. Rev. Genet. 35:275-302(2001). RN [17] RP REVIEW. RX PubMed=11983066; DOI=10.1186/gb-2002-3-4-reviews3006; RA Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.; RT "Retroviral proteases."; RL Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002). RN [18] RP REVIEW. RX PubMed=12873766; DOI=10.1016/s0005-2736(03)00163-9; RA Scarlata S., Carter C.; RT "Role of HIV-1 Gag domains in viral assembly."; RL Biochim. Biophys. Acta 1614:62-72(2003). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 489-587. RX PubMed=2645523; DOI=10.1038/337615a0; RA Navia M.A., Fitzgerald P.M.D., McKeever B.M., Leu C.-T., Heimbach J.C., RA Herber W.K., Sigal I.S., Darke P.L., Springer J.P.; RT "Three-dimensional structure of aspartyl protease from human RT immunodeficiency virus HIV-1."; RL Nature 337:615-620(1989). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587. RX PubMed=2548279; DOI=10.1126/science.2548279; RA Wlodawer A., Miller M., Jaskolski M., Sathyanarayana B.K., Baldwin E., RA Weber I.T., Selk L.M., Clawson L., Schneider J., Kent S.B.H.; RT "Conserved folding in retroviral proteases: crystal structure of a RT synthetic HIV-1 protease."; RL Science 245:616-621(1989). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587. RX PubMed=2201682; DOI=10.1016/s0021-9258(18)77288-8; RA Fitzgerald P.M.D., McKeever B.M., van Middlesworth J.F., Springer J.P., RA Heimbach J.C., Leu C.-T., Herber W.K., Dixon R.A.F., Darke P.L.; RT "Crystallographic analysis of a complex between human immunodeficiency RT virus type 1 protease and acetyl-pepstatin at 2.0-A resolution."; RL J. Biol. Chem. 265:14209-14219(1990). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 489-587. RX PubMed=2200122; DOI=10.1126/science.2200122; RA Erickson J., Neidhart D.J., Vandrie J., Kempf D.J., Wang X.C., RA Norbeck D.W., Plattner J.J., Rittenhouse J.W., Turon M., Wideburg N.E., RA Kohlbrenner W.E., Simmer R., Helfrich R., Paul D.A., Knigge M.; RT "Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor RT complexed to HIV-1 protease."; RL Science 249:527-533(1990). RN [23] RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 133-283. RX PubMed=2123631; DOI=10.1089/aid.1990.6.1169; RA Ehrlich L.S., Krausslich H.G., Wimmer E., Carter C.A.; RT "Expression in Escherichia coli and purification of human immunodeficiency RT virus type 1 capsid protein (p24)."; RL AIDS Res. Hum. Retroviruses 6:1169-1175(1990). RN [24] RP STRUCTURE BY NMR OF 1-132. RX PubMed=7966331; DOI=10.1006/jmbi.1994.1719; RA Massiah M.A., Starich M.R., Paschall C., Summers M.F., Christensen A.M., RA Sundquist W.I.; RT "Three-dimensional structure of the human immunodeficiency virus type 1 RT matrix protein."; RL J. Mol. Biol. 244:198-223(1994). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE RP INHIBITOR L-736,524. RX PubMed=7929352; DOI=10.1016/s0021-9258(18)47199-2; RA Chen Z., Li Y., Chen E., Hall D.L., Darke P.L., Culberson C., Shafer J.A., RA Kuo L.C.; RT "Crystal structure at 1.9-A resolution of human immunodeficiency virus RT (HIV) II protease complexed with L-735,524, an orally bioavailable RT inhibitor of the HIV proteases."; RL J. Biol. Chem. 269:26344-26348(1994). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1197-1359. RX PubMed=7801124; DOI=10.1126/science.7801124; RA Dyda F., Hickman A.B., Jenkins T.M., Engelman A., Craigie R., Davies D.R.; RT "Crystal structure of the catalytic domain of HIV-1 integrase: similarity RT to other polynucleotidyl transferases."; RL Science 266:1981-1986(1994). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-132. RX PubMed=8610175; DOI=10.1073/pnas.93.7.3099; RA Hill C.P., Worthylake D.K., Bancroft D.P., Christensen A.M., RA Sundquist W.I.; RT "Crystal structures of the trimeric human immunodeficiency virus type 1 RT matrix protein: implications for membrane association and assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 93:3099-3104(1996). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 133-277, AND INTERACTION WITH RP HUMAN PPIA/CYPA (CAPSID PROTEIN P24). RX PubMed=8980234; DOI=10.1016/s0092-8674(00)81823-1; RA Gamble T.R., Vajdos F.F., Yoo S., Worthylake D.K., Houseweart M., RA Sundquist W.I., Hill C.P.; RT "Crystal structure of human cyclophilin A bound to the amino-terminal RT domain of HIV-1 capsid."; RL Cell 87:1285-1294(1996). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1197-1359, AND ACTIVE SITES RP (INTEGRASE). RX PubMed=8977101; DOI=10.1016/s0014-5793(96)01236-7; RA Bujacz G., Alexandratos J., Qing Z.L., Clement-Mella C., Wlodawer A.; RT "The catalytic domain of human immunodeficiency virus integrase: ordered RT active site in the F185H mutant."; RL FEBS Lett. 398:175-178(1996). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 278-377. RX PubMed=9346481; DOI=10.1126/science.278.5339.849; RA Gamble T.R., Yoo S., Vajdos F.F., von Schwedler U.K., Worthylake D.K., RA Wang H., McCutcheon J.P., Sundquist W.I., Hill C.P.; RT "Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid RT protein."; RL Science 278:849-853(1997). RN [31] RP STRUCTURE BY NMR OF 1148-1202. RX PubMed=9228950; DOI=10.1038/nsb0797-567; RA Cai M., Zheng R., Caffrey M., Craigie R., Clore G.M., Gronenborn A.M.; RT "Solution structure of the N-terminal zinc binding domain of HIV-1 RT integrase."; RL Nat. Struct. Biol. 4:567-577(1997). RN [32] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1197-1356. RX PubMed=9689049; DOI=10.1073/pnas.95.16.9150; RA Goldgur Y., Dyda F., Hickman A.B., Jenkins T.M., Craigie R., Davies D.R.; RT "Three new structures of the core domain of HIV-1 integrase: an active site RT that binds magnesium."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9150-9154(1998). RN [33] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1197-1359. RX PubMed=10413462; DOI=10.1021/bi9907173; RA Greenwald J., Le V., Butler S.L., Bushman F.D., Choe S.; RT "The mobility of an HIV-1 integrase active site loop is correlated with RT catalytic activity."; RL Biochemistry 38:8892-8898(1999). RN [34] RP STRUCTURE BY NMR OF 133-283. RX PubMed=12032547; DOI=10.1038/nsb806; RA Tang C., Ndassa Y., Summers M.F.; RT "Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag RT polyprotein."; RL Nat. Struct. Biol. 9:537-543(2002). RN [35] RP STRUCTURE BY NMR OF 1-132. RX PubMed=14699046; DOI=10.1073/pnas.0305665101; RA Tang C., Loeliger E., Luncsford P., Kinde I., Beckett D., Summers M.F.; RT "Entropic switch regulates myristate exposure in the HIV-1 matrix RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 101:517-522(2004). RN [36] RP STRUCTURE BY NMR OF 2-132, INTERACTION WITH PHOSPHATIDYLINOSITOL RP 4,5-BISPHOSPHATE (MATRIX PROTEIN P17), AND FUNCTION (MATRIX PROTEIN P17). RX PubMed=16840558; DOI=10.1073/pnas.0602818103; RA Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., Summers M.F.; RT "Structural basis for targeting HIV-1 Gag proteins to the plasma membrane RT for virus assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11364-11369(2006). CC -!- FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the CC essential events in virion assembly, including binding the plasma CC membrane, making the protein-protein interactions necessary to create CC spherical particles, recruiting the viral Env proteins, and packaging CC the genomic RNA via direct interactions with the RNA packaging sequence CC (Psi). Gag-Pol polyprotein may regulate its own translation, by the CC binding genomic RNA in the 5'-UTR. At low concentration, the CC polyprotein would promote translation, whereas at high concentration, CC the polyprotein would encapsidate genomic RNA and then shut off CC translation. {ECO:0000250}. CC -!- FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma CC membrane via a multipartite membrane-binding signal, that includes its CC myristoylated N-terminus (PubMed:16840558). Matrix protein is part of CC the pre-integration complex. Implicated in the release from host cell CC mediated by Vpu. Binds to RNA. {ECO:0000250, CC ECO:0000269|PubMed:16840558, ECO:0000269|PubMed:23552424}. CC -!- FUNCTION: [Capsid protein p24]: Forms the conical core that CC encapsulates the genomic RNA-nucleocapsid complex in the virion. Most CC core are conical, with only 7% tubular. The core is constituted by CC capsid protein hexamer subunits. The core is disassembled soon after CC virion entry (By similarity). Host restriction factors such as TRIM5- CC alpha or TRIMCyp bind retroviral capsids and cause premature capsid CC disassembly, leading to blocks in reverse transcription. Capsid CC restriction by TRIM5 is one of the factors which restricts HIV-1 to the CC human species. Host PIN1 apparently facilitates the virion uncoating CC (PubMed:24509437). On the other hand, interactions with PDZD8 or CYPA CC stabilize the capsid. {ECO:0000250|UniProtKB:P04585, CC ECO:0000269|PubMed:24509437}. CC -!- FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral CC dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc CC fingers. Acts as a nucleic acid chaperone which is involved in CC rearangement of nucleic acid secondary structure during gRNA CC retrotranscription. Also facilitates template switch leading to CC recombination. As part of the polyprotein, participates in gRNA CC dimerization, packaging, tRNA incorporation and virion assembly. CC {ECO:0000250|UniProtKB:P04585}. CC -!- FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the CC release of the virion from the plasma membrane. Cleavages take place as CC an ordered, step-wise cascade to yield mature proteins. This process is CC called maturation. Displays maximal activity during the budding process CC just prior to particle release from the cell. Also cleaves Nef and Vif, CC probably concomitantly with viral structural proteins on maturation of CC virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off CC the capped cellular mRNA translation. The resulting inhibition of CC cellular protein synthesis serves to ensure maximal viral gene CC expression and to evade host immune response. Also mediates cleavage of CC host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CC CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CC CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CC CARD8-sensing when its protease remains inactive in infected cells CC prior to viral budding (By similarity). {ECO:0000250|UniProtKB:P04585, CC ECO:0000255|PROSITE-ProRule:PRU00275}. CC -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional CC enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, CC shortly after virus entry into the cell. This enzyme displays a DNA CC polymerase activity that can copy either DNA or RNA templates, and a CC ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA- CC DNA heteroduplexes in a partially processive 3' to 5' endonucleasic CC mode. Conversion of viral genomic RNA into dsDNA requires many steps. A CC tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'- CC end of the viral RNA. RT uses the 3' end of the tRNA primer to perform CC a short round of RNA-dependent minus-strand DNA synthesis. The reading CC proceeds through the U5 region and ends after the repeated (R) region CC which is present at both ends of viral RNA. The portion of the RNA-DNA CC heteroduplex is digested by the RNase H, resulting in a ssDNA product CC attached to the tRNA primer. This ssDNA/tRNA hybridizes with the CC identical R region situated at the 3' end of viral RNA. This template CC exchange, known as minus-strand DNA strong stop transfer, can be either CC intra- or intermolecular. RT uses the 3' end of this newly synthesized CC short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of CC the whole template. RNase H digests the RNA template except for two CC polypurine tracts (PPTs) situated at the 5'-end and near the center of CC the genome. It is not clear if both polymerase and RNase H activities CC are simultaneous. RNase H probably can proceed both in a polymerase- CC dependent (RNA cut into small fragments by the same RT performing DNA CC synthesis) and a polymerase-independent mode (cleavage of remaining RNA CC fragments by free RTs). Secondly, RT performs DNA-directed plus-strand CC DNA synthesis using the PPTs that have not been removed by RNase H as CC primers. PPTs and tRNA primers are then removed by RNase H. The 3' and CC 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. CC Strand displacement synthesis by RT to the PBS and PPT ends produces a CC blunt ended, linear dsDNA copy of the viral genome that includes long CC terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}. CC -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host CC chromosome, by performing a series of DNA cutting and joining CC reactions. This enzyme activity takes place after virion entry into a CC cell and reverse transcription of the RNA genome in dsDNA. The first CC step in the integration process is 3' processing. This step requires a CC complex comprising the viral genome, matrix protein, Vpr and integrase. CC This complex is called the pre-integration complex (PIC). The integrase CC protein removes 2 nucleotides from each 3' end of the viral DNA, CC leaving recessed CA OH's at the 3' ends. In the second step, the PIC CC enters cell nucleus. This process is mediated through integrase and Vpr CC proteins, and allows the virus to infect a non dividing cell. This CC ability to enter the nucleus is specific of lentiviruses, other CC retroviruses cannot and rely on cell division to access cell CC chromosomes. In the third step, termed strand transfer, the integrase CC protein joins the previously processed 3' ends to the 5' ends of CC strands of target cellular DNA at the site of integration. The 5'-ends CC are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y- CC shaped, gapped, recombination intermediate results, with the 5'-ends of CC the viral DNA strands and the 3' ends of target DNA strands remaining CC unjoined, flanking a gap of 5 bp. The last step is viral DNA CC integration into host chromosome. This involves host DNA repair CC synthesis in which the 5 bp gaps between the unjoined strands are CC filled in and then ligated. Since this process occurs at both cuts CC flanking the HIV genome, a 5 bp duplication of host DNA is produced at CC the ends of HIV-1 integration. Alternatively, Integrase may catalyze CC the excision of viral DNA just after strand transfer, this is termed CC disintegration. {ECO:0000250|UniProtKB:P04585}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Specific for a P1 residue that is hydrophobic, and P1' CC variable, but often Pro.; EC=3.4.23.16; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human CC immunodeficiency virus type 1 and Moloney murine leukemia virus CC enzymes prefer to cleave the RNA strand one nucleotide away from the CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides CC away from the primer terminus.; EC=3.1.26.13; Evidence={ECO:0000250}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA CC hybrid.; EC=3.1.13.2; Evidence={ECO:0000250}; CC -!- CATALYTIC ACTIVITY: CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA- CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; CC EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA- CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; CC EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions for reverse transcriptase polymerase CC activity. {ECO:0000250}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. CC Substrate-binding is a precondition for magnesium binding. CC {ECO:0000250}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Magnesium ions are required for integrase activity. Binds at least CC 1, maybe 2 magnesium ions. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Protease: The viral protease is inhibited by many CC synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, CC indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. Use of CC protease inhibitors in tritherapy regimens permit more ambitious CC therapeutic strategies. Reverse transcriptase/ribonuclease H: RT can be CC inhibited either by nucleoside RT inhibitors (NRTIs) or by non CC nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, CC whereas NNRTIs inhibit DNA polymerization by binding a small CC hydrophobic pocket near the RT active site and inducing an allosteric CC change in this region. Classical NRTIs are abacavir, adefovir (PMEA), CC didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), CC zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are CC atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine CC (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic CC effective treatment of AIDS associate two NRTIs and one NNRTI. CC {ECO:0000250}. CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as CC hexamers of trimers (By similarity). Matrix protein p17: Interacts with CC gp41 (via C-terminus) (PubMed:8918455). Interacts with host CALM1; this CC interaction induces a conformational change in the Matrix protein, CC triggering exposure of the myristate group (PubMed:21799007). Interacts CC with host AP3D1; this interaction allows the polyprotein trafficking to CC multivesicular bodies during virus assembly (PubMed:15766529). Part of CC the pre-integration complex (PIC) which is composed of viral genome, CC matrix protein, Vpr and integrase (By similarity). CC {ECO:0000250|UniProtKB:P04585, ECO:0000269|PubMed:15766529, CC ECO:0000269|PubMed:21799007, ECO:0000269|PubMed:8918455}. CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further CC multimerizes as homohexamers or homopentamers (PubMed:24066695). CC Interacts with human PPIA/CYPA; This interaction stabilizes the capsid CC (PubMed:8980234). Interacts with human NUP153 (PubMed:24130490). CC Interacts with host PDZD8; this interaction stabilizes the capsid (By CC similarity). Interacts with monkey TRIM5; this interaction destabilizes CC the capsid (By similarity). {ECO:0000250|UniProtKB:P04585, CC ECO:0000269|PubMed:24066695, ECO:0000269|PubMed:24130490, CC ECO:0000269|PubMed:8980234}. CC -!- SUBUNIT: [Protease]: Homodimer, whose active site consists of two CC apposed aspartic acid residues. {ECO:0000250|UniProtKB:P04585}. CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: Heterodimer of p66 RT CC and p51 RT (RT p66/p51) (By similarity). Heterodimerization of RT is CC essential for DNA polymerase activity (By similarity). The overall CC folding of the subdomains is similar in p66 RT and p51 RT but the CC spatial arrangements of the subdomains are dramatically different (By CC similarity). {ECO:0000250|UniProtKB:P03366}. CC -!- SUBUNIT: [Integrase]: Homotetramer; may further associate as a CC homohexadecamer (By similarity). Part of the pre-integration complex CC (PIC) which is composed of viral genome, matrix protein, Vpr and CC integrase (By similarity). Interacts with human SMARCB1/INI1 and human CC PSIP1/LEDGF isoform 1 (By similarity). Interacts with human KPNA3; this CC interaction might play a role in nuclear import of the pre-integration CC complex (By similarity). Interacts with human NUP153; this interaction CC might play a role in nuclear import of the pre-integration complex CC (PubMed:19369352). {ECO:0000250|UniProtKB:P03367, CC ECO:0000250|UniProtKB:P04585, ECO:0000269|PubMed:19369352}. CC -!- INTERACTION: CC PRO_0000042395; PRO_0000042395 [P12497]: gag-pol; NbExp=3; IntAct=EBI-2369107, EBI-2369107; CC PRO_0000042402; O75475-1: PSIP1; Xeno; NbExp=3; IntAct=EBI-10131955, EBI-5279836; CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid- CC anchor {ECO:0000269|PubMed:19297499}. Host endosome, host CC multivesicular body {ECO:0000269|PubMed:19297499}. Note=These locations CC are linked to virus assembly sites. The main location is the cell CC membrane, but under some circumstances, late endosomal compartments can CC serve as productive sites for virion assembly. CC {ECO:0000269|PubMed:19297499}. CC -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid- CC anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus CC {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial CC phase, cytoplasmic at assembly. {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Ribosomal frameshifting; Named isoforms=2; CC Comment=Translation results in the formation of the Gag polyprotein CC most of the time. Ribosomal frameshifting at the gag-pol genes CC boundary occurs at low frequency and produces the Gag-Pol CC polyprotein. This strategy of translation probably allows the virus CC to modulate the quantity of each viral protein. Maintenance of a CC correct Gag to Gag-Pol ratio is essential for RNA dimerization and CC viral infectivity.; CC Name=Gag-Pol polyprotein; CC IsoId=P12497-1; Sequence=Displayed; CC Name=Gag polyprotein; CC IsoId=P12493-1; Sequence=External; CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: RT is structured in CC five subdomains: finger, palm, thumb, connection and RNase H. Within CC the palm subdomain, the 'primer grip' region is thought to be involved CC in the positioning of the primer terminus for accommodating the CC incoming nucleotide. The RNase H domain stabilizes the association of CC RT with primer-template. {ECO:0000250}. CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: The tryptophan repeat CC motif is involved in RT p66/p51 dimerization (By similarity). CC {ECO:0000250}. CC -!- DOMAIN: [Integrase]: The core domain contains the D-x(n)-D-x(35)-E CC motif, named for the phylogenetically conserved glutamic acid and CC aspartic acid residues and the invariant 35 amino acid spacing between CC the second and third acidic residues. Each acidic residue of the CC D,D(35)E motif is independently essential for the 3'-processing and CC strand transfer activities of purified integrase protein. CC {ECO:0000250}. CC -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral CC protease yield mature proteins. The protease is released by CC autocatalytic cleavage. The polyprotein is cleaved during and after CC budding, this process is termed maturation. Proteolytic cleavage of p66 CC RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid CC protein p7 might be further cleaved after virus entry. CC {ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:22334652}. CC -!- PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the CC virion by a host kinase. Phosphorylation is apparently not a major CC regulator of membrane association. {ECO:0000250|UniProtKB:P04585}. CC -!- PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this CC phosphorylation is necessary for Pin1-mediated virion uncoating. CC {ECO:0000269|PubMed:24509437}. CC -!- PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its CC function by reducing RNA annealing and the initiation of reverse CC transcription. {ECO:0000250|UniProtKB:P03347}. CC -!- MISCELLANEOUS: [Reverse transcriptase/ribonuclease H]: Error-prone CC enzyme that lacks a proof-reading function. High mutations rate is a CC direct consequence of this characteristic. RT also displays frequent CC template switching leading to high recombination rate. Recombination CC mostly occurs between homologous regions of the two copackaged RNA CC genomes. If these two RNA molecules derive from different viral CC strains, reverse transcription will give rise to highly recombinated CC proviral DNAs. {ECO:0000250}. CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast CC majority of strains found worldwide belong to the group M. Group O CC seems to be endemic to and largely confined to Cameroon and neighboring CC countries in West Central Africa, where these viruses represent a small CC minority of HIV-1 strains. The group N is represented by a limited CC number of isolates from Cameroonian persons. The group M is further CC subdivided in 9 clades or subtypes (A to D, F to H, J and K). CC {ECO:0000250}. CC -!- MISCELLANEOUS: Resistance to inhibitors associated with mutations are CC observed both in viral protease and in reverse transcriptase. Most of CC the time, single mutations confer only a modest reduction in drug CC susceptibility. Combination of several mutations is usually required to CC develop a high-level drug resistance. These mutations are predominantly CC found in clade B viruses and not in other genotypes. They are listed in CC the clade B representative isolate HXB2 (AC P04585). {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal CC frameshifting. CC -!- WEB RESOURCE: Name=HIV drug resistance mutations; CC URL="https://www.iasusa.org/hiv-drug-resistance/hiv-drug-resistance-mutations/"; CC -!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database; CC URL="https://hivdb.stanford.edu"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M19921; AAA44988.2; ALT_SEQ; Genomic_RNA. DR PDB; 1A43; X-ray; 2.60 A; A=277-363. DR PDB; 1A8O; X-ray; 1.70 A; A=283-352. DR PDB; 1AFV; X-ray; 3.70 A; A/B=133-283. DR PDB; 1AK4; X-ray; 2.36 A; C/D=133-277. DR PDB; 1AUM; X-ray; 3.00 A; A=283-352. DR PDB; 1B92; X-ray; 2.02 A; A=1197-1359. DR PDB; 1B9D; X-ray; 1.70 A; A=1197-1359. DR PDB; 1B9F; X-ray; 1.70 A; A=1197-1359. DR PDB; 1BAJ; X-ray; 2.60 A; A=277-377. DR PDB; 1BHL; X-ray; 2.20 A; A=1204-1354. DR PDB; 1BI4; X-ray; 2.50 A; A/B/C=1197-1356. DR PDB; 1BIS; X-ray; 1.95 A; A/B=1194-1356. DR PDB; 1BIU; X-ray; 2.50 A; A/B/C=1194-1359. DR PDB; 1BIZ; X-ray; 1.95 A; A/B=1194-1359. DR PDB; 1BL3; X-ray; 2.00 A; A/B/C=1197-1356. DR PDB; 1GWP; NMR; -; A=133-283. DR PDB; 1HIW; X-ray; 2.30 A; A/B/C/Q/R/S=1-132. DR PDB; 1HYV; X-ray; 1.70 A; A=1194-1359. DR PDB; 1HYZ; X-ray; 2.30 A; A=1194-1359. DR PDB; 1ITG; X-ray; 2.30 A; A=1194-1359. DR PDB; 1K6Y; X-ray; 2.40 A; A/B/C/D=1148-1359. DR PDB; 1M9D; X-ray; 1.90 A; C/D=133-278. DR PDB; 1QS4; X-ray; 2.10 A; A/B/C=1203-1356. DR PDB; 1UPH; NMR; -; A=2-132. DR PDB; 1WJB; NMR; -; A/B=1148-1202. DR PDB; 1WJD; NMR; -; A/B=1148-1202. DR PDB; 20XX; X-ray; 2.20 A; A=1197-1359. DR PDB; 2B4J; X-ray; 2.02 A; A/B=1197-1359. DR PDB; 2GOL; X-ray; 2.20 A; A=2-131, B/D=133-277. DR PDB; 2GON; X-ray; 1.90 A; A/B/C/D=133-278. DR PDB; 2H3F; NMR; -; A=2-132. DR PDB; 2H3I; NMR; -; A=2-132. DR PDB; 2H3Q; NMR; -; A=2-132. DR PDB; 2H3V; NMR; -; A=2-132. DR PDB; 2H3Z; NMR; -; A=2-132. DR PDB; 2HMX; NMR; -; A=1-132. DR PDB; 2HVP; X-ray; 3.00 A; A=489-587. DR PDB; 2ITG; X-ray; 2.60 A; A=1197-1359. DR PDB; 2JPR; NMR; -; A=133-277. DR PDB; 2JYG; NMR; -; A=280-363. DR PDB; 2JYL; NMR; -; A=280-363. DR PDB; 2LF4; NMR; -; A=133-363. DR PDB; 2LYA; NMR; -; A=2-132. DR PDB; 2LYB; NMR; -; A=2-132. DR PDB; 2M3Z; NMR; -; A=378-432. DR PDB; 2M8L; NMR; -; A/B=133-363. DR PDB; 2M8N; NMR; -; A=133-363. DR PDB; 2M8P; NMR; -; A=133-363. DR PDB; 2ONT; X-ray; 2.40 A; A=278-353. DR PDB; 2PWM; X-ray; 1.90 A; A/B/C/D/E/F/G/H=133-278. DR PDB; 2PWO; X-ray; 1.45 A; A/B/C/D=133-278. DR PDB; 2PXR; X-ray; 1.50 A; C=133-278. DR PDB; 2X2D; X-ray; 1.95 A; D/E=132-278. DR PDB; 2XDE; X-ray; 1.40 A; A/B=133-278. DR PDB; 2XV6; X-ray; 1.89 A; A/C=278-352. DR PDB; 2XXM; X-ray; 1.65 A; A=278-352. DR PDB; 3AV9; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 3AVA; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 3AVB; X-ray; 1.85 A; A/B=1197-1359. DR PDB; 3AVC; X-ray; 1.77 A; A/B=1197-1359. DR PDB; 3AVF; X-ray; 1.70 A; A/B=1197-1356. DR PDB; 3AVG; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 3AVH; X-ray; 1.88 A; A/B=1197-1359. DR PDB; 3AVJ; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 3AVK; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 3AVL; X-ray; 1.88 A; A/B=1197-1359. DR PDB; 3AVM; X-ray; 1.88 A; A/B=1197-1359. DR PDB; 3AVN; X-ray; 2.10 A; A/B=1197-1359. DR PDB; 3DIK; EM; 9.00 A; A=133-351. DR PDB; 3DPH; X-ray; 2.01 A; A/B=278-363. DR PDB; 3DS0; X-ray; 1.60 A; A=278-363. DR PDB; 3DS1; X-ray; 1.60 A; A=278-363. DR PDB; 3DS2; X-ray; 1.20 A; A/B=278-363. DR PDB; 3DS3; X-ray; 2.70 A; A/B=278-363. DR PDB; 3DS4; X-ray; 1.12 A; A/B=278-363. DR PDB; 3DS5; X-ray; 2.40 A; A/B/C/D=278-363. DR PDB; 3DTJ; X-ray; 4.00 A; A/B/C/D=278-363. DR PDB; 3GV2; X-ray; 7.00 A; A/B/C/D/E/F=133-351. DR PDB; 3H47; X-ray; 1.90 A; A=133-363. DR PDB; 3H4E; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363. DR PDB; 3L3U; X-ray; 1.40 A; A/B=1197-1359. DR PDB; 3L3V; X-ray; 2.00 A; A/B=1197-1359. DR PDB; 3LPT; X-ray; 2.00 A; A=1197-1359. DR PDB; 3LPU; X-ray; 1.95 A; A=1197-1359. DR PDB; 3LRY; X-ray; 1.98 A; A/B=278-363. DR PDB; 3MGE; X-ray; 1.90 A; A=133-363. DR PDB; 3NF6; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 3NF7; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 3NF8; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 3NF9; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 3NFA; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 3P05; X-ray; 2.50 A; A/B/C/D/E=133-363. DR PDB; 3P0A; X-ray; 5.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=133-363. DR PDB; 3S85; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=489-587. DR PDB; 3WNE; X-ray; 1.70 A; A/B=1203-1359. DR PDB; 3WNF; X-ray; 1.45 A; A/B=1203-1359. DR PDB; 3WNG; X-ray; 1.75 A; A/B=1203-1359. DR PDB; 3WNH; X-ray; 1.50 A; A/B=1203-1359. DR PDB; 3ZCM; X-ray; 1.80 A; A/B=1203-1359. DR PDB; 3ZSO; X-ray; 1.75 A; A/B=1203-1359. DR PDB; 3ZSQ; X-ray; 1.70 A; A/B=1203-1359. DR PDB; 3ZSR; X-ray; 1.70 A; A/B=1203-1359. DR PDB; 3ZSV; X-ray; 1.75 A; A/B=1203-1359. DR PDB; 3ZSW; X-ray; 1.80 A; A/B=1203-1359. DR PDB; 3ZSX; X-ray; 1.95 A; A/B=1203-1359. DR PDB; 3ZSY; X-ray; 2.20 A; A/B=1203-1359. DR PDB; 3ZSZ; X-ray; 2.00 A; A/B=1203-1359. DR PDB; 3ZT0; X-ray; 1.95 A; A/B=1203-1359. DR PDB; 3ZT1; X-ray; 1.75 A; A/B=1203-1359. DR PDB; 3ZT2; X-ray; 1.70 A; A/B=1203-1359. DR PDB; 3ZT3; X-ray; 1.95 A; A/B=1203-1359. DR PDB; 3ZT4; X-ray; 2.20 A; A/B=1203-1359. DR PDB; 4AH9; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4AHR; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 4AHS; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 4AHT; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4AHU; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 4AHV; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CE9; X-ray; 2.10 A; A/B=1197-1359. DR PDB; 4CEA; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CEB; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 4CEC; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 4CED; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 4CEE; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CEF; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CEO; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 4CEQ; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CER; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CES; X-ray; 1.85 A; A/B=1197-1359. DR PDB; 4CEZ; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CF0; X-ray; 1.85 A; A/B=1197-1359. DR PDB; 4CF1; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 4CF2; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 4CF8; X-ray; 1.65 A; A/B=1197-1359. DR PDB; 4CF9; X-ray; 2.10 A; A/B=1197-1359. DR PDB; 4CFA; X-ray; 2.05 A; A/B=1197-1359. DR PDB; 4CFB; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 4CFC; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 4CFD; X-ray; 2.15 A; A/B=1197-1359. DR PDB; 4CGD; X-ray; 2.00 A; A/B=1197-1359. DR PDB; 4CGF; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CGG; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 4CGH; X-ray; 1.76 A; A/B=1197-1359. DR PDB; 4CGI; X-ray; 2.07 A; A/B=1197-1359. DR PDB; 4CGJ; X-ray; 2.15 A; A/B=1197-1359. DR PDB; 4CHN; X-ray; 2.00 A; A/B=1197-1359. DR PDB; 4CHO; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CHP; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 4CHQ; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 4CHY; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CHZ; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CIE; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CIF; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CIG; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CJ3; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CJ4; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CJ5; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 4CJE; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 4CJF; X-ray; 1.90 A; A/B=1197-1359. DR PDB; 4CJK; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 4CJL; X-ray; 1.77 A; A=1197-1359. DR PDB; 4CJP; X-ray; 2.00 A; A/B=1197-1359. DR PDB; 4CJQ; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CJR; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CJS; X-ray; 1.80 A; A/B=1197-1359. DR PDB; 4CJT; X-ray; 1.71 A; A/B=1197-1359. DR PDB; 4CJU; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4CJV; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 4CJW; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 4CK1; X-ray; 1.75 A; A/B=1197-1359. DR PDB; 4CK2; X-ray; 1.85 A; A/B=1197-1359. DR PDB; 4CK3; X-ray; 1.79 A; A/B=1197-1359. DR PDB; 4COC; X-ray; 1.59 A; A/B/C=278-363. DR PDB; 4COP; X-ray; 1.85 A; A/B=278-363. DR PDB; 4DGA; X-ray; 1.90 A; C/D=132-277. DR PDB; 4DGE; X-ray; 2.20 A; C/D=132-277. DR PDB; 4DMN; X-ray; 2.45 A; A=1197-1359. DR PDB; 4E1M; X-ray; 1.90 A; A=1197-1359. DR PDB; 4E1N; X-ray; 2.00 A; A=1197-1359. DR PDB; 4E91; X-ray; 1.70 A; A/B=133-278. DR PDB; 4E92; X-ray; 1.80 A; A/B=133-278. DR PDB; 4GVM; X-ray; 2.16 A; A=1197-1359. DR PDB; 4GW6; X-ray; 2.65 A; A=1197-1359. DR PDB; 4ID1; X-ray; 1.87 A; A=1197-1359. DR PDB; 4IPY; X-ray; 1.64 A; A/B/C/D=278-363. DR PDB; 4JLH; X-ray; 2.09 A; A=1197-1359. DR PDB; 4JMU; X-ray; 2.00 A; A=1-111. DR PDB; 4LH4; X-ray; 1.80 A; A=1197-1359. DR PDB; 4LH5; X-ray; 2.19 A; A=1197-1359. DR PDB; 4LQW; X-ray; 1.95 A; C/D=133-278. DR PDB; 4NX4; X-ray; 1.50 A; C=133-278. DR PDB; 4O0J; X-ray; 2.05 A; A=1197-1359. DR PDB; 4O55; X-ray; 2.24 A; A=1197-1359. DR PDB; 4O5B; X-ray; 2.37 A; A=1197-1359. DR PDB; 4OVL; X-ray; 1.70 A; A/B=1197-1359. DR PDB; 4PHV; X-ray; 2.10 A; A/B=489-587. DR PDB; 4QNB; X-ray; 2.00 A; A=133-363. DR PDB; 4WYM; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363. DR PDB; 4Y1C; X-ray; 2.30 A; A/B=1197-1359. DR PDB; 4Y1D; X-ray; 1.93 A; A/B=1197-1359. DR PDB; 4ZHR; X-ray; 2.60 A; A=588-1147, B=588-1015. DR PDB; 5HVP; X-ray; 2.00 A; A/B=489-587. DR PDB; 5JL4; X-ray; 1.76 A; A/B=1197-1359. DR PDB; 5KGW; X-ray; 2.34 A; A=1197-1359. DR PDB; 5KGX; X-ray; 2.67 A; A=1197-1359. DR PDB; 5KRS; X-ray; 1.70 A; A=1204-1354. DR PDB; 5KRT; X-ray; 1.65 A; A=1204-1354. DR PDB; 5TEO; X-ray; 2.05 A; A/B=278-377. DR PDB; 5U1C; EM; 3.90 A; A/B/C/D=1132-1136, A/B/C/D=1148-1435. DR PDB; 5VCK; X-ray; 1.80 A; A/B=489-587. DR PDB; 5VEA; X-ray; 2.00 A; A=489-587. DR PDB; 5VJ3; X-ray; 2.00 A; A=489-587. DR PDB; 5XN0; X-ray; 2.60 A; A/C=588-1142, B/D=588-1015. DR PDB; 5XN1; X-ray; 2.45 A; A/C=588-1142, B/D=588-1015. DR PDB; 5XN2; X-ray; 2.38 A; A/C=588-1142, B/D=588-1015. DR PDB; 6ES8; X-ray; 1.90 A; A=133-351. DR PDB; 6IK9; X-ray; 2.44 A; B/D=588-1015. DR PDB; 6IKA; X-ray; 2.60 A; B/D=588-1015. DR PDB; 6JCF; X-ray; 2.15 A; A=1198-1359. DR PDB; 6JCG; X-ray; 2.50 A; A=1198-1359. DR PDB; 6KDJ; X-ray; 2.51 A; A/C=588-1142, B/D=588-1015. DR PDB; 6KDK; X-ray; 2.56 A; A/C=588-1142, B/D=588-1015. DR PDB; 6KDM; X-ray; 2.32 A; A/C=588-1142, B/D=588-1015. DR PDB; 6KDN; X-ray; 2.30 A; A/C=588-1142, B/D=588-1015. DR PDB; 6KDO; X-ray; 2.57 A; A/C=588-1142, B/D=588-1015. DR PDB; 6LMI; X-ray; 2.50 A; A=1197-1359. DR PDB; 6LMQ; X-ray; 2.10 A; A=1197-1359. DR PDB; 6MCR; X-ray; 1.48 A; A=489-587. DR PDB; 6MCS; X-ray; 1.52 A; A=489-587. DR PDB; 6OOS; X-ray; 1.90 A; A/B/C/D=489-587. DR PDB; 6OOT; X-ray; 1.82 A; A/B=489-587. DR PDB; 6OOU; X-ray; 2.13 A; A/B=489-587. DR PDB; 6OPW; X-ray; 2.10 A; A/B=489-587. DR PDB; 6OPY; X-ray; 2.13 A; A/B=489-587. DR PDB; 6OPZ; X-ray; 2.20 A; A/B=489-587. DR PDB; 6OXO; X-ray; 2.00 A; A/B=489-587. DR PDB; 6OXP; X-ray; 1.97 A; A/B=489-587. DR PDB; 6OXQ; X-ray; 1.89 A; A/B=489-587. DR PDB; 6OXR; X-ray; 2.04 A; A/B=489-587. DR PDB; 6OXS; X-ray; 1.99 A; A/B=489-587. DR PDB; 6OXT; X-ray; 1.86 A; A/B=489-587. DR PDB; 6OXU; X-ray; 1.86 A; A/B=489-587. DR PDB; 6OXV; X-ray; 1.99 A; A/B=489-587. DR PDB; 6OXW; X-ray; 1.98 A; A/B=489-587. DR PDB; 6OXX; X-ray; 1.96 A; A/B=489-587. DR PDB; 6OXY; X-ray; 1.96 A; A/B=489-587. DR PDB; 6OXZ; X-ray; 1.96 A; A/B=489-587. DR PDB; 6OY0; X-ray; 2.00 A; A/B=489-587. DR PDB; 6OY1; X-ray; 2.00 A; A/B=489-587. DR PDB; 6OY2; X-ray; 1.99 A; A/B=489-587. DR PDB; 6OYD; X-ray; 1.46 A; A=489-587. DR PDB; 6OYR; X-ray; 1.54 A; A=489-587. DR PDB; 6PJB; X-ray; 1.98 A; A/B=489-587. DR PDB; 6PJC; X-ray; 1.97 A; A/B/C/D=489-587. DR PDB; 6PJD; X-ray; 1.89 A; A/B=489-587. DR PDB; 6PJE; X-ray; 1.92 A; A/B=489-587. DR PDB; 6PJF; X-ray; 1.94 A; A/B=489-587. DR PDB; 6PJG; X-ray; 1.80 A; A/B=489-587. DR PDB; 6PJH; X-ray; 1.85 A; A/B=489-587. DR PDB; 6PJI; X-ray; 1.90 A; A/B=489-587. DR PDB; 6PJK; X-ray; 2.00 A; A/B=489-587. DR PDB; 6PJL; X-ray; 1.99 A; A/B=489-587. DR PDB; 6PJM; X-ray; 1.93 A; A/B=489-587. DR PDB; 6PJN; X-ray; 1.98 A; A/B=489-587. DR PDB; 6PJO; X-ray; 1.95 A; A/B=489-587. DR PDB; 6PUT; EM; 2.90 A; A/B/C/D=1148-1435. DR PDB; 6PUW; EM; 2.90 A; A/B/C/D=1148-1435. DR PDB; 6PUY; EM; 2.80 A; A/B/C/D=1148-1435. DR PDB; 6PUZ; EM; 2.80 A; A/B/C/D=1148-1435. DR PDB; 6T6E; X-ray; 1.30 A; A=1366-1417. DR PDB; 6U8Q; EM; 4.67 A; A/B/C/D/I/J/K/L/M/N/O/P=1148-1435. DR PDB; 6UM8; X-ray; 2.33 A; A/B=1204-1359. DR PDB; 6V3K; EM; 3.40 A; A/B/C/D=1148-1435. DR PDB; 6VDK; EM; 4.50 A; A/B/C/D/I/J/M/P=1148-1435. DR PDB; 6VQS; X-ray; 2.38 A; A=1197-1359. DR PDB; 6VRG; X-ray; 2.40 A; A/B/C/D=1148-1359. DR PDB; 6VX2; X-ray; 2.40 A; A=1197-1359. DR PDB; 6W0U; X-ray; 2.19 A; A=1197-1359. DR PDB; 6W42; X-ray; 2.26 A; A=1196-1359. DR PDB; 6W6T; X-ray; 1.84 A; A/B=489-587. DR PDB; 7D83; X-ray; 2.43 A; A=1197-1359. DR PDB; 7DBM; X-ray; 2.43 A; A/C=588-1142, B/D=588-1015. DR PDB; 7DBN; X-ray; 2.67 A; A/C=588-1142, B/D=588-1015. DR PDB; 7KE0; X-ray; 2.19 A; A=1197-1359. DR PDB; 7L1P; X-ray; 1.85 A; A/B=1197-1359. DR PDB; 7L23; X-ray; 2.26 A; A=1204-1353. DR PDB; 7LDY; X-ray; 1.98 A; A/B=489-587. DR PDB; 7LDZ; X-ray; 1.86 A; A/B=489-587. DR PDB; 7LE0; X-ray; 1.95 A; A/B=489-587. DR PDB; 7LE1; X-ray; 2.00 A; A/B=489-587. DR PDB; 7LE2; X-ray; 1.97 A; A/B=489-587. DR PDB; 7LE3; X-ray; 1.87 A; A/B=489-587. DR PDB; 7LE4; X-ray; 1.99 A; A/B=489-587. DR PDB; 7LE5; X-ray; 1.86 A; A/B=489-587. DR PDB; 7LE6; X-ray; 1.96 A; A/B=489-587. DR PDB; 7LE7; X-ray; 1.98 A; A/B=489-587. DR PDB; 7LE8; X-ray; 1.64 A; A/B=489-587. DR PDB; 7LE9; X-ray; 1.80 A; A/B=489-587. DR PDB; 7LEA; X-ray; 2.00 A; A/B=489-587. DR PDB; 7LEB; X-ray; 1.89 A; A/B=489-587. DR PDB; 7LEC; X-ray; 1.94 A; A/B=489-587. DR PDB; 7LED; X-ray; 2.00 A; A/B=489-587. DR PDB; 7LEE; X-ray; 1.79 A; A/B=489-587. DR PDB; 7LEF; X-ray; 1.93 A; A/B=489-587. DR PDB; 7LEG; X-ray; 1.96 A; A/B=489-587. DR PDB; 7LEH; X-ray; 2.00 A; A/B=489-587. DR PDB; 7LEI; X-ray; 1.94 A; A/B=489-587. DR PDB; 7LQP; X-ray; 2.07 A; A/B=1204-1359. DR PDB; 7RQ0; X-ray; 1.95 A; A/B=1197-1359. DR PDB; 7SIA; X-ray; 1.85 A; A/B=1197-1359. DR PDB; 7T9H; X-ray; 2.53 A; A/B=1194-1359. DR PDB; 7T9O; X-ray; 1.95 A; A=1194-1356. DR PDB; 7U2U; X-ray; 1.84 A; A=1197-1356. DR PDB; 7UE1; X-ray; 3.00 A; A/B=1197-1359. DR PDB; 7UOQ; X-ray; 1.89 A; A=1197-1356. DR PDB; 7WBS; X-ray; 1.85 A; A/B=489-587. DR PDB; 7WCE; X-ray; 1.85 A; A=1197-1359. DR PDB; 7WCQ; X-ray; 2.01 A; A=489-587. DR PDB; 7YF6; X-ray; 2.01 A; A/B=489-587. DR PDB; 7ZUD; X-ray; 2.93 A; A=133-363. DR PDB; 8A1P; X-ray; 1.80 A; A/B/C/D=1191-1359. DR PDB; 8A1Q; X-ray; 2.06 A; A/B/C/D=1191-1359. DR PDB; 8BUV; X-ray; 2.04 A; A/B/C/D=1191-1359. DR PDB; 8BV2; X-ray; 2.00 A; A=1197-1359. DR PDB; 8CBR; X-ray; 1.80 A; A/B/C/D=1191-1359. DR PDB; 8CBS; X-ray; 1.70 A; A/B/C/D=1191-1359. DR PDB; 8CBT; X-ray; 2.14 A; A/B/C/D=1191-1359. DR PDB; 8CBU; X-ray; 2.44 A; A/B/C/D=1191-1359. DR PDB; 8CBV; X-ray; 1.82 A; A/B/C/D=1191-1359. DR PDB; 8CT5; X-ray; 1.97 A; A=1197-1357. DR PDB; 8CT7; X-ray; 2.13 A; A=1197-1357. DR PDB; 8CTA; X-ray; 2.93 A; A/B/E/F/I/J/M/N=1198-1357, C/D/G/H/K/L/O/P=1367-1418. DR PDB; 8D3S; X-ray; 1.84 A; A=1197-1359. DR PDB; 8F22; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=133-356. DR PDB; 8FN7; EM; 2.80 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FND; EM; 3.00 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNG; EM; 2.20 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNH; EM; 2.50 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNJ; EM; 2.40 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNL; EM; 2.80 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNM; EM; 2.80 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNN; EM; 2.70 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNO; EM; 2.50 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNP; EM; 2.20 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8FNQ; EM; 2.80 A; A/B/C/D/G/H/I/J=1148-1435. DR PDB; 8S9Q; X-ray; 2.26 A; A=1197-1359. DR PDB; 8T52; X-ray; 2.07 A; A=1188-1359. DR PDB; 8T5A; X-ray; 1.93 A; A=1203-1355. DR PDB; 8T5B; X-ray; 2.08 A; A/B=1204-1358, C/D=1368-1424. DR PDB; 8TOV; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363. DR PDB; 8TQP; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363. DR PDB; 8USY; X-ray; 4.40 A; A/B=1149-1435. DR PDB; 8V0Z; X-ray; 4.56 A; A/B=1149-1435. DR PDB; 8V23; X-ray; 2.00 A; A=133-278. DR PDB; 8V9C; X-ray; 4.40 A; A/B=1149-1435. DR PDB; 8VC0; X-ray; 3.46 A; A/B/C/D/E/F/G/H/I/J=133-363. DR PDB; 8VXV; EM; 3.70 A; A=133-363. DR PDB; 8VXW; EM; 4.40 A; A/B/C/D/E=133-363. DR PDB; 8W09; EM; 3.20 A; A/B/C/D/I/K/L/M=1148-1435. DR PDB; 8W2R; EM; 3.23 A; A/B/C/D/I/K/L/M=1148-1435. DR PDB; 8W34; EM; 2.83 A; A/B/C/D/I/K/L/M=1148-1435. DR PDB; 8WF7; X-ray; 1.55 A; A=1203-1359. DR PDB; 8X1Z; X-ray; 2.62 A; A/C=588-1142, B/D=588-1015. DR PDB; 8X20; X-ray; 2.70 A; A/C=588-1142, B/D=588-1015. DR PDB; 8X21; X-ray; 2.33 A; A/C=588-1142, B/D=588-1015. DR PDB; 8X22; X-ray; 2.31 A; A/C=588-1142, B/D=588-1015. DR PDB; 8ZH4; X-ray; 1.82 A; A=1197-1359. DR PDB; 8ZHA; X-ray; 1.95 A; A=1197-1359. DR PDB; 9BW9; EM; 4.10 A; A/B/C/D=1148-1435. DR PDB; 9C29; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1148-1435. DR PDB; 9C9M; EM; 2.01 A; A/B/C/I/K/L=1148-1435, D/M=1332-1435. DR PDB; 9EK1; EM; 7.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=2-116. DR PDB; 9EK2; EM; 8.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=2-116. DR PDB; 9EK3; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=2-116. DR PDB; 9HVP; X-ray; 2.80 A; A/B=489-587. DR PDB; 9N0V; X-ray; 2.98 A; A/B/C/D=133-352. DR PDB; 9NLP; EM; 3.53 A; A=588-1147, B=588-1027. DR PDB; 9ON8; NMR; -; G/H/I/J/K/L=278-377. DR PDB; 9ON9; NMR; -; G/H/I/J/K/L=278-377. DR PDB; 9ONA; NMR; -; G/H/I/J/K/L=278-377. DR PDB; 9ONB; NMR; -; G/H/I/J/K/L=278-377. DR PDB; 9PYX; X-ray; 1.73 A; A/B=489-587. DR PDB; 9PZ1; X-ray; 1.80 A; A/B=489-587. DR PDB; 9Q0T; X-ray; 1.87 A; A/B=489-587. DR PDB; 9Q13; X-ray; 1.72 A; A/B=489-587. DR PDB; 9Q1C; X-ray; 1.94 A; A/B=489-587. DR PDB; 9Q1P; X-ray; 1.87 A; A/B=489-587. DR PDB; 9Q3P; X-ray; 1.90 A; A/B=489-587. DR PDB; 9Q3T; X-ray; 1.87 A; A/B=489-587. DR PDB; 9Q50; EM; 2.33 A; A/B/C/D=1148-1435. DR PDB; 9Q57; EM; 2.28 A; A/B/C/D=1148-1435. DR PDB; 9Q5D; X-ray; 1.94 A; A/B=489-587. DR PDB; 9RMX; EM; 4.63 A; A/B/C/D/E/F/G/H/I/J/K/L=1148-1435. DR BMRB; P12497; -. DR EMDB; EMD-1529; -. DR EMDB; EMD-29307; -. DR EMDB; EMD-29309; -. DR EMDB; EMD-29312; -. DR EMDB; EMD-29313; -. DR EMDB; EMD-29315; -. DR EMDB; EMD-29317; -. DR EMDB; EMD-29318; -. DR EMDB; EMD-29319; -. DR EMDB; EMD-29320; -. DR EMDB; EMD-29321; -. DR EMDB; EMD-29322; -. DR EMDB; EMD-43641; -. DR EMDB; EMD-43642; -. DR EMDB; EMD-44962; -. DR EMDB; EMD-45151; -. DR EMDB; EMD-45364; -. DR EMDB; EMD-49521; -. DR EMDB; EMD-54071; -. DR EMDB; EMD-70530; -. DR EMDB; EMD-72221; -. DR EMDB; EMD-72222; -. DR MDposit; P12497; -. DR MDRepo; P12497; -. DR SASBDB; P12497; -. DR SMR; P12497; -. DR IntAct; P12497; 5. DR BindingDB; P12497; -. DR DrugBank; DB03118; (2Z)-1-(5-Chloro-1H-indol-3-yl)-3-hydroxy-3-(1H-tetrazol-5-yl)-2-propen-1-one. DR DrugBank; DB02086; (3,4-Dihydroxy-Phenyl)-Triphenyl-Arsonium. DR DrugBank; DB07575; 2,4-DIAMINO-1,5-DIPHENYL-3-HYDROXYPENTANE. DR DrugBank; DB02994; Cacodylic acid. DR DrugBank; DB08027; CAP-1. DR DrugBank; DB03676; Cystein-S-Yl Cacodylate. DR DrugBank; DB08231; Myristic acid. DR DrugBank; DB03963; S-(Dimethylarsenic)Cysteine. DR MEROPS; A02.001; -. DR iPTMnet; P12497; -. DR ABCD; P12497; 26 sequenced antibodies. DR SABIO-RK; P12497; -. DR EvolutionaryTrace; P12497; -. DR PRO; PR:P12497; -. DR GO; GO:0043657; C:host cell; IEA:GOC. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0052151; P:symbiont-mediated activation of host apoptosis; IEA:UniProtKB-KW. DR GO; GO:0039657; P:symbiont-mediated suppression of host gene expression; IEA:UniProtKB-KW. DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW. DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW. DR GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW. DR CDD; cd05482; HIV_retropepsin_like; 1. DR CDD; cd01645; RT_Rtv; 1. DR DisProt; DP00410; -. DR FunFam; 1.10.1200.30:FF:000001; Gag polyprotein; 1. DR FunFam; 1.10.150.90:FF:000001; Gag polyprotein; 1. DR FunFam; 1.10.375.10:FF:000001; Gag polyprotein; 1. DR FunFam; 4.10.60.10:FF:000001; Gag polyprotein; 1. DR FunFam; 2.40.70.10:FF:000001; Gag-Pol polyprotein; 1. DR FunFam; 3.30.420.10:FF:000025; Gag-Pol polyprotein; 1. DR FunFam; 2.30.30.10:FF:000001; POL polyprotein; 1. DR FunFam; 3.30.420.10:FF:000017; POL polyprotein; 1. DR FunFam; 3.30.70.270:FF:000016; POL polyprotein; 1. DR Gene3D; 1.10.10.200; -; 1. DR Gene3D; 1.10.1200.30; -; 1. DR Gene3D; 3.30.70.270; -; 3. DR Gene3D; 2.40.70.10; Acid Proteases; 1. DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1. DR Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1. DR Gene3D; 1.10.150.90; Immunodeficiency lentiviruses, gag gene matrix protein p17; 1. DR Gene3D; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2. DR Gene3D; 1.20.5.760; Single helix bin; 1. DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR045345; Gag_p24_C. DR InterPro; IPR017856; Integrase-like_N. DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir. DR InterPro; IPR001037; Integrase_C_retrovir. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR003308; Integrase_Zn-bd_dom_N. DR InterPro; IPR000071; Lentvrl_matrix_N. DR InterPro; IPR012344; Matrix_HIV/RSV_N. DR InterPro; IPR001995; Peptidase_A2_cat. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR InterPro; IPR034170; Retropepsin-like_cat_dom. DR InterPro; IPR018061; Retropepsins. DR InterPro; IPR008916; Retrov_capsid_C. DR InterPro; IPR008919; Retrov_capsid_N. DR InterPro; IPR010999; Retrovr_matrix. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR002156; RNaseH_domain. DR InterPro; IPR036397; RNaseH_sf. DR InterPro; IPR000477; RT_dom. DR InterPro; IPR010659; RVT_connect. DR InterPro; IPR010661; RVT_thumb. DR InterPro; IPR001878; Znf_CCHC. DR InterPro; IPR036875; Znf_CCHC_sf. DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1. DR PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1. DR Pfam; PF00540; Gag_p17; 1. DR Pfam; PF19317; Gag_p24_C; 1. DR Pfam; PF00552; IN_DBD_C; 1. DR Pfam; PF02022; Integrase_Zn; 1. DR Pfam; PF00075; RNase_H; 1. DR Pfam; PF00665; rve; 1. DR Pfam; PF00077; RVP; 1. DR Pfam; PF00078; RVT_1; 1. DR Pfam; PF06815; RVT_connect; 1. DR Pfam; PF06817; RVT_thumb; 1. DR Pfam; PF00098; zf-CCHC; 2. DR PRINTS; PR00234; HIV1MATRIX. DR SMART; SM00343; ZnF_C2HC; 2. DR SUPFAM; SSF50630; Acid proteases; 1. DR SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1. DR SUPFAM; SSF47836; Retroviral matrix proteins; 1. DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1. DR SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1. DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 2. DR PROSITE; PS50175; ASP_PROT_RETROV; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. DR PROSITE; PS50994; INTEGRASE; 1. DR PROSITE; PS51027; INTEGRASE_DBD; 1. DR PROSITE; PS50879; RNASE_H_1; 1. DR PROSITE; PS50878; RT_POL; 1. DR PROSITE; PS50158; ZF_CCHC; 2. DR PROSITE; PS50876; ZF_INTEGRASE; 1. DR PDBsum; 1A43; -. DR PDBsum; 1A8O; -. DR PDBsum; 1AFV; -. DR PDBsum; 1AK4; -. DR PDBsum; 1AUM; -. DR PDBsum; 1B92; -. DR PDBsum; 1B9D; -. DR PDBsum; 1B9F; -. DR PDBsum; 1BAJ; -. DR PDBsum; 1BHL; -. DR PDBsum; 1BI4; -. DR PDBsum; 1BIS; -. DR PDBsum; 1BIU; -. DR PDBsum; 1BIZ; -. DR PDBsum; 1BL3; -. DR PDBsum; 1GWP; -. DR PDBsum; 1HIW; -. DR PDBsum; 1HYV; -. DR PDBsum; 1HYZ; -. DR PDBsum; 1ITG; -. DR PDBsum; 1K6Y; -. DR PDBsum; 1M9D; -. DR PDBsum; 1QS4; -. DR PDBsum; 1UPH; -. DR PDBsum; 1WJB; -. DR PDBsum; 1WJD; -. DR PDBsum; 20XX; -. DR PDBsum; 2B4J; -. DR PDBsum; 2GOL; -. DR PDBsum; 2GON; -. DR PDBsum; 2H3F; -. DR PDBsum; 2H3I; -. DR PDBsum; 2H3Q; -. DR PDBsum; 2H3V; -. DR PDBsum; 2H3Z; -. DR PDBsum; 2HMX; -. DR PDBsum; 2HVP; -. DR PDBsum; 2ITG; -. DR PDBsum; 2JPR; -. DR PDBsum; 2JYG; -. DR PDBsum; 2JYL; -. DR PDBsum; 2LF4; -. DR PDBsum; 2LYA; -. DR PDBsum; 2LYB; -. DR PDBsum; 2M3Z; -. DR PDBsum; 2M8L; -. DR PDBsum; 2M8N; -. DR PDBsum; 2M8P; -. DR PDBsum; 2ONT; -. DR PDBsum; 2PWM; -. DR PDBsum; 2PWO; -. DR PDBsum; 2PXR; -. DR PDBsum; 2X2D; -. DR PDBsum; 2XDE; -. DR PDBsum; 2XV6; -. DR PDBsum; 2XXM; -. DR PDBsum; 3AV9; -. DR PDBsum; 3AVA; -. DR PDBsum; 3AVB; -. DR PDBsum; 3AVC; -. DR PDBsum; 3AVF; -. DR PDBsum; 3AVG; -. DR PDBsum; 3AVH; -. DR PDBsum; 3AVJ; -. DR PDBsum; 3AVK; -. DR PDBsum; 3AVL; -. DR PDBsum; 3AVM; -. DR PDBsum; 3AVN; -. DR PDBsum; 3DIK; -. DR PDBsum; 3DPH; -. DR PDBsum; 3DS0; -. DR PDBsum; 3DS1; -. DR PDBsum; 3DS2; -. DR PDBsum; 3DS3; -. DR PDBsum; 3DS4; -. DR PDBsum; 3DS5; -. DR PDBsum; 3DTJ; -. DR PDBsum; 3GV2; -. DR PDBsum; 3H47; -. DR PDBsum; 3H4E; -. DR PDBsum; 3L3U; -. DR PDBsum; 3L3V; -. DR PDBsum; 3LPT; -. DR PDBsum; 3LPU; -. DR PDBsum; 3LRY; -. DR PDBsum; 3MGE; -. DR PDBsum; 3NF6; -. DR PDBsum; 3NF7; -. DR PDBsum; 3NF8; -. DR PDBsum; 3NF9; -. DR PDBsum; 3NFA; -. DR PDBsum; 3P05; -. DR PDBsum; 3P0A; -. DR PDBsum; 3S85; -. DR PDBsum; 3WNE; -. DR PDBsum; 3WNF; -. DR PDBsum; 3WNG; -. DR PDBsum; 3WNH; -. DR PDBsum; 3ZCM; -. DR PDBsum; 3ZSO; -. DR PDBsum; 3ZSQ; -. DR PDBsum; 3ZSR; -. DR PDBsum; 3ZSV; -. DR PDBsum; 3ZSW; -. DR PDBsum; 3ZSX; -. DR PDBsum; 3ZSY; -. DR PDBsum; 3ZSZ; -. DR PDBsum; 3ZT0; -. DR PDBsum; 3ZT1; -. DR PDBsum; 3ZT2; -. DR PDBsum; 3ZT3; -. DR PDBsum; 3ZT4; -. DR PDBsum; 4AH9; -. DR PDBsum; 4AHR; -. DR PDBsum; 4AHS; -. DR PDBsum; 4AHT; -. DR PDBsum; 4AHU; -. DR PDBsum; 4AHV; -. DR PDBsum; 4CE9; -. DR PDBsum; 4CEA; -. DR PDBsum; 4CEB; -. DR PDBsum; 4CEC; -. DR PDBsum; 4CED; -. DR PDBsum; 4CEE; -. DR PDBsum; 4CEF; -. DR PDBsum; 4CEO; -. DR PDBsum; 4CEQ; -. DR PDBsum; 4CER; -. DR PDBsum; 4CES; -. DR PDBsum; 4CEZ; -. DR PDBsum; 4CF0; -. DR PDBsum; 4CF1; -. DR PDBsum; 4CF2; -. DR PDBsum; 4CF8; -. DR PDBsum; 4CF9; -. DR PDBsum; 4CFA; -. DR PDBsum; 4CFB; -. DR PDBsum; 4CFC; -. DR PDBsum; 4CFD; -. DR PDBsum; 4CGD; -. DR PDBsum; 4CGF; -. DR PDBsum; 4CGG; -. DR PDBsum; 4CGH; -. DR PDBsum; 4CGI; -. DR PDBsum; 4CGJ; -. DR PDBsum; 4CHN; -. DR PDBsum; 4CHO; -. DR PDBsum; 4CHP; -. DR PDBsum; 4CHQ; -. DR PDBsum; 4CHY; -. DR PDBsum; 4CHZ; -. DR PDBsum; 4CIE; -. DR PDBsum; 4CIF; -. DR PDBsum; 4CIG; -. DR PDBsum; 4CJ3; -. DR PDBsum; 4CJ4; -. DR PDBsum; 4CJ5; -. DR PDBsum; 4CJE; -. DR PDBsum; 4CJF; -. DR PDBsum; 4CJK; -. DR PDBsum; 4CJL; -. DR PDBsum; 4CJP; -. DR PDBsum; 4CJQ; -. DR PDBsum; 4CJR; -. DR PDBsum; 4CJS; -. DR PDBsum; 4CJT; -. DR PDBsum; 4CJU; -. DR PDBsum; 4CJV; -. DR PDBsum; 4CJW; -. DR PDBsum; 4CK1; -. DR PDBsum; 4CK2; -. DR PDBsum; 4CK3; -. DR PDBsum; 4COC; -. DR PDBsum; 4COP; -. DR PDBsum; 4DGA; -. DR PDBsum; 4DGE; -. DR PDBsum; 4DMN; -. DR PDBsum; 4E1M; -. DR PDBsum; 4E1N; -. DR PDBsum; 4E91; -. DR PDBsum; 4E92; -. DR PDBsum; 4GVM; -. DR PDBsum; 4GW6; -. DR PDBsum; 4ID1; -. DR PDBsum; 4IPY; -. DR PDBsum; 4JLH; -. DR PDBsum; 4JMU; -. DR PDBsum; 4LH4; -. DR PDBsum; 4LH5; -. DR PDBsum; 4LQW; -. DR PDBsum; 4NX4; -. DR PDBsum; 4O0J; -. DR PDBsum; 4O55; -. DR PDBsum; 4O5B; -. DR PDBsum; 4OVL; -. DR PDBsum; 4PHV; -. DR PDBsum; 4QNB; -. DR PDBsum; 4WYM; -. DR PDBsum; 4Y1C; -. DR PDBsum; 4Y1D; -. DR PDBsum; 4ZHR; -. DR PDBsum; 5HVP; -. DR PDBsum; 5JL4; -. DR PDBsum; 5KGW; -. DR PDBsum; 5KGX; -. DR PDBsum; 5KRS; -. DR PDBsum; 5KRT; -. DR PDBsum; 5TEO; -. DR PDBsum; 5U1C; -. DR PDBsum; 5VCK; -. DR PDBsum; 5VEA; -. DR PDBsum; 5VJ3; -. DR PDBsum; 5XN0; -. DR PDBsum; 5XN1; -. DR PDBsum; 5XN2; -. DR PDBsum; 6ES8; -. DR PDBsum; 6IK9; -. DR PDBsum; 6IKA; -. DR PDBsum; 6JCF; -. DR PDBsum; 6JCG; -. DR PDBsum; 6KDJ; -. DR PDBsum; 6KDK; -. DR PDBsum; 6KDM; -. DR PDBsum; 6KDN; -. DR PDBsum; 6KDO; -. DR PDBsum; 6LMI; -. DR PDBsum; 6LMQ; -. DR PDBsum; 6MCR; -. DR PDBsum; 6MCS; -. DR PDBsum; 6OOS; -. DR PDBsum; 6OOT; -. DR PDBsum; 6OOU; -. DR PDBsum; 6OPW; -. DR PDBsum; 6OPY; -. DR PDBsum; 6OPZ; -. DR PDBsum; 6OXO; -. DR PDBsum; 6OXP; -. DR PDBsum; 6OXQ; -. DR PDBsum; 6OXR; -. DR PDBsum; 6OXS; -. DR PDBsum; 6OXT; -. DR PDBsum; 6OXU; -. DR PDBsum; 6OXV; -. DR PDBsum; 6OXW; -. DR PDBsum; 6OXX; -. DR PDBsum; 6OXY; -. DR PDBsum; 6OXZ; -. DR PDBsum; 6OY0; -. DR PDBsum; 6OY1; -. DR PDBsum; 6OY2; -. DR PDBsum; 6OYD; -. DR PDBsum; 6OYR; -. DR PDBsum; 6PJB; -. DR PDBsum; 6PJC; -. DR PDBsum; 6PJD; -. DR PDBsum; 6PJE; -. DR PDBsum; 6PJF; -. DR PDBsum; 6PJG; -. DR PDBsum; 6PJH; -. DR PDBsum; 6PJI; -. DR PDBsum; 6PJK; -. DR PDBsum; 6PJL; -. DR PDBsum; 6PJM; -. DR PDBsum; 6PJN; -. DR PDBsum; 6PJO; -. DR PDBsum; 6PUT; -. DR PDBsum; 6PUW; -. DR PDBsum; 6PUY; -. DR PDBsum; 6PUZ; -. DR PDBsum; 6T6E; -. DR PDBsum; 6U8Q; -. DR PDBsum; 6UM8; -. DR PDBsum; 6V3K; -. DR PDBsum; 6VDK; -. DR PDBsum; 6VQS; -. DR PDBsum; 6VRG; -. DR PDBsum; 6VX2; -. DR PDBsum; 6W0U; -. DR PDBsum; 6W42; -. DR PDBsum; 6W6T; -. DR PDBsum; 7D83; -. DR PDBsum; 7DBM; -. DR PDBsum; 7DBN; -. DR PDBsum; 7KE0; -. DR PDBsum; 7L1P; -. DR PDBsum; 7L23; -. DR PDBsum; 7LDY; -. DR PDBsum; 7LDZ; -. DR PDBsum; 7LE0; -. DR PDBsum; 7LE1; -. DR PDBsum; 7LE2; -. DR PDBsum; 7LE3; -. DR PDBsum; 7LE4; -. DR PDBsum; 7LE5; -. DR PDBsum; 7LE6; -. DR PDBsum; 7LE7; -. DR PDBsum; 7LE8; -. DR PDBsum; 7LE9; -. DR PDBsum; 7LEA; -. DR PDBsum; 7LEB; -. DR PDBsum; 7LEC; -. DR PDBsum; 7LED; -. DR PDBsum; 7LEE; -. DR PDBsum; 7LEF; -. DR PDBsum; 7LEG; -. DR PDBsum; 7LEH; -. DR PDBsum; 7LEI; -. DR PDBsum; 7LQP; -. DR PDBsum; 7RQ0; -. DR PDBsum; 7SIA; -. DR PDBsum; 7T9H; -. DR PDBsum; 7T9O; -. DR PDBsum; 7U2U; -. DR PDBsum; 7UE1; -. DR PDBsum; 7UOQ; -. DR PDBsum; 7WBS; -. DR PDBsum; 7WCE; -. DR PDBsum; 7WCQ; -. DR PDBsum; 7YF6; -. DR PDBsum; 7ZUD; -. DR PDBsum; 8A1P; -. DR PDBsum; 8A1Q; -. DR PDBsum; 8BUV; -. DR PDBsum; 8BV2; -. DR PDBsum; 8CBR; -. DR PDBsum; 8CBS; -. DR PDBsum; 8CBT; -. DR PDBsum; 8CBU; -. DR PDBsum; 8CBV; -. DR PDBsum; 8CT5; -. DR PDBsum; 8CT7; -. DR PDBsum; 8CTA; -. DR PDBsum; 8D3S; -. DR PDBsum; 8F22; -. DR PDBsum; 8FN7; -. DR PDBsum; 8FND; -. DR PDBsum; 8FNG; -. DR PDBsum; 8FNH; -. DR PDBsum; 8FNJ; -. DR PDBsum; 8FNL; -. DR PDBsum; 8FNM; -. DR PDBsum; 8FNN; -. DR PDBsum; 8FNO; -. DR PDBsum; 8FNP; -. DR PDBsum; 8FNQ; -. DR PDBsum; 8S9Q; -. DR PDBsum; 8T52; -. DR PDBsum; 8T5A; -. DR PDBsum; 8T5B; -. DR PDBsum; 8TOV; -. DR PDBsum; 8TQP; -. DR PDBsum; 8USY; -. DR PDBsum; 8V0Z; -. DR PDBsum; 8V23; -. DR PDBsum; 8V9C; -. DR PDBsum; 8VC0; -. DR PDBsum; 8VXV; -. DR PDBsum; 8VXW; -. DR PDBsum; 8W09; -. DR PDBsum; 8W2R; -. DR PDBsum; 8W34; -. DR PDBsum; 8WF7; -. DR PDBsum; 8X1Z; -. DR PDBsum; 8X20; -. DR PDBsum; 8X21; -. DR PDBsum; 8X22; -. DR PDBsum; 8ZH4; -. DR PDBsum; 8ZHA; -. DR PDBsum; 9BW9; -. DR PDBsum; 9C29; -. DR PDBsum; 9C9M; -. DR PDBsum; 9EK1; -. DR PDBsum; 9EK2; -. DR PDBsum; 9EK3; -. DR PDBsum; 9HVP; -. DR PDBsum; 9N0V; -. DR PDBsum; 9NLP; -. DR PDBsum; 9ON8; -. DR PDBsum; 9ON9; -. DR PDBsum; 9ONA; -. DR PDBsum; 9ONB; -. DR PDBsum; 9PYX; -. DR PDBsum; 9PZ1; -. DR PDBsum; 9Q0T; -. DR PDBsum; 9Q13; -. DR PDBsum; 9Q1C; -. DR PDBsum; 9Q1P; -. DR PDBsum; 9Q3P; -. DR PDBsum; 9Q3T; -. DR PDBsum; 9Q50; -. DR PDBsum; 9Q57; -. DR PDBsum; 9Q5D; -. DR PDBsum; 9RMX; -. PE 1: Evidence at protein level; KW 3D-structure; Activation of host caspases by virus; AIDS; KW Aspartyl protease; Capsid protein; DNA integration; DNA recombination; KW DNA-binding; DNA-directed DNA polymerase; Endonuclease; KW Eukaryotic host gene expression shutoff by virus; KW Eukaryotic host translation shutoff by virus; Host cell membrane; KW Host cytoplasm; Host endosome; Host gene expression shutoff by virus; KW Host membrane; Host nucleus; Host-virus interaction; Hydrolase; KW Lipid-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Modulation of host cell apoptosis by virus; Multifunctional enzyme; KW Myristate; Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease; KW Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase; KW Transferase; Viral genome integration; Viral nucleoprotein; KW Viral penetration into host nucleus; Viral release from host cell; Virion; KW Virion maturation; Virus entry into host cell; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed; by host" FT /evidence="ECO:0000250" FT CHAIN 2..1435 FT /note="Gag-Pol polyprotein" FT /id="PRO_0000261276" FT CHAIN 2..132 FT /note="Matrix protein p17" FT /evidence="ECO:0000250" FT /id="PRO_0000042394" FT CHAIN 133..363 FT /note="Capsid protein p24" FT /evidence="ECO:0000250" FT /id="PRO_0000042395" FT PEPTIDE 364..377 FT /note="Spacer peptide 1" FT /evidence="ECO:0000250" FT /id="PRO_0000042396" FT CHAIN 378..432 FT /note="Nucleocapsid protein p7" FT /evidence="ECO:0000250" FT /id="PRO_0000042397" FT PEPTIDE 433..440 FT /note="Transframe peptide" FT /evidence="ECO:0000255" FT /id="PRO_0000246725" FT CHAIN 441..488 FT /note="p6-pol" FT /evidence="ECO:0000255" FT /id="PRO_0000042398" FT CHAIN 489..587 FT /note="Protease" FT /evidence="ECO:0000250" FT /id="PRO_0000038660" FT CHAIN 588..1147 FT /note="Reverse transcriptase/ribonuclease H" FT /evidence="ECO:0000250" FT /id="PRO_0000042399" FT CHAIN 588..1027 FT /note="p51 RT" FT /evidence="ECO:0000250" FT /id="PRO_0000042400" FT CHAIN 1028..1147 FT /note="p15" FT /evidence="ECO:0000250" FT /id="PRO_0000042401" FT CHAIN 1148..1435 FT /note="Integrase" FT /evidence="ECO:0000250" FT /id="PRO_0000042402" FT DOMAIN 508..577 FT /note="Peptidase A2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275" FT DOMAIN 631..821 FT /note="Reverse transcriptase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405" FT DOMAIN 1021..1144 FT /note="RNase H type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408" FT DOMAIN 1201..1351 FT /note="Integrase catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457" FT ZN_FING 390..407 FT /note="CCHC-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT ZN_FING 411..428 FT /note="CCHC-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT ZN_FING 1150..1191 FT /note="Integrase-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450" FT DNA_BIND 1370..1417 FT /note="Integrase-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506" FT REGION 7..31 FT /note="Interaction with Gp41" FT /evidence="ECO:0000269|PubMed:8918455" FT REGION 8..43 FT /note="Interaction with host CALM1" FT /evidence="ECO:0000250|UniProtKB:P04585" FT REGION 12..19 FT /note="Interaction with host AP3D1" FT /evidence="ECO:0000269|PubMed:15766529" FT REGION 14..33 FT /note="Interaction with membrane phosphatidylinositol 4,5- FT bisphosphate and RNA" FT /evidence="ECO:0000269|PubMed:16840558" FT REGION 73..77 FT /note="Interaction with membrane phosphatidylinositol 4,5- FT bisphosphate" FT /evidence="ECO:0000269|PubMed:16840558" FT REGION 106..128 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 189..227 FT /note="Interaction with human PPIA/CYPA and NUP153" FT /evidence="ECO:0000269|PubMed:19369352, FT ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:8980234" FT REGION 277..363 FT /note="Dimerization/Multimerization of capsid protein p24" FT /evidence="ECO:0000250|UniProtKB:P04585" FT REGION 444..464 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 489..493 FT /note="Dimerization of protease" FT /evidence="ECO:0000250|UniProtKB:P04585" FT REGION 537..543 FT /note="Dimerization of protease" FT /evidence="ECO:0000250|UniProtKB:P04585" FT REGION 576..588 FT /note="Dimerization of protease" FT /evidence="ECO:0000250|UniProtKB:P04585" FT REGION 814..822 FT /note="RT 'primer grip'" FT /evidence="ECO:0000250" FT MOTIF 16..22 FT /note="Nuclear export signal" FT /evidence="ECO:0000250" FT MOTIF 26..32 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT MOTIF 985..1001 FT /note="Tryptophan repeat motif" FT /evidence="ECO:0000250" FT ACT_SITE 513 FT /note="For protease activity; shared with dimeric partner" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" FT BINDING 697 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for reverse transcriptase FT activity" FT /evidence="ECO:0000250" FT BINDING 772 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for reverse transcriptase FT activity" FT /evidence="ECO:0000250" FT BINDING 773 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for reverse transcriptase FT activity" FT /evidence="ECO:0000250" FT BINDING 1030 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for RNase H activity" FT /evidence="ECO:0000250" FT BINDING 1065 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for RNase H activity" FT /evidence="ECO:0000250" FT BINDING 1085 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for RNase H activity" FT /evidence="ECO:0000250" FT BINDING 1136 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for RNase H activity" FT /evidence="ECO:0000250" FT BINDING 1159 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450" FT BINDING 1163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450" FT BINDING 1187 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450" FT BINDING 1190 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450" FT BINDING 1211 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for integrase activity" FT BINDING 1263 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for integrase activity" FT BINDING 1299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for integrase activity" FT /evidence="ECO:0000250|UniProtKB:P04585" FT SITE 132..133 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250" FT SITE 221..222 FT /note="Cis/trans isomerization of proline peptide bond; by FT human PPIA/CYPA" FT /evidence="ECO:0000250" FT SITE 363..364 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250" FT SITE 377..378 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250" FT SITE 432..433 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000255" FT SITE 440..441 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250" FT SITE 488..489 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250" FT SITE 587..588 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250" FT SITE 988 FT /note="Essential for RT p66/p51 heterodimerization" FT /evidence="ECO:0000250" FT SITE 1001 FT /note="Essential for RT p66/p51 heterodimerization" FT /evidence="ECO:0000250" FT SITE 1027..1028 FT /note="Cleavage; by viral protease; partial" FT /evidence="ECO:0000250" FT SITE 1147..1148 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250" FT MOD_RES 132 FT /note="Phosphotyrosine; by host" FT /evidence="ECO:0000250" FT MOD_RES 148 FT /note="Phosphoserine; by host MAPK1" FT /evidence="ECO:0000269|PubMed:24509437" FT LIPID 2 FT /note="N-myristoyl glycine; by host" FT /evidence="ECO:0000250" FT MUTAGEN 9 FT /note="S->A: Loss of ability to fuse with target cell FT membranes and infect host cell." FT /evidence="ECO:0000269|PubMed:19059618" FT MUTAGEN 67 FT /note="S->A: Loss of ability to fuse with target cell FT membranes and infect host cell." FT /evidence="ECO:0000269|PubMed:19059618" FT MUTAGEN 72 FT /note="S->A: Loss of ability to fuse with target cell FT membranes and infect host cell." FT /evidence="ECO:0000269|PubMed:19059618" FT MUTAGEN 77 FT /note="S->A: Loss of ability to fuse with target cell FT membranes and infect host cell." FT /evidence="ECO:0000269|PubMed:19059618" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:1UPH" FT HELIX 10..18 FT /evidence="ECO:0007829|PDB:4JMU" FT STRAND 20..22 FT /evidence="ECO:0007829|PDB:4JMU" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:1UPH" FT HELIX 31..43 FT /evidence="ECO:0007829|PDB:4JMU" FT HELIX 48..52 FT /evidence="ECO:0007829|PDB:4JMU" FT HELIX 54..64 FT /evidence="ECO:0007829|PDB:4JMU" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:4JMU" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:4JMU" FT HELIX 73..90 FT /evidence="ECO:0007829|PDB:4JMU" FT HELIX 97..108 FT /evidence="ECO:0007829|PDB:4JMU" FT HELIX 109..112 FT /evidence="ECO:0007829|PDB:2H3Q" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:2H3F" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:2H3F" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:2H3Q" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:2XDE" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:4E92" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:2XDE" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:2XDE" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:2XDE" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:2GOL" FT HELIX 168..175 FT /evidence="ECO:0007829|PDB:2XDE" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:2XDE" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:2XDE" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:2PXR" FT HELIX 195..215 FT /evidence="ECO:0007829|PDB:2XDE" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:2PXR" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:1M9D" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:2PWO" FT HELIX 233..236 FT /evidence="ECO:0007829|PDB:2XDE" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:2PXR" FT HELIX 243..251 FT /evidence="ECO:0007829|PDB:2XDE" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:2XDE" FT HELIX 258..277 FT /evidence="ECO:0007829|PDB:2XDE" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:3DS4" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:2ONT" FT HELIX 293..306 FT /evidence="ECO:0007829|PDB:3DS4" FT TURN 308..310 FT /evidence="ECO:0007829|PDB:4QNB" FT HELIX 311..324 FT /evidence="ECO:0007829|PDB:3DS4" FT HELIX 328..337 FT /evidence="ECO:0007829|PDB:3DS4" FT HELIX 343..350 FT /evidence="ECO:0007829|PDB:3DS4" FT TURN 351..354 FT /evidence="ECO:0007829|PDB:3DS0" FT HELIX 356..361 FT /evidence="ECO:0007829|PDB:4IPY" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:2M3Z" FT STRAND 385..389 FT /evidence="ECO:0007829|PDB:2M3Z" FT STRAND 393..395 FT /evidence="ECO:0007829|PDB:2M3Z" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:2M3Z" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:2M3Z" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:2M3Z" FT TURN 423..425 FT /evidence="ECO:0007829|PDB:2M3Z" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:2M3Z" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:9HVP" FT STRAND 493..495 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 498..503 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 506..512 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 517..521 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 531..537 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 540..554 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 557..566 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 569..573 FT /evidence="ECO:0007829|PDB:7LEB" FT HELIX 575..578 FT /evidence="ECO:0007829|PDB:6OYD" FT TURN 579..582 FT /evidence="ECO:0007829|PDB:6OYD" FT STRAND 584..586 FT /evidence="ECO:0007829|PDB:7LE8" FT HELIX 593..596 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 604..606 FT /evidence="ECO:0007829|PDB:5XN1" FT HELIX 609..612 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 615..630 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 633..636 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 647..651 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 653..655 FT /evidence="ECO:0007829|PDB:8X22" FT STRAND 658..662 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 665..670 FT /evidence="ECO:0007829|PDB:6KDN" FT TURN 674..678 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 681..683 FT /evidence="ECO:0007829|PDB:4ZHR" FT HELIX 684..686 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 687..689 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 691..697 FT /evidence="ECO:0007829|PDB:6KDN" FT TURN 699..701 FT /evidence="ECO:0007829|PDB:6KDM" FT HELIX 702..704 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 709..715 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 717..719 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 721..726 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 729..735 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 743..761 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 765..770 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 773..780 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 782..798 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 805..807 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 811..816 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 819..821 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 823..828 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 829..831 FT /evidence="ECO:0007829|PDB:5XN2" FT HELIX 832..834 FT /evidence="ECO:0007829|PDB:7DBM" FT STRAND 837..840 FT /evidence="ECO:0007829|PDB:8X21" FT HELIX 841..854 FT /evidence="ECO:0007829|PDB:6KDN" FT TURN 855..857 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 858..860 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 864..868 FT /evidence="ECO:0007829|PDB:6KDN" FT TURN 869..872 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 881..883 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 884..898 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 908..910 FT /evidence="ECO:0007829|PDB:4ZHR" FT STRAND 913..920 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 923..931 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 935..941 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 946..949 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 951..970 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 975..980 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 982..991 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 992..995 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1000..1003 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1009..1011 FT /evidence="ECO:0007829|PDB:4ZHR" FT STRAND 1017..1019 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1024..1033 FT /evidence="ECO:0007829|PDB:6KDN" FT TURN 1035..1037 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1040..1046 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1051..1056 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 1061..1074 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1078..1084 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 1087..1094 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1098..1101 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 1103..1114 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1116..1122 FT /evidence="ECO:0007829|PDB:6KDN" FT STRAND 1125..1127 FT /evidence="ECO:0007829|PDB:8X22" FT HELIX 1132..1139 FT /evidence="ECO:0007829|PDB:6KDN" FT HELIX 1149..1152 FT /evidence="ECO:0007829|PDB:8FNP" FT HELIX 1159..1162 FT /evidence="ECO:0007829|PDB:6PUY" FT HELIX 1166..1173 FT /evidence="ECO:0007829|PDB:8FNP" FT HELIX 1177..1185 FT /evidence="ECO:0007829|PDB:8FNG" FT HELIX 1188..1190 FT /evidence="ECO:0007829|PDB:8FNG" FT HELIX 1204..1206 FT /evidence="ECO:0007829|PDB:3WNE" FT STRAND 1207..1215 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1218..1225 FT /evidence="ECO:0007829|PDB:3L3U" FT TURN 1226..1228 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1231..1238 FT /evidence="ECO:0007829|PDB:3L3U" FT HELIX 1241..1254 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1259..1262 FT /evidence="ECO:0007829|PDB:3L3U" FT HELIX 1266..1269 FT /evidence="ECO:0007829|PDB:3L3U" FT HELIX 1271..1280 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1283..1286 FT /evidence="ECO:0007829|PDB:3L3U" FT HELIX 1288..1290 FT /evidence="ECO:0007829|PDB:3L3U" FT TURN 1293..1296 FT /evidence="ECO:0007829|PDB:4E1M" FT HELIX 1301..1312 FT /evidence="ECO:0007829|PDB:3L3U" FT HELIX 1313..1315 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1316..1318 FT /evidence="ECO:0007829|PDB:1B9D" FT HELIX 1319..1332 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1334..1337 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1340..1342 FT /evidence="ECO:0007829|PDB:3L3U" FT HELIX 1343..1351 FT /evidence="ECO:0007829|PDB:3L3U" FT STRAND 1370..1374 FT /evidence="ECO:0007829|PDB:6T6E" FT STRAND 1379..1381 FT /evidence="ECO:0007829|PDB:8FNO" FT STRAND 1383..1391 FT /evidence="ECO:0007829|PDB:6T6E" FT STRAND 1393..1400 FT /evidence="ECO:0007829|PDB:6T6E" FT STRAND 1403..1408 FT /evidence="ECO:0007829|PDB:6T6E" FT HELIX 1409..1411 FT /evidence="ECO:0007829|PDB:6T6E" FT STRAND 1412..1416 FT /evidence="ECO:0007829|PDB:6T6E" FT HELIX 1420..1423 FT /evidence="ECO:0007829|PDB:8FNG" SQ SEQUENCE 1435 AA; 161789 MW; 798E74FD27C21244 CRC64; MGARASVLSG GELDKWEKIR LRPGGKKQYK LKHIVWASRE LERFAVNPGL LETSEGCRQI LGQLQPSLQT GSEELRSLYN TIAVLYCVHQ RIDVKDTKEA LDKIEEEQNK SKKKAQQAAA DTGNNSQVSQ NYPIVQNLQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM THNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPG ATLEEMMTAC QGVGGPGHKA RVLAEAMSQV TNPATIMIQK GNFRNQRKTV KCFNCGKEGH IAKNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLREDLAF PQGKAREFSS EQTRANSPTR RELQVWGRDN NSLSEAGADR QGTVSFSFPQ ITLWQRPLVT IKIGGQLKEA LLDTGADDTV LEEMNLPGRW KPKMIGGIGG FIKVRQYDQI LIEICGHKAI GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI KKKDSTKWRK LVDFRELNKR TQDFWEVQLG IPHPAGLKQK KSVTVLDVGD AYFSVPLDKD FRKYTAFTIP SINNETPGIR YQYNVLPQGW KGSPAIFQCS MTKILEPFRK QNPDIVIYQY MDDLYVGSDL EIGQHRTKIE ELRQHLLRWG FTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT VNDIQKLVGK LNWASQIYAG IKVRQLCKLL RGTKALTEVV PLTEEAELEL AENREILKEP VHGVYYDPSK DLIAEIQKQG QGQWTYQIYQ EPFKNLKTGK YARMKGAHTN DVKQLTEAVQ KIATESIVIW GKTPKFKLPI QKETWEAWWT EYWQATWIPE WEFVNTPPLV KLWYQLEKEP IIGAETFYVD GAANRETKLG KAGYVTDRGR QKVVPLTDTT NQKTELQAIH LALQDSGLEV NIVTDSQYAL GIIQAQPDKS ESELVSQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDGLVS AGIRKVLFLD GIDKAQEEHE KYHSNWRAMA SDFNLPPVVA KEIVASCDKC QLKGEAMHGQ VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK LAGRWPVKTV HTDNGSNFTS TTVKAACWWA GIKQEFGIPY NPQSQGVIES MNKELKKIIG QVRDQAEHLK TAVQMAVFIH NFKRKGGIGG YSAGERIVDI IATDIQTKEL QKQITKIQNF RVYYRDSRDP VWKGPAKLLW KGEGAVVIQD NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED //