POL_HV1H2
ID POL_HV1H2 Reviewed; 1435 AA.
AC P04585; O09777; Q9WJC5;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, 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:0000250|UniProtKB:P12497};
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 {ECO:0000269|PubMed:32053707, ECO:0000269|PubMed:33542150};
DE AltName: Full=PR;
DE AltName: Full=Retropepsin;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE EC=2.7.7.49 {ECO:0000250|UniProtKB:P03366};
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P03366};
DE EC=3.1.26.13 {ECO:0000250|UniProtKB:P03366};
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:0000305|PubMed:2349226};
DE EC=3.1.-.- {ECO:0000305|PubMed:2349226};
GN Name=gag-pol;
OS Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11706;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3040055; DOI=10.1089/aid.1987.3.57;
RA Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C.,
RA Wong-Staal F.;
RT "Complete nucleotide sequences of functional clones of the AIDS virus.";
RL AIDS Res. Hum. Retroviruses 3:57-69(1987).
RN [2]
RP SEQUENCE REVISION.
RA Ogata N., Alter H.J., Miller R.H., Purcell R.H.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Chappey C.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION (INTEGRASE).
RX PubMed=2349226; DOI=10.1073/pnas.87.11.4164;
RA Farnet C.M., Haseltine W.A.;
RT "Integration of human immunodeficiency virus type 1 DNA in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4164-4168(1990).
RN [5]
RP DIMERIZATION (PROTEASE).
RX PubMed=2162350; DOI=10.1016/s0021-9258(18)86974-5;
RA Weber I.T.;
RT "Comparison of the crystal structures and intersubunit interactions of
RT human immunodeficiency and Rous sarcoma virus proteases.";
RL J. Biol. Chem. 265:10492-10496(1990).
RN [6]
RP MUTAGENESIS OF HIS-1159; HIS-1163; GLN-1200; ASP-1211; SER-1228; ASP-1263;
RP GLU-1299; ARG-1346 AND TRP-1382.
RX PubMed=8420982; DOI=10.1016/s0021-9258(18)53969-7;
RA Leavitt A.D., Shiue L., Varmus H.E.;
RT "Site-directed mutagenesis of HIV-1 integrase demonstrates differential
RT effects on integrase functions in vitro.";
RL J. Biol. Chem. 268:2113-2119(1993).
RN [7]
RP MUTAGENESIS OF CYS-1187; CYS-1190; TRP-1208; ASP-1211; THR-1213; VAL-1222;
RP SER-1228; THR-1262; ASP-1263; GLY-1270; ILE-1282; VAL-1298; GLU-1299;
RP LYS-1306; ALA-1326 AND TRP-1382.
RC STRAIN=Isolate WI3;
RX PubMed=8035478; DOI=10.1128/jvi.68.8.4768-4775.1994;
RA Cannon P.M., Wilson W., Byles E., Kingsman S.M., Kingsman A.J.;
RT "Human immunodeficiency virus type 1 integrase: effect on viral replication
RT of mutations at highly conserved residues.";
RL J. Virol. 68:4768-4775(1994).
RN [8]
RP INTERACTION OF CAPSID WITH HUMAN PPIA/CYPA.
RX PubMed=8513493; DOI=10.1016/0092-8674(93)90637-6;
RA Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.;
RT "Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A
RT and B.";
RL Cell 73:1067-1078(1993).
RN [9]
RP INTERACTION WITH HUMAN SMARCB1/INI1 (INTEGRASE).
RX PubMed=7801128; DOI=10.1126/science.7801128;
RA Kalpana G.V., Marmon S., Wang W., Crabtree G.R., Goff S.P.;
RT "Binding and stimulation of HIV-1 integrase by a human homolog of yeast
RT transcription factor SNF5.";
RL Science 266:2002-2006(1994).
RN [10]
RP FUNCTION (PROTEASE).
RX PubMed=7835426; DOI=10.1016/0014-5793(94)01370-g;
RA Gaedigk-Nitschko K., Schoen A., Wachinger G., Erfle V., Kohleisen B.;
RT "Cleavage of recombinant and cell derived human immunodeficiency virus 1
RT (HIV-1) Nef protein by HIV-1 protease.";
RL FEBS Lett. 357:275-278(1995).
RN [11]
RP FUNCTION (CAPSID PROTEIN P24).
RX PubMed=8648689; DOI=10.1128/jvi.70.6.3551-3560.1996;
RA Braaten D., Franke E.K., Luban J.;
RT "Cyclophilin A is required for an early step in the life cycle of human
RT immunodeficiency virus type 1 before the initiation of reverse
RT transcription.";
RL J. Virol. 70:3551-3560(1996).
RN [12]
RP MUTAGENESIS OF PRO-217; VAL-218; HIS-219; ALA-220; GLY-221; PRO-222;
RP ILE-223; ALA-224 AND PRO-225, AND INTERACTION WITH HUMAN CYPA.
RX PubMed=9223641; DOI=10.1006/jmbi.1997.1051;
RA Yoo S., Myszka D.G., Yeh C., McMurray M., Hill C.P., Sundquist W.I.;
RT "Molecular recognition in the HIV-1 capsid/cyclophilin A complex.";
RL J. Mol. Biol. 269:780-795(1997).
RN [13]
RP MUTAGENESIS OF ASP-1211; ASP-1263 AND GLU-1299.
RX PubMed=9573231; DOI=10.1128/jvi.72.6.4678-4685.1998;
RA Gaur M., Leavitt A.D.;
RT "Mutations in the human immunodeficiency virus type 1 integrase D,D(35)E
RT motif do not eliminate provirus formation.";
RL J. Virol. 72:4678-4685(1998).
RN [14]
RP MUTAGENESIS OF LYS-18; ARG-22 AND LYS-27.
RX PubMed=10604476; DOI=10.1038/45272;
RA Dupont S., Sharova N., DeHoratius C., Virbasius C.M., Zhu X.,
RA Bukrinskaya A.G., Stevenson M., Green M.R.;
RT "A novel nuclear export activity in HIV-1 matrix protein required for viral
RT replication.";
RL Nature 402:681-685(1999).
RN [15]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=10494040; DOI=10.1159/000025405;
RA Chang Y.Y., Yu S.L., Syu W.J.;
RT "Organization of HIV-1 pol is critical for Pol polyprotein processing.";
RL J. Biomed. Sci. 6:333-341(1999).
RN [16]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=9931246; DOI=10.1006/jmbi.1998.2460;
RA Negroni M., Buc H.;
RT "Recombination during reverse transcription: an evaluation of the role of
RT the nucleocapsid protein.";
RL J. Mol. Biol. 286:15-31(1999).
RN [17]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=11044125; DOI=10.1128/jvi.74.22.10796-10800.2000;
RA Cen S., Khorchid A., Gabor J., Rong L., Wainberg M.A., Kleiman L.;
RT "Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the
RT initiation step of reverse transcription in human immunodeficiency virus
RT type 1.";
RL J. Virol. 74:10796-10800(2000).
RN [18]
RP GAG/GAG-POL RATIO.
RX PubMed=11160682; DOI=10.1128/jvi.75.4.1834-1841.2001;
RA Shehu-Xhilaga M., Crowe S.M., Mak J.;
RT "Maintenance of the Gag/Gag-Pol ratio is important for human
RT immunodeficiency virus type 1 RNA dimerization and viral infectivity.";
RL J. Virol. 75:1834-1841(2001).
RN [19]
RP ACTIVE SITES (REVERSE TRANSCRIPTASE/RIBONUCLEASE H), AND MUTAGENESIS OF
RP GLU-1065 AND ASP-1136.
RX PubMed=12206668; DOI=10.1021/bi025871v;
RA Cristofaro J.V., Rausch J.W., Le Grice S.F., DeStefano J.J.;
RT "Mutations in the ribonuclease H active site of HIV-RT reveal a role for
RT this site in stabilizing enzyme-primer-template binding.";
RL Biochemistry 41:10968-10975(2002).
RN [20]
RP CIS/TRANS ISOMERIZATION (CAPSID PROTEIN P24).
RX PubMed=11929983; DOI=10.1073/pnas.082100499;
RA Bosco D.A., Eisenmesser E.Z., Pochapsky S., Sundquist W.I., Kern D.;
RT "Catalysis of cis/trans isomerization in native HIV-1 capsid by human
RT cyclophilin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5247-5252(2002).
RN [21]
RP MUTAGENESIS OF HIS-400; CYS-405; HIS-421 AND CYS-426.
RX PubMed=11932404; DOI=10.1128/jvi.76.9.4370-4378.2002;
RA Guo J., Wu T., Kane B.F., Johnson D.G., Henderson L.E., Gorelick R.J.,
RA Levin J.G.;
RT "Subtle alterations of the native zinc finger structures have dramatic
RT effects on the nucleic acid chaperone activity of human immunodeficiency
RT virus type 1 nucleocapsid protein.";
RL J. Virol. 76:4370-4378(2002).
RN [22]
RP PROTEOLYTIC PROCESSING (GAG-POL POLYPROTEIN).
RX PubMed=12477841; DOI=10.1128/jvi.77.1.366-374.2003;
RA Pettit S.C., Gulnik S., Everitt L., Kaplan A.H.;
RT "The dimer interfaces of protease and extra-protease domains influence the
RT activation of protease and the specificity of GagPol cleavage.";
RL J. Virol. 77:366-374(2003).
RN [23]
RP QUATERNARY STRUCTURE (CAPSID PROTEIN P24).
RX PubMed=12660176; DOI=10.1093/emboj/cdg143;
RA Briggs J.A., Wilk T., Welker R., Krausslich H.G., Fuller S.D.;
RT "Structural organization of authentic, mature HIV-1 virions and cores.";
RL EMBO J. 22:1707-1715(2003).
RN [24]
RP FUNCTION (PROTEASE).
RX PubMed=12505164; DOI=10.1016/s0014-5793(02)03764-x;
RA Perales C., Carrasco L., Ventoso I.;
RT "Cleavage of eIF4G by HIV-1 protease: effects on translation.";
RL FEBS Lett. 533:89-94(2003).
RN [25]
RP CLEAVAGE (NUCLEOCAPSID PROTEIN P7).
RX PubMed=15065874; DOI=10.1021/bi035625z;
RA Tozser J., Shulenin S., Louis J.M., Copeland T.D., Oroszlan S.;
RT "In vitro processing of HIV-1 nucleocapsid protein by the viral proteinase:
RT effects of amino acid substitutions at the scissile bond in the proximal
RT zinc finger sequence.";
RL Biochemistry 43:4304-4312(2004).
RN [26]
RP SUBUNIT (REVERSE TRANSCRIPTASE/RIBONUCLEASE H), MUTAGENESIS OF
RP 488-PHE--GLN-490 AND LEU-821, AND PROTEOLYTIC CLEAVAGE (GAG-POL
RP POLYPROTEIN).
RX PubMed=15183348; DOI=10.1016/j.biocel.2004.02.020;
RA Sluis-Cremer N., Arion D., Abram M.E., Parniak M.A.;
RT "Proteolytic processing of an HIV-1 pol polyprotein precursor: insights
RT into the mechanism of reverse transcriptase p66/p51 heterodimer
RT formation.";
RL Int. J. Biochem. Cell Biol. 36:1836-1847(2004).
RN [27]
RP FUNCTION (REVERSE TRANSCRIPTASE/RIBONUCLEASE H).
RX PubMed=16221683; DOI=10.1074/jbc.m507839200;
RA Purohit V., Balakrishnan M., Kim B., Bambara R.A.;
RT "Evidence that HIV-1 reverse transcriptase employs the DNA 3' end directed
RT primary/secondary RNase H cleavage mechanism during synthesis and strand
RT transfer.";
RL J. Biol. Chem. 280:40534-40543(2005).
RN [28]
RP MUTAGENESIS OF ASN-394.
RX PubMed=16904152; DOI=10.1016/j.virol.2006.07.011;
RA Thomas J.A., Shulenin S., Coren L.V., Bosche W.J., Gagliardi T.D.,
RA Gorelick R.J., Oroszlan S.;
RT "Characterization of human immunodeficiency virus type 1 (HIV-1) containing
RT mutations in the nucleocapsid protein at a putative HIV-1 protease cleavage
RT site.";
RL Virology 354:261-270(2006).
RN [29]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=17070549; DOI=10.1016/j.jmb.2006.09.081;
RA Hagan N.A., Fabris D.;
RT "Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-
RT mediated dimerization and isomerization of HIV-1 stemloop 1.";
RL J. Mol. Biol. 365:396-410(2007).
RN [30]
RP SUBUNIT (MATRIX PROTEIN P17).
RX PubMed=17108052; DOI=10.1128/jvi.02122-06;
RA Alfadhli A., Huseby D., Kapit E., Colman D., Barklis E.;
RT "Human immunodeficiency virus type 1 matrix protein assembles on membranes
RT as a hexamer.";
RL J. Virol. 81:1472-1478(2007).
RN [31]
RP MUTAGENESIS OF SER-6; SER-9; SER-67 AND SER-72, AND POST-TRANSCRIPTIONAL
RP MODIFICATION.
RX PubMed=17656588; DOI=10.1110/ps.072987607;
RA Saad J.S., Kim A., Ghanam R.H., Dalton A.K., Vogt V.M., Wu Z., Lu W.,
RA Summers M.F.;
RT "Mutations that mimic phosphorylation of the HIV-1 matrix protein do not
RT perturb the myristyl switch.";
RL Protein Sci. 16:1793-1797(2007).
RN [32]
RP SUBCELLULAR LOCATION (INTEGRASE).
RX PubMed=18722123; DOI=10.1016/j.cub.2008.07.079;
RA Christ F., Thys W., De Rijck J., Gijsbers R., Albanese A., Arosio D.,
RA Emiliani S., Rain J.C., Benarous R., Cereseto A., Debyser Z.;
RT "Transportin-SR2 imports HIV into the nucleus.";
RL Curr. Biol. 18:1192-1202(2008).
RN [33]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=18343475; DOI=10.1016/j.virol.2008.02.001;
RA Kafaie J., Song R., Abrahamyan L., Mouland A.J., Laughrea M.;
RT "Mapping of nucleocapsid residues important for HIV-1 genomic RNA
RT dimerization and packaging.";
RL Virology 375:592-610(2008).
RN [34]
RP SUBUNIT (CAPSID PROTEIN P24), AND FUNCTION (CAPSID PROTEIN P24).
RX PubMed=19914170; DOI=10.1016/j.cell.2009.10.010;
RA Byeon I.J., Meng X., Jung J., Zhao G., Yang R., Ahn J., Shi J., Concel J.,
RA Aiken C., Zhang P., Gronenborn A.M.;
RT "Structural convergence between Cryo-EM and NMR reveals intersubunit
RT interactions critical for HIV-1 capsid function.";
RL Cell 139:780-790(2009).
RN [35]
RP FUNCTION (PROTEASE).
RX PubMed=19956697; DOI=10.1371/journal.pone.0007997;
RA Castello A., Franco D., Moral-Lopez P., Berlanga J.J., Alvarez E.,
RA Wimmer E., Carrasco L.;
RT "HIV- 1 protease inhibits Cap- and poly(A)-dependent translation upon
RT eIF4GI and PABP cleavage.";
RL PLoS ONE 4:E7997-E7997(2009).
RN [36]
RP SUBUNIT (MATRIX PROTEIN P17).
RX PubMed=19327811; DOI=10.1016/j.virol.2009.02.048;
RA Alfadhli A., Barklis R.L., Barklis E.;
RT "HIV-1 matrix organizes as a hexamer of trimers on membranes containing
RT phosphatidylinositol-(4,5)-bisphosphate.";
RL Virology 387:466-472(2009).
RN [37]
RP INTERACTION OF GAG POLYPROTEIN WITH PDZD8.
RX PubMed=20573829; DOI=10.1128/jvi.00843-10;
RA Henning M.S., Morham S.G., Goff S.P., Naghavi M.H.;
RT "PDZD8 is a novel Gag-interacting factor that promotes retroviral
RT infection.";
RL J. Virol. 84:8990-8995(2010).
RN [38]
RP FUNCTION (INTEGRASE), AND INTERACTION OF INTEGRASE WITH HUMAN KPNA3.
RX PubMed=20554775; DOI=10.1128/jvi.00508-10;
RA Ao Z., Danappa Jayappa K., Wang B., Zheng Y., Kung S., Rassart E.,
RA Depping R., Kohler M., Cohen E.A., Yao X.;
RT "Importin alpha3 interacts with HIV-1 integrase and contributes to HIV-1
RT nuclear import and replication.";
RL J. Virol. 84:8650-8663(2010).
RN [39]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=20828778; DOI=10.1016/j.virol.2010.08.013;
RA Jalalirad M., Laughrea M.;
RT "Formation of immature and mature genomic RNA dimers in wild-type and
RT protease-inactive HIV-1: differential roles of the Gag polyprotein,
RT nucleocapsid proteins NCp15, NCp9, NCp7, and the dimerization initiation
RT site.";
RL Virology 407:225-236(2010).
RN [40]
RP INTERACTION WITH MONKEY TRIM5.
RX PubMed=23785198; DOI=10.1128/jvi.00713-13;
RA Shi J., Friedman D.B., Aiken C.;
RT "Retrovirus restriction by TRIM5 proteins requires recognition of only a
RT small fraction of viral capsid subunits.";
RL J. Virol. 87:9271-9278(2013).
RN [41]
RP DIMERIZATION (PROTEASE).
RX PubMed=24132393; DOI=10.1007/s10930-013-9517-y;
RA Naicker P., Seele P., Dirr H.W., Sayed Y.;
RT "F99 is critical for dimerization and activation of South African HIV-1
RT subtype C protease.";
RL Protein J. 32:560-567(2013).
RN [42]
RP INTERACTION OF CAPSID-NUCLEOCAPSID COMPLEX WITH HUMAN PDZD8.
RX PubMed=24554657; DOI=10.1128/jvi.02945-13;
RA Guth C.A., Sodroski J.;
RT "Contribution of PDZD8 to stabilization of the human immunodeficiency virus
RT type 1 capsid.";
RL J. Virol. 88:4612-4623(2014).
RN [43]
RP INTERACTION OF MATRIX PROTEIN P17 WITH RAT CALM1.
RX PubMed=24500712; DOI=10.1074/jbc.m113.543694;
RA Vlach J., Samal A.B., Saad J.S.;
RT "Solution structure of calmodulin bound to the binding domain of the HIV-1
RT matrix protein.";
RL J. Biol. Chem. 289:8697-8705(2014).
RN [44]
RP FUNCTION (PROTEASE), AND CATALYTIC ACTIVITY (PROTEASE).
RX PubMed=32053707; DOI=10.1371/journal.ppat.1008305;
RA Jurczyszak D., Zhang W., Terry S.N., Kehrer T., Bermudez Gonzalez M.C.,
RA McGregor E., Mulder L.C.F., Eckwahl M.J., Pan T., Simon V.;
RT "HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral
RT particle.";
RL PLoS Pathog. 16:e1008305-e1008305(2020).
RN [45]
RP FUNCTION (PROTEASE), CATALYTIC ACTIVITY (PROTEASE), ACTIVE SITE (PROTEASE),
RP AND MUTAGENESIS OF ASP-513.
RX PubMed=33542150; DOI=10.1126/science.abe1707;
RA Wang Q., Gao H., Clark K.M., Mugisha C.S., Davis K., Tang J.P.,
RA Harlan G.H., DeSelm C.J., Presti R.M., Kutluay S.B., Shan L.;
RT "CARD8 is an inflammasome sensor for HIV-1 protease activity.";
RL Science 0:0-0(2021).
RN [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
RP REVIEW.
RX PubMed=15353349; DOI=10.2741/1472;
RA Turlure F., Devroe E., Silver P.A., Engelman A.;
RT "Human cell proteins and human immunodeficiency virus DNA integration.";
RL Front. Biosci. 9:3187-3208(2004).
RN [52]
RP REVIEW.
RX PubMed=16815734; DOI=10.1016/j.mib.2006.06.011;
RA Sokolskaja E., Luban J.;
RT "Cyclophilin, TRIM5, and innate immunity to HIV-1.";
RL Curr. Opin. Microbiol. 9:404-408(2006).
RN [53]
RP REVIEW.
RX PubMed=21762797; DOI=10.1016/j.jmb.2011.04.015;
RA Chukkapalli V., Ono A.;
RT "Molecular determinants that regulate plasma membrane association of HIV-1
RT Gag.";
RL J. Mol. Biol. 410:512-524(2011).
RN [54]
RP REVIEW.
RX PubMed=24907482; DOI=10.1016/j.virusres.2014.05.011;
RA Darlix J.L., de Rocquigny H., Mauffret O., Mely Y.;
RT "Retrospective on the all-in-one retroviral nucleocapsid protein.";
RL Virus Res. 193:2-15(2014).
RN [55]
RP REVIEW.
RX PubMed=24933691; DOI=10.1016/j.tim.2014.04.012;
RA Tedbury P.R., Freed E.O.;
RT "The role of matrix in HIV-1 envelope glycoprotein incorporation.";
RL Trends Microbiol. 22:372-378(2014).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 489-587.
RX PubMed=2682266; DOI=10.1038/342299a0;
RA Lapatto R., Blundell T., Hemmings A., Overington J., Wilderspin A.,
RA Wood S., Merson J.R., Whittle P.J., Danley D.E., Geoghegan K.F.,
RA Hawrylik S.J., Lee S.E., Scheld K.G., Hobart P.M.;
RT "X-ray analysis of HIV-1 proteinase at 2.7-A resolution confirms structural
RT homology among retroviral enzymes.";
RL Nature 342:299-302(1989).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 489-587 IN COMPLEX WITH THE
RP INHIBITOR RO 32-8959.
RX PubMed=1956054; DOI=10.1021/jm00115a028;
RA Krohn A., Redshaw S., Ritchie J.C., Graves B.J., Hatada M.H.;
RT "Novel binding mode of highly potent HIV-proteinase inhibitors
RT incorporating the (R)-hydroxyethylamine isostere.";
RL J. Med. Chem. 34:3340-3342(1991).
RN [58]
RP STRUCTURE BY NMR OF 390-406.
RX PubMed=1959614; DOI=10.1016/0014-5793(91)80825-n;
RA Omichinski J.G., Clore G.M., Sakaguchi K., Appella E., Gronenborn A.M.;
RT "Structural characterization of a 39-residue synthetic peptide containing
RT the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD
RT and NMR spectroscopy.";
RL FEBS Lett. 292:25-30(1991).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587 IN COMPLEX WITH A
RP DIHYDROXYETHYLENE-CONTAINING INHIBITOR.
RX PubMed=1304383; DOI=10.1002/pro.5560010811;
RA Thanki N., Rao J.K., Foundling S.I., Howe W.J., Moon J.B., Hui J.O.,
RA Tomasselli A.G., Heinrikson R.L., Thaisrivongs S., Wlodawer A.;
RT "Crystal structure of a complex of HIV-1 protease with a dihydroxyethylene-
RT containing inhibitor: comparisons with molecular modeling.";
RL Protein Sci. 1:1061-1072(1992).
RN [60]
RP STRUCTURE BY NMR OF 390-430.
RX PubMed=8289249; DOI=10.1016/s0022-2836(05)80033-6;
RA Morellet N., de Rocquigny H., Mely Y., Jullian N., Demene H., Ottmann M.,
RA Gerard D., Darlix J.L., Fournie-Zaluski M.-C., Roques B.P.;
RT "Conformational behaviour of the active and inactive forms of the
RT nucleocapsid NCp7 of HIV-1 studied by 1H NMR.";
RL J. Mol. Biol. 235:287-301(1994).
RN [61]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587 IN COMPLEX WITH THE
RP INHIBITOR XK263.
RX PubMed=8278812; DOI=10.1126/science.8278812;
RA Lam P.Y.S., Jadhav P.K., Eyermann C.J., Hodge C.N., Ru Y., Bacheler L.T.,
RA Meek J.L., Otto M.J., Rayner M.M., Wong Y.N., Chang C.-H., Weber P.C.,
RA Jackson D.A., Sharpe T.R., Erickson-Viitanen S.;
RT "Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV
RT protease inhibitors.";
RL Science 263:380-384(1994).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 588-1147.
RX PubMed=7523679; DOI=10.1006/jmbi.1994.1604;
RA Stammers D.K., Somers D.O., Ross C.K., Kirby I., Ray P.H., Wilson J.E.,
RA Norman M., Ren J.S., Esnouf R.M., Garman E.F., Jones E.Y., Stuart D.I.;
RT "Crystals of HIV-1 reverse transcriptase diffracting to 2.2 A resolution.";
RL J. Mol. Biol. 242:586-588(1994).
RN [63]
RP STRUCTURE BY NMR OF 1-132.
RX PubMed=8654825; DOI=10.1042/bst0230725;
RA Matthews S., Barlow P., Clark N., Kingsman S., Kingsman A., Campbell I.;
RT "Refined solution structure of p17, the HIV matrix protein.";
RL Biochem. Soc. Trans. 23:725-729(1995).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 588-1027.
RX PubMed=8535785; DOI=10.1016/s0969-2126(01)00226-x;
RA Ren J.S., Esnouf R.M., Hopkins A.L., Ross C.K., Jones E.Y., Stammers D.K.,
RA Stuart D.I.;
RT "The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO:
RT lessons for inhibitor design.";
RL Structure 3:915-926(1995).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 588-1147.
RX PubMed=7540935; DOI=10.1038/nsb0495-303;
RA Esnouf R.M., Ren J.S., Ross C.K., Jones E.Y., Stammers D.K., Stuart D.I.;
RT "Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside
RT inhibitors.";
RL Nat. Struct. Biol. 2:303-308(1995).
RN [66]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 588-1027.
RX PubMed=8648598; DOI=10.1021/jm960056x;
RA Hopkins A.L., Ren J.S., Esnouf R.M., Willcox B.E., Jones E.Y., Ross C.K.,
RA Miyasaka T., Walker R.T., Tanaka H., Stammers D.K., Stuart D.I.;
RT "Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT
RT series reveal conformational changes relevant to the design of potent non-
RT nucleoside inhibitors.";
RL J. Med. Chem. 39:1589-1600(1996).
RN [67]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587 IN COMPLEX WITH COMPLEX
RP WITH DMP450.
RX PubMed=8807858; DOI=10.1016/s1074-5521(96)90110-6;
RA Hodge C.N., Aldrich P.E., Bacheler L.T., Chang C.-H., Eyermann C.J.,
RA Garber S.S., Grubb M., Jackson D.A., Jadhav P.K., Korant B.D., Lam P.Y.S.,
RA Maurin M.B., Meek J.L., Otto M.J., Rayner M.M., Reid C., Sharpe T.R.,
RA Shum L., Winslow D.L., Erickson-Viitanen S.;
RT "Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency,
RT resistance profile, human pharmacokinetics and X-ray crystal structure of
RT DMP 450.";
RL Chem. Biol. 3:301-314(1996).
RN [68]
RP STRUCTURE BY NMR OF 489-587 IN COMPLEX WITH THE INHIBITOR DMP323.
RX PubMed=8868486; DOI=10.1002/pro.5560050311;
RA Yamazaki T., Hinck A.P., Wang Y.X., Nicholson L.K., Torchia D.A.,
RA Wingfield P., Stahl S.J., Kaufman J.D., Chang C.-H., Domaille P.J.,
RA Lam P.Y.S.;
RT "Three-dimensional solution structure of the HIV-1 protease complexed with
RT DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic
RT resonance spectroscopy.";
RL Protein Sci. 5:495-506(1996).
RN [69]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 588-1130.
RX PubMed=9108091; DOI=10.1073/pnas.94.8.3984;
RA Esnouf R.M., Ren J.S., Hopkins A.L., Ross C.K., Jones E.Y., Stammers D.K.,
RA Stuart D.I.;
RT "Unique features in the structure of the complex between HIV-1 reverse
RT transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain
RT resistance mutations for this nonnucleoside inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3984-3989(1997).
RN [70]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
RX PubMed=9003516; DOI=10.1021/jm960586t;
RA Jadhav P.K., Ala P.J., Woerner F.J., Chang C.-H., Garber S.S., Anton E.D.,
RA Bacheler L.T.;
RT "Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency
RT against both wild type and protease inhibitor resistant mutants of HIV.";
RL J. Med. Chem. 40:181-191(1997).
RN [71]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587 IN COMPLEX WITH THE
RP INHIBITOR LP-130.
RX PubMed=9827997; DOI=10.1002/pro.5560071108;
RA Kervinen J., Lubkowski J., Zdanov A., Bhatt D., Dunn B.M., Hui K.Y.,
RA Powell D.J., Kay J., Wlodawer A., Gustchina A.;
RT "Toward a universal inhibitor of retroviral proteases: comparative analysis
RT of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and
RT EIAV.";
RL Protein Sci. 7:2314-2323(1998).
RN [72]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
RX PubMed=9554878; DOI=10.1021/jm970524i;
RA Jadhav P.K., Woerner F.J., Lam P.Y., Hodge C.N., Eyermann C.J., Man H.W.,
RA Daneker W.F., Bacheler L.T., Rayner M.M., Meek J.L., Erickson-Viitanen S.,
RA Jackson D.A., Calabrese J.C., Schadt M.C., Chang C.-H.;
RT "Nonpeptide cyclic cyanoguanidines as HIV-1 protease inhibitors: synthesis,
RT structure-activity relationships, and X-ray crystal structure studies.";
RL J. Med. Chem. 41:1446-1455(1998).
RN [73]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
RX PubMed=9790666; DOI=10.1021/bi980386e;
RA Ala P.J., Huston E.E., Klabe R.M., Jadhav P.K., Lam P.Y.S., Chang C.-H.;
RT "Counteracting HIV-1 protease drug resistance: structural analysis of
RT mutant proteases complexed with XV638 and SD146, cyclic urea amides with
RT broad specificities.";
RL Biochemistry 37:15042-15049(1998).
RN [74]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
RX PubMed=9575185; DOI=10.1074/jbc.273.20.12325;
RA Ala P.J., DeLoskey R.J., Huston E.E., Jadhav P.K., Lam P.Y.S.,
RA Eyermann C.J., Hodge C.N., Schadt M.C., Lewandowski F.A., Weber P.C.,
RA McCabe D.D., Duke J.L., Chang C.-H.;
RT "Molecular recognition of cyclic urea HIV-1 protease inhibitors.";
RL J. Biol. Chem. 273:12325-12331(1998).
RN [75]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 490-587 IN COMPLEX WITH A
RP TRIPEPTIDE INHIBITOR.
RX PubMed=9485357; DOI=10.1021/bi972059x;
RA Louis J.M., Dyda F., Nashed N.T., Kimmel A.R., Davies D.R.;
RT "Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit
RT the HIV-1 protease.";
RL Biochemistry 37:2105-2110(1998).
RN [76]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 588-1130.
RX PubMed=9689112; DOI=10.1073/pnas.95.16.9518;
RA Ren J.S., Esnouf R.M., Hopkins A.L., Jones E.Y., Kirby I., Keeling J.,
RA Ross C.K., Larder B.A., Stuart D.I., Stammers D.K.;
RT "3'-azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse
RT transcriptase can induce long range conformational changes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9518-9523(1998).
RN [77]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 588-1147 IN COMPLEX WITH
RP CARBOXANILIDE DERIVATIVES.
RX PubMed=9772165; DOI=10.1021/bi981309m;
RA Ren J.S., Esnouf R.M., Hopkins A.L., Warren J., Balzarini J., Stuart D.I.,
RA Stammers D.K.;
RT "Crystal structures of HIV-1 reverse transcriptase in complex with
RT carboxanilide derivatives.";
RL Biochemistry 37:14394-14403(1998).
RN [78]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 501-599.
RX PubMed=10429209; DOI=10.1046/j.1432-1327.1999.00514.x;
RA Mahalingam B., Louis J.M., Reed C.C., Adomat J.M., Krouse J., Wang Y.-F.,
RA Harrison R.W., Weber I.T.;
RT "Structural and kinetic analysis of drug resistant mutants of HIV-1
RT protease.";
RL Eur. J. Biochem. 263:238-245(1999).
RN [79]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1199-1435.
RX PubMed=10890912; DOI=10.1073/pnas.150220297;
RA Chen J.C., Krucinski J., Miercke L.J., Finer-Moore J.S., Tang A.H.,
RA Leavitt A.D., Stroud R.M.;
RT "Crystal structure of the HIV-1 integrase catalytic core and C-terminal
RT domains: a model for viral DNA binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8233-8238(2000).
RN [80]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-587.
RX PubMed=11170214;
RX DOI=10.1002/1097-0134(20010401)43:1<57::aid-prot1017>3.0.co;2-d;
RA Pillai B., Kannan K.K., Hosur M.V.;
RT "1.9 A X-ray study shows closed flap conformation in crystals of tethered
RT HIV-1 PR.";
RL Proteins 43:57-64(2001).
RN [81]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 588-1147 IN COMPLEX WITH
RP INHIBITORS.
RX PubMed=11575933; DOI=10.1006/jmbi.2001.4988;
RA Ren J.S., Nichols C.E., Bird L.E., Chamberlain P.P., Weaver K.L.,
RA Short S.A., Stuart D.I., Stammers D.K.;
RT "Structural mechanisms of drug resistance for mutations at codons 181 and
RT 188 in HIV-1 reverse transcriptase and the improved resilience of second
RT generation non-nucleoside inhibitors.";
RL J. Mol. Biol. 312:795-805(2001).
RN [82]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 489-587.
RX PubMed=12051725; DOI=10.1016/s0006-291x(02)00482-5;
RA Kumar M., Kannan K.K., Hosur M.V., Bhavesh N.S., Chatterjee A., Mittal R.,
RA Hosur R.V.;
RT "Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR
RT investigations.";
RL Biochem. Biophys. Res. Commun. 294:395-401(2002).
RN [83]
RP STRUCTURE BY NMR OF 1014-1147.
RX PubMed=12534276; DOI=10.1021/bi0204894;
RA Pari K., Mueller G.A., DeRose E.F., Kirby T.W., London R.E.;
RT "Solution structure of the RNase H domain of the HIV-1 reverse
RT transcriptase in the presence of magnesium.";
RL Biochemistry 42:639-650(2003).
RN [84]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 588-1147 IN COMPLEX WITH
RP INHIBITORS.
RX PubMed=15095972; DOI=10.1016/j.jmb.2003.12.055;
RA Ren J.S., Nichols C.E., Chamberlain P.P., Weaver K.L., Short S.A.,
RA Stammers D.K.;
RT "Crystal structures of HIV-1 reverse transcriptases mutated at codons 100,
RT 106 and 108 and mechanisms of resistance to non-nucleoside inhibitors.";
RL J. Mol. Biol. 336:569-578(2004).
RN [85]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 588-1147 IN COMPLEX WITH
RP INHIBITORS.
RX PubMed=15537347; DOI=10.1021/jm040072r;
RA Freeman G.A., Andrews C.W. III, Hopkins A.L., Lowell G.S., Schaller L.T.,
RA Cowan J.R., Gonzales S.S., Koszalka G.W., Hazen R.J., Boone L.R.,
RA Ferris R.G., Creech K.L., Roberts G.B., Short S.A., Weaver K.L.,
RA Reynolds D.J., Milton J., Ren J.S., Stuart D.I., Stammers D.K., Chan J.H.;
RT "Design of non-nucleoside inhibitors of HIV-1 reverse transcriptase with
RT improved drug resistance properties. 2.";
RL J. Med. Chem. 47:5923-5936(2004).
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.
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 (By similarity). Matrix protein is part of the
CC pre-integration complex. Implicated in the release from host cell
CC mediated by Vpu. Binds to RNA (By similarity).
CC {ECO:0000250|UniProtKB:P12497}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the conical core that
CC encapsulates the genomic RNA-nucleocapsid complex in the virion
CC (PubMed:8648689). Most core are conical, with only 7% tubular. The core
CC is constituted by capsid protein hexamer subunits. The core is
CC disassembled soon after virion entry (PubMed:12660176). Host
CC restriction factors such as monkey TRIM5-alpha or TRIMCyp bind
CC retroviral capsids and cause premature capsid disassembly, leading to
CC blocks in reverse transcription. Capsid restriction by TRIM5 is one of
CC the factors which restricts HIV-1 to the human species
CC (PubMed:23785198). Host PIN1 apparently facilitates the virion
CC uncoating (By similarity). On the other hand, interactions with PDZD8
CC or CYPA stabilize the capsid (PubMed:24554657).
CC {ECO:0000250|UniProtKB:P12497, ECO:0000269|PubMed:12660176,
CC ECO:0000269|PubMed:23785198, ECO:0000269|PubMed:24554657,
CC ECO:0000269|PubMed:8648689}.
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:0000269|PubMed:11044125, ECO:0000269|PubMed:17070549,
CC ECO:0000269|PubMed:18343475, ECO:0000269|PubMed:20828778,
CC ECO:0000269|PubMed:9931246}.
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 (PubMed:9573231,
CC PubMed:11932404). Cleavages take place as an ordered, step-wise cascade
CC to yield mature proteins (PubMed:9573231, PubMed:11932404). This
CC process is called maturation (PubMed:9573231, PubMed:11932404).
CC Displays maximal activity during the budding process just prior to
CC particle release from the cell (PubMed:9573231, PubMed:11932404). Also
CC cleaves Nef and Vif, probably concomitantly with viral structural
CC proteins on maturation of virus particles (PubMed:7835426). Hydrolyzes
CC host EIF4GI and PABP1 in order to shut off the capped cellular mRNA
CC translation. The resulting inhibition of cellular protein synthesis
CC serves to ensure maximal viral gene expression and to evade host immune
CC response (PubMed:12660176, PubMed:19914170). 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 (PubMed:32053707). Mediates cleavage of host
CC CARD8, thereby activating the CARD8 inflammasome, leading to the
CC clearance of latent HIV-1 in patient CD4(+) T-cells after viral
CC reactivation; in contrast, HIV-1 can evade CARD8-sensing when its
CC protease remains inactive in infected cells prior to viral budding
CC (PubMed:33542150). {ECO:0000255|PROSITE-ProRule:PRU00275,
CC ECO:0000269|PubMed:12505164, ECO:0000269|PubMed:19956697,
CC ECO:0000269|PubMed:32053707, ECO:0000269|PubMed:33542150,
CC ECO:0000269|PubMed:7835426}.
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:0000269|PubMed:16221683}.
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:0000269|PubMed:20554775,
CC ECO:0000269|PubMed:2349226}.
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 ECO:0000269|PubMed:32053707, ECO:0000269|PubMed:33542150};
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;
CC Evidence={ECO:0000250|UniProtKB:P03366};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC 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 -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC hexamers of trimers (PubMed:19327811). Interacts with gp41 (via C-
CC terminus) (By similarity). Interacts with host CALM1; this interaction
CC induces a conformational change in the Matrix protein, triggering
CC exposure of the myristate group (PubMed:24500712). Interacts with host
CC AP3D1; this interaction allows the polyprotein trafficking to
CC multivesicular bodies during virus assembly (By similarity). 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:P12497, ECO:0000269|PubMed:19327811,
CC ECO:0000269|PubMed:24500712}.
CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers (PubMed:19914170).
CC Interacts with human PPIA/CYPA (PubMed:9223641, PubMed:8513493); this
CC interaction stabilizes the capsid. Interacts with human NUP153 (By
CC similarity). Interacts with host PDZD8; this interaction stabilizes the
CC capsid (PubMed:20573829). Interacts with monkey TRIM5; this interaction
CC destabilizes the capsid (PubMed:23785198).
CC {ECO:0000250|UniProtKB:P12497, ECO:0000269|PubMed:19914170,
CC ECO:0000269|PubMed:20573829, ECO:0000269|PubMed:23785198,
CC ECO:0000269|PubMed:8513493, ECO:0000269|PubMed:9223641}.
CC -!- SUBUNIT: [Protease]: Homodimer, whose active site consists of two
CC apposed aspartic acid residues (PubMed:2162350, PubMed:24132393).
CC {ECO:0000269|PubMed:2162350, ECO:0000269|PubMed:24132393}.
CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: Heterodimer of p66 RT
CC and p51 RT (RT p66/p51) (PubMed:15183348). 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 ECO:0000269|PubMed:15183348}.
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. Interacts with human SMARCB1/INI1 and human PSIP1/LEDGF
CC isoform 1 (PubMed:7801128). Interacts with human KPNA3; this
CC interaction might play a role in nuclear import of the pre-.
CC integration complex (PubMed:19914170). Interacts with human NUP153;
CC this interaction might play a role in nuclear import of the pre-
CC integration complex (By similarity). {ECO:0000250|UniProtKB:P03367,
CC ECO:0000250|UniProtKB:P12497, ECO:0000269|PubMed:19914170,
CC ECO:0000269|PubMed:7801128}.
CC -!- INTERACTION:
CC P04585; P04585: gag-pol; NbExp=29; IntAct=EBI-3989067, EBI-3989067;
CC P04585; O75475: PSIP1; Xeno; NbExp=21; IntAct=EBI-3989067, EBI-1801773;
CC P04585; P69718: rev; Xeno; NbExp=8; IntAct=EBI-3989067, EBI-8540156;
CC PRO_0000042440; PRO_0000042440 [P04585]: gag-pol; NbExp=5; IntAct=EBI-2504097, EBI-2504097;
CC PRO_0000042447; O00629: KPNA4; Xeno; NbExp=4; IntAct=EBI-9872653, EBI-396343;
CC PRO_0000042447; O75475-1: PSIP1; Xeno; NbExp=2; IntAct=EBI-9872653, EBI-5279836;
CC PRO_0000042447; Q12824: SMARCB1; Xeno; NbExp=3; IntAct=EBI-9872653, EBI-358419;
CC PRO_0000042447; Q9Y5L0: TNPO3; Xeno; NbExp=6; IntAct=EBI-9872653, EBI-1042571;
CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-
CC anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host
CC multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These
CC locations are linked to virus assembly sites. The main location is the
CC cell membrane, but under some circumstances, late endosomal
CC compartments can serve as productive sites for virion assembly.
CC {ECO:0000250|UniProtKB:P12493}.
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:0000269|PubMed:18722123}. Host cytoplasm {ECO:0000305}.
CC Note=Nuclear at initial 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=P04585-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P04591-1; 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 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: The tryptophan repeat
CC motif is involved in RT p66/p51 dimerization.
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 -!- 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:10494040,
CC ECO:0000269|PubMed:12477841, ECO:0000269|PubMed:15065874}.
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 (PubMed:17656588).
CC {ECO:0000269|PubMed:17656588}.
CC -!- PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this
CC phosphorylation is necessary for Pin1-mediated virion uncoating.
CC {ECO:0000250|UniProtKB:P12493}.
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:P03366}.
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.
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 -!- 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 this entry which is a representative of clade B.
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/content/hiv-drug-resistance-mutations";
CC -!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database;
CC URL="https://hivdb.stanford.edu";
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DR EMBL; K03455; AAB50259.1; ALT_SEQ; Genomic_RNA.
DR EMBL; AF033819; AAC82598.2; ALT_SEQ; Genomic_RNA.
DR RefSeq; NP_057849.4; NC_001802.1.
DR PDB; 1A30; X-ray; 2.00 A; A/B=489-587.
DR PDB; 1BV7; X-ray; 2.00 A; A/B=489-587.
DR PDB; 1BV9; X-ray; 2.00 A; A/B=489-587.
DR PDB; 1BVE; NMR; -; A/B=489-587.
DR PDB; 1BVG; NMR; -; A/B=489-587.
DR PDB; 1BWA; X-ray; 1.90 A; A/B=489-587.
DR PDB; 1BWB; X-ray; 1.80 A; A/B=489-587.
DR PDB; 1C0T; X-ray; 2.70 A; A=588-1147, B=588-1027.
DR PDB; 1C0U; X-ray; 2.52 A; A=588-1147, B=588-1027.
DR PDB; 1C1B; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 1C1C; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 1DMP; X-ray; 2.00 A; A/B=489-587.
DR PDB; 1DTQ; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 1DTT; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1E6J; X-ray; 3.00 A; P=143-352.
DR PDB; 1EP4; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 1ESK; NMR; -; A=390-430.
DR PDB; 1EX4; X-ray; 2.80 A; A/B=1199-1435.
DR PDB; 1EXQ; X-ray; 1.60 A; A/B=1203-1356.
DR PDB; 1FB7; X-ray; 2.60 A; A=489-587.
DR PDB; 1FK9; X-ray; 2.50 A; A=588-1130, B=588-1027.
DR PDB; 1FKO; X-ray; 2.90 A; A=588-1130, B=588-1027.
DR PDB; 1FKP; X-ray; 2.90 A; A=588-1130, B=588-1027.
DR PDB; 1G6L; X-ray; 1.90 A; A=484-587.
DR PDB; 1HIV; X-ray; 2.00 A; A/B=489-587.
DR PDB; 1HVH; X-ray; 1.80 A; A/B=489-587.
DR PDB; 1HVR; X-ray; 1.80 A; A/B=489-587.
DR PDB; 1HWR; X-ray; 1.80 A; A/B=489-587.
DR PDB; 1HXB; X-ray; 2.30 A; A/B=489-587.
DR PDB; 1JKH; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 1JLA; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 1JLB; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1JLC; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1JLE; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 1JLF; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 1JLG; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 1JLQ; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1KLM; X-ray; 2.65 A; A=588-1147, B=588-1027.
DR PDB; 1LV1; X-ray; 2.10 A; A=484-587.
DR PDB; 1LW0; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 1LW2; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1LWC; X-ray; 2.62 A; A=588-1147, B=588-1027.
DR PDB; 1LWE; X-ray; 2.81 A; A=588-1147, B=588-1027.
DR PDB; 1LWF; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 1NCP; NMR; -; N=390-406.
DR PDB; 1O1W; NMR; -; A=1014-1147.
DR PDB; 1ODW; X-ray; 2.10 A; A/B=489-587.
DR PDB; 1ODY; X-ray; 2.00 A; A/B=489-587.
DR PDB; 1QBR; X-ray; 1.80 A; A/B=489-587.
DR PDB; 1QBS; X-ray; 1.80 A; A/B=489-587.
DR PDB; 1QBT; X-ray; 2.10 A; A/B=489-587.
DR PDB; 1QBU; X-ray; 1.80 A; A/B=489-587.
DR PDB; 1REV; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 1RT1; X-ray; 2.55 A; A=588-1147, B=588-1027.
DR PDB; 1RT2; X-ray; 2.55 A; A=588-1147, B=588-1027.
DR PDB; 1RT3; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1RT4; X-ray; 2.90 A; A=588-1147, B=588-1027.
DR PDB; 1RT5; X-ray; 2.90 A; A=588-1147, B=588-1027.
DR PDB; 1RT6; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 1RT7; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1RTD; X-ray; 3.20 A; B/D=588-1027.
DR PDB; 1RTH; X-ray; 2.20 A; A=588-1147, B=588-1027.
DR PDB; 1RTI; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1RTJ; X-ray; 2.35 A; A=588-1147, B=588-1027.
DR PDB; 1S1T; X-ray; 2.40 A; A=588-1147, B=588-1027.
DR PDB; 1S1U; X-ray; 3.00 A; A=588-1147, B=588-1027.
DR PDB; 1S1V; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 1S1W; X-ray; 2.70 A; A=588-1147, B=588-1027.
DR PDB; 1S1X; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 1T05; X-ray; 3.00 A; B=588-1016.
DR PDB; 1TAM; NMR; -; A=1-132.
DR PDB; 1TKT; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 1TKX; X-ray; 2.85 A; A=588-1147, B=588-1027.
DR PDB; 1TKZ; X-ray; 2.81 A; A=588-1147, B=588-1027.
DR PDB; 1TL1; X-ray; 2.90 A; A=588-1147, B=588-1027.
DR PDB; 1TL3; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 1VRT; X-ray; 2.20 A; A=588-1147, B=588-1027.
DR PDB; 1VRU; X-ray; 2.40 A; A=588-1147, B=588-1027.
DR PDB; 2HND; X-ray; 2.50 A; A=591-1124.
DR PDB; 2HNY; X-ray; 2.50 A; A=591-1124.
DR PDB; 2HNZ; X-ray; 3.00 A; A=591-1124, B=594-1015.
DR PDB; 2KOD; NMR; -; A/B=276-363.
DR PDB; 2NPH; X-ray; 1.65 A; A/B=489-587.
DR PDB; 2OPP; X-ray; 2.55 A; A=591-1132, B=592-1018.
DR PDB; 2OPQ; X-ray; 2.80 A; A=591-1124, B=592-1015.
DR PDB; 2OPR; X-ray; 2.90 A; A=589-1135, B=593-1018.
DR PDB; 2OPS; X-ray; 2.30 A; A=589-1130, B=593-1027.
DR PDB; 2RF2; X-ray; 2.40 A; A=588-1147, B=588-1027.
DR PDB; 2RKI; X-ray; 2.30 A; A=588-1147, B=588-1027.
DR PDB; 2WHH; X-ray; 1.69 A; A=489-587.
DR PDB; 2WOM; X-ray; 3.20 A; A=588-1147, B=588-1027.
DR PDB; 2WON; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 2YNF; X-ray; 2.36 A; A=588-1147, B=588-1015.
DR PDB; 2YNG; X-ray; 2.12 A; A=588-1147, B=588-1015.
DR PDB; 2YNH; X-ray; 2.90 A; A=588-1147, B=588-1015.
DR PDB; 2YNI; X-ray; 2.49 A; A=588-1147, B=588-1015.
DR PDB; 3AO2; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 3C6T; X-ray; 2.70 A; A=588-1147, B=588-1027.
DR PDB; 3C6U; X-ray; 2.70 A; A=588-1147, B=588-1027.
DR PDB; 3DI6; X-ray; 2.65 A; A=588-1148, B=588-1027.
DR PDB; 3DLE; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 3DLG; X-ray; 2.20 A; A=588-1147, B=588-1027.
DR PDB; 3DM2; X-ray; 3.10 A; A=588-1147, B=588-1027.
DR PDB; 3DMJ; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 3DOK; X-ray; 2.90 A; A=588-1147, B=588-1027.
DR PDB; 3DOL; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 3DOX; X-ray; 2.00 A; A=484-587.
DR PDB; 3DRP; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 3DRR; X-ray; 2.89 A; A=588-1147, B=588-1027.
DR PDB; 3DRS; X-ray; 3.15 A; A=588-1147, B=588-1027.
DR PDB; 3DYA; X-ray; 2.30 A; A=588-1148, B=588-1027.
DR PDB; 3E01; X-ray; 2.95 A; A=588-1148, B=588-1027.
DR PDB; 3FFI; X-ray; 2.60 A; A=588-1147, B=588-1027.
DR PDB; 3I0R; X-ray; 2.98 A; A=588-1147, B=588-1027.
DR PDB; 3I0S; X-ray; 2.70 A; A=588-1147, B=588-1027.
DR PDB; 3KJV; X-ray; 3.10 A; A=588-1147, B=588-1027.
DR PDB; 3KK1; X-ray; 2.70 A; A=588-1147, B=588-1027.
DR PDB; 3KK2; X-ray; 2.90 A; A=588-1147, B=588-1027.
DR PDB; 3KK3; X-ray; 2.90 A; A=588-1147, B=588-1027.
DR PDB; 3KT2; X-ray; 1.65 A; A=484-587.
DR PDB; 3KT5; X-ray; 1.80 A; A=484-587.
DR PDB; 3LAK; X-ray; 2.30 A; A/B=588-1147.
DR PDB; 3LAL; X-ray; 2.51 A; A/B=588-1147.
DR PDB; 3LAM; X-ray; 2.76 A; A/B=588-1147.
DR PDB; 3LAN; X-ray; 2.55 A; A/B=588-1147.
DR PDB; 3LP0; X-ray; 2.79 A; A=588-1147, B=588-1027.
DR PDB; 3LP1; X-ray; 2.23 A; A=588-1147, B=588-1027.
DR PDB; 3LP2; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 3M8P; X-ray; 2.67 A; A=588-1148, B=588-1027.
DR PDB; 3M8Q; X-ray; 2.70 A; A=588-1148, B=588-1027.
DR PDB; 3MEC; X-ray; 2.30 A; A=588-1147, B=588-1027.
DR PDB; 3MED; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 3MEE; X-ray; 2.40 A; A=588-1147, B=588-1027.
DR PDB; 3MEG; X-ray; 2.80 A; A=588-1147, B=588-1027.
DR PDB; 3N3I; X-ray; 2.50 A; A=484-587.
DR PDB; 3NBP; X-ray; 2.95 A; A=588-1148, B=588-1027.
DR PDB; 3PHV; X-ray; 2.70 A; A=489-587.
DR PDB; 3QIN; X-ray; 1.70 A; A=1014-1103, A=1142-1148.
DR PDB; 3QIO; X-ray; 1.40 A; A=1014-1148.
DR PDB; 3QIP; X-ray; 2.09 A; A=588-1147, B=588-1027.
DR PDB; 3T19; X-ray; 2.60 A; A/B=588-1147.
DR PDB; 3T1A; X-ray; 2.40 A; A/B=588-1147.
DR PDB; 3TAM; X-ray; 2.51 A; A=590-1147, B=588-1027.
DR PDB; 4B3O; X-ray; 3.30 A; A=588-1145, B=588-1027.
DR PDB; 4B3P; X-ray; 4.84 A; A=588-1145, B=588-1027.
DR PDB; 4B3Q; X-ray; 5.00 A; A=588-1145, B=588-1027.
DR PDB; 4I7F; X-ray; 2.50 A; A=588-1147, B=588-1027.
DR PDB; 4KSE; X-ray; 2.68 A; B=588-1017.
DR PDB; 4KV8; X-ray; 2.30 A; A=588-1147, B=588-1027.
DR PDB; 4NCG; X-ray; 2.58 A; A=588-1147, B=585-1027.
DR PDB; 4Q1W; X-ray; 1.85 A; A/B=496-587.
DR PDB; 4Q1X; X-ray; 1.90 A; A/B=496-587.
DR PDB; 4Q1Y; X-ray; 1.50 A; A/B=496-587.
DR PDB; 4Q5M; X-ray; 1.79 A; A=484-587.
DR PDB; 4QLH; X-ray; 2.45 A; A=489-592.
DR PDB; 4U1H; X-ray; 1.59 A; C=180-188.
DR PDB; 4U1I; X-ray; 1.92 A; C=180-188.
DR PDB; 4U1J; X-ray; 1.38 A; C=180-188.
DR PDB; 4U7Q; X-ray; 1.70 A; A/B=496-587.
DR PDB; 4U7V; X-ray; 1.38 A; A/B=496-587.
DR PDB; 5DGU; X-ray; 1.22 A; A/B=496-587.
DR PDB; 5DGW; X-ray; 1.62 A; A/B=496-587.
DR PDB; 5EU7; X-ray; 2.64 A; A/B=1204-1356.
DR PDB; 5HRN; X-ray; 1.75 A; A=1197-1359.
DR PDB; 5HRP; X-ray; 1.81 A; A=1197-1359.
DR PDB; 5HRR; X-ray; 1.88 A; A=1197-1359.
DR PDB; 5HRS; X-ray; 1.86 A; A=1197-1359.
DR PDB; 5IM7; X-ray; 2.50 A; E/F=308-316.
DR PDB; 5J2M; X-ray; 2.43 A; A=588-1147, B=588-1027.
DR PDB; 5J2N; X-ray; 2.90 A; A=588-1147, B=588-1027.
DR PDB; 5J2P; X-ray; 2.53 A; A=588-1147, B=588-1027.
DR PDB; 5J2Q; X-ray; 2.79 A; A=588-1147, B=588-1027.
DR PDB; 5K14; X-ray; 2.40 A; A=588-1147.
DR PDB; 5KAO; X-ray; 1.80 A; A/B=489-587.
DR PDB; 5T82; NMR; -; A=824-905.
DR PDB; 5TC2; X-ray; 1.84 A; A/B=1366-1420.
DR PDB; 5VZ6; X-ray; 2.60 A; A=585-1147, B=585-1027.
DR PDB; 5XOS; X-ray; 1.70 A; C=880-888.
DR PDB; 5XOT; X-ray; 2.79 A; C=880-888.
DR PDB; 5YRS; X-ray; 1.76 A; A/B=489-587.
DR PDB; 6BJ2; X-ray; 3.35 A; C=880-888.
DR PDB; 6BJ3; X-ray; 1.90 A; C=880-888.
DR PDB; 6BSG; X-ray; 2.44 A; A=588-1144, B=588-1027.
DR PDB; 6BSH; X-ray; 2.65 A; A=588-1144, B=588-1027.
DR PDB; 6BSI; X-ray; 3.25 A; A=588-1144, B=588-1027.
DR PDB; 6BSJ; X-ray; 2.89 A; A=588-1144, B=588-1027.
DR PDB; 6DIF; X-ray; 1.20 A; A/B=489-587.
DR PDB; 6DIL; X-ray; 1.48 A; A/B=489-587.
DR PDB; 6DJ1; X-ray; 1.26 A; A/B=489-587.
DR PDB; 6DJ2; X-ray; 1.36 A; A/B=489-587.
DR PDB; 6DJ5; X-ray; 1.75 A; A/B=489-587.
DR PDB; 6DJ7; X-ray; 1.31 A; A/B=489-587.
DR PDB; 6DV0; X-ray; 1.20 A; A/B=489-587.
DR PDB; 6DV4; X-ray; 1.14 A; A/B=489-587.
DR PDB; 6E7J; X-ray; 1.30 A; A/B=489-587.
DR PDB; 6E9A; X-ray; 1.22 A; A/B=489-587.
DR PDB; 6EWA; X-ray; 2.39 A; C/G=896-904.
DR PDB; 6EX9; X-ray; 2.01 A; A=1204-1355.
DR PDB; 6GL1; X-ray; 2.62 A; P/Q/R/T=275-283.
DR PDB; 6J1V; X-ray; 2.00 A; C=745-753.
DR PDB; 6J1W; X-ray; 1.50 A; C=745-753.
DR PDB; 6OR7; X-ray; 2.53 A; A=588-1147, B=588-1027.
DR PDB; 6OTZ; X-ray; 2.86 A; A=588-1145, B=588-1027.
DR PDB; 6P1I; X-ray; 2.74 A; A=588-1147, B=588-1027.
DR PDB; 6P1X; X-ray; 2.55 A; A=588-1147, B=588-1027.
DR PDB; 6P2G; X-ray; 2.99 A; A=588-1147, B=588-1027.
DR PDB; 6PYL; X-ray; 1.52 A; C=263-272.
DR PDB; 6SKK; EM; 3.60 A; A/B/C/D/E/F=133-363.
DR PDB; 6SKM; EM; 4.90 A; A/B/C/D/E/F=133-363.
DR PDB; 6SKN; EM; 4.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=133-363.
DR PDB; 6SLQ; EM; 4.40 A; A/B/C/D/E/F=133-363.
DR PDB; 6SLU; EM; 4.70 A; A/B/C/D/E/F=133-363.
DR PDB; 6SMU; EM; 5.00 A; A/B/C/D/E/F=133-363.
DR PDB; 6UIR; X-ray; 2.64 A; A=588-1147, B=588-1027.
DR PDB; 6UIS; X-ray; 2.75 A; A=588-1147, B=588-1027.
DR PDB; 6UIT; X-ray; 2.81 A; A=588-1147, B=588-1027.
DR PDB; 6UJX; X-ray; 2.70 A; A=588-1147, B=588-1027.
DR PDB; 6UJY; X-ray; 2.59 A; A=588-1147, B=588-1027.
DR PDB; 6UJZ; X-ray; 2.56 A; A=588-1147, B=588-1027.
DR PDB; 6UK0; X-ray; 2.76 A; A=588-1147, B=588-1027.
DR PDB; 6VPZ; X-ray; 2.10 A; C=263-273.
DR PDB; 6VQ2; X-ray; 2.25 A; C=263-276.
DR PDB; 6VQD; X-ray; 1.88 A; C=263-270.
DR PDB; 6VQE; X-ray; 1.77 A; C=263-275.
DR PDB; 6VQY; X-ray; 2.57 A; F/G=263-269.
DR PDB; 6VQZ; X-ray; 2.25 A; F/G=263-268.
DR PDB; 6WAZ; EM; 4.10 A; B=588-1027.
DR PDB; 6WB1; EM; 4.70 A; B=588-1027.
DR PDB; 6WPF; X-ray; 2.53 A; A=588-1147, B=588-1027.
DR PDB; 6WPH; X-ray; 2.72 A; A=588-1147, B=588-1027.
DR PDB; 6WPJ; X-ray; 2.73 A; A=588-1147, B=588-1027.
DR PDBsum; 1A30; -.
DR PDBsum; 1BV7; -.
DR PDBsum; 1BV9; -.
DR PDBsum; 1BVE; -.
DR PDBsum; 1BVG; -.
DR PDBsum; 1BWA; -.
DR PDBsum; 1BWB; -.
DR PDBsum; 1C0T; -.
DR PDBsum; 1C0U; -.
DR PDBsum; 1C1B; -.
DR PDBsum; 1C1C; -.
DR PDBsum; 1DMP; -.
DR PDBsum; 1DTQ; -.
DR PDBsum; 1DTT; -.
DR PDBsum; 1E6J; -.
DR PDBsum; 1EP4; -.
DR PDBsum; 1ESK; -.
DR PDBsum; 1EX4; -.
DR PDBsum; 1EXQ; -.
DR PDBsum; 1FB7; -.
DR PDBsum; 1FK9; -.
DR PDBsum; 1FKO; -.
DR PDBsum; 1FKP; -.
DR PDBsum; 1G6L; -.
DR PDBsum; 1HIV; -.
DR PDBsum; 1HVH; -.
DR PDBsum; 1HVR; -.
DR PDBsum; 1HWR; -.
DR PDBsum; 1HXB; -.
DR PDBsum; 1JKH; -.
DR PDBsum; 1JLA; -.
DR PDBsum; 1JLB; -.
DR PDBsum; 1JLC; -.
DR PDBsum; 1JLE; -.
DR PDBsum; 1JLF; -.
DR PDBsum; 1JLG; -.
DR PDBsum; 1JLQ; -.
DR PDBsum; 1KLM; -.
DR PDBsum; 1LV1; -.
DR PDBsum; 1LW0; -.
DR PDBsum; 1LW2; -.
DR PDBsum; 1LWC; -.
DR PDBsum; 1LWE; -.
DR PDBsum; 1LWF; -.
DR PDBsum; 1NCP; -.
DR PDBsum; 1O1W; -.
DR PDBsum; 1ODW; -.
DR PDBsum; 1ODY; -.
DR PDBsum; 1QBR; -.
DR PDBsum; 1QBS; -.
DR PDBsum; 1QBT; -.
DR PDBsum; 1QBU; -.
DR PDBsum; 1REV; -.
DR PDBsum; 1RT1; -.
DR PDBsum; 1RT2; -.
DR PDBsum; 1RT3; -.
DR PDBsum; 1RT4; -.
DR PDBsum; 1RT5; -.
DR PDBsum; 1RT6; -.
DR PDBsum; 1RT7; -.
DR PDBsum; 1RTD; -.
DR PDBsum; 1RTH; -.
DR PDBsum; 1RTI; -.
DR PDBsum; 1RTJ; -.
DR PDBsum; 1S1T; -.
DR PDBsum; 1S1U; -.
DR PDBsum; 1S1V; -.
DR PDBsum; 1S1W; -.
DR PDBsum; 1S1X; -.
DR PDBsum; 1T05; -.
DR PDBsum; 1TAM; -.
DR PDBsum; 1TKT; -.
DR PDBsum; 1TKX; -.
DR PDBsum; 1TKZ; -.
DR PDBsum; 1TL1; -.
DR PDBsum; 1TL3; -.
DR PDBsum; 1VRT; -.
DR PDBsum; 1VRU; -.
DR PDBsum; 2HND; -.
DR PDBsum; 2HNY; -.
DR PDBsum; 2HNZ; -.
DR PDBsum; 2KOD; -.
DR PDBsum; 2NPH; -.
DR PDBsum; 2OPP; -.
DR PDBsum; 2OPQ; -.
DR PDBsum; 2OPR; -.
DR PDBsum; 2OPS; -.
DR PDBsum; 2RF2; -.
DR PDBsum; 2RKI; -.
DR PDBsum; 2WHH; -.
DR PDBsum; 2WOM; -.
DR PDBsum; 2WON; -.
DR PDBsum; 2YNF; -.
DR PDBsum; 2YNG; -.
DR PDBsum; 2YNH; -.
DR PDBsum; 2YNI; -.
DR PDBsum; 3AO2; -.
DR PDBsum; 3C6T; -.
DR PDBsum; 3C6U; -.
DR PDBsum; 3DI6; -.
DR PDBsum; 3DLE; -.
DR PDBsum; 3DLG; -.
DR PDBsum; 3DM2; -.
DR PDBsum; 3DMJ; -.
DR PDBsum; 3DOK; -.
DR PDBsum; 3DOL; -.
DR PDBsum; 3DOX; -.
DR PDBsum; 3DRP; -.
DR PDBsum; 3DRR; -.
DR PDBsum; 3DRS; -.
DR PDBsum; 3DYA; -.
DR PDBsum; 3E01; -.
DR PDBsum; 3FFI; -.
DR PDBsum; 3I0R; -.
DR PDBsum; 3I0S; -.
DR PDBsum; 3KJV; -.
DR PDBsum; 3KK1; -.
DR PDBsum; 3KK2; -.
DR PDBsum; 3KK3; -.
DR PDBsum; 3KT2; -.
DR PDBsum; 3KT5; -.
DR PDBsum; 3LAK; -.
DR PDBsum; 3LAL; -.
DR PDBsum; 3LAM; -.
DR PDBsum; 3LAN; -.
DR PDBsum; 3LP0; -.
DR PDBsum; 3LP1; -.
DR PDBsum; 3LP2; -.
DR PDBsum; 3M8P; -.
DR PDBsum; 3M8Q; -.
DR PDBsum; 3MEC; -.
DR PDBsum; 3MED; -.
DR PDBsum; 3MEE; -.
DR PDBsum; 3MEG; -.
DR PDBsum; 3N3I; -.
DR PDBsum; 3NBP; -.
DR PDBsum; 3PHV; -.
DR PDBsum; 3QIN; -.
DR PDBsum; 3QIO; -.
DR PDBsum; 3QIP; -.
DR PDBsum; 3T19; -.
DR PDBsum; 3T1A; -.
DR PDBsum; 3TAM; -.
DR PDBsum; 4B3O; -.
DR PDBsum; 4B3P; -.
DR PDBsum; 4B3Q; -.
DR PDBsum; 4I7F; -.
DR PDBsum; 4KSE; -.
DR PDBsum; 4KV8; -.
DR PDBsum; 4NCG; -.
DR PDBsum; 4Q1W; -.
DR PDBsum; 4Q1X; -.
DR PDBsum; 4Q1Y; -.
DR PDBsum; 4Q5M; -.
DR PDBsum; 4QLH; -.
DR PDBsum; 4U1H; -.
DR PDBsum; 4U1I; -.
DR PDBsum; 4U1J; -.
DR PDBsum; 4U7Q; -.
DR PDBsum; 4U7V; -.
DR PDBsum; 5DGU; -.
DR PDBsum; 5DGW; -.
DR PDBsum; 5EU7; -.
DR PDBsum; 5HRN; -.
DR PDBsum; 5HRP; -.
DR PDBsum; 5HRR; -.
DR PDBsum; 5HRS; -.
DR PDBsum; 5IM7; -.
DR PDBsum; 5J2M; -.
DR PDBsum; 5J2N; -.
DR PDBsum; 5J2P; -.
DR PDBsum; 5J2Q; -.
DR PDBsum; 5K14; -.
DR PDBsum; 5KAO; -.
DR PDBsum; 5T82; -.
DR PDBsum; 5TC2; -.
DR PDBsum; 5VZ6; -.
DR PDBsum; 5XOS; -.
DR PDBsum; 5XOT; -.
DR PDBsum; 5YRS; -.
DR PDBsum; 6BJ2; -.
DR PDBsum; 6BJ3; -.
DR PDBsum; 6BSG; -.
DR PDBsum; 6BSH; -.
DR PDBsum; 6BSI; -.
DR PDBsum; 6BSJ; -.
DR PDBsum; 6DIF; -.
DR PDBsum; 6DIL; -.
DR PDBsum; 6DJ1; -.
DR PDBsum; 6DJ2; -.
DR PDBsum; 6DJ5; -.
DR PDBsum; 6DJ7; -.
DR PDBsum; 6DV0; -.
DR PDBsum; 6DV4; -.
DR PDBsum; 6E7J; -.
DR PDBsum; 6E9A; -.
DR PDBsum; 6EWA; -.
DR PDBsum; 6EX9; -.
DR PDBsum; 6GL1; -.
DR PDBsum; 6J1V; -.
DR PDBsum; 6J1W; -.
DR PDBsum; 6OR7; -.
DR PDBsum; 6OTZ; -.
DR PDBsum; 6P1I; -.
DR PDBsum; 6P1X; -.
DR PDBsum; 6P2G; -.
DR PDBsum; 6PYL; -.
DR PDBsum; 6SKK; -.
DR PDBsum; 6SKM; -.
DR PDBsum; 6SKN; -.
DR PDBsum; 6SLQ; -.
DR PDBsum; 6SLU; -.
DR PDBsum; 6SMU; -.
DR PDBsum; 6UIR; -.
DR PDBsum; 6UIS; -.
DR PDBsum; 6UIT; -.
DR PDBsum; 6UJX; -.
DR PDBsum; 6UJY; -.
DR PDBsum; 6UJZ; -.
DR PDBsum; 6UK0; -.
DR PDBsum; 6VPZ; -.
DR PDBsum; 6VQ2; -.
DR PDBsum; 6VQD; -.
DR PDBsum; 6VQE; -.
DR PDBsum; 6VQY; -.
DR PDBsum; 6VQZ; -.
DR PDBsum; 6WAZ; -.
DR PDBsum; 6WB1; -.
DR PDBsum; 6WPF; -.
DR PDBsum; 6WPH; -.
DR PDBsum; 6WPJ; -.
DR BMRB; P04585; -.
DR SASBDB; P04585; -.
DR SMR; P04585; -.
DR BioGRID; 1205538; 130.
DR IntAct; P04585; 6.
DR MINT; P04585; -.
DR BindingDB; P04585; -.
DR ChEMBL; CHEMBL3638360; -.
DR DrugBank; DB07910; (2S)-2-amino-3-phenylpropane-1,1-diol.
DR DrugBank; DB07473; (R)-(+) 5(9BH)-OXO-9B-PHENYL-2,3-DIHYDROTHIAZOLO[2,3-A]ISOINDOL-3-CARBOXYLIC ACID METHYL ESTER.
DR DrugBank; DB07472; (R)-(+)9B-(3-METHYL)PHENYL-2,3-DIHYDROTHIAZOLO[2,3-A]ISOINDOL-5(9BH)-ONE.
DR DrugBank; DB07892; 1-(2-HYDROXYETHYLOXYMETHYL)-6-PHENYL THIOTHYMINE.
DR DrugBank; DB08372; 1-[2-(4-ETHOXY-3-FLUOROPYRIDIN-2-YL)ETHYL]-3-(5-METHYLPYRIDIN-2-YL)THIOUREA.
DR DrugBank; DB08682; 1-METHYL ETHYL 1-CHLORO-5-[[(5,6DIHYDRO-2-METHYL-1,4-OXATHIIN-3-YL)CARBONYL]AMINO]BENZOATE.
DR DrugBank; DB08681; 1-METHYL ETHYL 2-CHLORO-5-[[[(1-METHYLETHOXY)THIOOXO]METHYL]AMINO]-BENZOATE.
DR DrugBank; DB08286; 1-Naphthoxyacetic acid.
DR DrugBank; DB07826; 2-[4-chloro-2-(phenylcarbonyl)phenoxy]-N-phenylacetamide.
DR DrugBank; DB08528; 2-AMINO-6-(3,5-DIMETHYLPHENYL)SULFONYLBENZONITRILE.
DR DrugBank; DB08444; 3-[2-bromo-4-(1H-pyrazolo[3,4-c]pyridazin-3-ylmethyl)phenoxy]-5-methylbenzonitrile.
DR DrugBank; DB08446; 3-[6-bromo-2-fluoro-3-(1H-pyrazolo[3,4-c]pyridazin-3-ylmethyl)phenoxy]-5-chlorobenzonitrile.
DR DrugBank; DB08154; 3-chloro-5-[2-chloro-5-(1H-indazol-3-ylmethoxy)phenoxy]benzonitrile.
DR DrugBank; DB08459; 3-chloro-5-[2-chloro-5-(1H-pyrazolo[3,4-b]pyridin-3-ylmethoxy)phenoxy]benzonitrile.
DR DrugBank; DB07864; 4-[(CYCLOPROPYLETHYNYL)OXY]-6-FLUORO-3-ISOPROPYLQUINOLIN-2(1H)-ONE.
DR DrugBank; DB08211; 5-bromo-3-(pyrrolidin-1-ylsulfonyl)-1H-indole-2-carboxamide.
DR DrugBank; DB08665; 6,11-DIHYDRO-11-ETHYL-6-METHYL-9-NITRO-5H-PYRIDO[2,3-B][1,5]BENZODIAZEPIN-5-ONE.
DR DrugBank; DB07820; 6-(3',5'-DIMETHYLBENZYL)-1-ETHOXYMETHYL-5-ISOPROPYLURACIL.
DR DrugBank; DB08379; 6-(4-chloro-2-fluoro-3-phenoxybenzyl)pyridazin-3(2H)-one.
DR DrugBank; DB07184; 6-(cyclohexylsulfanyl)-1-(ethoxymethyl)-5-(1-methylethyl)pyrimidine-2,4(1H,3H)-dione.
DR DrugBank; DB08634; 6-BENZYL-1-BENZYLOXYMETHYL-5-ISOPROPYL URACIL.
DR DrugBank; DB07871; 6-CHLORO-4-(CYCLOHEXYLOXY)-3-ISOPROPYLQUINOLIN-2(1H)-ONE.
DR DrugBank; DB07867; 6-CHLORO-4-(CYCLOHEXYLOXY)-3-PROPYLQUINOLIN-2(1H)-ONE.
DR DrugBank; DB07868; 6-CHLORO-4-(CYCLOHEXYLSULFANYL)-3-PROPYLQUINOLIN-2(1H)-ONE.
DR DrugBank; DB07869; 6-Chloro-4-[(R)-cyclohexylsulfinyl]-3-propyl-2(1H)-quinolinone.
DR DrugBank; DB06910; [4-R-(4-ALPHA,6-BETA,7-BETA]-HEXAHYDRO-5,6-DI(HYDROXY)-1,3-DI(ALLYL)-4,7-BISPHENYLMETHYL)-2H-1,3-DIAZEPINONE.
DR DrugBank; DB07332; ALPHA-(2,6-DICHLOROPHENYL)-ALPHA-(2-ACETYL-5-METHYLANILINO)ACETAMIDE.
DR DrugBank; DB06581; Bevirimat.
DR DrugBank; DB08502; Capravirine.
DR DrugBank; DB08188; Emivirine.
DR DrugBank; DB06414; Etravirine.
DR DrugBank; DB13119; GSK-364735.
DR DrugBank; DB04609; INHIBITOR Q8467 OF DUPONT MERCK.
DR DrugBank; DB08460; MK-4965.
DR DrugBank; DB02102; Mozenavir.
DR DrugBank; DB07797; N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-CHLORO-PYRIDYL]-THIOUREA.
DR DrugBank; DB07781; N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-NITRILOMETHYL-PYRIDYL]-THIOUREA.
DR DrugBank; DB08680; N-{3-[(E)-(tert-butoxyimino)methyl]-4-chlorophenyl}-2-methylfuran-3-carbimidothioic acid.
DR DrugBank; DB07884; Opaviraline.
DR DrugBank; DB08598; R-82913.
DR DrugBank; DB08494; S-{2-[(2-chloro-4-sulfamoylphenyl)amino]-2-oxoethyl} 6-methyl-3,4-dihydroquinoline-1(2H)-carbothioate.
DR DrugBank; DB02729; SD146.
DR DrugBank; DB05328; VGV-1.
DR DrugBank; DB02702; XV638.
DR MEROPS; A02.001; -.
DR PRIDE; P04585; -.
DR ABCD; P04585; 3 sequenced antibodies.
DR GeneID; 155348; -.
DR KEGG; vg:155348; -.
DR Reactome; R-HSA-162585; Uncoating of the HIV Virion.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-162592; Integration of provirus.
DR Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
DR Reactome; R-HSA-164516; Minus-strand DNA synthesis.
DR Reactome; R-HSA-164525; Plus-strand DNA synthesis.
DR Reactome; R-HSA-164843; 2-LTR circle formation.
DR Reactome; R-HSA-173107; Binding and entry of HIV virion.
DR Reactome; R-HSA-175474; Assembly Of The HIV Virion.
DR Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
DR Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
DR Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR SABIO-RK; P04585; -.
DR EvolutionaryTrace; P04585; -.
DR PRO; PR:P04585; -.
DR Proteomes; UP000002241; Genome.
DR Proteomes; UP000105453; Genome.
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:0016020; C:membrane; IEA:UniProtKB-KW.
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; IDA:UniProtKB.
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:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008907; F:integrase activity; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; TAS:Reactome.
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; IDA:CAFA.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
DR GO; GO:0039651; P:induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR GO; GO:0019072; P:viral genome packaging; IMP:UniProtKB.
DR GO; GO:0019058; P:viral life cycle; TAS:Reactome.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 3.
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 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; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
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.
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 Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
KW RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW Viral nucleoprotein; Viral penetration into host nucleus;
KW Viral release from host cell; Virion; Virion maturation;
KW 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_0000223620"
FT CHAIN 2..132
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042439"
FT CHAIN 133..363
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042440"
FT PEPTIDE 364..377
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042441"
FT CHAIN 378..432
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042442"
FT PEPTIDE 433..440
FT /note="Transframe peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000246716"
FT CHAIN 441..488
FT /note="p6-pol"
FT /evidence="ECO:0000255"
FT /id="PRO_0000042443"
FT CHAIN 489..587
FT /note="Protease"
FT /id="PRO_0000038665"
FT CHAIN 588..1147
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000042444"
FT CHAIN 588..1027
FT /note="p51 RT"
FT /id="PRO_0000042445"
FT CHAIN 1028..1147
FT /note="p15"
FT /id="PRO_0000042446"
FT CHAIN 1148..1435
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042447"
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:0000250|UniProtKB:P12497"
FT REGION 8..43
FT /note="Interaction with host CALM1"
FT /evidence="ECO:0000269|PubMed:24500712"
FT REGION 12..19
FT /note="Interaction with host AP3D1"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 14..33
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate and RNA"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 73..77
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..227
FT /note="Interaction with host PPIA/CYPA and NUP153"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 217..225
FT /note="PPIA/CYPA-binding loop"
FT REGION 277..363
FT /note="Dimerization/Multimerization of capsid protein p24"
FT REGION 448..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..493
FT /note="Dimerization of protease"
FT /evidence="ECO:0000269|PubMed:2162350"
FT REGION 537..543
FT /note="Dimerization of protease"
FT /evidence="ECO:0000269|PubMed:2162350"
FT REGION 576..588
FT /note="Dimerization of protease"
FT /evidence="ECO:0000269|PubMed:2162350"
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 ECO:0000305|PubMed:33542150"
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 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:0000269|PubMed:12206668"
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 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:0000269|PubMed:12206668"
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 /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
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:0000305"
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 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 393..394
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 426..427
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
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:0000305|PubMed:15183348"
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 LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT VARIANT 496
FT /note="R -> K (confers to resistance to A-77003; when
FT associated with other amino acid changes)"
FT VARIANT 496
FT /note="R -> Q (confers to resistance to A-77003)"
FT VARIANT 498
FT /note="L -> F (confers resistance to amprenavir,
FT atazanavir, lopinavir; when associated with other amino
FT acid changes)"
FT VARIANT 498
FT /note="L -> I (confers resistance to indinavir, lopinavir,
FT ritonavir and saquinavir; when associated with other amino
FT acid changes)"
FT VARIANT 498
FT /note="L -> R (confers resistance to indinavir and
FT lopinavir; when associated with other amino acid changes)"
FT VARIANT 498
FT /note="L -> V (confers resistance to indinavir and
FT lopinavir; when associated with other amino acid changes)"
FT VARIANT 498
FT /note="L -> Y (confers resistance to atazanavir; when
FT associated with other amino acid changes)"
FT VARIANT 503
FT /note="I -> V (confers resistance to tipranavir)"
FT VARIANT 504
FT /note="G -> E (confers resistance to lopinavir, ritonavir
FT and saquinavir; when associated with other amino acid
FT changes)"
FT VARIANT 508
FT /note="K -> I (confers resistance to lopinavir)"
FT VARIANT 508
FT /note="K -> M (confers resistance to indinavir, lopinavir
FT and nelfinavir; when associated with other amino acid
FT changes)"
FT VARIANT 508
FT /note="K -> R (confers resistance to indinavir, lopinavir
FT and ritonavir; when associated with other amino acid
FT changes)"
FT VARIANT 511
FT /note="L -> I (confers resistance to BILA 2185 BS)"
FT VARIANT 512
FT /note="L -> I (confers resistance to amprenavir, indinavir,
FT lopinavir, ritonavir and saquinavir; when associated with
FT other amino acid changes)"
FT VARIANT 518
FT /note="D -> N (confers resistance to nelfinavir; when
FT associated with other amino acid changes)"
FT VARIANT 520
FT /note="V -> I (confers resistance to A-77003, amprenavir,
FT atazanavir, indinavir, kynostatin, lopinavir, ritonavir and
FT saquinavir; when associated with other amino acid changes)"
FT VARIANT 521
FT /note="L -> F (confers resistance to atazanavir nelfinavir
FT and ritonavir; when associated with other amino acid
FT changes)"
FT VARIANT 522
FT /note="E -> Q (confers resistance to lopinavir; when
FT associated with other amino acid changes)"
FT VARIANT 523
FT /note="E -> D (confers resistance to tipranavir)"
FT VARIANT 524
FT /note="M -> I (confers resistance to nelfinavir and
FT ritonavir; when associated with other amino acid changes)"
FT VARIANT 524
FT /note="M -> L (confers resistance to ritonavir; when
FT associated with other amino acid changes)"
FT VARIANT 525
FT /note="S -> D (confers resistance to indinavir and
FT tipranavir; when associated with other amino acid changes)"
FT VARIANT 529
FT /note="R -> K (confers resistance to tipranavir)"
FT VARIANT 533
FT /note="K -> I (confers resistance to DMD-323; when
FT associated with other amino acid changes)"
FT VARIANT 534
FT /note="M -> F (confers resistance to A-77003)"
FT VARIANT 534
FT /note="M -> I (confers resistance to A-77003, amprenavir,
FT atazanavir, indinavir, kynostatin, lopinavir, ritonavir,
FT saquinavir and telinavir; when associated with other amino
FT acid changes)"
FT VARIANT 534
FT /note="M -> L (confers resistance to A-77003, amprenavir,
FT indinavir, lopinavir, ritonavir and saquinavir; when
FT associated with other amino acid changes)"
FT VARIANT 535
FT /note="I -> V (confers resistance to amprenavir, lopinavir,
FT kynostatin, ritonavir and saquinavir; when associated with
FT other amino acid changes)"
FT VARIANT 536
FT /note="G -> V (confers resistance to A-77003, amprenavir,
FT indinavir, ritonavir, saquinavir and telinavir; when
FT associated with other amino acid changes)"
FT VARIANT 538
FT /note="I -> L (confers resistance to atazanavir; when
FT associated with other amino acid changes)"
FT VARIANT 538
FT /note="I -> V (confers resistance to amprenavir, lopinavir
FT and ritonavir; when associated with other amino acid
FT changes)"
FT VARIANT 541
FT /note="F -> L (confers resistance to lopinavir and
FT telinavir; when associated with other amino acid changes)"
FT VARIANT 541
FT /note="F -> Y (confers resistance to indinavir, ritonavir
FT and saquinavir; when associated with other amino acid
FT changes)"
FT VARIANT 542
FT /note="I -> A (confers resistance to lopinavir)"
FT VARIANT 542
FT /note="I -> L (confers resistance to amprenavir and
FT lopinavir; when associated with other amino acid changes)"
FT VARIANT 542
FT /note="I -> M (confers resistance to amprenavir and
FT lopinavir)"
FT VARIANT 542
FT /note="I -> S (confers resistance to lopinavir)"
FT VARIANT 542
FT /note="I -> T (confers resistance to lopinavir; when
FT associated with other amino acid changes)"
FT VARIANT 542
FT /note="I -> V (confers resistance to indinavir, lopinavir,
FT ritonavir and saquinavir; when associated with other amino
FT acid changes)"
FT VARIANT 543
FT /note="K -> R (confers resistance to nelfinavir)"
FT VARIANT 545
FT /note="R -> K (confers resistance to nelfinavir)"
FT VARIANT 546
FT /note="Q -> E (confers resistance to lopinavir and
FT ritonavir; when associated with other amino acid changes)"
FT VARIANT 548
FT /note="D -> E (confers resistance to tripanavir)"
FT VARIANT 549
FT /note="Q -> H (confers resistance to lopinavir; when
FT associated with other amino acid changes)"
FT VARIANT 551
FT /note="L -> P (confers resistance to atazanavir, indinavir,
FT lopinavir, ritonavir and saquinavir; when associated with
FT other amino acid changes)"
FT VARIANT 551
FT /note="L -> T (confers resistance to lopinavir)"
FT VARIANT 553
FT /note="E -> Q (confers resistance to lopinavir; when
FT associated with other amino acid changes)"
FT VARIANT 554
FT /note="I -> F (confers resistance to indinavir, ritonavir
FT and saquinavir; when associated with other amino acid
FT changes)"
FT VARIANT 557
FT /note="H -> Y (confers resistance to lopinavir; when
FT associated with other amino acid changes)"
FT VARIANT 559
FT /note="A -> I (confers resistance to lopinavir; when
FT associated with other amino acid changes)"
FT VARIANT 559
FT /note="A -> L (confers resistance to lopinavir; when
FT associated with other amino acid changes)"
FT VARIANT 559
FT /note="A -> T (confers resistance to A-77003, indinavir,
FT lopinavir, nelfinavir and tripanavir; when associated with
FT other amino acid changes)"
FT VARIANT 559
FT /note="A -> V (confers resistance to amprenavir,
FT atazanavir, indinavir, kynostatin, lopinavir, nelfinavir,
FT ritonavir, saquinavir and telinavir; when associated with
FT other amino acid changes)"
FT VARIANT 561
FT /note="G -> S (confers resistance to indinavir, nelfinavir,
FT ritonavir and saquinavir; when associated with other amino
FT acid changes)"
FT VARIANT 565
FT /note="V -> I (confers resistance to indinavir, nelfinavir,
FT ritonavir and saquinavir; when associated with other amino
FT acid changes)"
FT VARIANT 570
FT /note="V -> A (confers resistance to A-77003, indinavir,
FT lopinavir, nelfinavir, ritonavir and saquinavir; when
FT associated with other amino acid changes)"
FT VARIANT 570
FT /note="V -> F (confers resistance to lopinavir and
FT ritonavir; when associated with other amino acid changes)"
FT VARIANT 570
FT /note="V -> I (confers resistance to A-77003 and
FT kynostatin; when associated with other amino acid changes)"
FT VARIANT 570
FT /note="V -> S (confers resistance to lopinavir and
FT ritonavir)"
FT VARIANT 570
FT /note="V -> T (confers resistance to indinavir, lopinavir,
FT ritonavir and saquinavir; when associated with other amino
FT acid changes)"
FT VARIANT 572
FT /note="I -> A (confers resistance to atazanavir, indinavir,
FT lopinavir, nelfinavir, ritonavir and saquinavir; when
FT associated with other amino acid changes)"
FT VARIANT 572
FT /note="I -> V (confers resistance to amprenavir,
FT atazanavir, indinavir, kynostatin, lopinavir, nelfinavir,
FT ritonavir, saquinavir and telinavir; when associated with
FT other amino acid changes)"
FT VARIANT 576
FT /note="N -> D (confers resistance to nelfinavir; when
FT associated with other amino acid changes)"
FT VARIANT 576
FT /note="N -> S (confers resistance to atazanavir, indinavir
FT and nelfinavir; when associated with other amino acid
FT changes)"
FT VARIANT 577
FT /note="L -> M (confers resistance to atazanavir; when
FT associated with other amino acid changes)"
FT VARIANT 578
FT /note="L -> M (confers resistance to indinavir, lopinavir,
FT nelfinavir, ritonavir and saquinavir; when associated with
FT other amino acid changes)"
FT VARIANT 579
FT /note="T -> S (confers resistance to lopinavir, ritonavir
FT and saquinavir; when associated with other amino acid
FT changes)"
FT VARIANT 581
FT /note="I -> L (confers resistance to indinavir)"
FT VARIANT 628
FT /note="M -> L (confers resistance to zidovudine; when
FT associated with other amino acid changes)"
FT VARIANT 631
FT /note="E -> A (confers resistance to lamivudine)"
FT VARIANT 631
FT /note="E -> D (confers resistance to zidovudine; when
FT associated with other amino acid changes)"
FT VARIANT 639
FT /note="P -> R (confers resistance to stavudine)"
FT VARIANT 641
FT /note="N -> D (confers resistance to stavudine)"
FT VARIANT 649
FT /note="A -> V (confers multi-NRTI resistance; when
FT associated with other amino acid changes)"
FT VARIANT 652
FT /note="K -> R (confers resistance to abacavir, adefovir,
FT didenosine, lamivudine, stavudine, tenofir and zidovuline;
FT when associated with other amino acid changes)"
FT VARIANT 654
FT /note="D -> A (confers resistance to zidovudine)"
FT VARIANT 654
FT /note="D -> E (confers multi-NRTI resistance)"
FT VARIANT 654
FT /note="D -> G (confers multi-NRTI resistance)"
FT VARIANT 654
FT /note="D -> N (confers resistance to zidovudine)"
FT VARIANT 654
FT /note="D -> S (confers multi-NRTI resistance)"
FT VARIANT 655
FT /note="S -> G (confers multi-NRTI resistance; when
FT associated with other amino acid changes)"
FT VARIANT 655
FT /note="S -> N (confers multi-NRTI resistance)"
FT VARIANT 655
FT /note="S -> Y (confers multi-NRTI resistance)"
FT VARIANT 656
FT /note="T -> A (confers resistance to lamivudine and
FT stavudine)"
FT VARIANT 656
FT /note="T -> D (confers resistance to lamivudine, stavudine
FT and rarely to zalcitabine)"
FT VARIANT 656
FT /note="T -> G (confers resistance to didanosine,
FT zalcitabine and zidovudine)"
FT VARIANT 656
FT /note="T -> N (confers resistance to lamivudine and
FT stavudine)"
FT VARIANT 657
FT /note="K -> E (confers resistance to adefovir and
FT lamivudine)"
FT VARIANT 657
FT /note="K -> R (confers resistance to zidovudine; when
FT associated with other amino acid changes)"
FT VARIANT 657
FT /note="K -> S (confers resistance to didanosine and
FT stavudine)"
FT VARIANT 661
FT /note="L -> I (confers resistance to HBY 097)"
FT VARIANT 661
FT /note="L -> V (confers resistance to abacavir, didanosine,
FT HBY 097 and zalcitabine; when associated with other amino
FT acid changes)"
FT VARIANT 662
FT /note="V -> I (confers multi-NRTI resistance; when
FT associated with other amino acid changes)"
FT VARIANT 662
FT /note="V -> L (confers resistance to HBY 097)"
FT VARIANT 662
FT /note="V -> M (confers resistance to stavudine and
FT zalcitabine)"
FT VARIANT 662
FT /note="V -> T (confers resistance to d4C, didanosine,
FT stavudine and zalcitabine)"
FT VARIANT 664
FT /note="F -> L (confers multi-NRTI resistance; when
FT associated with other amino acid changes)"
FT VARIANT 675
FT /note="W -> G (confers resistance to pyrophosphate analog
FT PFA)"
FT VARIANT 675
FT /note="W -> S (confers resistance to pyrophosphate analog
FT PFA)"
FT VARIANT 676
FT /note="E -> G (confers resistance to pyrophosphate analog
FT PFA)"
FT VARIANT 676
FT /note="E -> K (confers resistance to pyrophosphate analog
FT PFA)"
FT VARIANT 679
FT /note="L -> I (confers resistance to pyrophosphate analog
FT PFA)"
FT VARIANT 687
FT /note="L -> I (confers resistance to nevirapine and
FT efavirenz)"
FT VARIANT 688
FT /note="K -> E (confers resistance to atevirdine, efavirenz,
FT nevirapine and zidovudine)"
FT VARIANT 688
FT /note="K -> P (confers resistance to TMC125; when
FT associated with E-142)"
FT VARIANT 688
FT /note="K -> Q (confers resistance to efavirenz; when
FT associated with I-19)"
FT VARIANT 690
FT /note="K -> E (confers resistance to atevirdine; when
FT associated with other amino acid changes)"
FT VARIANT 690
FT /note="K -> N (confers resistance to atevirdine, efavirenz,
FT emivirine and nevirapine; when associated with other amino
FT acid changes)"
FT VARIANT 690
FT /note="K -> R (confers resistance to emivirine and
FT trovirdine; when associated with other D-179 and C-181)"
FT VARIANT 693
FT /note="V -> A (confers resistance to nevirapine)"
FT VARIANT 693
FT /note="V -> I (confers resistance to HBY 097)"
FT VARIANT 693
FT /note="V -> M (confers resistance to delavirdine, efavirenz
FT and nevirapine)"
FT VARIANT 695
FT /note="V -> I (confers resistance to efavirenz, emivirine,
FT nevirapine and trovirdine; when associated with other amino
FT acid changes)"
FT VARIANT 702
FT /note="Y -> F (confers resistance to abacavir; when
FT associated with other amino acid changes)"
FT VARIANT 703
FT /note="F -> Y (confers multi-NRTI resistance; when
FT associated with other amino acid changes)"
FT VARIANT 705
FT /note="V -> I (confers resistance to zidovudine; when
FT associated with other amino acid changes)"
FT VARIANT 706
FT /note="P -> S (confers resistance to lodenosine)"
FT VARIANT 722
FT /note="I -> L (confers resistance to delavirdine, efavirenz
FT and nevirapine; when associated with I-239)"
FT VARIANT 722
FT /note="I -> M (confers resistance to delavirdine, efavirenz
FT and nevirapine; when associated with I-239)"
FT VARIANT 722
FT /note="I -> T (confers resistance to delavirdine, efavirenz
FT and nevirapine; when associated with I-239)"
FT VARIANT 725
FT /note="E -> K (confers resistance to emivirine)"
FT VARIANT 732
FT /note="Q -> M (confers both multi-NRTI and multi-NNRTI
FT resistance)"
FT VARIANT 738
FT /note="Q -> M (confers multi-NRTI resistance; when
FT associated with other amino acid changes)"
FT VARIANT 743
FT /note="S -> A (confers resistance to pyrophosphate analog
FT PFA)"
FT VARIANT 744
FT /note="P -> S (confers resistance to lamivudine)"
FT VARIANT 748
FT /note="Q -> L (confers resistance to pyrophosphate analog
FT PFA)"
FT VARIANT 766
FT /note="V -> D (confers resistance to efavirenz, tivirapine
FT and trovirdine; when associated with other amino acid
FT changes)"
FT VARIANT 768
FT /note="Y -> C (confers multi-NNRTI resistance)"
FT VARIANT 771
FT /note="M -> I (confers resistance to lamivudine and
FT emtricitabine)"
FT VARIANT 771
FT /note="M -> T (confers resistance to abacavir, didanosine,
FT emtricitabine, lamivudine and zalcitabine)"
FT VARIANT 771
FT /note="M -> V (confers resistance to lamivudine)"
FT VARIANT 775
FT /note="Y -> C (confers resistance to nevirapine)"
FT VARIANT 775
FT /note="Y -> H (confers resistance to atevirdine, efavirenz,
FT loviride and zidovudine)"
FT VARIANT 775
FT /note="Y -> L (confers resistance to efavirenz)"
FT VARIANT 776
FT /note="V -> I (confers resistance to HBY 097)"
FT VARIANT 777
FT /note="G -> A (confers resistance to efavirenz and
FT nevirapine)"
FT VARIANT 777
FT /note="G -> C (confers resistance to efavirenz and
FT nevirapine)"
FT VARIANT 777
FT /note="G -> E (confers resistance to efavirenz, nevirapine
FT and quinoxaline)"
FT VARIANT 777
FT /note="G -> Q (confers resistance to efavirenz, HBY 097 and
FT nevirapine)"
FT VARIANT 777
FT /note="G -> S (confers resistance to efavirenz and
FT nevirapine)"
FT VARIANT 777
FT /note="G -> T (confers resistance to efavirenz, HBY 097 and
FT nevirapine)"
FT VARIANT 777
FT /note="G -> V (confers resistance to efavirenz and
FT nevirapine)"
FT VARIANT 795
FT /note="H -> Y (confers resistance to lamivudine,
FT pyrophosphate analog PFA and zidovudine)"
FT VARIANT 797
FT /note="L -> W (confers resistance to zidovudine)"
FT VARIANT 798
FT /note="R -> K (confers resistance to lamivudine and
FT zidovudine)"
FT VARIANT 801
FT /note="L -> F (confers resistance to ph-AZT and
FT zidovudine)"
FT VARIANT 802
FT /note="T -> F (confers resistance to zidovudine; when
FT associated with other amino acid changes)"
FT VARIANT 802
FT /note="T -> Y (confers resistance to zidovudine; when
FT associated with other amino acid changes)"
FT VARIANT 806
FT /note="K -> E (confers resistance to zidovudine)"
FT VARIANT 806
FT /note="K -> Q (confers resistance to zidovudine; when
FT associated with other amino acid changes)"
FT VARIANT 806
FT /note="K -> R (confers resistance to lamivudine, stavudine,
FT zalcicabine and zidovudine)"
FT VARIANT 812
FT /note="P -> H (confers resistance to efavirenz, emivirine,
FT HBY 097 and quinoxaline; when associated with A-17)"
FT VARIANT 823
FT /note="P -> L (confers resistance to atevirdine and
FT delavirdine)"
FT VARIANT 825
FT /note="K -> T (confers resistance to atevirdine and
FT zidovudine; when associated with other amino acid changes)"
FT VARIANT 870
FT /note="L -> I (confers resistance to delavirdine, efavirenz
FT and nevirapine)"
FT VARIANT 905
FT /note="Y -> F (confers resistance to delavirdine and
FT nevirapine)"
FT VARIANT 920
FT /note="G -> D (confers resistance to abacavir, lamivudine
FT and zidovudine)"
FT VARIANT 920
FT /note="G -> E (confers resistance to abacavir, lamivudine
FT and zidovudine)"
FT VARIANT 973
FT /note="T -> I (confers resistance to abacavir, lamivudine
FT and zidovudine)"
FT MUTAGEN 6
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 9
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 18
FT /note="K->A: Replication-defective, induces nuclear
FT mislocalization of matrix protein; when associated with G-
FT 22."
FT /evidence="ECO:0000269|PubMed:10604476"
FT MUTAGEN 22
FT /note="R->G: Replication-defective, induces nuclear
FT mislocalization of matrix protein; when associated with A-
FT 18."
FT /evidence="ECO:0000269|PubMed:10604476"
FT MUTAGEN 27
FT /note="K->A: No effect on subcellular localization of
FT matrix protein; when associated with A-18 and G-22."
FT /evidence="ECO:0000269|PubMed:10604476"
FT MUTAGEN 67
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 72
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 217
FT /note="P->A: 3-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 218
FT /note="V->A: 2.7-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 219
FT /note="H->A,Q: 8-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 220
FT /note="A->G: 44-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 220
FT /note="A->V: 3.4-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 221
FT /note="G->A: 31-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 221
FT /note="G->V: 154-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 222
FT /note="P->A: 36-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 222
FT /note="P->V: More than 150-fold decrease of PPIA-binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 223
FT /note="I->A: 1.2-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 223
FT /note="I->V: 1.0-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 224
FT /note="A->G: 2.3-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 224
FT /note="A->V: 1.7-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 225
FT /note="P->A: 1.6-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 394
FT /note="N->F,G: Decreases infectivity and replication."
FT /evidence="ECO:0000269|PubMed:16904152"
FT MUTAGEN 400
FT /note="H->C: Complete loss of infectivity and in vitro
FT chaperone activity."
FT /evidence="ECO:0000269|PubMed:11932404"
FT MUTAGEN 405
FT /note="C->H: Complete loss of infectivity and DNA
FT synthesis."
FT /evidence="ECO:0000269|PubMed:11932404"
FT MUTAGEN 421
FT /note="H->C: Partial loss of infectivity. Complete loss of
FT in vitro chaperone activity."
FT /evidence="ECO:0000269|PubMed:11932404"
FT MUTAGEN 426
FT /note="C->H: Partial loss of infectivity."
FT /evidence="ECO:0000269|PubMed:11932404"
FT MUTAGEN 488..490
FT /note="FPQ->IPK: Complete loss of RT p66/p51 cleavage."
FT /evidence="ECO:0000269|PubMed:15183348"
FT MUTAGEN 513
FT /note="D->H: Abolished protease activity."
FT /evidence="ECO:0000269|PubMed:33542150"
FT MUTAGEN 821
FT /note="L->A: Complete loss of RT dimerization."
FT /evidence="ECO:0000269|PubMed:15183348"
FT MUTAGEN 1065
FT /note="E->Q: Complete loss of RNase H activity."
FT /evidence="ECO:0000269|PubMed:12206668"
FT MUTAGEN 1136
FT /note="D->N: Complete loss of RNase H activity."
FT /evidence="ECO:0000269|PubMed:12206668"
FT MUTAGEN 1159
FT /note="H->C: No effect on integrase activity in vitro."
FT /evidence="ECO:0000269|PubMed:8420982"
FT MUTAGEN 1163
FT /note="H->C,V: 75% increase of integrase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:8420982"
FT MUTAGEN 1187
FT /note="C->A: Complete loss of integrase activity in vivo."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1190
FT /note="C->A: Complete loss of integrase activity in vivo."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1200
FT /note="Q->C: 75% increase of integrase activity in vitro."
FT /evidence="ECO:0000269|PubMed:8420982"
FT MUTAGEN 1208
FT /note="W->A: Complete loss of integrase activity in vivo."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1211
FT /note="D->A,V: Complete loss of integrase activity in vivo
FT and in vitro."
FT /evidence="ECO:0000269|PubMed:8035478,
FT ECO:0000269|PubMed:8420982, ECO:0000269|PubMed:9573231"
FT MUTAGEN 1213
FT /note="T->A: No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1222
FT /note="V->P: Complete loss of integrase activity."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1228
FT /note="S->A: Complete loss of integrase activity in vivo."
FT /evidence="ECO:0000269|PubMed:8035478,
FT ECO:0000269|PubMed:8420982"
FT MUTAGEN 1228
FT /note="S->R: No effect on integrase activity in vitro."
FT /evidence="ECO:0000269|PubMed:8035478,
FT ECO:0000269|PubMed:8420982"
FT MUTAGEN 1262
FT /note="T->A: No effect infectivity."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1263
FT /note="D->A,I: Complete loss of integrase activity in vivo
FT and in vitro."
FT /evidence="ECO:0000269|PubMed:8035478,
FT ECO:0000269|PubMed:8420982, ECO:0000269|PubMed:9573231"
FT MUTAGEN 1270
FT /note="G->A: No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1282
FT /note="I->P: Complete loss of integrase activity in vivo."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1298
FT /note="V->A: No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1299
FT /note="E->G,P: Complete loss of integrase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:8035478,
FT ECO:0000269|PubMed:8420982, ECO:0000269|PubMed:9573231"
FT MUTAGEN 1306
FT /note="K->P: Slow down virus replication."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1326
FT /note="A->P: Complete loss of integrase activity in vivo."
FT /evidence="ECO:0000269|PubMed:8035478"
FT MUTAGEN 1346
FT /note="R->C: 75% increase of integrase activity in vitro."
FT /evidence="ECO:0000269|PubMed:8420982"
FT MUTAGEN 1382
FT /note="W->A: Complete loss of infectivity. No effect on
FT integrase activity in vitro."
FT /evidence="ECO:0000269|PubMed:8035478,
FT ECO:0000269|PubMed:8420982"
FT MUTAGEN 1382
FT /note="W->E: 75% increase of integrase activity in vitro."
FT /evidence="ECO:0000269|PubMed:8035478,
FT ECO:0000269|PubMed:8420982"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1TAM"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:1TAM"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1TAM"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1TAM"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:1TAM"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1TAM"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1TAM"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:1TAM"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1TAM"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:1TAM"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1TAM"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1TAM"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1TAM"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:6VPZ"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:2KOD"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:2KOD"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:2KOD"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:2KOD"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:2KOD"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:2KOD"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:2KOD"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1ESK"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1ESK"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:1ESK"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:1ESK"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:1HVR"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 530..537
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 540..554
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 557..566
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:1ODW"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:6DV4"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:6DV4"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:4Q5M"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:2RF2"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:2WHH"
FT STRAND 613..618
FT /evidence="ECO:0007829|PDB:3KT2"
FT HELIX 625..629
FT /evidence="ECO:0007829|PDB:3KJV"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:1VRU"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:2RF2"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:3QIP"
FT TURN 653..656
FT /evidence="ECO:0007829|PDB:3LAK"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 665..670
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:3QIP"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 691..697
FT /evidence="ECO:0007829|PDB:3QIP"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:1EP4"
FT HELIX 709..715
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:1VRU"
FT STRAND 729..735
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 743..761
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 762..765
FT /evidence="ECO:0007829|PDB:1C0T"
FT STRAND 766..770
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 773..778
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 782..798
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 806..808
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 812..816
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 819..821
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 823..825
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:1RTH"
FT HELIX 841..854
FT /evidence="ECO:0007829|PDB:3QIP"
FT TURN 855..857
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 858..860
FT /evidence="ECO:0007829|PDB:1JLG"
FT HELIX 864..869
FT /evidence="ECO:0007829|PDB:3QIP"
FT TURN 870..872
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 876..879
FT /evidence="ECO:0007829|PDB:2YNI"
FT HELIX 884..896
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 902..904
FT /evidence="ECO:0007829|PDB:1JLG"
FT STRAND 908..910
FT /evidence="ECO:0007829|PDB:6P1X"
FT STRAND 913..918
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 920..922
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 924..931
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 935..941
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 945..949
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 951..970
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 975..980
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 982..991
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 992..995
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 1000..1003
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 1008..1013
FT /evidence="ECO:0007829|PDB:3QIP"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:1RT2"
FT STRAND 1025..1033
FT /evidence="ECO:0007829|PDB:3QIO"
FT TURN 1035..1037
FT /evidence="ECO:0007829|PDB:3QIO"
FT STRAND 1040..1046
FT /evidence="ECO:0007829|PDB:3QIO"
FT STRAND 1047..1049
FT /evidence="ECO:0007829|PDB:3DRP"
FT STRAND 1051..1058
FT /evidence="ECO:0007829|PDB:3QIO"
FT HELIX 1061..1075
FT /evidence="ECO:0007829|PDB:3QIO"
FT STRAND 1078..1085
FT /evidence="ECO:0007829|PDB:3QIO"
FT HELIX 1087..1093
FT /evidence="ECO:0007829|PDB:3QIO"
FT STRAND 1098..1102
FT /evidence="ECO:0007829|PDB:3QIP"
FT HELIX 1105..1112
FT /evidence="ECO:0007829|PDB:3QIO"
FT STRAND 1116..1122
FT /evidence="ECO:0007829|PDB:3QIO"
FT STRAND 1125..1127
FT /evidence="ECO:0007829|PDB:3LP1"
FT HELIX 1130..1140
FT /evidence="ECO:0007829|PDB:3QIO"
FT TURN 1141..1143
FT /evidence="ECO:0007829|PDB:3QIO"
FT HELIX 1204..1206
FT /evidence="ECO:0007829|PDB:1EXQ"
FT STRAND 1207..1215
FT /evidence="ECO:0007829|PDB:1EXQ"
FT STRAND 1218..1225
FT /evidence="ECO:0007829|PDB:1EXQ"
FT TURN 1226..1228
FT /evidence="ECO:0007829|PDB:1EXQ"
FT STRAND 1231..1240
FT /evidence="ECO:0007829|PDB:1EXQ"
FT HELIX 1241..1254
FT /evidence="ECO:0007829|PDB:1EXQ"
FT STRAND 1259..1261
FT /evidence="ECO:0007829|PDB:1EXQ"
FT HELIX 1266..1268
FT /evidence="ECO:0007829|PDB:1EXQ"
FT HELIX 1271..1280
FT /evidence="ECO:0007829|PDB:1EXQ"
FT STRAND 1283..1285
FT /evidence="ECO:0007829|PDB:6EX9"
FT HELIX 1292..1294
FT /evidence="ECO:0007829|PDB:5HRN"
FT HELIX 1302..1312
FT /evidence="ECO:0007829|PDB:1EXQ"
FT HELIX 1313..1315
FT /evidence="ECO:0007829|PDB:1EXQ"
FT HELIX 1319..1332
FT /evidence="ECO:0007829|PDB:1EXQ"
FT STRAND 1335..1339
FT /evidence="ECO:0007829|PDB:1EXQ"
FT HELIX 1343..1355
FT /evidence="ECO:0007829|PDB:1EXQ"
FT HELIX 1358..1368
FT /evidence="ECO:0007829|PDB:1EX4"
FT STRAND 1371..1375
FT /evidence="ECO:0007829|PDB:5TC2"
FT STRAND 1377..1380
FT /evidence="ECO:0007829|PDB:5TC2"
FT STRAND 1382..1392
FT /evidence="ECO:0007829|PDB:5TC2"
FT STRAND 1395..1400
FT /evidence="ECO:0007829|PDB:5TC2"
FT STRAND 1403..1408
FT /evidence="ECO:0007829|PDB:5TC2"
FT HELIX 1409..1411
FT /evidence="ECO:0007829|PDB:5TC2"
FT STRAND 1412..1415
FT /evidence="ECO:0007829|PDB:5TC2"
SQ SEQUENCE 1435 AA; 162042 MW; 8487B36BDEAC5FE4 CRC64;
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA
DTGHSNQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA
RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH TARNCRAPRK KGCWKCGKEG
HQMKDCTERQ ANFLREDLAF LQGKAREFSS EQTRANSPTR RELQVWGRDN NSPSEAGADR
QGTVSFNFPQ VTLWQRPLVT IKIGGQLKEA LLDTGADDTV LEEMSLPGRW KPKMIGGIGG
FIKVRQYDQI LIEICGHKAI GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK
PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI KKKDSTKWRK
LVDFRELNKR TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD AYFSVPLDED FRKYTAFTIP
SINNETPGIR YQYNVLPQGW KGSPAIFQSS MTKILEPFRK QNPDIVIYQY MDDLYVGSDL
EIGQHRTKIE ELRQHLLRWG LTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT
VNDIQKLVGK LNWASQIYPG IKVRQLCKLL RGTKALTEVI PLTEEAELEL AENREILKEP
VHGVYYDPSK DLIAEIQKQG QGQWTYQIYQ EPFKNLKTGK YARMRGAHTN DVKQLTEAVQ
KITTESIVIW GKTPKFKLPI QKETWETWWT EYWQATWIPE WEFVNTPPLV KLWYQLEKEP
IVGAETFYVD GAANRETKLG KAGYVTNRGR QKVVTLTDTT NQKTELQAIY LALQDSGLEV
NIVTDSQYAL GIIQAQPDQS ESELVNQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDKLVS
AGIRKVLFLD GIDKAQDEHE KYHSNWRAMA SDFNLPPVVA KEIVASCDKC QLKGEAMHGQ
VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK LAGRWPVKTI
HTDNGSNFTG ATVRAACWWA GIKQEFGIPY NPQSQGVVES MNKELKKIIG QVRDQAEHLK
TAVQMAVFIH NFKRKGGIGG YSAGERIVDI IATDIQTKEL QKQITKIQNF RVYYRDSRNP
LWKGPAKLLW KGEGAVVIQD NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED
