POL_HV1B1
ID POL_HV1B1 Reviewed; 1447 AA.
AC P03366; P03368;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 252.
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;
DE AltName: Full=PR;
DE AltName: Full=Retropepsin;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE EC=2.7.7.49 {ECO:0000269|PubMed:2476069};
DE EC=2.7.7.7 {ECO:0000269|PubMed:2476069};
DE EC=3.1.26.13 {ECO:0000269|PubMed:2476069};
DE AltName: Full=Exoribonuclease H;
DE EC=3.1.13.2;
DE AltName: Full=p66 RT;
DE Contains:
DE RecName: Full=p51 RT;
DE Contains:
DE RecName: Full=p15;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
GN Name=gag-pol;
OS Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11678;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2578615; DOI=10.1038/313277a0;
RA Ratner L., Haseltine W.A., Patarca R., Livak K.J., Starcich B.R.,
RA Josephs S.F., Doran E.R., Rafalski J.A., Whitehorn E.A., Baumeister K.,
RA Ivanoff L., Petteway S.R. Jr., Pearson M.L., Lautenberger J.A., Papas T.S.,
RA Ghrayeb J., Chang N.T., Gallo R.C., Wong-Staal F.;
RT "Complete nucleotide sequence of the AIDS virus, HTLV-III.";
RL Nature 313:277-284(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate PV22;
RX PubMed=2982104; DOI=10.1038/313450a0;
RA Muesing M.A., Smith D.H., Cabradilla C.D., Benton C.V., Lasky L.A.,
RA Capon D.J.;
RT "Nucleic acid structure and expression of the human AIDS/lymphadenopathy
RT retrovirus.";
RL Nature 313:450-458(1985).
RN [3]
RP SEQUENCE REVISION.
RA Muesing M.A.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 600-607, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF
RP 600-1159, CATALYTIC ACTIVITY (REVERSE TRANSCRIPTASE/RIBONUCLEASE H), AND
RP PROTEOLYTIC CLEAVAGE (GAG-POL POLYPROTEIN).
RX PubMed=2476069; DOI=10.1016/0003-9861(89)90493-1;
RA Mizrahi V., Lazarus G.M., Miles L.M., Meyers C.A., Debouck C.;
RT "Recombinant HIV-1 reverse transcriptase: purification, primary structure,
RT and polymerase/ribonuclease H activities.";
RL Arch. Biochem. Biophys. 273:347-358(1989).
RN [5]
RP CHARACTERIZATION OF RNASE H.
RX PubMed=1722202; DOI=10.1016/s0021-9258(18)54227-7;
RA DeStefano J.J., Buiser R.G., Mallaber L.M., Bambara R.A., Fay P.J.;
RT "Human immunodeficiency virus reverse transcriptase displays a partially
RT processive 3' to 5' endonuclease activity.";
RL J. Biol. Chem. 266:24295-24301(1991).
RN [6]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF PHE-1039 AND
RP LEU-1159.
RX PubMed=2044756; DOI=10.1016/0014-5793(91)80583-o;
RA Jupp R.A., Phylip L.H., Mills J.S., Le Grice S.F.J., Kay J.;
RT "Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol
RT polyprotein. Effects on hydrolysis by HIV-1 proteinase.";
RL FEBS Lett. 283:180-184(1991).
RN [7]
RP MUTAGENESIS OF HIS-1138.
RX PubMed=1714505; DOI=10.1016/0022-2836(91)90119-q;
RA Wohrl B.M., Volkmann S., Moelling K.;
RT "Mutations of a conserved residue within HIV-1 ribonuclease H affect its
RT exo- and endonuclease activities.";
RL J. Mol. Biol. 220:801-818(1991).
RN [8]
RP ACTIVE SITES OF REVERSE TRANSCRIPTASE, AND MUTAGENESIS OF ASP-709; ASP-784
RP AND ASP-785.
RX PubMed=8794733; DOI=10.1021/bi960364x;
RA Kaushik N., Rege N., Yadav P.N.S., Sarafianos S.G., Modak M.J.,
RA Pandey V.N.;
RT "Biochemical analysis of catalytically crucial aspartate mutants of human
RT immunodeficiency virus type 1 reverse transcriptase.";
RL Biochemistry 35:11536-11546(1996).
RN [9]
RP MUTAGENESIS OF GLU-823; PRO-824; PRO-825; PHE-826; LEU-827; TRP-828;
RP MET-829; GLY-830; TYR-831; GLU-832 AND HIS-834.
RX PubMed=9111014; DOI=10.1074/jbc.272.17.11157;
RA Palaniappan C., Wisniewski M., Jacques P.S., Le Grice S.F., Fay P.J.,
RA Bambara R.A.;
RT "Mutations within the primer grip region of HIV-1 reverse transcriptase
RT result in loss of RNase H function.";
RL J. Biol. Chem. 272:11157-11164(1997).
RN [10]
RP MUTAGENESIS OF PRO-651; PRO-654; LEU-673; SER-755; PRO-756; MET-783;
RP ILE-856; GLY-861; LEU-863; TRP-865; LEU-878; ALA-898; LEU-902; LEU-909 AND
RP GLU-1077.
RX PubMed=9533880; DOI=10.1006/jmbi.1998.1624;
RA Gao H.-Q., Boyer P.L., Arnold E., Hughes S.H.;
RT "Effects of mutations in the polymerase domain on the polymerase, RNase H
RT and strand transfer activities of human immunodeficiency virus type 1
RT reverse transcriptase.";
RL J. Mol. Biol. 277:559-572(1998).
RN [11]
RP MUTAGENESIS OF TYR-782; MET-783; ASP-784 AND ASP-785.
RX PubMed=9657675; DOI=10.1021/bi980549z;
RA Harris D., Yadav P.N.S., Pandey V.N.;
RT "Loss of polymerase activity due to Tyr to Phe substitution in the YMDD
RT motif of human immunodeficiency virus type-1 reverse transcriptase is
RT compensated by Met to Val substitution within the same motif.";
RL Biochemistry 37:9630-9640(1998).
RN [12]
RP FUNCTION OF RNASE H.
RX PubMed=9658129; DOI=10.1128/jvi.72.8.6805-6812.1998;
RA Smith C.M., Leon O., Smith J.S., Roth M.J.;
RT "Sequence requirements for removal of tRNA by an isolated human
RT immunodeficiency virus type 1 RNase H domain.";
RL J. Virol. 72:6805-6812(1998).
RN [13]
RP MUTAGENESIS OF LYS-664.
RX PubMed=10794716; DOI=10.1042/bj3480077;
RA Sluis-Cremer N., Arion D., Kaushik N., Lim H., Parniak M.A.;
RT "Mutational analysis of Lys65 of HIV-1 reverse transcriptase.";
RL Biochem. J. 348:77-82(2000).
RN [14]
RP CHARACTERIZATION OF RNASE H.
RX PubMed=11035788; DOI=10.1073/pnas.210392297;
RA Wisniewski M., Balakrishnan M., Palaniappan C., Fay P.J., Bambara R.A.;
RT "Unique progressive cleavage mechanism of HIV reverse transcriptase RNase
RT H.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11978-11983(2000).
RN [15]
RP RIBOSOMAL FRAMESHIFT, PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND
RP MUTAGENESIS OF PHE-440 AND PHE-500.
RX PubMed=11172099; DOI=10.1099/0022-1317-82-3-581;
RA Chen N., Morag A., Almog N., Blumenzweig I., Dreazin O., Kotler M.;
RT "Extended nucleocapsid protein is cleaved from the Gag-Pol precursor of
RT human immunodeficiency virus type 1.";
RL J. Gen. Virol. 82:581-590(2001).
RN [16]
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 [17]
RP ACTIVE SITE OF PROTEASE.
RX PubMed=12924029;
RA Koval'skii D.B., Kanibolotskii D.S., Dubina V.N., Korneliuk A.I.;
RT "Conformational changes in HIV-1 proteinase: effect of protonation of the
RT active center on conformation of HIV-1 proteinase in water.";
RL Ukr. Biokhim. Zh. 74:135-138(2002).
RN [18]
RP MUTAGENESIS OF TRP-752; ILE-766; LEU-786 AND VAL-788.
RX PubMed=12501197; DOI=10.1021/bi026311z;
RA Sharma B., Kaushik N., Singh K., Kumar S., Pandey V.N.;
RT "Substitution of conserved hydrophobic residues in motifs B and C of HIV-1
RT RT alters the geometry of its catalytic pocket.";
RL Biochemistry 41:15685-15697(2002).
RN [19]
RP MUTAGENESIS OF TYR-1100.
RX PubMed=11684697; DOI=10.1074/jbc.m110254200;
RA Arion D., Sluis-Cremer N., Min K.-L., Abram M.E., Fletcher R.S.,
RA Parniak M.A.;
RT "Mutational analysis of Tyr-501 of HIV-1 reverse transcriptase. Effects on
RT ribonuclease H activity and inhibition of this activity by N-
RT acylhydrazones.";
RL J. Biol. Chem. 277:1370-1374(2002).
RN [20]
RP DOMAIN TRYPTOPHAN REPEAT MOTIF, AND MUTAGENESIS OF TRP-997; TRP-1000;
RP TRP-1001; TYR-1004; TRP-1005; TRP-1009 AND TRP-1013.
RX PubMed=12559908; DOI=10.1016/s0022-2836(02)01433-x;
RA Tachedjian G., Aronson H.-E., de los Santos M., Seehra J., McCoy J.M.,
RA Goff S.P.;
RT "Role of residues in the tryptophan repeat motif for HIV-1 reverse
RT transcriptase dimerization.";
RL J. Mol. Biol. 326:381-396(2003).
RN [21]
RP CHARACTERIZATION OF RNASE H.
RX PubMed=15533434; DOI=10.1016/j.jmb.2004.09.081;
RA Schultz S.J., Zhang M., Champoux J.J.;
RT "Recognition of internal cleavage sites by retroviral RNases H.";
RL J. Mol. Biol. 344:635-652(2004).
RN [22]
RP CHARACTERIZATION OF REVERSE TRANSCRIPTASE, AND MUTAGENESIS OF TRP-1000.
RX PubMed=15852304; DOI=10.1002/prot.20480;
RA Tachedjian G., Radzio J., Sluis-Cremer N.;
RT "Relationship between enzyme activity and dimeric structure of recombinant
RT HIV-1 reverse transcriptase.";
RL Proteins 60:5-13(2005).
RN [23]
RP CHARACTERIZATION OF RNASE H.
RX PubMed=16141194; DOI=10.1093/nar/gki779;
RA Mulder B.A., Anaya S., Yu P., Lee K.W., Nguyen A., Murphy J., Willson R.,
RA Briggs J.M., Gao X., Hardin S.H.;
RT "Nucleotide modification at the gamma-phosphate leads to the improved
RT fidelity of HIV-1 reverse transcriptase.";
RL Nucleic Acids Res. 33:4865-4873(2005).
RN [24]
RP MUTAGENESIS OF ALA-1036; GLU-1037; THR-1038; PHE-1039; TYR-1040 AND
RP VAL-1041.
RX PubMed=16140771; DOI=10.1128/jvi.79.18.11952-11961.2005;
RA Abram M.E., Parniak M.A.;
RT "Virion instability of human immunodeficiency virus type 1 reverse
RT transcriptase (RT) mutated in the protease cleavage site between RT p51 and
RT the RT RNase H domain.";
RL J. Virol. 79:11952-11961(2005).
RN [25]
RP METHYLATION AT ARG-387 AND ARG-409 BY HUMAN PRMT6, AND INTERACTION WITH
RP HUMAN PRMT6.
RX PubMed=17415034; DOI=10.1097/qad.0b013e32803277ae;
RA Invernizzi C.F., Xie B., Frankel F.A., Feldhammer M., Roy B.B., Richard S.,
RA Wainberg M.A.;
RT "Arginine methylation of the HIV-1 nucleocapsid protein results in its
RT diminished function.";
RL AIDS 21:795-805(2007).
RN [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
RP 3D-STRUCTURE MODELING OF PROTEASE DOMAIN.
RX PubMed=2537531; DOI=10.1126/science.2537531;
RA Weber I.T., Miller M., Jaskolski M., Leis J., Skalka A.M., Wlodawer A.;
RT "Molecular modeling of the HIV-1 protease and its substrate binding site.";
RL Science 243:928-931(1989).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 501-599 IN COMPLEX WITH A C2
RP SYMMETRIC INHIBITOR.
RX PubMed=2200122; DOI=10.1126/science.2200122;
RA Erickson J., Neidhart D.J., Vandrie J., Kempf D.J., Wang X.C.,
RA Norbeck D.W., Plattner J.J., Rittenhouse J.W., Turon M., Wideburg N.E.,
RA Kohlbrenner W.E., Simmer R., Helfrich R., Paul D.A., Knigge M.;
RT "Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor
RT complexed to HIV-1 protease.";
RL Science 249:527-533(1990).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1026-1161.
RX PubMed=1707186; DOI=10.1126/science.1707186;
RA Davies J.F. II, Hostomska Z., Hostomsky Z., Jordan S.R., Matthews D.A.;
RT "Crystal structure of the ribonuclease H domain of HIV-1 reverse
RT transcriptase.";
RL Science 252:88-95(1991).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1026-1159.
RX PubMed=1718968; DOI=10.1016/s0021-9258(18)54747-5;
RA Evans D.B., Brawn K., Deibel M.R. Jr., Tarpley W.G., Sharma S.K.;
RT "A recombinant ribonuclease H domain of HIV-1 reverse transcriptase that is
RT enzymatically active.";
RL J. Biol. Chem. 266:20583-20585(1991).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1026-1161.
RX PubMed=1713588; DOI=10.1016/s0021-9258(18)98742-9;
RA Hostomska Z., Matthews D.A., Davies J.F. II, Nodes B.R., Hostomsky Z.;
RT "Proteolytic release and crystallization of the RNase H domain of human
RT immunodeficiency virus type 1 reverse transcriptase.";
RL J. Biol. Chem. 266:14697-14702(1991).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 600-1155 IN COMPLEX WITH AN
RP INHIBITOR.
RX PubMed=1377403; DOI=10.1126/science.1377403;
RA Kohlstaedt L.A., Wang J., Friedman J.M., Rice P.A., Steitz T.A.;
RT "Crystal structure at 3.5-A resolution of HIV-1 reverse transcriptase
RT complexed with an inhibitor.";
RL Science 256:1783-1790(1992).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1157.
RX PubMed=1374166; DOI=10.1038/357085a0;
RA Arnold E., Jacobo-Molina A., Nanni R.G., Williams R.L., Lu X., Ding J.,
RA Clark A.D. Jr., Zhang A., Ferris A.L., Clark P., Hizi A., Hughes S.H.;
RT "Structure of HIV-1 reverse transcriptase/DNA complex at 7 A resolution
RT showing active site locations.";
RL Nature 357:85-89(1992).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 501-599.
RX PubMed=8230097; DOI=10.1021/jm00073a010;
RA Wonacott A., Cooke R., Hayes F.R., Hann M.M., Jhoti H., McMeekin P.,
RA Mistry A., Murray-Rust P., Singh O.M., Weir M.P.;
RT "A series of penicillin-derived C2-symmetric inhibitors of HIV-1
RT proteinase: structural and modeling studies.";
RL J. Med. Chem. 36:3113-3119(1993).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH A NOVEL
RP GAMMA-TURN MIMETIC INHIBITOR.
RX PubMed=8360876; DOI=10.1021/jm00068a008;
RA Newlander K.A., Callahan J.F., Moore M.L., Tomaszek T.A. Jr., Huffman W.F.;
RT "A novel constrained reduced-amide inhibitor of HIV-1 protease derived from
RT the sequential incorporation of gamma-turn mimetics into a model
RT substrate.";
RL J. Med. Chem. 36:2321-2331(1993).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1155, AND SUBUNIT (REVERSE
RP TRANSCRIPTASE/RIBONUCLEASE H).
RX PubMed=7687065; DOI=10.1073/pnas.90.13.6320;
RA Jacobo-Molina A., Ding J., Nanni R.G., Clark A.D. Jr., Lu X., Tantillo C.,
RA Williams R.L., Kamer G., Ferris A.L., Clark P., Hizi A., Hughes S.H.,
RA Arnold E.;
RT "Crystal structure of human immunodeficiency virus type 1 reverse
RT transcriptase complexed with double-stranded DNA at 3.0-A resolution shows
RT bent DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6320-6324(1993).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1159.
RX PubMed=7513427; DOI=10.1073/pnas.91.9.3911;
RA Smerdon S.J., Jager J., Wang J., Kohlstaedt L.A., Chirino A.J.,
RA Friedman J.M., Rice P.A., Steitz T.A.;
RT "Structure of the binding site for nonnucleoside inhibitors of the reverse
RT transcriptase of human immunodeficiency virus type 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3911-3915(1994).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 501-599 IN COMPLEX WITH A NOVEL
RP PSEUDOSYMMETRIC INHIBITOR.
RX PubMed=7613867; DOI=10.1016/s0969-2126(01)00169-1;
RA Priestle J.P., Fassler A., Rosel J., Tintelnot-Blomley M., Strop P.,
RA Gruetter M.G.;
RT "Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases
RT in complex with CGP 53820, a novel pseudosymmetric inhibitor.";
RL Structure 3:381-389(1995).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 600-1155 IN COMPLEX WITH A
RP NONNUCLEOSIDE INHIBITOR.
RX PubMed=7545077; DOI=10.1038/nsb0595-407;
RA Ding J., Das K., Moereels H., Koymans L., Andries K., Janssen P.A.,
RA Hughes S.H., Arnold E.;
RT "Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the
RT binding of diverse nonnucleoside inhibitors.";
RL Nat. Struct. Biol. 2:407-415(1995).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1157 IN COMPLEX WITH A
RP NON-NUCLEOSIDE INHIBITOR.
RX PubMed=7542140; DOI=10.1016/s0969-2126(01)00168-x;
RA Ding J., Das K., Tantillo C., Zhang W., Clark A.D. Jr., Jessen S., Lu X.,
RA Hsiou Y., Jacobo-Molina A., Andries K., Et A.L.;
RT "Structure of HIV-1 reverse transcriptase in a complex with the non-
RT nucleoside inhibitor alpha-APA R 95845 at 2.8-A resolution.";
RL Structure 3:365-379(1995).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 600-1159.
RX PubMed=7532306; DOI=10.1073/pnas.92.4.1222;
RA Rodgers D.W., Gamblin S.J., Harris B.A., Ray S., Culp J.S., Hellmig B.,
RA Woolf D.J., Debouck C., Harrison S.C.;
RT "The structure of unliganded reverse transcriptase from the human
RT immunodeficiency virus type 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1222-1226(1995).
RN [46]
RP STRUCTURE BY NMR OF 1379-1429.
RX PubMed=7552753; DOI=10.1038/nsb0995-807;
RA Eijkelenboom A.P.A.M., Lutzke R.A., Boelens R., Plasterk R.H.A.,
RA Kaptein R., Hard K.;
RT "The DNA-binding domain of HIV-1 integrase has an SH3-like fold.";
RL Nat. Struct. Biol. 2:807-810(1995).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE
RP PEPTIDIC INHIBITOR U-89360E.
RX PubMed=7827064; DOI=10.1021/bi00004a007;
RA Lin Y.Z., Lin X.L., Hong L., Foundling S.I., Heinrikson R.L.,
RA Thaisrivongs S., Leelamanit W., Raterman D., Shah M., Dunn B.M., Tang J.;
RT "Effect of point mutations on the kinetics and the inhibition of human
RT immunodeficiency virus type 1 protease: relationship to drug resistance.";
RL Biochemistry 34:1143-1152(1995).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 600-1155, AND SUBUNIT (REVERSE
RP TRANSCRIPTASE/RIBONUCLEASE H).
RX PubMed=8805568; DOI=10.1016/s0969-2126(96)00091-3;
RA Hsiou Y., Ding J., Das K., Clark A.D. Jr., Hughes S.H., Arnold E.;
RT "Structure of unliganded HIV-1 reverse transcriptase at 2.7-A resolution:
RT implications of conformational changes for polymerization and inhibition
RT mechanisms.";
RL Structure 4:853-860(1996).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH A
RP SULFAMIDE AND A UREA DERIVATIVE.
RX PubMed=9083478; DOI=10.1021/jm960588d;
RA Backbro K., Lowgren S., Osterlund K., Atepo J., Unge T., Hulten J.,
RA Bonham N.M., Schaal W., Karlen A., Hallberg A.;
RT "Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.";
RL J. Med. Chem. 40:898-902(1997).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 502-599 IN COMPLEX WITH A CYCLIC
RP UREA INHIBITOR.
RX PubMed=9048541; DOI=10.1021/bi962234u;
RA Ala P.J., Huston E.E., Klabe R.M., McCabe D.D., Duke J.L., Rizzo C.J.,
RA Korant B.D., DeLoskey R.J., Lam P.Y.S., Hodge C.N., Chang C.-H.;
RT "Molecular basis of HIV-1 protease drug resistance: structural analysis of
RT mutant proteases complexed with cyclic urea inhibitors.";
RL Biochemistry 36:1573-1580(1997).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE
RP PEPTIDIC INHIBITOR U-89360E.
RX PubMed=9450540; DOI=10.1016/s0014-5793(97)01477-4;
RA Hong L., Zhang X.-J., Foundling S.I., Hartsuck J.A., Tang J.;
RT "Structure of a G48H mutant of HIV-1 protease explains how glycine-48
RT replacements produce mutants resistant to inhibitor drugs.";
RL FEBS Lett. 420:11-16(1997).
RN [52]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599.
RX PubMed=9258349; DOI=10.1021/jm970195u;
RA Smith A.B. III, Hirschmann R., Pasternak A., Yao W., Sprengeler P.A.,
RA Holloway M.K., Kuo L.C., Chen Z., Darke P.L., Schleif W.A.;
RT "An orally bioavailable pyrrolinone inhibitor of HIV-1 protease:
RT computational analysis and X-ray crystal structure of the enzyme complex.";
RL J. Med. Chem. 40:2440-2444(1997).
RN [53]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH A PEPTIDIC
RP INHIBITOR.
RX PubMed=9521105; DOI=10.1002/pro.5560070209;
RA Hong L., Hartsuck J.A., Foundling S.I., Ermolieff J., Tang J.;
RT "Active-site mobility in human immunodeficiency virus, type 1, protease as
RT demonstrated by crystal structure of A28S mutant.";
RL Protein Sci. 7:300-305(1998).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 588-1027.
RX PubMed=9831551; DOI=10.1126/science.282.5394.1669;
RA Huang H., Chopra R., Verdine G.L., Harrison S.C.;
RT "Structure of a covalently trapped catalytic complex of HIV-1 reverse
RT transcriptase: implications for drug resistance.";
RL Science 282:1669-1675(1998).
RN [55]
RP X-RAY CRYSTALLOGRAPHY (4.75 ANGSTROMS) OF 600-1153 IN COMPLEX WITH AN RNA
RP PSEUDOKNOT INHIBITOR.
RX PubMed=9687519; DOI=10.1093/emboj/17.15.4535;
RA Jaeger J., Restle T., Steitz T.A.;
RT "The structure of HIV-1 reverse transcriptase complexed with an RNA
RT pseudoknot inhibitor.";
RL EMBO J. 17:4535-4542(1998).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 600-1155 IN COMPLEX WITH A
RP NON-NUCLEOSIDE INHIBITOR.
RX PubMed=9813120; DOI=10.1006/jmbi.1998.2171;
RA Hsiou Y., Das K., Ding J., Clark A.D. Jr., Kleim J.P., Rosner M.,
RA Winkler I., Riess G., Hughes S.H., Arnold E.;
RT "Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase
RT complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility
RT is a useful design feature for reducing drug resistance.";
RL J. Mol. Biol. 284:313-323(1998).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 600-1157.
RX PubMed=10468556; DOI=10.1073/pnas.96.18.10027;
RA Sarafianos S.G., Das K., Clark A.D. Jr., Ding J., Boyer P.L., Hughes S.H.,
RA Arnold E.;
RT "Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric
RT hindrance with beta-branched amino acids.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10027-10032(1999).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 600-1156.
RX PubMed=10650066; DOI=10.1021/jm990572y;
RA Hogberg M., Sahlberg C., Engelhardt P., Noreen R., Kangasmetsa J.,
RA Johansson N.G., Oberg B., Vrang L., Zhang H., Sahlberg B.L., Unge T.,
RA Lovgren S., Fridborg K., Backbro K.;
RT "Urea-PETT compounds as a new class of HIV-1 reverse transcriptase
RT inhibitors. 3. Synthesis and further structure-activity relationship
RT studies of PETT analogues.";
RL J. Med. Chem. 43:304-304(2000).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1152 IN COMPLEX WITH AN
RP OLIGONUCLEOTIDE, AND ACTIVE SITES OF RNASE H.
RX PubMed=11250910; DOI=10.1093/emboj/20.6.1449;
RA Sarafianos S.G., Das K., Tantillo C., Clark A.D. Jr., Ding J.,
RA Whitcomb J.M., Boyer P.L., Hughes S.H., Arnold E.;
RT "Crystal structure of HIV-1 reverse transcriptase in complex with a
RT polypurine tract RNA:DNA.";
RL EMBO J. 20:1449-1461(2001).
RN [60]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1159.
RX PubMed=11371163; DOI=10.1006/jmbi.2001.4648;
RA Hsiou Y., Ding J., Das K., Clark A.D. Jr., Boyer P.L., Lewi P.,
RA Janssen P.A., Kleim J.P., Rosner M., Hughes S.H., Arnold E.;
RT "The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug
RT resistance.";
RL J. Mol. Biol. 309:437-445(2001).
RN [61]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 600-1157.
RX PubMed=12456667; DOI=10.1093/emboj/cdf637;
RA Sarafianos S.G., Clark A.D. Jr., Das K., Tuske S., Birktoft J.J.,
RA Ilankumaran P., Ramesha A.R., Sayer J.M., Jerina D.M., Boyer P.L.,
RA Hughes S.H., Arnold E.;
RT "Structures of HIV-1 reverse transcriptase with pre- and post-translocation
RT AZTMP-terminated DNA.";
RL EMBO J. 21:6614-6624(2002).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1159 IN COMPLEX WITH
RP EFIVARENZ.
RX PubMed=11895437; DOI=10.1046/j.1432-1327.2002.02811.x;
RA Lindberg J., Sigurdsson S., Lowgren S., Andersson H.O., Sahlberg C.,
RA Noreen R., Fridborg K., Zhang H., Unge T.;
RT "Structural basis for the inhibitory efficacy of efavirenz (DMP-266),
RT MSC194 and PNU142721 towards the HIV-1 RT K103N mutant.";
RL Eur. J. Biochem. 269:1670-1677(2002).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 501-599.
RX PubMed=12694187; DOI=10.1046/j.1432-1033.2003.03533.x;
RA Andersson H.O., Fridborg K., Lowgren S., Alterman M., Muhlman A.,
RA Bjorsne M., Garg N., Kvarnstrom I., Schaal W., Classon B., Karlen A.,
RA Danielsson U.H., Ahlsen G., Nillroth U., Vrang L., Oberg B., Samuelsson B.,
RA Hallberg A., Unge T.;
RT "Optimization of P1-P3 groups in symmetric and asymmetric HIV-1 protease
RT inhibitors.";
RL Eur. J. Biochem. 270:1746-1758(2003).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH
RP MONOPYRROLINONE-BASED INHIBITORS LDC271 AND LGZ479.
RX PubMed=12723947; DOI=10.1021/jm0204587;
RA Smith A.B. III, Cantin L.D., Pasternak A., Guise-Zawacki L., Yao W.,
RA Charnley A.K., Barbosa J., Sprengeler P.A., Hirschmann R., Munshi S.,
RA Olsen D.B., Schleif W.A., Kuo L.C.;
RT "Design, synthesis, and biological evaluation of monopyrrolinone-based HIV-
RT 1 protease inhibitors.";
RL J. Med. Chem. 46:1831-1844(2003).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 501-599.
RX PubMed=15560801; DOI=10.1111/j.1432-1033.2004.04431.x;
RA Lindberg J., Pyring D., Lowgren S., Rosenquist A., Zuccarello G.,
RA Kvarnstrom I., Zhang H., Vrang L., Classon B., Hallberg A., Samuelsson B.,
RA Unge T.;
RT "Symmetric fluoro-substituted diol-based HIV protease inhibitors. Ortho-
RT fluorinated and meta-fluorinated P1/P1'-benzyloxy side groups significantly
RT improve the antiviral activity and preserve binding efficacy.";
RL Eur. J. Biochem. 271:4594-4602(2004).
RN [66]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1157.
RX PubMed=15016861; DOI=10.1128/jvi.78.7.3387-3397.2004;
RA Peletskaya E.N., Kogon A.A., Tuske S., Arnold E., Hughes S.H.;
RT "Nonnucleoside inhibitor binding affects the interactions of the fingers
RT subdomain of human immunodeficiency virus type 1 reverse transcriptase with
RT DNA.";
RL J. Virol. 78:3387-3397(2004).
RN [67]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 600-1157 IN COMPLEX WITH DNA BOUND
RP TO TENOFOVIR.
RX PubMed=15107837; DOI=10.1038/nsmb760;
RA Tuske S., Sarafianos S.G., Clark A.D. Jr., Ding J., Naeger L.K.,
RA White K.L., Miller M.D., Gibbs C.S., Boyer P.L., Clark P., Wang G.,
RA Gaffney B.L., Jones R.A., Jerina D.M., Hughes S.H., Arnold E.;
RT "Structures of HIV-1 RT-DNA complexes before and after incorporation of the
RT anti-AIDS drug tenofovir.";
RL Nat. Struct. Mol. Biol. 11:469-474(2004).
RN [68]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH
RP ARYLSULFONAMIDE AZACYCLIC UREA INHIBITORS.
RX PubMed=15225729; DOI=10.1016/j.bmcl.2004.05.036;
RA Huang P.P., Randolph J.T., Klein L.L., Vasavanonda S., Dekhtyar T.,
RA Stoll V.S., Kempf D.J.;
RT "Synthesis and antiviral activity of P1' arylsulfonamide azacyclic urea HIV
RT protease inhibitors.";
RL Bioorg. Med. Chem. Lett. 14:4075-4078(2004).
RN [69]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH
RP OXIMINOARYLSULFONAMIDE INHIBITOR.
RX PubMed=15837308; DOI=10.1016/j.bmcl.2005.03.008;
RA Yeung C.M., Klein L.L., Flentge C.A., Randolph J.T., Zhao C., Sun M.,
RA Dekhtyar T., Stoll V.S., Kempf D.J.;
RT "Oximinoarylsulfonamides as potent HIV protease inhibitors.";
RL Bioorg. Med. Chem. Lett. 15:2275-2278(2005).
CC -!- FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the
CC essential events in virion assembly, including binding the plasma
CC membrane, making the protein-protein interactions necessary to create
CC spherical particles, recruiting the viral Env proteins, and packaging
CC the genomic RNA via direct interactions with the RNA packaging sequence
CC (Psi). Gag-Pol polyprotein may regulate its own translation, by the
CC binding genomic RNA in the 5'-UTR. At low concentration, the
CC polyprotein would promote translation, whereas at high concentration,
CC the polyprotein would encapsidate genomic RNA and then shut off
CC translation. {ECO:0000250}.
CC -!- FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma
CC membrane via a multipartite membrane-binding signal, that includes its
CC myristoylated N-terminus. Matrix protein is part of the pre-integration
CC complex. Implicated in the release from host cell mediated by Vpu.
CC Binds to RNA. {ECO:0000250|UniProtKB:P12497}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the conical core that
CC encapsulates the genomic RNA-nucleocapsid complex in the virion. Most
CC core are conical, with only 7% tubular. The core is constituted by
CC capsid protein hexamer subunits. The core is disassembled soon after
CC virion entry (By similarity). Host restriction factors such as TRIM5-
CC alpha or TRIMCyp bind retroviral capsids and cause premature capsid
CC disassembly, leading to blocks in reverse transcription. Capsid
CC restriction by TRIM5 is one of the factors which restricts HIV-1 to the
CC human species. Host PIN1 apparently facilitates the virion uncoating.
CC On the other hand, interactions with PDZD8 or CYPA stabilize the
CC capsid. {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
CC -!- FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral
CC dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc
CC fingers. Acts as a nucleic acid chaperone which is involved in
CC rearangement of nucleic acid secondary structure during gRNA
CC retrotranscription. Also facilitates template switch leading to
CC recombination. As part of the polyprotein, participates in gRNA
CC dimerization, packaging, tRNA incorporation and virion assembly.
CC {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. Also cleaves Nef and Vif,
CC probably concomitantly with viral structural proteins on maturation of
CC virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off
CC the capped cellular mRNA translation. The resulting inhibition of
CC cellular protein synthesis serves to ensure maximal viral gene
CC expression and to evade host immune response. Also mediates cleavage of
CC host YTHDF3. Mediates cleavage of host CARD8, thereby activating the
CC CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient
CC CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade
CC CARD8-sensing when its protease remains inactive in infected cells
CC prior to viral budding (By similarity). {ECO:0000250|UniProtKB:P04585,
CC ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional
CC enzyme that converts the viral RNA genome into dsDNA in the cytoplasm,
CC shortly after virus entry into the cell. This enzyme displays a DNA
CC polymerase activity that can copy either DNA or RNA templates, and a
CC ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-
CC DNA heteroduplexes in a partially processive 3' to 5' endonucleasic
CC mode. Conversion of viral genomic RNA into dsDNA requires many steps. A
CC tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-
CC end of the viral RNA. RT uses the 3' end of the tRNA primer to perform
CC a short round of RNA-dependent minus-strand DNA synthesis. The reading
CC proceeds through the U5 region and ends after the repeated (R) region
CC which is present at both ends of viral RNA. The portion of the RNA-DNA
CC heteroduplex is digested by the RNase H, resulting in a ssDNA product
CC attached to the tRNA primer. This ssDNA/tRNA hybridizes with the
CC identical R region situated at the 3' end of viral RNA. This template
CC exchange, known as minus-strand DNA strong stop transfer, can be either
CC intra- or intermolecular. RT uses the 3' end of this newly synthesized
CC short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of
CC the whole template. RNase H digests the RNA template except for two
CC polypurine tracts (PPTs) situated at the 5'-end and near the center of
CC the genome. It is not clear if both polymerase and RNase H activities
CC are simultaneous. RNase H probably can proceed both in a polymerase-
CC dependent (RNA cut into small fragments by the same RT performing DNA
CC synthesis) and a polymerase-independent mode (cleavage of remaining RNA
CC fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
CC DNA synthesis using the PPTs that have not been removed by RNase H as
CC primers. PPTs and tRNA primers are then removed by RNase H. The 3' and
CC 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC blunt ended, linear dsDNA copy of the viral genome that includes long
CC terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC chromosome, by performing a series of DNA cutting and joining
CC reactions. This enzyme activity takes place after virion entry into a
CC cell and reverse transcription of the RNA genome in dsDNA. The first
CC step in the integration process is 3' processing. This step requires a
CC complex comprising the viral genome, matrix protein, Vpr and integrase.
CC This complex is called the pre-integration complex (PIC). The integrase
CC protein removes 2 nucleotides from each 3' end of the viral DNA,
CC leaving recessed CA OH's at the 3' ends. In the second step, the PIC
CC enters cell nucleus. This process is mediated through integrase and Vpr
CC proteins, and allows the virus to infect a non dividing cell. This
CC ability to enter the nucleus is specific of lentiviruses, other
CC retroviruses cannot and rely on cell division to access cell
CC chromosomes. In the third step, termed strand transfer, the integrase
CC protein joins the previously processed 3' ends to the 5' ends of
CC strands of target cellular DNA at the site of integration. The 5'-ends
CC are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-
CC shaped, gapped, recombination intermediate results, with the 5'-ends of
CC the viral DNA strands and the 3' ends of target DNA strands remaining
CC unjoined, flanking a gap of 5 bp. The last step is viral DNA
CC integration into host chromosome. This involves host DNA repair
CC synthesis in which the 5 bp gaps between the unjoined strands are
CC filled in and then ligated. Since this process occurs at both cuts
CC flanking the HIV genome, a 5 bp duplication of host DNA is produced at
CC the ends of HIV-1 integration. Alternatively, Integrase may catalyze
CC the excision of viral DNA just after strand transfer, this is termed
CC disintegration. {ECO:0000250|UniProtKB:P04585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific for a P1 residue that is hydrophobic, and P1'
CC variable, but often Pro.; EC=3.4.23.16;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00275};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2; Evidence={ECO:0000250};
CC -!- CATALYTIC ACTIVITY: [Reverse transcriptase/ribonuclease H]:
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:0000269|PubMed:2476069};
CC -!- CATALYTIC ACTIVITY: [Reverse transcriptase/ribonuclease H]:
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, ECO:0000269|PubMed:2476069};
CC -!- CATALYTIC ACTIVITY: [Reverse transcriptase/ribonuclease H]:
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, ECO:0000269|PubMed:2476069};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for reverse transcriptase polymerase
CC activity. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
CC Substrate-binding is a precondition for magnesium binding.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Magnesium ions are required for integrase activity. Binds at least
CC 1, maybe 2 magnesium ions. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Protease: The viral protease is inhibited by many
CC synthetic protease inhibitors (PIs), such as amprenavir, atazanavir,
CC indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. Use of
CC protease inhibitors in tritherapy regimens permit more ambitious
CC therapeutic strategies. Reverse transcriptase/ribonuclease H: RT can be
CC inhibited either by nucleoside RT inhibitors (NRTIs) or by non
CC nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators,
CC whereas NNRTIs inhibit DNA polymerization by binding a small
CC hydrophobic pocket near the RT active site and inducing an allosteric
CC change in this region. Classical NRTIs are abacavir, adefovir (PMEA),
CC didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA),
CC zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are
CC atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine
CC (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic
CC effective treatment of AIDS associate two NRTIs and one NNRTI.
CC {ECO:0000250}.
CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC hexamers of trimers (By similarity). 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 (By similarity). 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:P04585, ECO:0000250|UniProtKB:P12497}.
CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers. Interacts with human
CC PPIA/CYPA (By similarity); This interaction stabilizes the capsid.
CC Interacts with human NUP153 (By similarity). Interacts with host PDZD8;
CC this interaction stabilizes the capsid (By similarity). Interacts with
CC monkey TRIM5; this interaction destabilizes the capsid (By similarity).
CC {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
CC -!- SUBUNIT: [Protease]: Homodimer, whose active site consists of two
CC apposed aspartic acid residues. {ECO:0000250|UniProtKB:P04585,
CC ECO:0000250|UniProtKB:P12497}.
CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: Heterodimer of p66 RT
CC and p51 RT (RT p66/p51) (PubMed:8805568, PubMed:7687065).
CC Heterodimerization of RT is essential for DNA polymerase activity
CC (PubMed:8805568, PubMed:7687065). The overall folding of the subdomains
CC is similar in p66 RT and p51 RT but the spatial arrangements of the
CC subdomains are dramatically different (PubMed:7687065).
CC {ECO:0000269|PubMed:7687065, ECO:0000269|PubMed:8805568}.
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. Interacts with human KPNA3; this interaction might play a
CC role in nuclear import of the pre-integration complex (By similarity).
CC Interacts with human NUP153; this interaction might play a role in
CC nuclear import of the pre-integration complex (By similarity).
CC {ECO:0000250|UniProtKB:P03367, ECO:0000250|UniProtKB:P04585,
CC ECO:0000250|UniProtKB:P12497}.
CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-
CC anchor. Host endosome, host multivesicular body. Note=These locations
CC are linked to virus assembly sites. The main location is the cell
CC membrane, but under some circumstances, late endosomal compartments can
CC serve as productive sites for virion assembly.
CC {ECO:0000250|UniProtKB:P12497}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-
CC anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus
CC {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial
CC phase, cytoplasmic at assembly. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Translation results in the formation of the Gag polyprotein
CC most of the time. Ribosomal frameshifting at the gag-pol genes
CC boundary occurs at low frequency and produces the Gag-Pol
CC polyprotein. This strategy of translation probably allows the virus
CC to modulate the quantity of each viral protein. Maintenance of a
CC correct Gag to Gag-Pol ratio is essential for RNA dimerization and
CC viral infectivity. {ECO:0000269|PubMed:11172099};
CC Name=Gag-Pol polyprotein;
CC IsoId=P03366-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P03347-1; Sequence=External;
CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: RT is structured in
CC five subdomains: finger, palm, thumb, connection and RNase H. Within
CC the palm subdomain, the 'primer grip' region is thought to be involved
CC in the positioning of the primer terminus for accommodating the
CC incoming nucleotide. The RNase H domain stabilizes the association of
CC RT with primer-template. {ECO:0000250}.
CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: The tryptophan repeat
CC motif is involved in RT p66/p51 dimerization (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: [Integrase]: The core domain contains the D-x(n)-D-x(35)-E
CC motif, named for the phylogenetically conserved glutamic acid and
CC aspartic acid residues and the invariant 35 amino acid spacing between
CC the second and third acidic residues. Each acidic residue of the
CC D,D(35)E motif is independently essential for the 3'-processing and
CC strand transfer activities of purified integrase protein.
CC {ECO:0000250}.
CC -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The protease is released by
CC autocatalytic cleavage. The polyprotein is cleaved during and after
CC budding, this process is termed maturation. Proteolytic cleavage of p66
CC RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid
CC protein p7 might be further cleaved after virus entry.
CC {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00405}.
CC -!- PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the
CC virion by a host kinase. Phosphorylation is apparently not a major
CC regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.
CC -!- PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this
CC phosphorylation is necessary for Pin1-mediated virion uncoating.
CC {ECO:0000250|UniProtKB:P12497}.
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:0000269|PubMed:17415034}.
CC -!- MISCELLANEOUS: [Reverse transcriptase/ribonuclease H]: Error-prone
CC enzyme that lacks a proof-reading function. High mutations rate is a
CC direct consequence of this characteristic. RT also displays frequent
CC template switching leading to high recombination rate. Recombination
CC mostly occurs between homologous regions of the two copackaged RNA
CC genomes. If these two RNA molecules derive from different viral
CC strains, reverse transcription will give rise to highly recombinated
CC proviral DNAs. {ECO:0000250}.
CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC majority of strains found worldwide belong to the group M. Group O
CC seems to be endemic to and largely confined to Cameroon and neighboring
CC countries in West Central Africa, where these viruses represent a small
CC minority of HIV-1 strains. The group N is represented by a limited
CC number of isolates from Cameroonian persons. The group M is further
CC subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC -!- MISCELLANEOUS: Resistance to inhibitors associated with mutations are
CC observed both in viral protease and in reverse transcriptase. Most of
CC the time, single mutations confer only a modest reduction in drug
CC susceptibility. Combination of several mutations is usually required to
CC develop a high-level drug resistance. These mutations are predominantly
CC found in clade B viruses and not in other genotypes. They are listed in
CC the clade B representative isolate HXB2 (AC P04585).
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; M15654; AAA44198.1; ALT_SEQ; Genomic_RNA.
DR EMBL; K02083; AAB59867.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X01762; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; A03965; GNVWH3.
DR PIR; A03967; GNVWVL.
DR PDB; 1A9M; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1AJV; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1AJX; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1AXA; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1BQM; X-ray; 3.10 A; A=600-1155, B=600-1029.
DR PDB; 1BQN; X-ray; 3.30 A; A=600-1157, B=600-1029.
DR PDB; 1D4H; X-ray; 1.81 A; A/B=501-599.
DR PDB; 1D4I; X-ray; 1.81 A; A/B=501-599.
DR PDB; 1D4J; X-ray; 1.81 A; A/B=501-599.
DR PDB; 1DLO; X-ray; 2.70 A; A=600-1155, B=600-1026.
DR PDB; 1DW6; X-ray; 1.88 A; C/D=501-599.
DR PDB; 1EBK; X-ray; 2.06 A; C/D/E/F=501-599.
DR PDB; 1EBW; X-ray; 1.81 A; A/B=501-599.
DR PDB; 1EBY; X-ray; 2.29 A; A/B=501-599.
DR PDB; 1EBZ; X-ray; 2.01 A; A/B=501-599.
DR PDB; 1EC0; X-ray; 1.79 A; A/B=501-599.
DR PDB; 1EC1; X-ray; 2.10 A; A/B=501-599.
DR PDB; 1EC2; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1EC3; X-ray; 1.80 A; A/B=501-599.
DR PDB; 1EET; X-ray; 2.73 A; A=600-1156, B=600-1026.
DR PDB; 1G35; X-ray; 1.80 A; A/B=501-599.
DR PDB; 1GNM; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1GNN; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1GNO; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1HAR; X-ray; 2.20 A; A=600-815.
DR PDB; 1HBV; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1HEF; X-ray; 2.20 A; E=501-599.
DR PDB; 1HEG; X-ray; 2.20 A; E=501-599.
DR PDB; 1HIH; X-ray; 2.20 A; A/B=501-599.
DR PDB; 1HMV; X-ray; 3.20 A; A/C/E/G=600-1159, B/D/F/H=600-1039.
DR PDB; 1HNI; X-ray; 2.80 A; A=600-1157.
DR PDB; 1HNV; X-ray; 3.00 A; A=600-1157, B=600-1026.
DR PDB; 1HOS; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1HPS; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1HPZ; X-ray; 3.00 A; A=600-1159, B=600-1029.
DR PDB; 1HQE; X-ray; 2.70 A; A=600-1159, B=600-1029.
DR PDB; 1HQU; X-ray; 2.70 A; A=600-1159, B=600-1029.
DR PDB; 1HRH; X-ray; 2.40 A; A/B=1026-1161.
DR PDB; 1HTE; X-ray; 2.80 A; A/B=501-599.
DR PDB; 1HTF; X-ray; 2.20 A; A/B=501-599.
DR PDB; 1HTG; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1HVI; X-ray; 1.80 A; A/B=501-599.
DR PDB; 1HVK; X-ray; 1.80 A; A/B=501-599.
DR PDB; 1HVU; X-ray; 4.75 A; A/D/G/J=600-1153, B/E/H/K=604-1026.
DR PDB; 1HYS; X-ray; 3.00 A; A=600-1152, B=600-1024.
DR PDB; 1IKV; X-ray; 3.00 A; A=600-1159, B=600-1026.
DR PDB; 1IKW; X-ray; 3.00 A; A=600-1159, B=600-1026.
DR PDB; 1IKX; X-ray; 2.80 A; A=600-1159, B=600-1026.
DR PDB; 1IKY; X-ray; 3.00 A; A=600-1159, B=600-1026.
DR PDB; 1J5O; X-ray; 3.50 A; A=600-1157, B=600-1029.
DR PDB; 1KJH; X-ray; 2.00 A; P=1155-1164.
DR PDB; 1MER; X-ray; 1.90 A; A/B=501-599.
DR PDB; 1MES; X-ray; 1.90 A; A/B=501-599.
DR PDB; 1MET; X-ray; 1.90 A; A/B=501-599.
DR PDB; 1MEU; X-ray; 1.90 A; A/B=501-599.
DR PDB; 1N5Y; X-ray; 3.10 A; A=600-1157, B=600-1029.
DR PDB; 1N6Q; X-ray; 3.00 A; A=600-1157, B=600-1029.
DR PDB; 1NPA; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1NPV; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1NPW; X-ray; 2.00 A; A/B=501-599.
DR PDB; 1QE1; X-ray; 2.85 A; A=600-1157, B=600-1026.
DR PDB; 1QMC; NMR; -; A/B=1379-1429.
DR PDB; 1R0A; X-ray; 2.80 A; A=600-1157, B=600-1028.
DR PDB; 1RDH; X-ray; 2.80 A; A/B=1026-1159.
DR PDB; 1RTD; X-ray; 3.20 A; A/C=600-1153.
DR PDB; 1S6P; X-ray; 2.90 A; A=600-1159, B=600-1029.
DR PDB; 1S6Q; X-ray; 3.00 A; A=600-1159, B=600-1029.
DR PDB; 1S9E; X-ray; 2.60 A; A=600-1159, B=600-1029.
DR PDB; 1S9G; X-ray; 2.80 A; A=600-1159, B=600-1029.
DR PDB; 1SBG; X-ray; 2.30 A; A/B=501-599.
DR PDB; 1SUQ; X-ray; 3.00 A; A=600-1159, B=600-1029.
DR PDB; 1SV5; X-ray; 2.90 A; A=600-1159, B=600-1029.
DR PDB; 1T03; X-ray; 3.10 A; A=600-1157, B=600-1028.
DR PDB; 1T05; X-ray; 3.00 A; A=600-1157.
DR PDB; 1T7K; X-ray; 2.10 A; A/B=501-599.
DR PDB; 1TV6; X-ray; 2.80 A; A=600-1159, B=600-1039.
DR PDB; 1TVR; X-ray; 3.00 A; A=600-1157, B=600-1026.
DR PDB; 1UWB; X-ray; 3.20 A; A=600-1157, B=600-1026.
DR PDB; 1W5V; X-ray; 1.80 A; A/B=490-599.
DR PDB; 1W5W; X-ray; 1.80 A; A/B=490-599.
DR PDB; 1W5X; X-ray; 1.90 A; A/B=490-599.
DR PDB; 1W5Y; X-ray; 1.90 A; A/B=490-599.
DR PDB; 1YT9; X-ray; 3.00 A; A/B=501-599.
DR PDB; 1ZP8; X-ray; 2.02 A; A=501-599.
DR PDB; 1ZPA; X-ray; 2.02 A; A=501-599.
DR PDB; 1ZSF; X-ray; 1.98 A; A/B=501-599.
DR PDB; 1ZSR; X-ray; 2.06 A; A/B=501-599.
DR PDB; 2AQU; X-ray; 2.00 A; A/B=501-599.
DR PDB; 2B5J; X-ray; 2.90 A; A=600-1159, B=600-1029.
DR PDB; 2B6A; X-ray; 2.65 A; A=600-1159, B=600-1029.
DR PDB; 2BAN; X-ray; 2.95 A; A=600-1159, B=600-1029.
DR PDB; 2BBB; X-ray; 1.70 A; A/B=501-599.
DR PDB; 2BE2; X-ray; 2.43 A; A=600-1159, B=600-1029.
DR PDB; 2EXF; NMR; -; A=390-432.
DR PDB; 2G69; X-ray; 1.35 A; A=501-599.
DR PDB; 2HB3; X-ray; 1.35 A; A/B=501-598.
DR PDB; 2HMI; X-ray; 2.80 A; A=600-1157, B=600-1029.
DR PDB; 2HNZ; X-ray; 3.00 A; B=606-1027.
DR PDB; 2HS1; X-ray; 0.84 A; A/B=501-599.
DR PDB; 2HS2; X-ray; 1.22 A; A/B=501-599.
DR PDB; 2I4D; X-ray; 1.50 A; A/B=501-599.
DR PDB; 2I4U; X-ray; 1.50 A; A/B=501-599.
DR PDB; 2I4V; X-ray; 1.50 A; A/B=501-599.
DR PDB; 2I4W; X-ray; 1.55 A; A/B=501-599.
DR PDB; 2I4X; X-ray; 1.55 A; A/B=501-599.
DR PDB; 2I5J; X-ray; 3.15 A; A=600-1150, B=600-1027.
DR PDB; 2IAJ; X-ray; 2.50 A; A=600-1158, B=600-1045.
DR PDB; 2IC3; X-ray; 3.00 A; A=600-1158, B=600-1045.
DR PDB; 2IDW; X-ray; 1.10 A; A/B=501-599.
DR PDB; 2IEO; X-ray; 1.53 A; A/B=501-599.
DR PDB; 2JZW; NMR; -; A=390-432.
DR PDB; 2L45; NMR; -; A=411-429.
DR PDB; 2L46; NMR; -; A=411-429.
DR PDB; 2L4L; NMR; -; A=388-432.
DR PDB; 2UXZ; X-ray; 1.75 A; A/B=501-599.
DR PDB; 2UY0; X-ray; 1.76 A; A/B=501-599.
DR PDB; 2VG5; X-ray; 2.80 A; A=600-1156, B=600-1027.
DR PDB; 2VG6; X-ray; 3.01 A; A=600-1156, B=600-1027.
DR PDB; 2VG7; X-ray; 2.82 A; A=600-1156, B=600-1027.
DR PDB; 2X4U; X-ray; 2.10 A; C/F=908-916.
DR PDB; 2YKM; X-ray; 2.90 A; A=600-1156, B=600-1027.
DR PDB; 2YKN; X-ray; 2.12 A; A=600-1156, B=600-1027.
DR PDB; 2ZD1; X-ray; 1.80 A; A=600-1154, B=600-1027.
DR PDB; 2ZE2; X-ray; 2.90 A; A=600-1154, B=600-1027.
DR PDB; 3AVI; X-ray; 1.70 A; A/B=1209-1371.
DR PDB; 3BGR; X-ray; 2.10 A; A=600-1154, B=600-1027.
DR PDB; 3DLK; X-ray; 1.85 A; A=600-1154, B=605-1027.
DR PDB; 3GGA; X-ray; 2.50 A; A/B/C/D/G/H=501-599.
DR PDB; 3GGV; X-ray; 3.09 A; A/B/C/D/E/F/G/H/I=501-599.
DR PDB; 3GGX; X-ray; 2.70 A; A/B/C/D/E/F/G/H=501-599.
DR PDB; 3HVT; X-ray; 2.90 A; A=600-1155, B=600-1027.
DR PDB; 3IG1; X-ray; 2.80 A; A=600-1154, B=600-1027.
DR PDB; 3IRX; X-ray; 2.80 A; A=600-1154, B=600-1027.
DR PDB; 3IS9; X-ray; 2.55 A; A=600-1154, B=600-1027.
DR PDB; 3ISN; X-ray; 2.50 A; C=600-1159, D=600-1026.
DR PDB; 3ITH; X-ray; 2.80 A; A/C=600-1159, B/D=600-1026.
DR PDB; 3JSM; X-ray; 3.00 A; A=600-1157, B=600-1028.
DR PDB; 3JYT; X-ray; 3.30 A; A=600-1157, B=600-1028.
DR PDB; 3K2P; X-ray; 2.04 A; A/B=1026-1159.
DR PDB; 3K4V; X-ray; 1.39 A; A/B/C/D=501-599.
DR PDB; 3KLE; X-ray; 3.20 A; A/E/I/M=600-1157, B/F/J/N=600-1027.
DR PDB; 3KLF; X-ray; 3.15 A; A/E/I/M=600-1154, B/F/J/N=600-1027.
DR PDB; 3KLG; X-ray; 3.65 A; A/E=600-1157, B/F=600-1027.
DR PDB; 3KLH; X-ray; 2.90 A; A=600-1159, B=600-1027.
DR PDB; 3KLI; X-ray; 2.65 A; A=600-1157, B=600-1027.
DR PDB; 3NDT; X-ray; 1.72 A; A/B/C/D=501-599.
DR PDB; 3NU3; X-ray; 1.02 A; A/B=501-599.
DR PDB; 3NU4; X-ray; 1.20 A; A/B=501-599.
DR PDB; 3NU5; X-ray; 1.29 A; A/B=501-599.
DR PDB; 3NU6; X-ray; 1.16 A; A/B=501-599.
DR PDB; 3NU9; X-ray; 1.85 A; A/B=501-599.
DR PDB; 3NUJ; X-ray; 1.50 A; A/B=501-599.
DR PDB; 3NUO; X-ray; 1.35 A; A/B=501-599.
DR PDB; 3OK9; X-ray; 1.27 A; A/B=501-599.
DR PDB; 3PSU; X-ray; 2.07 A; A=501-599.
DR PDB; 3QAA; X-ray; 1.40 A; A/B=501-599.
DR PDB; 3QLH; X-ray; 2.70 A; A=600-1153, B=605-1027.
DR PDB; 3QO9; X-ray; 2.60 A; A=600-1154, B=600-1027.
DR PDB; 3TKG; X-ray; 1.36 A; A/B/C/D=497-599.
DR PDB; 3TKW; X-ray; 1.55 A; A/B=497-599.
DR PDB; 3TL9; X-ray; 1.32 A; A/B=497-599.
DR PDB; 3TLH; X-ray; 2.00 A; A=501-599.
DR PDB; 3V4I; X-ray; 2.80 A; A/C=600-1153, B/D=600-1027.
DR PDB; 3V6D; X-ray; 2.70 A; A/C=600-1153, B/D=600-1027.
DR PDB; 3V81; X-ray; 2.85 A; A/C=600-1153, B/D=600-1027.
DR PDB; 3ZPS; X-ray; 1.55 A; A/B=501-599.
DR PDB; 3ZPT; X-ray; 1.54 A; A/B=501-599.
DR PDB; 3ZPU; X-ray; 1.80 A; A/B=501-599.
DR PDB; 4COE; X-ray; 2.45 A; A/B=501-599.
DR PDB; 4CP7; X-ray; 1.80 A; A/B=501-599.
DR PDB; 4CPQ; X-ray; 2.35 A; A/B=501-599.
DR PDB; 4CPR; X-ray; 1.80 A; A/B=501-599.
DR PDB; 4CPS; X-ray; 1.55 A; A/B=501-599.
DR PDB; 4CPT; X-ray; 1.70 A; A/B=501-599.
DR PDB; 4CPU; X-ray; 1.82 A; A/B=501-599.
DR PDB; 4CPW; X-ray; 1.70 A; A/B=501-599.
DR PDB; 4CPX; X-ray; 1.85 A; A/B=501-599.
DR PDB; 4DG1; X-ray; 2.15 A; A=600-1148, B=600-1026.
DR PDB; 4G1Q; X-ray; 1.51 A; A=600-1154, B=600-1027.
DR PDB; 4G8G; X-ray; 2.40 A; C=263-272.
DR PDB; 4G8I; X-ray; 1.60 A; C=263-272.
DR PDB; 4G9D; X-ray; 1.60 A; C=263-272.
DR PDB; 4G9F; X-ray; 1.90 A; C=263-272.
DR PDB; 4H4M; X-ray; 2.85 A; A=600-1154, B=600-1027.
DR PDB; 4H4O; X-ray; 2.90 A; A=600-1154, B=600-1027.
DR PDB; 4I2P; X-ray; 2.30 A; A=600-1154, B=600-1027.
DR PDB; 4I2Q; X-ray; 2.70 A; A=600-1154, B=600-1027.
DR PDB; 4ICL; X-ray; 1.80 A; A=600-1154, B=600-1027.
DR PDB; 4ID5; X-ray; 1.95 A; A=600-1154, B=600-1027.
DR PDB; 4IDK; X-ray; 2.10 A; A=600-1154, B=600-1027.
DR PDB; 4IFV; X-ray; 2.05 A; A=600-1154, B=600-1027.
DR PDB; 4IFY; X-ray; 2.10 A; A=600-1154, B=600-1027.
DR PDB; 4IG0; X-ray; 2.50 A; A=600-1154, B=600-1027.
DR PDB; 4IG3; X-ray; 1.95 A; A=600-1154, B=600-1027.
DR PDB; 4KFB; X-ray; 1.85 A; A=600-1154, B=604-1027.
DR PDB; 4KKO; X-ray; 2.89 A; A=600-1154, B=600-1027.
DR PDB; 4KO0; X-ray; 1.95 A; A=600-1154, B=600-1027.
DR PDB; 4LSL; X-ray; 2.69 A; A=600-1154, B=600-1027.
DR PDB; 4LSN; X-ray; 3.10 A; A=600-1154, B=600-1027.
DR PDB; 4MFB; X-ray; 2.88 A; A=600-1154, B=600-1027.
DR PDB; 4O44; X-ray; 2.89 A; A=600-1154, B=600-1027.
DR PDB; 4O4G; X-ray; 2.71 A; A=600-1154, B=600-1027.
DR PDB; 4OJR; X-ray; 1.82 A; A=1209-1371.
DR PDB; 4PQU; X-ray; 2.51 A; A/C=600-1153, B/D=600-1027.
DR PDB; 4PUO; X-ray; 2.90 A; A/C=600-1153, B/D=600-1027.
DR PDB; 4PWD; X-ray; 3.00 A; A/C=600-1153, B/D=600-1027.
DR PDB; 4Q0B; X-ray; 3.30 A; A/C=600-1153, B/D=600-1027.
DR PDB; 4QAG; X-ray; 1.71 A; A/B=1024-1156.
DR PDB; 4R5P; X-ray; 2.89 A; A/C=600-1153, B/D=600-1027.
DR PDB; 4RW4; X-ray; 2.67 A; A=600-1154, B=600-1027.
DR PDB; 4RW6; X-ray; 2.63 A; A=600-1154, B=600-1027.
DR PDB; 4RW7; X-ray; 3.01 A; A=600-1154, B=600-1027.
DR PDB; 4RW8; X-ray; 2.88 A; A=600-1154, B=600-1027.
DR PDB; 4RW9; X-ray; 2.99 A; A=600-1154, B=600-1027.
DR PDB; 4U8W; X-ray; 1.30 A; A/B=501-599.
DR PDB; 4WE1; X-ray; 2.49 A; A=600-1154, B=600-1027.
DR PDB; 4YE3; X-ray; 1.35 A; A/B=501-599.
DR PDB; 4YHQ; X-ray; 1.30 A; A/B=501-599.
DR PDB; 4ZIP; X-ray; 1.11 A; A/B=501-599.
DR PDB; 4ZLS; X-ray; 1.53 A; A/B=501-599.
DR PDB; 5AGZ; X-ray; 1.20 A; A/B=501-599.
DR PDB; 5AH6; X-ray; 1.50 A; A/B=501-599.
DR PDB; 5AH7; X-ray; 1.55 A; A/B=501-599.
DR PDB; 5AH8; X-ray; 1.26 A; A/B=501-599.
DR PDB; 5AH9; X-ray; 1.44 A; A/B=501-599.
DR PDB; 5AHA; X-ray; 1.35 A; A/B=501-599.
DR PDB; 5AHB; X-ray; 1.50 A; A/B=501-599.
DR PDB; 5AHC; X-ray; 1.50 A; A/B=501-599.
DR PDB; 5BRY; X-ray; 1.34 A; A/B=501-599.
DR PDB; 5BS4; X-ray; 1.29 A; A/B=501-599.
DR PDB; 5C24; X-ray; 2.60 A; A=600-1144, B=604-1027.
DR PDB; 5C25; X-ray; 2.84 A; A=600-1154, B=600-1027.
DR PDB; 5C42; X-ray; 3.50 A; A=600-1154, B=600-1027.
DR PDB; 5CYM; X-ray; 2.10 A; A=600-1154, B=600-1027.
DR PDB; 5CYQ; X-ray; 2.15 A; A=600-1154, B=600-1027.
DR PDB; 5D3G; X-ray; 2.30 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5FDL; X-ray; 3.10 A; A=600-1156, B=600-1039.
DR PDB; 5HBM; X-ray; 3.04 A; A=600-1154, B=600-1027.
DR PDB; 5HLF; X-ray; 2.95 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5HP1; X-ray; 2.90 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5HRO; X-ray; 2.75 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5I3U; X-ray; 3.00 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5I42; X-ray; 3.30 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5J1E; X-ray; 2.90 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5JFP; X-ray; 1.49 A; A/B=501-599.
DR PDB; 5JFU; X-ray; 1.70 A; A/B=501-599.
DR PDB; 5JG1; X-ray; 1.16 A; A/B=501-599.
DR PDB; 5OI2; X-ray; 2.20 A; A=1209-1371.
DR PDB; 5OI3; X-ray; 2.30 A; A=1209-1371.
DR PDB; 5OI5; X-ray; 2.40 A; A=1209-1371.
DR PDB; 5OI8; X-ray; 2.35 A; A=1209-1371.
DR PDB; 5OIA; X-ray; 2.20 A; A=1209-1371.
DR PDB; 5T6Z; X-ray; 2.00 A; C=240-249.
DR PDB; 5T70; X-ray; 2.10 A; C=240-249.
DR PDB; 5TER; X-ray; 2.70 A; A=600-1154, B=600-1027.
DR PDB; 5TUQ; X-ray; 2.71 A; A=600-1154, B=600-1027.
DR PDB; 5TW3; X-ray; 2.85 A; A=600-1154, B=600-1027.
DR PDB; 5TXL; X-ray; 2.50 A; A/C=600-1153, B/D=600-1027.
DR PDB; 5TXM; X-ray; 2.70 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5TXN; X-ray; 2.55 A; A/C=600-1153, B/D=600-1027.
DR PDB; 5TXO; X-ray; 2.55 A; A/C=600-1153, B/D=600-1027.
DR PDB; 5TXP; X-ray; 2.70 A; A/C=600-1153, B/D=600-1027.
DR PDB; 5UFZ; X-ray; 1.65 A; A/B=501-599.
DR PDB; 5ULT; X-ray; 1.53 A; A/B=501-599.
DR PDB; 5UOV; X-ray; 1.33 A; A/B=501-599.
DR PDB; 5UPZ; X-ray; 1.27 A; A/B=501-599.
DR PDB; 5UV5; X-ray; 3.00 A; A/C=600-1154, B/D=600-1027.
DR PDB; 5V5L; X-ray; 2.00 A; E/F=240-249.
DR PDB; 5V5M; X-ray; 2.88 A; E/F=240-249.
DR PDB; 5VQQ; X-ray; 2.55 A; A=600-1154, B=600-1027.
DR PDB; 5VQR; X-ray; 2.55 A; A=600-1154, B=600-1027.
DR PDB; 5VQS; X-ray; 2.50 A; A=600-1154, B=600-1027.
DR PDB; 5VQT; X-ray; 2.56 A; A=600-1154, B=600-1027.
DR PDB; 5VQU; X-ray; 2.60 A; A=600-1154, B=600-1027.
DR PDB; 5VQV; X-ray; 2.58 A; A=600-1154, B=600-1027.
DR PDB; 5VQW; X-ray; 2.50 A; A=600-1154, B=600-1027.
DR PDB; 5VQX; X-ray; 2.40 A; A=600-1154, B=600-1027.
DR PDB; 5VQY; X-ray; 2.35 A; A=600-1154, B=600-1027.
DR PDB; 5VQZ; X-ray; 2.23 A; A=600-1154, B=600-1027.
DR PDB; 5W5W; X-ray; 3.00 A; A/B=501-599.
DR PDB; 5YOJ; X-ray; 1.50 A; A/B=500-599.
DR PDB; 6AMO; X-ray; 2.50 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6AN2; X-ray; 2.70 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6AN8; X-ray; 2.60 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6ANQ; X-ray; 2.59 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6AOC; X-ray; 1.80 A; A/C=600-1154, B/D=600-1027.
DR PDB; 6ASW; X-ray; 2.60 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6AVM; X-ray; 2.50 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6AVT; X-ray; 2.60 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6B19; EM; 4.50 A; A=600-1159, B=600-1039.
DR PDB; 6BZ2; X-ray; 1.67 A; A/B=501-599.
DR PDB; 6C0J; X-ray; 1.92 A; A=600-1154, B=600-1027.
DR PDB; 6C0K; X-ray; 1.96 A; A=600-1154, B=600-1027.
DR PDB; 6C0L; X-ray; 1.95 A; A=600-1154, B=600-1027.
DR PDB; 6C0N; X-ray; 2.00 A; A=600-1154, B=600-1027.
DR PDB; 6C0O; X-ray; 1.90 A; A=600-1154, B=600-1027.
DR PDB; 6C0P; X-ray; 2.05 A; A=600-1154, B=600-1027.
DR PDB; 6C0R; X-ray; 2.05 A; A=600-1154, B=600-1027.
DR PDB; 6C8X; X-ray; 1.61 A; A/B=501-599.
DR PDB; 6C8Y; X-ray; 1.94 A; A/B=501-599.
DR PDB; 6CGF; X-ray; 1.94 A; A=600-1154, B=600-1027.
DR PDB; 6D0D; X-ray; 1.85 A; A/B=501-599.
DR PDB; 6D0E; X-ray; 1.95 A; A/B=501-599.
DR PDB; 6DTW; X-ray; 2.74 A; A=600-1154, B=600-1027.
DR PDB; 6DTX; X-ray; 3.33 A; A=600-1154, B=600-1027.
DR PDB; 6DUF; X-ray; 1.96 A; A=600-1154, B=600-1027.
DR PDB; 6DUG; X-ray; 2.23 A; A=600-1154, B=600-1027.
DR PDB; 6DUH; X-ray; 2.00 A; A=600-1154, B=600-1027.
DR PDB; 6ECL; X-ray; 2.38 A; A=600-1154, B=600-1027.
DR PDB; 6ELI; X-ray; 2.20 A; A=600-1154, B=600-1027.
DR PDB; 6HAK; X-ray; 3.95 A; A/C=600-1153, B/D=600-1027.
DR PDB; 6KMP; X-ray; 1.31 A; A/B=501-599.
DR PDB; 6O48; X-ray; 1.46 A; A/B=501-599.
DR PDB; 6O9E; X-ray; 2.40 A; A/C=600-1154, B/D=600-1027.
DR PDB; 6OE3; X-ray; 2.90 A; A=600-1154, B=600-1027.
DR PDB; 6OUN; X-ray; 2.66 A; A=600-1157, B=600-1039.
DR PDB; 6PRF; X-ray; 1.21 A; A/B=501-599.
DR PDB; 6UL5; X-ray; 2.23 A; A=600-1154, B=600-1027.
DR PDB; 6VUG; X-ray; 3.00 A; A=600-1154.
DR PDB; 6WAZ; EM; 4.10 A; A=600-1159, B=600-1039.
DR PDB; 6WB0; EM; 4.20 A; A=600-1159, B=600-1039.
DR PDB; 6WB1; EM; 4.70 A; A=600-1159, B=600-1039.
DR PDB; 6WB2; EM; 4.50 A; A=600-1159, B=600-1039.
DR PDB; 6X47; X-ray; 2.77 A; A=600-1154, B=600-1027.
DR PDB; 6X49; X-ray; 2.75 A; A=600-1154, B=600-1027.
DR PDB; 6X4A; X-ray; 2.54 A; A=600-1154, B=600-1027.
DR PDB; 6X4B; X-ray; 2.50 A; A=600-1154, B=600-1027.
DR PDB; 6X4C; X-ray; 2.86 A; A=600-1154, B=600-1027.
DR PDB; 6X4D; X-ray; 2.65 A; A=600-1154, B=600-1027.
DR PDB; 6X4E; X-ray; 2.60 A; A=600-1154, B=600-1027.
DR PDB; 6X4F; X-ray; 2.72 A; A=600-1154, B=600-1027.
DR PDB; 7AHX; X-ray; 2.73 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7AID; X-ray; 3.15 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7AIF; X-ray; 2.75 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7AIG; X-ray; 2.95 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7AII; X-ray; 2.62 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7AIJ; X-ray; 2.95 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7KJV; EM; 2.80 A; A=600-1159, B=600-1039.
DR PDB; 7KJW; EM; 2.90 A; A=600-1159, B=600-1039.
DR PDB; 7KJX; EM; 3.10 A; A=600-1159, B=600-1039.
DR PDB; 7KRC; X-ray; 2.65 A; A=600-1154, B=600-1027.
DR PDB; 7KRD; X-ray; 2.70 A; A=600-1154, B=600-1027.
DR PDB; 7KRE; X-ray; 2.73 A; A=600-1154, B=600-1027.
DR PDB; 7KRF; X-ray; 2.60 A; A=600-1154, B=600-1027.
DR PDB; 7KWU; X-ray; 2.02 A; A=600-1154, B=600-1027.
DR PDB; 7LPW; X-ray; 2.32 A; A=600-1154, B=600-1027.
DR PDB; 7LPX; X-ray; 2.45 A; A=600-1154, B=600-1027.
DR PDB; 7LQU; X-ray; 2.60 A; A=600-1154, B=600-1027.
DR PDB; 7LRI; X-ray; 3.05 A; A/C=600-1154, B/D=600-1027.
DR PDB; 7LRM; X-ray; 3.14 A; A/C=600-1154, B/D=600-1027.
DR PDB; 7LRX; X-ray; 2.90 A; A/C=600-1154, B/D=600-1027.
DR PDB; 7LRY; X-ray; 2.45 A; A/C=600-1154, B/D=600-1027.
DR PDB; 7LSK; X-ray; 2.70 A; A/C=600-1154, B/D=600-1027.
DR PDB; 7OT6; X-ray; 3.20 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OTA; X-ray; 3.00 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OTK; X-ray; 2.95 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OTN; X-ray; 3.40 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OTX; X-ray; 3.45 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OTZ; X-ray; 3.10 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OUT; X-ray; 3.20 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OXQ; X-ray; 3.30 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OZ2; X-ray; 2.85 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OZ5; X-ray; 3.37 A; A/C=600-1153, B/D=600-1027.
DR PDB; 7OZW; EM; 3.38 A; A=600-1153, B=600-1027.
DR PDB; 7P15; EM; 3.58 A; A=600-1153, B=600-1027.
DR PDB; 7SNP; X-ray; 2.89 A; A=600-1154, B=600-1027.
DR PDB; 7SNZ; X-ray; 2.37 A; A=600-1154, B=600-1027.
DR PDB; 7SO1; X-ray; 2.73 A; A=600-1154, B=600-1027.
DR PDB; 7SO2; X-ray; 3.09 A; A=600-1154, B=600-1027.
DR PDB; 7SO3; X-ray; 2.77 A; A=600-1154, B=600-1027.
DR PDB; 7SO4; X-ray; 2.95 A; A=600-1154, B=600-1027.
DR PDB; 7SO6; X-ray; 2.79 A; A=600-1154, B=600-1027.
DR PDBsum; 1A9M; -.
DR PDBsum; 1AJV; -.
DR PDBsum; 1AJX; -.
DR PDBsum; 1AXA; -.
DR PDBsum; 1BQM; -.
DR PDBsum; 1BQN; -.
DR PDBsum; 1D4H; -.
DR PDBsum; 1D4I; -.
DR PDBsum; 1D4J; -.
DR PDBsum; 1DLO; -.
DR PDBsum; 1DW6; -.
DR PDBsum; 1EBK; -.
DR PDBsum; 1EBW; -.
DR PDBsum; 1EBY; -.
DR PDBsum; 1EBZ; -.
DR PDBsum; 1EC0; -.
DR PDBsum; 1EC1; -.
DR PDBsum; 1EC2; -.
DR PDBsum; 1EC3; -.
DR PDBsum; 1EET; -.
DR PDBsum; 1G35; -.
DR PDBsum; 1GNM; -.
DR PDBsum; 1GNN; -.
DR PDBsum; 1GNO; -.
DR PDBsum; 1HAR; -.
DR PDBsum; 1HBV; -.
DR PDBsum; 1HEF; -.
DR PDBsum; 1HEG; -.
DR PDBsum; 1HIH; -.
DR PDBsum; 1HMV; -.
DR PDBsum; 1HNI; -.
DR PDBsum; 1HNV; -.
DR PDBsum; 1HOS; -.
DR PDBsum; 1HPS; -.
DR PDBsum; 1HPZ; -.
DR PDBsum; 1HQE; -.
DR PDBsum; 1HQU; -.
DR PDBsum; 1HRH; -.
DR PDBsum; 1HTE; -.
DR PDBsum; 1HTF; -.
DR PDBsum; 1HTG; -.
DR PDBsum; 1HVI; -.
DR PDBsum; 1HVK; -.
DR PDBsum; 1HVU; -.
DR PDBsum; 1HYS; -.
DR PDBsum; 1IKV; -.
DR PDBsum; 1IKW; -.
DR PDBsum; 1IKX; -.
DR PDBsum; 1IKY; -.
DR PDBsum; 1J5O; -.
DR PDBsum; 1KJH; -.
DR PDBsum; 1MER; -.
DR PDBsum; 1MES; -.
DR PDBsum; 1MET; -.
DR PDBsum; 1MEU; -.
DR PDBsum; 1N5Y; -.
DR PDBsum; 1N6Q; -.
DR PDBsum; 1NPA; -.
DR PDBsum; 1NPV; -.
DR PDBsum; 1NPW; -.
DR PDBsum; 1QE1; -.
DR PDBsum; 1QMC; -.
DR PDBsum; 1R0A; -.
DR PDBsum; 1RDH; -.
DR PDBsum; 1RTD; -.
DR PDBsum; 1S6P; -.
DR PDBsum; 1S6Q; -.
DR PDBsum; 1S9E; -.
DR PDBsum; 1S9G; -.
DR PDBsum; 1SBG; -.
DR PDBsum; 1SUQ; -.
DR PDBsum; 1SV5; -.
DR PDBsum; 1T03; -.
DR PDBsum; 1T05; -.
DR PDBsum; 1T7K; -.
DR PDBsum; 1TV6; -.
DR PDBsum; 1TVR; -.
DR PDBsum; 1UWB; -.
DR PDBsum; 1W5V; -.
DR PDBsum; 1W5W; -.
DR PDBsum; 1W5X; -.
DR PDBsum; 1W5Y; -.
DR PDBsum; 1YT9; -.
DR PDBsum; 1ZP8; -.
DR PDBsum; 1ZPA; -.
DR PDBsum; 1ZSF; -.
DR PDBsum; 1ZSR; -.
DR PDBsum; 2AQU; -.
DR PDBsum; 2B5J; -.
DR PDBsum; 2B6A; -.
DR PDBsum; 2BAN; -.
DR PDBsum; 2BBB; -.
DR PDBsum; 2BE2; -.
DR PDBsum; 2EXF; -.
DR PDBsum; 2G69; -.
DR PDBsum; 2HB3; -.
DR PDBsum; 2HMI; -.
DR PDBsum; 2HNZ; -.
DR PDBsum; 2HS1; -.
DR PDBsum; 2HS2; -.
DR PDBsum; 2I4D; -.
DR PDBsum; 2I4U; -.
DR PDBsum; 2I4V; -.
DR PDBsum; 2I4W; -.
DR PDBsum; 2I4X; -.
DR PDBsum; 2I5J; -.
DR PDBsum; 2IAJ; -.
DR PDBsum; 2IC3; -.
DR PDBsum; 2IDW; -.
DR PDBsum; 2IEO; -.
DR PDBsum; 2JZW; -.
DR PDBsum; 2L45; -.
DR PDBsum; 2L46; -.
DR PDBsum; 2L4L; -.
DR PDBsum; 2UXZ; -.
DR PDBsum; 2UY0; -.
DR PDBsum; 2VG5; -.
DR PDBsum; 2VG6; -.
DR PDBsum; 2VG7; -.
DR PDBsum; 2X4U; -.
DR PDBsum; 2YKM; -.
DR PDBsum; 2YKN; -.
DR PDBsum; 2ZD1; -.
DR PDBsum; 2ZE2; -.
DR PDBsum; 3AVI; -.
DR PDBsum; 3BGR; -.
DR PDBsum; 3DLK; -.
DR PDBsum; 3GGA; -.
DR PDBsum; 3GGV; -.
DR PDBsum; 3GGX; -.
DR PDBsum; 3HVT; -.
DR PDBsum; 3IG1; -.
DR PDBsum; 3IRX; -.
DR PDBsum; 3IS9; -.
DR PDBsum; 3ISN; -.
DR PDBsum; 3ITH; -.
DR PDBsum; 3JSM; -.
DR PDBsum; 3JYT; -.
DR PDBsum; 3K2P; -.
DR PDBsum; 3K4V; -.
DR PDBsum; 3KLE; -.
DR PDBsum; 3KLF; -.
DR PDBsum; 3KLG; -.
DR PDBsum; 3KLH; -.
DR PDBsum; 3KLI; -.
DR PDBsum; 3NDT; -.
DR PDBsum; 3NU3; -.
DR PDBsum; 3NU4; -.
DR PDBsum; 3NU5; -.
DR PDBsum; 3NU6; -.
DR PDBsum; 3NU9; -.
DR PDBsum; 3NUJ; -.
DR PDBsum; 3NUO; -.
DR PDBsum; 3OK9; -.
DR PDBsum; 3PSU; -.
DR PDBsum; 3QAA; -.
DR PDBsum; 3QLH; -.
DR PDBsum; 3QO9; -.
DR PDBsum; 3TKG; -.
DR PDBsum; 3TKW; -.
DR PDBsum; 3TL9; -.
DR PDBsum; 3TLH; -.
DR PDBsum; 3V4I; -.
DR PDBsum; 3V6D; -.
DR PDBsum; 3V81; -.
DR PDBsum; 3ZPS; -.
DR PDBsum; 3ZPT; -.
DR PDBsum; 3ZPU; -.
DR PDBsum; 4COE; -.
DR PDBsum; 4CP7; -.
DR PDBsum; 4CPQ; -.
DR PDBsum; 4CPR; -.
DR PDBsum; 4CPS; -.
DR PDBsum; 4CPT; -.
DR PDBsum; 4CPU; -.
DR PDBsum; 4CPW; -.
DR PDBsum; 4CPX; -.
DR PDBsum; 4DG1; -.
DR PDBsum; 4G1Q; -.
DR PDBsum; 4G8G; -.
DR PDBsum; 4G8I; -.
DR PDBsum; 4G9D; -.
DR PDBsum; 4G9F; -.
DR PDBsum; 4H4M; -.
DR PDBsum; 4H4O; -.
DR PDBsum; 4I2P; -.
DR PDBsum; 4I2Q; -.
DR PDBsum; 4ICL; -.
DR PDBsum; 4ID5; -.
DR PDBsum; 4IDK; -.
DR PDBsum; 4IFV; -.
DR PDBsum; 4IFY; -.
DR PDBsum; 4IG0; -.
DR PDBsum; 4IG3; -.
DR PDBsum; 4KFB; -.
DR PDBsum; 4KKO; -.
DR PDBsum; 4KO0; -.
DR PDBsum; 4LSL; -.
DR PDBsum; 4LSN; -.
DR PDBsum; 4MFB; -.
DR PDBsum; 4O44; -.
DR PDBsum; 4O4G; -.
DR PDBsum; 4OJR; -.
DR PDBsum; 4PQU; -.
DR PDBsum; 4PUO; -.
DR PDBsum; 4PWD; -.
DR PDBsum; 4Q0B; -.
DR PDBsum; 4QAG; -.
DR PDBsum; 4R5P; -.
DR PDBsum; 4RW4; -.
DR PDBsum; 4RW6; -.
DR PDBsum; 4RW7; -.
DR PDBsum; 4RW8; -.
DR PDBsum; 4RW9; -.
DR PDBsum; 4U8W; -.
DR PDBsum; 4WE1; -.
DR PDBsum; 4YE3; -.
DR PDBsum; 4YHQ; -.
DR PDBsum; 4ZIP; -.
DR PDBsum; 4ZLS; -.
DR PDBsum; 5AGZ; -.
DR PDBsum; 5AH6; -.
DR PDBsum; 5AH7; -.
DR PDBsum; 5AH8; -.
DR PDBsum; 5AH9; -.
DR PDBsum; 5AHA; -.
DR PDBsum; 5AHB; -.
DR PDBsum; 5AHC; -.
DR PDBsum; 5BRY; -.
DR PDBsum; 5BS4; -.
DR PDBsum; 5C24; -.
DR PDBsum; 5C25; -.
DR PDBsum; 5C42; -.
DR PDBsum; 5CYM; -.
DR PDBsum; 5CYQ; -.
DR PDBsum; 5D3G; -.
DR PDBsum; 5FDL; -.
DR PDBsum; 5HBM; -.
DR PDBsum; 5HLF; -.
DR PDBsum; 5HP1; -.
DR PDBsum; 5HRO; -.
DR PDBsum; 5I3U; -.
DR PDBsum; 5I42; -.
DR PDBsum; 5J1E; -.
DR PDBsum; 5JFP; -.
DR PDBsum; 5JFU; -.
DR PDBsum; 5JG1; -.
DR PDBsum; 5OI2; -.
DR PDBsum; 5OI3; -.
DR PDBsum; 5OI5; -.
DR PDBsum; 5OI8; -.
DR PDBsum; 5OIA; -.
DR PDBsum; 5T6Z; -.
DR PDBsum; 5T70; -.
DR PDBsum; 5TER; -.
DR PDBsum; 5TUQ; -.
DR PDBsum; 5TW3; -.
DR PDBsum; 5TXL; -.
DR PDBsum; 5TXM; -.
DR PDBsum; 5TXN; -.
DR PDBsum; 5TXO; -.
DR PDBsum; 5TXP; -.
DR PDBsum; 5UFZ; -.
DR PDBsum; 5ULT; -.
DR PDBsum; 5UOV; -.
DR PDBsum; 5UPZ; -.
DR PDBsum; 5UV5; -.
DR PDBsum; 5V5L; -.
DR PDBsum; 5V5M; -.
DR PDBsum; 5VQQ; -.
DR PDBsum; 5VQR; -.
DR PDBsum; 5VQS; -.
DR PDBsum; 5VQT; -.
DR PDBsum; 5VQU; -.
DR PDBsum; 5VQV; -.
DR PDBsum; 5VQW; -.
DR PDBsum; 5VQX; -.
DR PDBsum; 5VQY; -.
DR PDBsum; 5VQZ; -.
DR PDBsum; 5W5W; -.
DR PDBsum; 5YOJ; -.
DR PDBsum; 6AMO; -.
DR PDBsum; 6AN2; -.
DR PDBsum; 6AN8; -.
DR PDBsum; 6ANQ; -.
DR PDBsum; 6AOC; -.
DR PDBsum; 6ASW; -.
DR PDBsum; 6AVM; -.
DR PDBsum; 6AVT; -.
DR PDBsum; 6B19; -.
DR PDBsum; 6BZ2; -.
DR PDBsum; 6C0J; -.
DR PDBsum; 6C0K; -.
DR PDBsum; 6C0L; -.
DR PDBsum; 6C0N; -.
DR PDBsum; 6C0O; -.
DR PDBsum; 6C0P; -.
DR PDBsum; 6C0R; -.
DR PDBsum; 6C8X; -.
DR PDBsum; 6C8Y; -.
DR PDBsum; 6CGF; -.
DR PDBsum; 6D0D; -.
DR PDBsum; 6D0E; -.
DR PDBsum; 6DTW; -.
DR PDBsum; 6DTX; -.
DR PDBsum; 6DUF; -.
DR PDBsum; 6DUG; -.
DR PDBsum; 6DUH; -.
DR PDBsum; 6ECL; -.
DR PDBsum; 6ELI; -.
DR PDBsum; 6HAK; -.
DR PDBsum; 6KMP; -.
DR PDBsum; 6O48; -.
DR PDBsum; 6O9E; -.
DR PDBsum; 6OE3; -.
DR PDBsum; 6OUN; -.
DR PDBsum; 6PRF; -.
DR PDBsum; 6UL5; -.
DR PDBsum; 6VUG; -.
DR PDBsum; 6WAZ; -.
DR PDBsum; 6WB0; -.
DR PDBsum; 6WB1; -.
DR PDBsum; 6WB2; -.
DR PDBsum; 6X47; -.
DR PDBsum; 6X49; -.
DR PDBsum; 6X4A; -.
DR PDBsum; 6X4B; -.
DR PDBsum; 6X4C; -.
DR PDBsum; 6X4D; -.
DR PDBsum; 6X4E; -.
DR PDBsum; 6X4F; -.
DR PDBsum; 7AHX; -.
DR PDBsum; 7AID; -.
DR PDBsum; 7AIF; -.
DR PDBsum; 7AIG; -.
DR PDBsum; 7AII; -.
DR PDBsum; 7AIJ; -.
DR PDBsum; 7KJV; -.
DR PDBsum; 7KJW; -.
DR PDBsum; 7KJX; -.
DR PDBsum; 7KRC; -.
DR PDBsum; 7KRD; -.
DR PDBsum; 7KRE; -.
DR PDBsum; 7KRF; -.
DR PDBsum; 7KWU; -.
DR PDBsum; 7LPW; -.
DR PDBsum; 7LPX; -.
DR PDBsum; 7LQU; -.
DR PDBsum; 7LRI; -.
DR PDBsum; 7LRM; -.
DR PDBsum; 7LRX; -.
DR PDBsum; 7LRY; -.
DR PDBsum; 7LSK; -.
DR PDBsum; 7OT6; -.
DR PDBsum; 7OTA; -.
DR PDBsum; 7OTK; -.
DR PDBsum; 7OTN; -.
DR PDBsum; 7OTX; -.
DR PDBsum; 7OTZ; -.
DR PDBsum; 7OUT; -.
DR PDBsum; 7OXQ; -.
DR PDBsum; 7OZ2; -.
DR PDBsum; 7OZ5; -.
DR PDBsum; 7OZW; -.
DR PDBsum; 7P15; -.
DR PDBsum; 7SNP; -.
DR PDBsum; 7SNZ; -.
DR PDBsum; 7SO1; -.
DR PDBsum; 7SO2; -.
DR PDBsum; 7SO3; -.
DR PDBsum; 7SO4; -.
DR PDBsum; 7SO6; -.
DR BMRB; P03366; -.
DR SMR; P03366; -.
DR IntAct; P03366; 39.
DR MINT; P03366; -.
DR ChEMBL; CHEMBL5823; -.
DR DrugBank; DB07035; (2E)-3-{3-[(5-ETHYL-3-IODO-6-METHYL-2-OXO-1,2-DIHYDROPYRIDIN-4-YL)OXY]PHENYL}ACRYLONITRILE.
DR DrugBank; DB02704; (2R,3R,4R,5R)-3,4-Dihydroxy-N,N'-bis[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-2,5-bis(2-phenylethyl)hexanediamide.
DR DrugBank; DB07806; (2R,4S)-2-[(R)-BENZYLCARBAMOYL-PHENYLACETYL-METHYL]-5,5-DIMETHYL-THIAZOLIDINE-4-CARBOXYLIC ACID.
DR DrugBank; DB02785; (2S)-1-[(2S,4R)-4-Benzyl-2-hydroxy-5-{[(1S,2R,5S)-2-hydroxy-5-methylcyclopentyl]amino}-5-oxopentyl]-4-{[6-chloro-5-(4-methyl-1-piperazinyl)-2-pyrazinyl]carbonyl}-N-(2-methyl-2-propanyl)-2-piperazineca rboxamide.
DR DrugBank; DB01824; (3S)-Tetrahydro-3-furanyl {(2S,3S)-4-[(2S,4R)-4-{(1S,2R)-2-[(S)-amino(hydroxy)methoxy]-2,3-dihydro-1H-inden-1-yl}-2-benzyl-3-oxo-2-pyrrolidinyl]-3-hydroxy-1-phenyl-2-butanyl}carbamate.
DR DrugBank; DB01732; (4R,5S,6S,7R)-1,3-dibenzyl-4,7-bis(phenoxymethyl)-5,6-dihydroxy-1,3 diazepan-2-one.
DR DrugBank; DB06874; (6-[4-(AMINOMETHYL)-2,6-DIMETHYLPHENOXY]-2-{[4-(AMINOMETHYL)PHENYL]AMINO}-5-BROMOPYRIMIDIN-4-YL)METHANOL.
DR DrugBank; DB08034; (E)-3,4-DIHYDROXY-N'-[(2-METHOXYNAPHTHALEN-1-YL)METHYLENE]BENZOHYDRAZIDE.
DR DrugBank; DB07961; 1-(4-Cyano-phenyl)-3-[2-(2,6-dichloro-phenyl)-1-imino-ethyl]-thiourea.
DR DrugBank; DB07451; 1-(5-BROMO-PYRIDIN-2-YL)-3-[2-(6-FLUORO-2-HYDROXY-3-PROPIONYL-PHENYL)-CYCLOPROPYL]-UREA.
DR DrugBank; DB08212; 1-[2-(3-ACETYL-2-HYDROXY-6-METHOXY-PHENYL)-CYCLOPROPYL]-3-(5-CYANO-PYRIDIN-2-YL)-THIOUREA.
DR DrugBank; DB08372; 1-[2-(4-ETHOXY-3-FLUOROPYRIDIN-2-YL)ETHYL]-3-(5-METHYLPYRIDIN-2-YL)THIOUREA.
DR DrugBank; DB02972; 1-Benzyl-(R)-Propylamine.
DR DrugBank; DB04190; 2,5-dibenzyloxy-3-hydroxy-hexanedioic acid bis-[(2-hydroxy-indan-1-yl)-amide].
DR DrugBank; DB04042; 2-[4-(Hydroxy-Methoxy-Methyl)-Benzyl]-7-(4-Hydroxymethyl-Benzyl)-1,1-Dioxo-3,6-Bis-Phenoxymethyl-1lambda6-[1,2,7]Thiadiazepane-4,5-Diol.
DR DrugBank; DB08428; 3(S)-AMINO-4-PHENYL-BUTAN-2(S)-OL.
DR DrugBank; DB03076; 3-[[(3R,4S,5S,6R)-7-Benzyl-4,5-dihydroxy-1,1-dioxo-3,6-bis(phenoxymethyl)-1,2,7-thiadiazepan-2-yl]methyl]-N-methylbenzamide.
DR DrugBank; DB03141; 3-{[(5R,6R)-5-Benzyl-6-hydroxy-2,4-bis(4-hydroxybenzyl)-3-oxo-1,2,4-triazepan-1-yl]sulfonyl}benzonitril.
DR DrugBank; DB08457; 4-(3,5-DIMETHYLPHENOXY)-5-(FURAN-2-YLMETHYLSULFANYLMETHYL)-3-IODO-6-METHYLPYRIDIN-2(1H)-ONE.
DR DrugBank; DB07343; 4-[4-AMINO-6-(2,6-DICHLORO-PHENOXY)-[1,3,5]TRIAZIN-2-YLAMINO]-BENZONITRILE.
DR DrugBank; DB07337; 4-[4-AMINO-6-(5-CHLORO-1H-INDOL-4-YLMETHYL)-[1,3,5]TRIAZIN-2-YLAMINO]-BENZONITRILE.
DR DrugBank; DB07018; 5-ETHYL-3-[(2-METHOXYETHYL)METHYLAMINO]-6-METHYL-4-(3-METHYLBENZYL)PYRIDIN-2(1H)-ONE.
DR DrugBank; DB07332; ALPHA-(2,6-DICHLOROPHENYL)-ALPHA-(2-ACETYL-5-METHYLANILINO)ACETAMIDE.
DR DrugBank; DB05398; C31G.
DR DrugBank; DB07578; CP-94707.
DR DrugBank; DB08639; Dapivirine.
DR DrugBank; DB06414; Etravirine.
DR DrugBank; DB04255; Inhibitor BEA388.
DR DrugBank; DB04547; Inhibitor BEA409.
DR DrugBank; DB02683; Inhibitor Bea428.
DR DrugBank; DB02009; L-756423.
DR DrugBank; DB03908; N,N-[2,5-O-[Dibenzyl]-glucaryl]-DI-[isoleucyl-amido-methane].
DR DrugBank; DB02629; N,N-[2,5-O-di-2-fluoro-benzyl-glucaryl]-di-[1-amino-indan-2-ol].
DR DrugBank; DB01887; N,N-[2,5-O-Dibenzyl-glucaryl]-DI-[1-amino-indan-2-OL].
DR DrugBank; DB03803; N,N-[2,5-O-dibenzyl-glucaryl]-DI-[valinyl-aminomethanyl-pyridine].
DR DrugBank; DB02033; N-(3-Cyclopropyl(5,6,7,8,9,10-Hexahydro-2-Oxo-2h-Cycloocta[B]Pyran-3-Yl)Methyl)Phenylbenzensulfonamide.
DR DrugBank; DB08281; O-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl] (4-bromophenyl)thiocarbamate.
DR DrugBank; DB08282; O-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl] (4-chlorophenyl)thiocarbamate.
DR DrugBank; DB08284; O-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl] (4-iodophenyl)thiocarbamate.
DR DrugBank; DB08414; PNU-142721.
DR DrugBank; DB08598; R-82913.
DR DrugBank; DB07327; R-95845.
DR DrugBank; DB07885; Talviraline.
DR DrugBank; DB02768; Tert-Butyloxycarbonyl Group.
DR DrugBank; DB08600; Tivirapine.
DR DrugBank; DB01891; Tl-3-093.
DR DrugBank; DB05871; UC-781.
DR MEROPS; A02.001; -.
DR iPTMnet; P03366; -.
DR ABCD; P03366; 16 sequenced antibodies.
DR BRENDA; 3.1.26.13; 16478.
DR SABIO-RK; P03366; -.
DR EvolutionaryTrace; P03366; -.
DR PRO; PR:P03366; -.
DR Proteomes; UP000007690; Genome.
DR Proteomes; UP000107234; Genome.
DR Proteomes; UP000126245; 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; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IDA:CACAO.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO: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: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; Direct protein sequencing;
KW DNA integration; DNA recombination; DNA-binding;
KW 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 Methylation; Modulation of host cell apoptosis by virus;
KW Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome; Repeat;
KW Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Viral genome integration; Viral nucleoprotein;
KW Viral penetration into host nucleus; Viral release from host cell; Virion;
KW Virion maturation; Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..1447
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000261261"
FT CHAIN 2..132
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042285"
FT CHAIN 133..363
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042286"
FT PEPTIDE 364..377
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042287"
FT CHAIN 378..432
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042288"
FT PEPTIDE 433..440
FT /note="Transframe peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000246710"
FT CHAIN 441..500
FT /note="p6-pol"
FT /evidence="ECO:0000255"
FT /id="PRO_0000042289"
FT CHAIN 501..599
FT /note="Protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038647"
FT CHAIN 600..1159
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042290"
FT CHAIN 600..1039
FT /note="p51 RT"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042291"
FT CHAIN 1040..1159
FT /note="p15"
FT /id="PRO_0000042292"
FT CHAIN 1160..1447
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042293"
FT DOMAIN 520..589
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 643..833
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1033..1156
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1213..1363
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 1162..1203
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1382..1429
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:0000250|UniProtKB:P04585"
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 human PPIA/CYPA and NUP153"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 277..363
FT /note="Dimerization/Multimerization of capsid protein p24"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 446..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..505
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 549..555
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 588..600
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 826..834
FT /note="RT 'primer grip'"
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 997..1013
FT /note="Tryptophan repeat motif"
FT ACT_SITE 525
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094,
FT ECO:0000269|PubMed:12924029"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT BINDING 784
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT BINDING 1042
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:0000305"
FT BINDING 1077
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:0000305"
FT BINDING 1097
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:0000305"
FT BINDING 1148
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:0000305"
FT BINDING 1171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1223
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 1275
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 1311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT SITE 132..133
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 221..222
FT /note="Cis/trans isomerization of proline peptide bond; by
FT human PPIA/CYPA"
FT /evidence="ECO:0000250"
FT SITE 363..364
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 377..378
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 432..433
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 440..441
FT /note="Cleavage; by viral protease"
FT SITE 500..501
FT /note="Cleavage; by viral protease"
FT SITE 599..600
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:2476069"
FT SITE 1000
FT /note="Essential for RT p66/p51 heterodimerization"
FT SITE 1013
FT /note="Essential for RT p66/p51 heterodimerization"
FT SITE 1039..1040
FT /note="Cleavage; by viral protease; partial"
FT SITE 1159..1160
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 387
FT /note="Asymmetric dimethylarginine; in Nucleocapsid protein
FT p7; by host PRMT6"
FT /evidence="ECO:0000269|PubMed:17415034"
FT MOD_RES 409
FT /note="Asymmetric dimethylarginine; in Nucleocapsid protein
FT p7; by host PRMT6"
FT /evidence="ECO:0000269|PubMed:17415034"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT VARIANT 297
FT /note="V -> L (in strain: Isolate PV22)"
FT VARIANT 434
FT /note="L -> F"
FT VARIANT 771
FT /note="K -> R (in strain: Isolate PV22)"
FT VARIANT 1050
FT /note="K -> R (in strain: Isolate PV22)"
FT VARIANT 1057
FT /note="V -> L (in strain: Isolate PV22)"
FT VARIANT 1111
FT /note="K -> Q (in strain: Isolate PV22)"
FT VARIANT 1128
FT /note="E -> Q (in strain: Isolate PV22)"
FT MUTAGEN 440
FT /note="F->I: Complete loss of cleavage between NC and TF."
FT /evidence="ECO:0000269|PubMed:11172099"
FT MUTAGEN 500
FT /note="F->I: Complete loss of cleavage between TF and p15."
FT /evidence="ECO:0000269|PubMed:11172099"
FT MUTAGEN 651
FT /note="P->G: 74% loss of polymerase activity. 86% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 654
FT /note="P->G: 64% loss of polymerase activity. 57% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 664
FT /note="K->A: Strong decrease in RT binding affinity for all
FT dNTP substrates and in catalytic efficiency. 100-fold
FT decreased sensitivity to ddNTP inhibitors."
FT /evidence="ECO:0000269|PubMed:10794716"
FT MUTAGEN 664
FT /note="K->E: Strong decrease in RT binding affinity for all
FT dNTP substrates and in catalytic efficiency. 100-fold
FT decreased sensitivity to ddNTP inhibitors."
FT /evidence="ECO:0000269|PubMed:10794716"
FT MUTAGEN 664
FT /note="K->Q: Strong decrease in RT binding affinity for all
FT dNTP substrates and in catalytic efficiency. 100-fold
FT decreased sensitivity to ddNTP inhibitors."
FT /evidence="ECO:0000269|PubMed:10794716"
FT MUTAGEN 664
FT /note="K->R: 10-fold decreased sensitivity to ddATP and
FT ddCTP inhibitors."
FT /evidence="ECO:0000269|PubMed:10794716"
FT MUTAGEN 673
FT /note="L->V: No loss of polymerase activity. No loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 709
FT /note="D->A: 5- to 12-fold decrease in affinity for dTTP
FT substrates. Strongly decreased RNA-directed and DNA-
FT directed DNA polymerase activities. No effect on RNase H
FT activity. Loss of pyrophosphorolysis (reverse of the
FT polymerase reaction)."
FT /evidence="ECO:0000269|PubMed:8794733"
FT MUTAGEN 709
FT /note="D->S: 5- to 12-fold decrease in affinity for dTTP
FT substrates. Strongly decreased RNA-directed DNA polymerase
FT activity. Slightly decreased DNA-directed DNA polymerase
FT activity. No effect on RNase H activity. Loss of
FT pyrophosphorolysis (reverse of the polymerase reaction)."
FT /evidence="ECO:0000269|PubMed:8794733"
FT MUTAGEN 752
FT /note="W->A: 73% loss of DNA-directed DNA polymerase
FT activity. 70% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 752
FT /note="W->F: 10% loss of DNA-directed DNA polymerase
FT activity. 22% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 752
FT /note="W->Y: 58% loss of DNA-directed DNA polymerase
FT activity. 42% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 755
FT /note="S->A: 74% loss of polymerase activity. 56% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 755
FT /note="S->G: Complete loss of polymerase activity. No loss
FT of RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 755
FT /note="S->T: Complete loss of polymerase activity. No loss
FT of RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 756
FT /note="P->G: 34% loss of polymerase activity. No loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 766
FT /note="I->A: 71% loss of DNA-directed DNA polymerase
FT activity. 61% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 766
FT /note="I->D: 16% loss of DNA-directed DNA polymerase
FT activity. 24% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 766
FT /note="I->L: 80% loss of DNA-directed DNA polymerase
FT activity. 23% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 766
FT /note="I->T: 34% increase of DNA-directed DNA polymerase
FT activity. 18% increase of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 766
FT /note="I->V: 70% loss of DNA-directed DNA polymerase
FT activity. 64% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 782
FT /note="Y->A: Almost complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:9657675"
FT MUTAGEN 782
FT /note="Y->F: 70% loss of polymerase activity. No loss of
FT polymerase activity; when associated with V-783."
FT /evidence="ECO:0000269|PubMed:9657675"
FT MUTAGEN 783
FT /note="M->I: 54% loss of polymerase activity according to
FT PubMed:9533880; increases polymerase activity according to
FT PubMed:9657675. No loss of RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 783
FT /note="M->L: 90% loss of polymerase activity. No loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 783
FT /note="M->V: 58% loss of polymerase activity. No loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 784
FT /note="D->A: Strongly decreased RNA-directed and DNA-
FT directed DNA polymerase activities. No effect on RNase H
FT activity."
FT /evidence="ECO:0000269|PubMed:8794733,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 784
FT /note="D->E: Strongly decreased RNA-directed and DNA-
FT directed DNA polymerase activities. No effect on RNase H
FT activity."
FT /evidence="ECO:0000269|PubMed:8794733,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 784
FT /note="D->N: Strongly decreased RNA-directed and DNA-
FT directed DNA polymerase activities. No effect on RNase H
FT activity."
FT /evidence="ECO:0000269|PubMed:8794733,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 785
FT /note="D->A: Strongly decreased RNA-directed and DNA-
FT directed DNA polymerase activities. Loss of
FT pyrophosphorolysis (reverse of the polymerase reaction). No
FT effect on RNase H activity."
FT /evidence="ECO:0000269|PubMed:8794733,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 785
FT /note="D->E: Drastically reduced incorporation of
FT phosphorothioate nucleotide. Loss of pyrophosphorolysis
FT (reverse of the polymerase reaction). No effect on RNase H
FT activity."
FT /evidence="ECO:0000269|PubMed:8794733,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 785
FT /note="D->N: Loss of pyrophosphorolysis (reverse of the
FT polymerase reaction). No effect on RNase H activity."
FT /evidence="ECO:0000269|PubMed:8794733,
FT ECO:0000269|PubMed:9657675"
FT MUTAGEN 786
FT /note="L->A: 76% loss of DNA-directed DNA polymerase
FT activity. 60% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 786
FT /note="L->I: 29% loss of DNA-directed DNA polymerase
FT activity. 46% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 786
FT /note="L->R: 20% loss of DNA-directed DNA polymerase
FT activity. 21% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 786
FT /note="L->V: 22% loss of DNA-directed DNA polymerase
FT activity. No loss of RNA-directed DNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 788
FT /note="V->A: 37% increase of DNA-directed DNA polymerase
FT activity. No loss of RNA-directed DNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 788
FT /note="V->I: 25% increase of DNA-directed DNA polymerase
FT activity. No loss of RNA-directed DNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 788
FT /note="V->M: 27% increase of DNA-directed DNA polymerase
FT activity. 10% loss of RNA-directed DNA polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:12501197"
FT MUTAGEN 823
FT /note="E->A: No effect on RNA-dependent DNA polymerase
FT activity. No effect on RNA 5'-end and 3'-end cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 824
FT /note="P->A: No effect on RNA-dependent DNA polymerase
FT activity. No effect on RNA 5'-end and 3'-end cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 825
FT /note="P->A: No effect on RNA-dependent DNA polymerase
FT activity. Complete loss of RNA 5'-end cleavage. No effect
FT on RNA 3'-end cleavage."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 826
FT /note="F->A: No effect on RNA-dependent DNA polymerase
FT activity. Complete loss of RNA 5'-end cleavage. No effect
FT on RNA 3'-end cleavage."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 827
FT /note="L->A: No effect on RNA-dependent DNA polymerase
FT activity. No effect on RNA 5'-end and 3'-end cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 828
FT /note="W->A: Complete loss of RNA-dependent DNA polymerase
FT activity. No effect on RNA 5'-end and 3'-end cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 829
FT /note="M->A: No effect on RNA-dependent DNA polymerase
FT activity. No effect on RNA 5'-end and 3'-end cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 830
FT /note="G->A: Complete loss of RNA-dependent DNA polymerase
FT activity. Complete loss of RNA 5'-end and 3'-end
FT cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 831
FT /note="Y->A: Complete loss of RNA-dependent DNA polymerase
FT activity. Complete loss of RNA 5'-end and 3'-end
FT cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 832
FT /note="E->A: Complete loss of RNA-dependent DNA polymerase
FT activity. Complete loss of RNA 5'-end and 3'-end
FT cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 834
FT /note="H->A: Complete loss of RNA-dependent DNA polymerase
FT activity. Complete loss of RNA 5'-end and 3'-end
FT cleavages."
FT /evidence="ECO:0000269|PubMed:9111014"
FT MUTAGEN 856
FT /note="I->T: 96% loss of polymerase activity. 45% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 861
FT /note="G->A: Complete loss of polymerase activity. 25% loss
FT of RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 863
FT /note="L->S: 17% loss of polymerase activity. 30% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 865
FT /note="W->T: Complete loss of polymerase activity. 87% loss
FT of RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 878
FT /note="L->S: 21% loss of polymerase activity. 16% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 898
FT /note="A->L: 68% loss of polymerase activity. 10% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 902
FT /note="L->S: 59% loss of polymerase activity. 8% loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 909
FT /note="L->S: 31% loss of polymerase activity. No loss of
FT RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 997
FT /note="W->L: No effect on RT p66/p51 heterodimerization."
FT /evidence="ECO:0000269|PubMed:12559908"
FT MUTAGEN 1000
FT /note="W->A: Almost complete loss of RT p66/p51
FT heterodimerization. Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:12559908,
FT ECO:0000269|PubMed:15852304"
FT MUTAGEN 1000
FT /note="W->F: No effect on RT p66/p51 heterodimerization."
FT /evidence="ECO:0000269|PubMed:12559908,
FT ECO:0000269|PubMed:15852304"
FT MUTAGEN 1000
FT /note="W->L: Almost complete loss of RT p66/p51
FT heterodimerization. Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:12559908,
FT ECO:0000269|PubMed:15852304"
FT MUTAGEN 1001
FT /note="W->L: No effect on RT p66/p51 heterodimerization."
FT /evidence="ECO:0000269|PubMed:12559908"
FT MUTAGEN 1004
FT /note="Y->L: No effect on RT p66/p51 heterodimerization."
FT /evidence="ECO:0000269|PubMed:12559908"
FT MUTAGEN 1005
FT /note="W->L: Decreased RT p66/p51 heterodimerization."
FT /evidence="ECO:0000269|PubMed:12559908"
FT MUTAGEN 1009
FT /note="W->L: No effect on RT p66/p51 heterodimerization."
FT /evidence="ECO:0000269|PubMed:12559908"
FT MUTAGEN 1013
FT /note="W->L: Almost complete loss of RT p66/p51
FT heterodimerization."
FT /evidence="ECO:0000269|PubMed:12559908"
FT MUTAGEN 1036
FT /note="A->I: Replication slightly delayed."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1037
FT /note="E->N: Virions contain primarily p51 RT."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1038
FT /note="T->S: Almost complete loss of virion production;
FT when associated with G-1041."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1039
FT /note="F->A: Virions contain primarily p51 RT."
FT /evidence="ECO:0000269|PubMed:16140771,
FT ECO:0000269|PubMed:2044756"
FT MUTAGEN 1039
FT /note="F->I: Loss of cleavage between p51 RT and p15."
FT /evidence="ECO:0000269|PubMed:16140771,
FT ECO:0000269|PubMed:2044756"
FT MUTAGEN 1039
FT /note="F->L: No effect on cleavage between p51 RT and p15."
FT /evidence="ECO:0000269|PubMed:16140771,
FT ECO:0000269|PubMed:2044756"
FT MUTAGEN 1039
FT /note="F->V: Slight delays in replication. Virions contain
FT primarily p51 RT."
FT /evidence="ECO:0000269|PubMed:16140771,
FT ECO:0000269|PubMed:2044756"
FT MUTAGEN 1039
FT /note="F->W: Slight delays in replication. Virions contain
FT primarily p51 RT."
FT /evidence="ECO:0000269|PubMed:16140771,
FT ECO:0000269|PubMed:2044756"
FT MUTAGEN 1040
FT /note="Y->A: Virions contain primarily p51 RT; when
FT associated with A-1039."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1040
FT /note="Y->I: Almost complete loss of virion production;
FT when associated with K-1041."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1040
FT /note="Y->W: Virions contain primarily p51 RT; when
FT associated with W-1039."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1041
FT /note="V->G: Almost complete loss of virion production;
FT when associated with S-1038."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1041
FT /note="V->K: Almost complete loss of virion production;
FT when associated with I-1038."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1041
FT /note="V->S: Slight delays in replication."
FT /evidence="ECO:0000269|PubMed:16140771"
FT MUTAGEN 1077
FT /note="E->Q: No loss of polymerase activity. complete loss
FT of RNase H activity."
FT /evidence="ECO:0000269|PubMed:9533880"
FT MUTAGEN 1100
FT /note="Y->A,G,H,L,S,Q: Complete loss of RNAase H activity."
FT /evidence="ECO:0000269|PubMed:11684697"
FT MUTAGEN 1100
FT /note="Y->E: Almost complete loss of RNAase H activity."
FT /evidence="ECO:0000269|PubMed:11684697"
FT MUTAGEN 1100
FT /note="Y->F: Almost no effect on RNAase H activity and
FT replication."
FT /evidence="ECO:0000269|PubMed:11684697"
FT MUTAGEN 1100
FT /note="Y->R: Almost no effect on RNAase H activity. Unable
FT to replicate. Completely resistant to inhibition by BBNH."
FT /evidence="ECO:0000269|PubMed:11684697"
FT MUTAGEN 1100
FT /note="Y->W: Almost no effect on RNAase H activity and
FT replication. 6-fold resistance to inhibition by BBNH."
FT /evidence="ECO:0000269|PubMed:11684697"
FT MUTAGEN 1138
FT /note="H->D,N: Severely reduces exonuclease activity of
FT RNase H. Probably also reduces substrate binding affinity.
FT Modifies cleavage preferences of RNase H. No effect on the
FT endonuclease activity."
FT /evidence="ECO:0000269|PubMed:1714505"
FT MUTAGEN 1138
FT /note="H->D: Severely reduced exonuclease activity of RNase
FT H, but no effect on endonucleonuclease activity."
FT /evidence="ECO:0000269|PubMed:1714505"
FT MUTAGEN 1138
FT /note="H->N: Severely reduced exonuclease activity of RNase
FT H, but no effect on endonucleonuclease activity."
FT /evidence="ECO:0000269|PubMed:1714505"
FT MUTAGEN 1159
FT /note="L->F: No effect on cleavage between reverse
FT transcriptase/ribonuclease H and integrase."
FT /evidence="ECO:0000269|PubMed:2044756"
FT MUTAGEN 1159
FT /note="L->I: Loss of cleavage between reverse
FT transcriptase/ribonuclease H and integrase."
FT /evidence="ECO:0000269|PubMed:2044756"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:2EXF"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:2EXF"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:2EXF"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:2EXF"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2EXF"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2EXF"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:2L4L"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:1MER"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 552..566
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 569..578
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 581..585
FT /evidence="ECO:0007829|PDB:5JG1"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:3NU3"
FT TURN 591..594
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:3NU3"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:1S9G"
FT STRAND 611..614
FT /evidence="ECO:0007829|PDB:7KRF"
FT HELIX 627..642
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:1S9E"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 665..668
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 677..682
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 684..687
FT /evidence="ECO:0007829|PDB:4PQU"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:4ICL"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 699..701
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:3ITH"
FT HELIX 713..716
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 721..727
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 734..736
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:5VQV"
FT STRAND 741..747
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:3IG1"
FT HELIX 755..773
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:5TXL"
FT STRAND 777..782
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 785..790
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 794..808
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 809..811
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 817..819
FT /evidence="ECO:0007829|PDB:5D3G"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:1R0A"
FT STRAND 824..828
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 835..837
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 849..852
FT /evidence="ECO:0007829|PDB:2ZD1"
FT HELIX 853..866
FT /evidence="ECO:0007829|PDB:4G1Q"
FT TURN 867..869
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 870..872
FT /evidence="ECO:0007829|PDB:6AOC"
FT HELIX 876..879
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:4G1Q"
FT TURN 883..885
FT /evidence="ECO:0007829|PDB:4O4G"
FT STRAND 888..891
FT /evidence="ECO:0007829|PDB:2IAJ"
FT HELIX 896..908
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 909..911
FT /evidence="ECO:0007829|PDB:6DUH"
FT STRAND 913..915
FT /evidence="ECO:0007829|PDB:6AOC"
FT STRAND 920..922
FT /evidence="ECO:0007829|PDB:2BE2"
FT STRAND 925..932
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 935..943
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 946..954
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 957..961
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 963..982
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 987..992
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 994..1003
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1004..1006
FT /evidence="ECO:0007829|PDB:6AOC"
FT STRAND 1012..1015
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1017..1019
FT /evidence="ECO:0007829|PDB:3HVT"
FT HELIX 1020..1022
FT /evidence="ECO:0007829|PDB:2IAJ"
FT HELIX 1023..1026
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1029..1031
FT /evidence="ECO:0007829|PDB:1HQU"
FT STRAND 1036..1045
FT /evidence="ECO:0007829|PDB:4G1Q"
FT TURN 1047..1049
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1052..1058
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1059..1061
FT /evidence="ECO:0007829|PDB:1HQE"
FT STRAND 1063..1070
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 1073..1087
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1090..1096
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 1099..1105
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1110..1114
FT /evidence="ECO:0007829|PDB:4G1Q"
FT HELIX 1115..1126
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1128..1134
FT /evidence="ECO:0007829|PDB:4G1Q"
FT STRAND 1137..1139
FT /evidence="ECO:0007829|PDB:2ZD1"
FT STRAND 1140..1142
FT /evidence="ECO:0007829|PDB:1SUQ"
FT HELIX 1144..1152
FT /evidence="ECO:0007829|PDB:4G1Q"
FT TURN 1153..1155
FT /evidence="ECO:0007829|PDB:4QAG"
FT STRAND 1219..1227
FT /evidence="ECO:0007829|PDB:3AVI"
FT STRAND 1230..1237
FT /evidence="ECO:0007829|PDB:3AVI"
FT TURN 1238..1240
FT /evidence="ECO:0007829|PDB:3AVI"
FT STRAND 1243..1250
FT /evidence="ECO:0007829|PDB:3AVI"
FT HELIX 1253..1266
FT /evidence="ECO:0007829|PDB:3AVI"
FT STRAND 1271..1273
FT /evidence="ECO:0007829|PDB:3AVI"
FT HELIX 1277..1281
FT /evidence="ECO:0007829|PDB:3AVI"
FT HELIX 1283..1292
FT /evidence="ECO:0007829|PDB:3AVI"
FT STRAND 1295..1297
FT /evidence="ECO:0007829|PDB:3AVI"
FT HELIX 1305..1324
FT /evidence="ECO:0007829|PDB:3AVI"
FT HELIX 1325..1327
FT /evidence="ECO:0007829|PDB:3AVI"
FT HELIX 1331..1344
FT /evidence="ECO:0007829|PDB:3AVI"
FT HELIX 1355..1367
FT /evidence="ECO:0007829|PDB:3AVI"
FT STRAND 1380..1386
FT /evidence="ECO:0007829|PDB:1QMC"
FT STRAND 1395..1403
FT /evidence="ECO:0007829|PDB:1QMC"
FT STRAND 1405..1420
FT /evidence="ECO:0007829|PDB:1QMC"
FT HELIX 1421..1423
FT /evidence="ECO:0007829|PDB:1QMC"
FT STRAND 1424..1428
FT /evidence="ECO:0007829|PDB:1QMC"
SQ SEQUENCE 1447 AA; 163288 MW; AC3EE1439592E0AD CRC64;
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA
DTGHSSQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA
RVLAEAMSQV TNTATIMMQR GNFRNQRKMV KCFNCGKEGH TARNCRAPRK KGCWKCGKEG
HQMKDCTERQ ANFLREDLAF LQGKAREFSS EQTRANSPTI SSEQTRANSP TRRELQVWGR
DNNSPSEAGA DRQGTVSFNF PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG
RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP
ISPIETVPVK LKPGMDGPKV KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF
AIKKKDSTKW RKLVDFRELN KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD
EDFRKYTAFT IPSINNETPG IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF KKQNPDIVIY
QYMDDLYVGS DLEIGQHRTK IEELRQHLLR WGLTTPDKKH QKEPPFLWMG YELHPDKWTV
QPIVLPEKDS WTVNDIQKLV GKLNWASQIY PGIKVRQLCK LLRGTKALTE VIPLTEEAEL
ELAENREILK EPVHGVYYDP SKDLIAEIQK QGQGQWTYQI YQEPFKNLKT GKYARMRGAH
TNDVKQLTEA VQKITTESIV IWGKTPKFKL PIQKETWETW WTEYWQATWI PEWEFVNTPP
LVKLWYQLEK EPIVGAETFY VDGAANRETK LGKAGYVTNK GRQKVVPLTN TTNQKTELQA
IYLALQDSGL EVNIVTDSQY ALGIIQAQPD KSESELVNQI IEQLIKKEKV YLAWVPAHKG
IGGNEQVDKL VSAGIRKILF LDGIDKAQDE HEKYHSNWRA MASDFNLPPV VAKEIVASCD
KCQLKGEAMH GQVDCSPGIW QLDCTHLEGK VILVAVHVAS GYIEAEVIPA ETGQETAYFL
LKLAGRWPVK TIHTDNGSNF TSATVKAACW WAGIKQEFGI PYNPQSQGVV ESMNKELKKI
IGQVRDQAEH LKTAVQMAVF IHNFKRKGGI GGYSAGERIV DIIATDIQTK ELQKQITKIQ
NFRVYYRDSR NPLWKGPAKL LWKGEGAVVI QDNSDIKVVP RRKAKIIRDY GKQMAGDDCV
ASRQDED
