POL_HV1N5
ID POL_HV1N5 Reviewed; 1435 AA.
AC P12497;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Gag-Pol polyprotein;
DE AltName: Full=Pr160Gag-Pol;
DE Contains:
DE RecName: Full=Matrix protein p17;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=Spacer peptide 1 {ECO:0000303|PubMed:22334652};
DE Short=SP1;
DE AltName: Full=p2;
DE Contains:
DE RecName: Full=Nucleocapsid protein p7;
DE Short=NC;
DE Contains:
DE RecName: Full=Transframe peptide;
DE Short=TF;
DE Contains:
DE RecName: Full=p6-pol;
DE Short=p6*;
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.16;
DE AltName: Full=PR;
DE AltName: Full=Retropepsin;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE EC=2.7.7.49;
DE EC=2.7.7.7;
DE EC=3.1.26.13;
DE AltName: Full=Exoribonuclease H;
DE EC=3.1.13.2;
DE AltName: Full=p66 RT;
DE Contains:
DE RecName: Full=p51 RT;
DE Contains:
DE RecName: Full=p15;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
GN Name=gag-pol;
OS Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11698;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone pNL4-3;
RA Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.;
RL Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION TO 545.
RA Strebel K.J., Martin M.A.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH HOST GP41 (MATRIX PROTEIN P17).
RX PubMed=8918455; DOI=10.1002/j.1460-2075.1996.tb00964.x;
RA Cosson P.;
RT "Direct interaction between the envelope and matrix proteins of HIV-1.";
RL EMBO J. 15:5783-5788(1996).
RN [4]
RP INTERACTION WITH HUMAN AP3D1 (MATRIX PROTEIN P17).
RX PubMed=15766529; DOI=10.1016/j.cell.2004.12.023;
RA Dong X., Li H., Derdowski A., Ding L., Burnett A., Chen X., Peters T.R.,
RA Dermody T.S., Woodruff E., Wang J.J., Spearman P.;
RT "AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a key
RT role in particle assembly.";
RL Cell 120:663-674(2005).
RN [5]
RP INTERACTION WITH HUMAN NUP153 (INTEGRASE).
RC STRAIN=Clone pNL4-3;
RX PubMed=19369352; DOI=10.1128/jvi.02061-08;
RA Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.;
RT "Integrase interacts with nucleoporin NUP153 to mediate the nuclear import
RT of human immunodeficiency virus type 1.";
RL J. Virol. 83:6522-6533(2009).
RN [6]
RP MUTAGENESIS OF SER-9; SER-67; SER-72 AND SER-77.
RX PubMed=19059618; DOI=10.1016/j.virol.2008.10.047;
RA Bhatia A.K., Kaushik R., Campbell N.A., Pontow S.E., Ratner L.;
RT "Mutation of critical serine residues in HIV-1 matrix result in an envelope
RT incorporation defect which can be rescued by truncation of the gp41
RT cytoplasmic tail.";
RL Virology 384:233-241(2009).
RN [7]
RP SUBCELLULAR LOCATION (GAG-POL POLYPROTEIN).
RX PubMed=19297499; DOI=10.1128/jvi.00109-09;
RA Joshi A., Ablan S.D., Soheilian F., Nagashima K., Freed E.O.;
RT "Evidence that productive human immunodeficiency virus type 1 assembly can
RT occur in an intracellular compartment.";
RL J. Virol. 83:5375-5387(2009).
RN [8]
RP INTERACTION WITH RAT CALM1 (MATRIX PROTEIN P17).
RX PubMed=21799007; DOI=10.1074/jbc.m111.273623;
RA Samal A.B., Ghanam R.H., Fernandez T.F., Monroe E.B., Saad J.S.;
RT "NMR, biophysical, and biochemical studies reveal the minimal Calmodulin
RT binding domain of the HIV-1 matrix protein.";
RL J. Biol. Chem. 286:33533-33543(2011).
RN [9]
RP PROTEOLYTIC PROCESSING (GAG-POL POLYPROTEIN).
RX PubMed=22334652; DOI=10.1074/jbc.m112.339374;
RA Lee S.K., Potempa M., Kolli M., Ozen A., Schiffer C.A., Swanstrom R.;
RT "Context surrounding processing sites is crucial in determining cleavage
RT rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol
RT polyprotein precursors by viral protease.";
RL J. Biol. Chem. 287:13279-13290(2012).
RN [10]
RP INTERACTION WITH HUMAN NUP153 (CAPSID PROTEIN P24).
RC STRAIN=Clone pNL4-3;
RX PubMed=24130490; DOI=10.1371/journal.ppat.1003693;
RA Matreyek K.A., Yucel S.S., Li X., Engelman A.;
RT "Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding
RT pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.";
RL PLoS Pathog. 9:E1003693-E1003693(2013).
RN [11]
RP SUBUNIT (CAPSID PROTEIN P24).
RX PubMed=24066695; DOI=10.1021/ja406246z;
RA Deshmukh L., Schwieters C.D., Grishaev A., Ghirlando R., Baber J.L.,
RA Clore G.M.;
RT "Structure and dynamics of full-length HIV-1 capsid protein in solution.";
RL J. Am. Chem. Soc. 135:16133-16147(2013).
RN [12]
RP RNA-BINDING (MATRIX PROTEIN P17).
RX PubMed=23552424; DOI=10.1128/jvi.00075-13;
RA Chukkapalli V., Inlora J., Todd G.C., Ono A.;
RT "Evidence in support of RNA-mediated inhibition of phosphatidylserine-
RT dependent HIV-1 Gag membrane binding in cells.";
RL J. Virol. 87:7155-7159(2013).
RN [13]
RP PHOSPHORYLATION AT SER-148 (CAPSID PROTEIN P24).
RX PubMed=24509437; DOI=10.1099/vir.0.060053-0;
RA Dochi T., Nakano T., Inoue M., Takamune N., Shoji S., Sano K., Misumi S.;
RT "Phosphorylation of human immunodeficiency virus type 1 capsid protein at
RT serine 16, required for peptidyl-prolyl isomerase-dependent uncoating, is
RT mediated by virion-incorporated extracellular signal-regulated kinase 2.";
RL J. Gen. Virol. 95:1156-1166(2014).
RN [14]
RP REVIEW.
RX PubMed=8791726; DOI=10.1007/978-3-642-80145-7_4;
RA Vogt V.M.;
RT "Proteolytic processing and particle maturation.";
RL Curr. Top. Microbiol. Immunol. 214:95-131(1996).
RN [15]
RP REVIEW.
RX PubMed=9878383; DOI=10.1006/jmbi.1998.2354;
RA Turner B.G., Summers M.F.;
RT "Structural biology of HIV.";
RL J. Mol. Biol. 285:1-32(1999).
RN [16]
RP REVIEW.
RX PubMed=11700285; DOI=10.1146/annurev.genet.35.102401.090551;
RA Negroni M., Buc H.;
RT "Mechanisms of retroviral recombination.";
RL Annu. Rev. Genet. 35:275-302(2001).
RN [17]
RP REVIEW.
RX PubMed=11983066; DOI=10.1186/gb-2002-3-4-reviews3006;
RA Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.;
RT "Retroviral proteases.";
RL Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002).
RN [18]
RP REVIEW.
RX PubMed=12873766; DOI=10.1016/s0005-2736(03)00163-9;
RA Scarlata S., Carter C.;
RT "Role of HIV-1 Gag domains in viral assembly.";
RL Biochim. Biophys. Acta 1614:62-72(2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 489-587.
RX PubMed=2645523; DOI=10.1038/337615a0;
RA Navia M.A., Fitzgerald P.M.D., McKeever B.M., Leu C.-T., Heimbach J.C.,
RA Herber W.K., Sigal I.S., Darke P.L., Springer J.P.;
RT "Three-dimensional structure of aspartyl protease from human
RT immunodeficiency virus HIV-1.";
RL Nature 337:615-620(1989).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587.
RX PubMed=2548279; DOI=10.1126/science.2548279;
RA Wlodawer A., Miller M., Jaskolski M., Sathyanarayana B.K., Baldwin E.,
RA Weber I.T., Selk L.M., Clawson L., Schneider J., Kent S.B.H.;
RT "Conserved folding in retroviral proteases: crystal structure of a
RT synthetic HIV-1 protease.";
RL Science 245:616-621(1989).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587.
RX PubMed=2201682; DOI=10.1016/s0021-9258(18)77288-8;
RA Fitzgerald P.M.D., McKeever B.M., van Middlesworth J.F., Springer J.P.,
RA Heimbach J.C., Leu C.-T., Herber W.K., Dixon R.A.F., Darke P.L.;
RT "Crystallographic analysis of a complex between human immunodeficiency
RT virus type 1 protease and acetyl-pepstatin at 2.0-A resolution.";
RL J. Biol. Chem. 265:14209-14219(1990).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 489-587.
RX PubMed=2200122; DOI=10.1126/science.2200122;
RA Erickson J., Neidhart D.J., Vandrie J., Kempf D.J., Wang X.C.,
RA Norbeck D.W., Plattner J.J., Rittenhouse J.W., Turon M., Wideburg N.E.,
RA Kohlbrenner W.E., Simmer R., Helfrich R., Paul D.A., Knigge M.;
RT "Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor
RT complexed to HIV-1 protease.";
RL Science 249:527-533(1990).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 133-283.
RX PubMed=2123631; DOI=10.1089/aid.1990.6.1169;
RA Ehrlich L.S., Krausslich H.G., Wimmer E., Carter C.A.;
RT "Expression in Escherichia coli and purification of human immunodeficiency
RT virus type 1 capsid protein (p24).";
RL AIDS Res. Hum. Retroviruses 6:1169-1175(1990).
RN [24]
RP STRUCTURE BY NMR OF 1-132.
RX PubMed=7966331; DOI=10.1006/jmbi.1994.1719;
RA Massiah M.A., Starich M.R., Paschall C., Summers M.F., Christensen A.M.,
RA Sundquist W.I.;
RT "Three-dimensional structure of the human immunodeficiency virus type 1
RT matrix protein.";
RL J. Mol. Biol. 244:198-223(1994).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE
RP INHIBITOR L-736,524.
RX PubMed=7929352; DOI=10.1016/s0021-9258(18)47199-2;
RA Chen Z., Li Y., Chen E., Hall D.L., Darke P.L., Culberson C., Shafer J.A.,
RA Kuo L.C.;
RT "Crystal structure at 1.9-A resolution of human immunodeficiency virus
RT (HIV) II protease complexed with L-735,524, an orally bioavailable
RT inhibitor of the HIV proteases.";
RL J. Biol. Chem. 269:26344-26348(1994).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1197-1359.
RX PubMed=7801124; DOI=10.1126/science.7801124;
RA Dyda F., Hickman A.B., Jenkins T.M., Engelman A., Craigie R., Davies D.R.;
RT "Crystal structure of the catalytic domain of HIV-1 integrase: similarity
RT to other polynucleotidyl transferases.";
RL Science 266:1981-1986(1994).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-132.
RX PubMed=8610175; DOI=10.1073/pnas.93.7.3099;
RA Hill C.P., Worthylake D.K., Bancroft D.P., Christensen A.M.,
RA Sundquist W.I.;
RT "Crystal structures of the trimeric human immunodeficiency virus type 1
RT matrix protein: implications for membrane association and assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3099-3104(1996).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 133-277, AND INTERACTION WITH
RP HUMAN PPIA/CYPA (CAPSID PROTEIN P24).
RX PubMed=8980234; DOI=10.1016/s0092-8674(00)81823-1;
RA Gamble T.R., Vajdos F.F., Yoo S., Worthylake D.K., Houseweart M.,
RA Sundquist W.I., Hill C.P.;
RT "Crystal structure of human cyclophilin A bound to the amino-terminal
RT domain of HIV-1 capsid.";
RL Cell 87:1285-1294(1996).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1197-1359, AND ACTIVE SITES
RP (INTEGRASE).
RX PubMed=8977101; DOI=10.1016/s0014-5793(96)01236-7;
RA Bujacz G., Alexandratos J., Qing Z.L., Clement-Mella C., Wlodawer A.;
RT "The catalytic domain of human immunodeficiency virus integrase: ordered
RT active site in the F185H mutant.";
RL FEBS Lett. 398:175-178(1996).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 278-377.
RX PubMed=9346481; DOI=10.1126/science.278.5339.849;
RA Gamble T.R., Yoo S., Vajdos F.F., von Schwedler U.K., Worthylake D.K.,
RA Wang H., McCutcheon J.P., Sundquist W.I., Hill C.P.;
RT "Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid
RT protein.";
RL Science 278:849-853(1997).
RN [31]
RP STRUCTURE BY NMR OF 1148-1202.
RX PubMed=9228950; DOI=10.1038/nsb0797-567;
RA Cai M., Zheng R., Caffrey M., Craigie R., Clore G.M., Gronenborn A.M.;
RT "Solution structure of the N-terminal zinc binding domain of HIV-1
RT integrase.";
RL Nat. Struct. Biol. 4:567-577(1997).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1197-1356.
RX PubMed=9689049; DOI=10.1073/pnas.95.16.9150;
RA Goldgur Y., Dyda F., Hickman A.B., Jenkins T.M., Craigie R., Davies D.R.;
RT "Three new structures of the core domain of HIV-1 integrase: an active site
RT that binds magnesium.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9150-9154(1998).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1197-1359.
RX PubMed=10413462; DOI=10.1021/bi9907173;
RA Greenwald J., Le V., Butler S.L., Bushman F.D., Choe S.;
RT "The mobility of an HIV-1 integrase active site loop is correlated with
RT catalytic activity.";
RL Biochemistry 38:8892-8898(1999).
RN [34]
RP STRUCTURE BY NMR OF 133-283.
RX PubMed=12032547; DOI=10.1038/nsb806;
RA Tang C., Ndassa Y., Summers M.F.;
RT "Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag
RT polyprotein.";
RL Nat. Struct. Biol. 9:537-543(2002).
RN [35]
RP STRUCTURE BY NMR OF 1-132.
RX PubMed=14699046; DOI=10.1073/pnas.0305665101;
RA Tang C., Loeliger E., Luncsford P., Kinde I., Beckett D., Summers M.F.;
RT "Entropic switch regulates myristate exposure in the HIV-1 matrix
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:517-522(2004).
RN [36]
RP STRUCTURE BY NMR OF 2-132, INTERACTION WITH PHOSPHATIDYLINOSITOL
RP 4,5-BISPHOSPHATE (MATRIX PROTEIN P17), AND FUNCTION (MATRIX PROTEIN P17).
RX PubMed=16840558; DOI=10.1073/pnas.0602818103;
RA Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., Summers M.F.;
RT "Structural basis for targeting HIV-1 Gag proteins to the plasma membrane
RT for virus assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11364-11369(2006).
CC -!- FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the
CC essential events in virion assembly, including binding the plasma
CC membrane, making the protein-protein interactions necessary to create
CC spherical particles, recruiting the viral Env proteins, and packaging
CC the genomic RNA via direct interactions with the RNA packaging sequence
CC (Psi). Gag-Pol polyprotein may regulate its own translation, by the
CC binding genomic RNA in the 5'-UTR. At low concentration, the
CC polyprotein would promote translation, whereas at high concentration,
CC the polyprotein would encapsidate genomic RNA and then shut off
CC translation. {ECO:0000250}.
CC -!- FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma
CC membrane via a multipartite membrane-binding signal, that includes its
CC myristoylated N-terminus (PubMed:16840558). Matrix protein is part of
CC the pre-integration complex. Implicated in the release from host cell
CC mediated by Vpu. Binds to RNA. {ECO:0000250,
CC ECO:0000269|PubMed:16840558, ECO:0000269|PubMed:23552424}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the conical core that
CC encapsulates the genomic RNA-nucleocapsid complex in the virion. Most
CC core are conical, with only 7% tubular. The core is constituted by
CC capsid protein hexamer subunits. The core is disassembled soon after
CC virion entry (By similarity). Host restriction factors such as TRIM5-
CC alpha or TRIMCyp bind retroviral capsids and cause premature capsid
CC disassembly, leading to blocks in reverse transcription. Capsid
CC restriction by TRIM5 is one of the factors which restricts HIV-1 to the
CC human species. Host PIN1 apparently facilitates the virion uncoating
CC (PubMed:24509437). On the other hand, interactions with PDZD8 or CYPA
CC stabilize the capsid. {ECO:0000250|UniProtKB:P04585,
CC ECO:0000269|PubMed:24509437}.
CC -!- FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral
CC dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc
CC fingers. Acts as a nucleic acid chaperone which is involved in
CC rearangement of nucleic acid secondary structure during gRNA
CC retrotranscription. Also facilitates template switch leading to
CC recombination. As part of the polyprotein, participates in gRNA
CC dimerization, packaging, tRNA incorporation and virion assembly.
CC {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. Also cleaves Nef and Vif,
CC probably concomitantly with viral structural proteins on maturation of
CC virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off
CC the capped cellular mRNA translation. The resulting inhibition of
CC cellular protein synthesis serves to ensure maximal viral gene
CC expression and to evade host immune response. Also mediates cleavage of
CC host YTHDF3. Mediates cleavage of host CARD8, thereby activating the
CC CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient
CC CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade
CC CARD8-sensing when its protease remains inactive in infected cells
CC prior to viral budding (By similarity). {ECO:0000250|UniProtKB:P04585,
CC ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional
CC enzyme that converts the viral RNA genome into dsDNA in the cytoplasm,
CC shortly after virus entry into the cell. This enzyme displays a DNA
CC polymerase activity that can copy either DNA or RNA templates, and a
CC ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-
CC DNA heteroduplexes in a partially processive 3' to 5' endonucleasic
CC mode. Conversion of viral genomic RNA into dsDNA requires many steps. A
CC tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-
CC end of the viral RNA. RT uses the 3' end of the tRNA primer to perform
CC a short round of RNA-dependent minus-strand DNA synthesis. The reading
CC proceeds through the U5 region and ends after the repeated (R) region
CC which is present at both ends of viral RNA. The portion of the RNA-DNA
CC heteroduplex is digested by the RNase H, resulting in a ssDNA product
CC attached to the tRNA primer. This ssDNA/tRNA hybridizes with the
CC identical R region situated at the 3' end of viral RNA. This template
CC exchange, known as minus-strand DNA strong stop transfer, can be either
CC intra- or intermolecular. RT uses the 3' end of this newly synthesized
CC short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of
CC the whole template. RNase H digests the RNA template except for two
CC polypurine tracts (PPTs) situated at the 5'-end and near the center of
CC the genome. It is not clear if both polymerase and RNase H activities
CC are simultaneous. RNase H probably can proceed both in a polymerase-
CC dependent (RNA cut into small fragments by the same RT performing DNA
CC synthesis) and a polymerase-independent mode (cleavage of remaining RNA
CC fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
CC DNA synthesis using the PPTs that have not been removed by RNase H as
CC primers. PPTs and tRNA primers are then removed by RNase H. The 3' and
CC 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC blunt ended, linear dsDNA copy of the viral genome that includes long
CC terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC chromosome, by performing a series of DNA cutting and joining
CC reactions. This enzyme activity takes place after virion entry into a
CC cell and reverse transcription of the RNA genome in dsDNA. The first
CC step in the integration process is 3' processing. This step requires a
CC complex comprising the viral genome, matrix protein, Vpr and integrase.
CC This complex is called the pre-integration complex (PIC). The integrase
CC protein removes 2 nucleotides from each 3' end of the viral DNA,
CC leaving recessed CA OH's at the 3' ends. In the second step, the PIC
CC enters cell nucleus. This process is mediated through integrase and Vpr
CC proteins, and allows the virus to infect a non dividing cell. This
CC ability to enter the nucleus is specific of lentiviruses, other
CC retroviruses cannot and rely on cell division to access cell
CC chromosomes. In the third step, termed strand transfer, the integrase
CC protein joins the previously processed 3' ends to the 5' ends of
CC strands of target cellular DNA at the site of integration. The 5'-ends
CC are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-
CC shaped, gapped, recombination intermediate results, with the 5'-ends of
CC the viral DNA strands and the 3' ends of target DNA strands remaining
CC unjoined, flanking a gap of 5 bp. The last step is viral DNA
CC integration into host chromosome. This involves host DNA repair
CC synthesis in which the 5 bp gaps between the unjoined strands are
CC filled in and then ligated. Since this process occurs at both cuts
CC flanking the HIV genome, a 5 bp duplication of host DNA is produced at
CC the ends of HIV-1 integration. Alternatively, Integrase may catalyze
CC the excision of viral DNA just after strand transfer, this is termed
CC disintegration. {ECO:0000250|UniProtKB:P04585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific for a P1 residue that is hydrophobic, and P1'
CC variable, but often Pro.; EC=3.4.23.16;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00275};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC immunodeficiency virus type 1 and Moloney murine leukemia virus
CC enzymes prefer to cleave the RNA strand one nucleotide away from the
CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC away from the primer terminus.; EC=3.1.26.13; Evidence={ECO:0000250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2; Evidence={ECO:0000250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for reverse transcriptase polymerase
CC activity. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
CC Substrate-binding is a precondition for magnesium binding.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Magnesium ions are required for integrase activity. Binds at least
CC 1, maybe 2 magnesium ions. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Protease: The viral protease is inhibited by many
CC synthetic protease inhibitors (PIs), such as amprenavir, atazanavir,
CC indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. Use of
CC protease inhibitors in tritherapy regimens permit more ambitious
CC therapeutic strategies. Reverse transcriptase/ribonuclease H: RT can be
CC inhibited either by nucleoside RT inhibitors (NRTIs) or by non
CC nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators,
CC whereas NNRTIs inhibit DNA polymerization by binding a small
CC hydrophobic pocket near the RT active site and inducing an allosteric
CC change in this region. Classical NRTIs are abacavir, adefovir (PMEA),
CC didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA),
CC zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are
CC atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine
CC (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic
CC effective treatment of AIDS associate two NRTIs and one NNRTI.
CC {ECO:0000250}.
CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC hexamers of trimers (By similarity). Matrix protein p17: Interacts with
CC gp41 (via C-terminus) (PubMed:8918455). Interacts with host CALM1; this
CC interaction induces a conformational change in the Matrix protein,
CC triggering exposure of the myristate group (PubMed:21799007). Interacts
CC with host AP3D1; this interaction allows the polyprotein trafficking to
CC multivesicular bodies during virus assembly (PubMed:15766529). Part of
CC the pre-integration complex (PIC) which is composed of viral genome,
CC matrix protein, Vpr and integrase (By similarity).
CC {ECO:0000250|UniProtKB:P04585, ECO:0000269|PubMed:15766529,
CC ECO:0000269|PubMed:21799007, ECO:0000269|PubMed:8918455}.
CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers (PubMed:24066695).
CC Interacts with human PPIA/CYPA; This interaction stabilizes the capsid
CC (PubMed:8980234). Interacts with human NUP153 (PubMed:24130490).
CC Interacts with host PDZD8; this interaction stabilizes the capsid (By
CC similarity). Interacts with monkey TRIM5; this interaction destabilizes
CC the capsid (By similarity). {ECO:0000250|UniProtKB:P04585,
CC ECO:0000269|PubMed:24066695, ECO:0000269|PubMed:24130490,
CC ECO:0000269|PubMed:8980234}.
CC -!- SUBUNIT: [Protease]: Homodimer, whose active site consists of two
CC apposed aspartic acid residues. {ECO:0000250|UniProtKB:P04585}.
CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: Heterodimer of p66 RT
CC and p51 RT (RT p66/p51) (By similarity). Heterodimerization of RT is
CC essential for DNA polymerase activity (By similarity). The overall
CC folding of the subdomains is similar in p66 RT and p51 RT but the
CC spatial arrangements of the subdomains are dramatically different (By
CC similarity). {ECO:0000250|UniProtKB:P03366}.
CC -!- SUBUNIT: [Integrase]: Homotetramer; may further associate as a
CC homohexadecamer (By similarity). Part of the pre-integration complex
CC (PIC) which is composed of viral genome, matrix protein, Vpr and
CC integrase (By similarity). Interacts with human SMARCB1/INI1 and human
CC PSIP1/LEDGF isoform 1 (By similarity). Interacts with human KPNA3; this
CC interaction might play a role in nuclear import of the pre-integration
CC complex (By similarity). Interacts with human NUP153; this interaction
CC might play a role in nuclear import of the pre-integration complex
CC (PubMed:19369352). {ECO:0000250|UniProtKB:P03367,
CC ECO:0000250|UniProtKB:P04585, ECO:0000269|PubMed:19369352}.
CC -!- INTERACTION:
CC PRO_0000042395; PRO_0000042395 [P12497]: gag-pol; NbExp=3; IntAct=EBI-2369107, EBI-2369107;
CC PRO_0000042402; O75475-1: PSIP1; Xeno; NbExp=3; IntAct=EBI-10131955, EBI-5279836;
CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-
CC anchor {ECO:0000269|PubMed:19297499}. Host endosome, host
CC multivesicular body {ECO:0000269|PubMed:19297499}. Note=These locations
CC are linked to virus assembly sites. The main location is the cell
CC membrane, but under some circumstances, late endosomal compartments can
CC serve as productive sites for virion assembly.
CC {ECO:0000269|PubMed:19297499}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-
CC anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus
CC {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial
CC phase, cytoplasmic at assembly. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Translation results in the formation of the Gag polyprotein
CC most of the time. Ribosomal frameshifting at the gag-pol genes
CC boundary occurs at low frequency and produces the Gag-Pol
CC polyprotein. This strategy of translation probably allows the virus
CC to modulate the quantity of each viral protein. Maintenance of a
CC correct Gag to Gag-Pol ratio is essential for RNA dimerization and
CC viral infectivity.;
CC Name=Gag-Pol polyprotein;
CC IsoId=P12497-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P12493-1; Sequence=External;
CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: RT is structured in
CC five subdomains: finger, palm, thumb, connection and RNase H. Within
CC the palm subdomain, the 'primer grip' region is thought to be involved
CC in the positioning of the primer terminus for accommodating the
CC incoming nucleotide. The RNase H domain stabilizes the association of
CC RT with primer-template. {ECO:0000250}.
CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: The tryptophan repeat
CC motif is involved in RT p66/p51 dimerization (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: [Integrase]: The core domain contains the D-x(n)-D-x(35)-E
CC motif, named for the phylogenetically conserved glutamic acid and
CC aspartic acid residues and the invariant 35 amino acid spacing between
CC the second and third acidic residues. Each acidic residue of the
CC D,D(35)E motif is independently essential for the 3'-processing and
CC strand transfer activities of purified integrase protein.
CC {ECO:0000250}.
CC -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The protease is released by
CC autocatalytic cleavage. The polyprotein is cleaved during and after
CC budding, this process is termed maturation. Proteolytic cleavage of p66
CC RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid
CC protein p7 might be further cleaved after virus entry.
CC {ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:22334652}.
CC -!- PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the
CC virion by a host kinase. Phosphorylation is apparently not a major
CC regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.
CC -!- PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this
CC phosphorylation is necessary for Pin1-mediated virion uncoating.
CC {ECO:0000269|PubMed:24509437}.
CC -!- PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its
CC function by reducing RNA annealing and the initiation of reverse
CC transcription. {ECO:0000250|UniProtKB:P03347}.
CC -!- MISCELLANEOUS: [Reverse transcriptase/ribonuclease H]: Error-prone
CC enzyme that lacks a proof-reading function. High mutations rate is a
CC direct consequence of this characteristic. RT also displays frequent
CC template switching leading to high recombination rate. Recombination
CC mostly occurs between homologous regions of the two copackaged RNA
CC genomes. If these two RNA molecules derive from different viral
CC strains, reverse transcription will give rise to highly recombinated
CC proviral DNAs. {ECO:0000250}.
CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC majority of strains found worldwide belong to the group M. Group O
CC seems to be endemic to and largely confined to Cameroon and neighboring
CC countries in West Central Africa, where these viruses represent a small
CC minority of HIV-1 strains. The group N is represented by a limited
CC number of isolates from Cameroonian persons. The group M is further
CC subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Resistance to inhibitors associated with mutations are
CC observed both in viral protease and in reverse transcriptase. Most of
CC the time, single mutations confer only a modest reduction in drug
CC susceptibility. Combination of several mutations is usually required to
CC develop a high-level drug resistance. These mutations are predominantly
CC found in clade B viruses and not in other genotypes. They are listed in
CC the clade B representative isolate HXB2 (AC P04585). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal
CC frameshifting.
CC -!- WEB RESOURCE: Name=HIV drug resistance mutations;
CC URL="https://www.iasusa.org/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; M19921; AAA44988.2; ALT_SEQ; Genomic_RNA.
DR PDB; 1A43; X-ray; 2.60 A; A=278-363.
DR PDB; 1A8O; X-ray; 1.70 A; A=284-352.
DR PDB; 1AFV; X-ray; 3.70 A; A/B=133-283.
DR PDB; 1AK4; X-ray; 2.36 A; C/D=133-277.
DR PDB; 1AUM; X-ray; 3.00 A; A=283-352.
DR PDB; 1B92; X-ray; 2.02 A; A=1197-1359.
DR PDB; 1B9D; X-ray; 1.70 A; A=1197-1359.
DR PDB; 1B9F; X-ray; 1.70 A; A=1197-1359.
DR PDB; 1BAJ; X-ray; 2.60 A; A=278-377.
DR PDB; 1BHL; X-ray; 2.20 A; A=1204-1354.
DR PDB; 1BI4; X-ray; 2.50 A; A/B/C=1197-1356.
DR PDB; 1BIS; X-ray; 1.95 A; A/B=1194-1356.
DR PDB; 1BIU; X-ray; 2.50 A; A/B/C=1194-1359.
DR PDB; 1BIZ; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 1BL3; X-ray; 2.00 A; A/B/C=1197-1356.
DR PDB; 1GWP; NMR; -; A=133-283.
DR PDB; 1HIW; X-ray; 2.30 A; A/B/C/Q/R/S=1-132.
DR PDB; 1HYV; X-ray; 1.70 A; A=1194-1359.
DR PDB; 1HYZ; X-ray; 2.30 A; A=1194-1359.
DR PDB; 1ITG; X-ray; 2.30 A; A=1194-1359.
DR PDB; 1K6Y; X-ray; 2.40 A; A/B/C/D=1148-1359.
DR PDB; 1M9D; X-ray; 1.90 A; C/D=133-278.
DR PDB; 1QS4; X-ray; 2.10 A; A/B/C=1203-1356.
DR PDB; 1UPH; NMR; -; A=2-132.
DR PDB; 1WJB; NMR; -; A/B=1148-1202.
DR PDB; 1WJD; NMR; -; A/B=1148-1202.
DR PDB; 2B4J; X-ray; 2.02 A; A/B=1197-1359.
DR PDB; 2GOL; X-ray; 2.20 A; A=2-131, B/D=133-277.
DR PDB; 2GON; X-ray; 1.90 A; A/B/C/D=133-278.
DR PDB; 2H3F; NMR; -; A=2-132.
DR PDB; 2H3I; NMR; -; A=2-132.
DR PDB; 2H3Q; NMR; -; A=2-132.
DR PDB; 2H3V; NMR; -; A=2-132.
DR PDB; 2H3Z; NMR; -; A=2-132.
DR PDB; 2HMX; NMR; -; A=1-132.
DR PDB; 2HVP; X-ray; 3.00 A; A=489-587.
DR PDB; 2ITG; X-ray; 2.60 A; A=1197-1359.
DR PDB; 2JPR; NMR; -; A=133-277.
DR PDB; 2JYG; NMR; -; A=280-363.
DR PDB; 2JYL; NMR; -; A=280-363.
DR PDB; 2LF4; NMR; -; A=133-363.
DR PDB; 2LYA; NMR; -; A=2-132.
DR PDB; 2LYB; NMR; -; A=2-132.
DR PDB; 2M3Z; NMR; -; A=378-432.
DR PDB; 2M8L; NMR; -; A/B=133-363.
DR PDB; 2M8N; NMR; -; A=133-363.
DR PDB; 2M8P; NMR; -; A=133-363.
DR PDB; 2ONT; X-ray; 2.40 A; A=278-352.
DR PDB; 2PWM; X-ray; 1.90 A; A/B/C/D/E/F/G/H=133-278.
DR PDB; 2PWO; X-ray; 1.45 A; A/B/C/D=133-278.
DR PDB; 2PXR; X-ray; 1.50 A; C=133-278.
DR PDB; 2X2D; X-ray; 1.95 A; D/E=133-278.
DR PDB; 2XDE; X-ray; 1.40 A; A/B=133-278.
DR PDB; 2XV6; X-ray; 1.89 A; A/C=278-352.
DR PDB; 2XXM; X-ray; 1.65 A; A=278-352.
DR PDB; 3AV9; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 3AVA; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 3AVB; X-ray; 1.85 A; A/B=1197-1359.
DR PDB; 3AVC; X-ray; 1.77 A; A/B=1197-1359.
DR PDB; 3AVF; X-ray; 1.70 A; A/B=1197-1356.
DR PDB; 3AVG; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 3AVH; X-ray; 1.88 A; A/B=1197-1359.
DR PDB; 3AVJ; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 3AVK; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 3AVL; X-ray; 1.88 A; A/B=1197-1359.
DR PDB; 3AVM; X-ray; 1.88 A; A/B=1197-1359.
DR PDB; 3AVN; X-ray; 2.10 A; A/B=1197-1359.
DR PDB; 3DIK; EM; 9.00 A; A=133-351.
DR PDB; 3DPH; X-ray; 2.01 A; A/B=278-363.
DR PDB; 3DS0; X-ray; 1.60 A; A=278-363.
DR PDB; 3DS1; X-ray; 1.60 A; A=278-363.
DR PDB; 3DS2; X-ray; 1.20 A; A/B=278-363.
DR PDB; 3DS3; X-ray; 2.70 A; A/B=278-363.
DR PDB; 3DS4; X-ray; 1.12 A; A/B=278-363.
DR PDB; 3DS5; X-ray; 2.40 A; A/B/C/D=278-363.
DR PDB; 3DTJ; X-ray; 4.00 A; A/B/C/D=278-363.
DR PDB; 3GV2; X-ray; 7.00 A; A/B/C/D/E/F=133-355.
DR PDB; 3H47; X-ray; 1.90 A; A=133-363.
DR PDB; 3H4E; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
DR PDB; 3L3U; X-ray; 1.40 A; A/B=1197-1359.
DR PDB; 3L3V; X-ray; 2.00 A; A/B=1197-1359.
DR PDB; 3LPT; X-ray; 2.00 A; A=1197-1359.
DR PDB; 3LPU; X-ray; 1.95 A; A=1197-1359.
DR PDB; 3LRY; X-ray; 1.98 A; A/B=278-363.
DR PDB; 3MGE; X-ray; 1.90 A; A=133-363.
DR PDB; 3NF6; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 3NF7; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 3NF8; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 3NF9; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 3NFA; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 3P05; X-ray; 2.50 A; A/B/C/D/E=133-363.
DR PDB; 3P0A; X-ray; 5.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=133-363.
DR PDB; 3S85; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=489-587.
DR PDB; 3WNE; X-ray; 1.70 A; A/B=1203-1359.
DR PDB; 3WNF; X-ray; 1.45 A; A/B=1203-1359.
DR PDB; 3WNG; X-ray; 1.75 A; A/B=1203-1359.
DR PDB; 3WNH; X-ray; 1.50 A; A/B=1203-1359.
DR PDB; 3ZCM; X-ray; 1.80 A; A/B=1203-1359.
DR PDB; 3ZSO; X-ray; 1.75 A; A/B=1203-1359.
DR PDB; 3ZSQ; X-ray; 1.70 A; A/B=1203-1359.
DR PDB; 3ZSR; X-ray; 1.70 A; A/B=1203-1359.
DR PDB; 3ZSV; X-ray; 1.75 A; A/B=1203-1359.
DR PDB; 3ZSW; X-ray; 1.80 A; A/B=1203-1359.
DR PDB; 3ZSX; X-ray; 1.95 A; A/B=1203-1359.
DR PDB; 3ZSY; X-ray; 2.20 A; A/B=1203-1359.
DR PDB; 3ZSZ; X-ray; 2.00 A; A/B=1203-1359.
DR PDB; 3ZT0; X-ray; 1.95 A; A/B=1203-1359.
DR PDB; 3ZT1; X-ray; 1.75 A; A/B=1203-1359.
DR PDB; 3ZT2; X-ray; 1.70 A; A/B=1203-1359.
DR PDB; 3ZT3; X-ray; 1.95 A; A/B=1203-1359.
DR PDB; 3ZT4; X-ray; 2.20 A; A/B=1203-1359.
DR PDB; 4AH9; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4AHR; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 4AHS; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 4AHT; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4AHU; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 4AHV; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CE9; X-ray; 2.10 A; A/B=1197-1359.
DR PDB; 4CEA; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CEB; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 4CEC; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 4CED; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 4CEE; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CEF; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CEO; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 4CEQ; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CER; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CES; X-ray; 1.85 A; A/B=1197-1359.
DR PDB; 4CEZ; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CF0; X-ray; 1.85 A; A/B=1197-1359.
DR PDB; 4CF1; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 4CF2; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 4CF8; X-ray; 1.65 A; A/B=1197-1359.
DR PDB; 4CF9; X-ray; 2.10 A; A/B=1197-1359.
DR PDB; 4CFA; X-ray; 2.05 A; A/B=1197-1359.
DR PDB; 4CFB; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 4CFC; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 4CFD; X-ray; 2.15 A; A/B=1197-1359.
DR PDB; 4CGD; X-ray; 2.00 A; A/B=1197-1359.
DR PDB; 4CGF; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CGG; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 4CGH; X-ray; 1.76 A; A/B=1197-1359.
DR PDB; 4CGI; X-ray; 2.07 A; A/B=1197-1359.
DR PDB; 4CGJ; X-ray; 2.15 A; A/B=1197-1359.
DR PDB; 4CHN; X-ray; 2.00 A; A/B=1197-1359.
DR PDB; 4CHO; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CHP; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 4CHQ; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 4CHY; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CHZ; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CIE; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CIF; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CIG; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CJ3; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CJ4; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CJ5; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 4CJE; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 4CJF; X-ray; 1.90 A; A/B=1197-1359.
DR PDB; 4CJK; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 4CJL; X-ray; 1.77 A; A=1197-1359.
DR PDB; 4CJP; X-ray; 2.00 A; A/B=1197-1359.
DR PDB; 4CJQ; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CJR; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CJS; X-ray; 1.80 A; A/B=1197-1359.
DR PDB; 4CJT; X-ray; 1.71 A; A/B=1197-1359.
DR PDB; 4CJU; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4CJV; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 4CJW; X-ray; 1.95 A; A/B=1197-1359.
DR PDB; 4CK1; X-ray; 1.75 A; A/B=1197-1359.
DR PDB; 4CK2; X-ray; 1.85 A; A/B=1197-1359.
DR PDB; 4CK3; X-ray; 1.79 A; A/B=1197-1359.
DR PDB; 4COC; X-ray; 1.59 A; A/B/C=278-363.
DR PDB; 4COP; X-ray; 1.85 A; A/B=278-363.
DR PDB; 4DGA; X-ray; 1.90 A; C/D=133-277.
DR PDB; 4DGE; X-ray; 2.20 A; C/D=133-277.
DR PDB; 4DMN; X-ray; 2.45 A; A=1197-1359.
DR PDB; 4E1M; X-ray; 1.90 A; A=1197-1359.
DR PDB; 4E1N; X-ray; 2.00 A; A=1197-1359.
DR PDB; 4E91; X-ray; 1.70 A; A/B=133-278.
DR PDB; 4E92; X-ray; 1.80 A; A/B=133-278.
DR PDB; 4GVM; X-ray; 2.16 A; A=1197-1359.
DR PDB; 4GW6; X-ray; 2.65 A; A=1197-1359.
DR PDB; 4ID1; X-ray; 1.87 A; A=1197-1359.
DR PDB; 4IPY; X-ray; 1.64 A; A/B/C/D=278-363.
DR PDB; 4JLH; X-ray; 2.09 A; A=1197-1359.
DR PDB; 4JMU; X-ray; 2.00 A; A=1-111.
DR PDB; 4LH4; X-ray; 1.80 A; A=1197-1359.
DR PDB; 4LH5; X-ray; 2.19 A; A=1197-1359.
DR PDB; 4LQW; X-ray; 1.95 A; C/D=133-278.
DR PDB; 4NX4; X-ray; 1.50 A; C=133-278.
DR PDB; 4O0J; X-ray; 2.05 A; A=1197-1359.
DR PDB; 4O55; X-ray; 2.24 A; A=1197-1359.
DR PDB; 4O5B; X-ray; 2.37 A; A=1197-1359.
DR PDB; 4OVL; X-ray; 1.70 A; A/B=1197-1359.
DR PDB; 4PHV; X-ray; 2.10 A; A/B=489-587.
DR PDB; 4QNB; X-ray; 2.00 A; A=133-363.
DR PDB; 4WYM; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
DR PDB; 4Y1C; X-ray; 2.30 A; A/B=1197-1359.
DR PDB; 4Y1D; X-ray; 1.93 A; A/B=1197-1359.
DR PDB; 4ZHR; X-ray; 2.60 A; A=588-1147, B=588-1015.
DR PDB; 5HVP; X-ray; 2.00 A; A/B=489-587.
DR PDB; 5JL4; X-ray; 1.76 A; A/B=1197-1359.
DR PDB; 5KGW; X-ray; 2.34 A; A=1197-1359.
DR PDB; 5KGX; X-ray; 2.67 A; A=1197-1359.
DR PDB; 5KRS; X-ray; 1.70 A; A=1204-1354.
DR PDB; 5KRT; X-ray; 1.65 A; A=1204-1354.
DR PDB; 5TEO; X-ray; 2.05 A; A/B=278-377.
DR PDB; 5U1C; EM; 3.90 A; A/B/C/D=1132-1136, A/B/C/D=1148-1435.
DR PDB; 5VCK; X-ray; 1.80 A; A/B=489-587.
DR PDB; 5VEA; X-ray; 2.00 A; A=489-587.
DR PDB; 5VJ3; X-ray; 2.00 A; A=489-587.
DR PDB; 5XN0; X-ray; 2.60 A; A/C=588-1142, B/D=588-1015.
DR PDB; 5XN1; X-ray; 2.45 A; A/C=588-1142, B/D=588-1015.
DR PDB; 5XN2; X-ray; 2.38 A; A/C=588-1142, B/D=588-1015.
DR PDB; 6ES8; X-ray; 1.90 A; A=133-351.
DR PDB; 6IK9; X-ray; 2.44 A; B/D=588-1015.
DR PDB; 6IKA; X-ray; 2.60 A; B/D=588-1015.
DR PDB; 6JCF; X-ray; 2.15 A; A=1198-1359.
DR PDB; 6JCG; X-ray; 2.50 A; A=1198-1359.
DR PDB; 6KDJ; X-ray; 2.51 A; B/D=588-1015.
DR PDB; 6KDK; X-ray; 2.56 A; B/D=588-1015.
DR PDB; 6KDM; X-ray; 2.32 A; B/D=588-1015.
DR PDB; 6KDN; X-ray; 2.30 A; B/D=588-1015.
DR PDB; 6KDO; X-ray; 2.57 A; B/D=588-1015.
DR PDB; 6LMI; X-ray; 2.50 A; A=1197-1359.
DR PDB; 6LMQ; X-ray; 2.10 A; A=1197-1359.
DR PDB; 6MCR; X-ray; 1.48 A; A=489-587.
DR PDB; 6MCS; X-ray; 1.52 A; A=489-587.
DR PDB; 6OOS; X-ray; 1.90 A; A/B/C/D=489-587.
DR PDB; 6OOT; X-ray; 1.82 A; A/B=489-587.
DR PDB; 6OOU; X-ray; 2.13 A; A/B=489-587.
DR PDB; 6OPW; X-ray; 2.10 A; A/B=489-587.
DR PDB; 6OPY; X-ray; 2.13 A; A/B=489-587.
DR PDB; 6OPZ; X-ray; 2.20 A; A/B=489-587.
DR PDB; 6OXO; X-ray; 2.00 A; A/B=489-587.
DR PDB; 6OXP; X-ray; 1.97 A; A/B=489-587.
DR PDB; 6OXQ; X-ray; 1.89 A; A/B=489-587.
DR PDB; 6OXR; X-ray; 2.04 A; A/B=489-587.
DR PDB; 6OXS; X-ray; 1.99 A; A/B=489-587.
DR PDB; 6OXT; X-ray; 1.86 A; A/B=489-587.
DR PDB; 6OXU; X-ray; 1.86 A; A/B=489-587.
DR PDB; 6OXV; X-ray; 1.99 A; A/B=489-587.
DR PDB; 6OXW; X-ray; 1.98 A; A/B=489-587.
DR PDB; 6OXX; X-ray; 1.96 A; A/B=489-587.
DR PDB; 6OXY; X-ray; 1.96 A; A/B=489-587.
DR PDB; 6OXZ; X-ray; 1.96 A; A/B=489-587.
DR PDB; 6OY0; X-ray; 2.00 A; A/B=489-587.
DR PDB; 6OY1; X-ray; 2.00 A; A/B=489-587.
DR PDB; 6OY2; X-ray; 1.99 A; A/B=489-587.
DR PDB; 6OYD; X-ray; 1.46 A; A=489-587.
DR PDB; 6OYR; X-ray; 1.54 A; A=489-587.
DR PDB; 6PJB; X-ray; 1.98 A; A/B=489-587.
DR PDB; 6PJC; X-ray; 1.97 A; A/B/C/D=489-587.
DR PDB; 6PJD; X-ray; 1.89 A; A/B=489-587.
DR PDB; 6PJE; X-ray; 1.92 A; A/B=489-587.
DR PDB; 6PJF; X-ray; 1.94 A; A/B=489-587.
DR PDB; 6PJG; X-ray; 1.80 A; A/B=489-587.
DR PDB; 6PJH; X-ray; 1.85 A; A/B=489-587.
DR PDB; 6PJI; X-ray; 1.90 A; A/B=489-587.
DR PDB; 6PJK; X-ray; 2.00 A; A/B=489-587.
DR PDB; 6PJL; X-ray; 1.99 A; A/B=489-587.
DR PDB; 6PJM; X-ray; 1.93 A; A/B=489-587.
DR PDB; 6PJN; X-ray; 1.98 A; A/B=489-587.
DR PDB; 6PJO; X-ray; 1.95 A; A/B=489-587.
DR PDB; 6PUT; EM; 2.90 A; A/B/C/D=1148-1435.
DR PDB; 6PUW; EM; 2.90 A; A/B/C/D=1148-1435.
DR PDB; 6PUY; EM; 2.80 A; A/B/C/D=1148-1435.
DR PDB; 6PUZ; EM; 2.80 A; A/B/C/D=1148-1435.
DR PDB; 6T6E; X-ray; 1.30 A; A=1366-1417.
DR PDB; 6U8Q; EM; 4.67 A; A/B/C/D/I/J/K/L/M/N/O/P=1148-1435.
DR PDB; 6UM8; X-ray; 2.33 A; A/B=1204-1359.
DR PDB; 6V3K; EM; 3.40 A; A/B/C/D=1148-1435.
DR PDB; 6VDK; EM; 4.50 A; A/B/C/D/I/J/M/P=1148-1435.
DR PDB; 6VQS; X-ray; 2.38 A; A=1197-1359.
DR PDB; 6VRG; X-ray; 2.40 A; A/B/C/D=1148-1359.
DR PDB; 6VX2; X-ray; 2.40 A; A=1197-1359.
DR PDB; 6W0U; X-ray; 2.19 A; A=1197-1359.
DR PDB; 6W42; X-ray; 2.26 A; A=1196-1359.
DR PDB; 6W6T; X-ray; 1.84 A; A/B=489-587.
DR PDB; 7D83; X-ray; 2.43 A; A=1197-1359.
DR PDB; 7DBM; X-ray; 2.43 A; B/D=588-1015.
DR PDB; 7DBN; X-ray; 2.67 A; B/D=588-1015.
DR PDB; 9HVP; X-ray; 2.80 A; A/B=489-587.
DR PDBsum; 1A43; -.
DR PDBsum; 1A8O; -.
DR PDBsum; 1AFV; -.
DR PDBsum; 1AK4; -.
DR PDBsum; 1AUM; -.
DR PDBsum; 1B92; -.
DR PDBsum; 1B9D; -.
DR PDBsum; 1B9F; -.
DR PDBsum; 1BAJ; -.
DR PDBsum; 1BHL; -.
DR PDBsum; 1BI4; -.
DR PDBsum; 1BIS; -.
DR PDBsum; 1BIU; -.
DR PDBsum; 1BIZ; -.
DR PDBsum; 1BL3; -.
DR PDBsum; 1GWP; -.
DR PDBsum; 1HIW; -.
DR PDBsum; 1HYV; -.
DR PDBsum; 1HYZ; -.
DR PDBsum; 1ITG; -.
DR PDBsum; 1K6Y; -.
DR PDBsum; 1M9D; -.
DR PDBsum; 1QS4; -.
DR PDBsum; 1UPH; -.
DR PDBsum; 1WJB; -.
DR PDBsum; 1WJD; -.
DR PDBsum; 2B4J; -.
DR PDBsum; 2GOL; -.
DR PDBsum; 2GON; -.
DR PDBsum; 2H3F; -.
DR PDBsum; 2H3I; -.
DR PDBsum; 2H3Q; -.
DR PDBsum; 2H3V; -.
DR PDBsum; 2H3Z; -.
DR PDBsum; 2HMX; -.
DR PDBsum; 2HVP; -.
DR PDBsum; 2ITG; -.
DR PDBsum; 2JPR; -.
DR PDBsum; 2JYG; -.
DR PDBsum; 2JYL; -.
DR PDBsum; 2LF4; -.
DR PDBsum; 2LYA; -.
DR PDBsum; 2LYB; -.
DR PDBsum; 2M3Z; -.
DR PDBsum; 2M8L; -.
DR PDBsum; 2M8N; -.
DR PDBsum; 2M8P; -.
DR PDBsum; 2ONT; -.
DR PDBsum; 2PWM; -.
DR PDBsum; 2PWO; -.
DR PDBsum; 2PXR; -.
DR PDBsum; 2X2D; -.
DR PDBsum; 2XDE; -.
DR PDBsum; 2XV6; -.
DR PDBsum; 2XXM; -.
DR PDBsum; 3AV9; -.
DR PDBsum; 3AVA; -.
DR PDBsum; 3AVB; -.
DR PDBsum; 3AVC; -.
DR PDBsum; 3AVF; -.
DR PDBsum; 3AVG; -.
DR PDBsum; 3AVH; -.
DR PDBsum; 3AVJ; -.
DR PDBsum; 3AVK; -.
DR PDBsum; 3AVL; -.
DR PDBsum; 3AVM; -.
DR PDBsum; 3AVN; -.
DR PDBsum; 3DIK; -.
DR PDBsum; 3DPH; -.
DR PDBsum; 3DS0; -.
DR PDBsum; 3DS1; -.
DR PDBsum; 3DS2; -.
DR PDBsum; 3DS3; -.
DR PDBsum; 3DS4; -.
DR PDBsum; 3DS5; -.
DR PDBsum; 3DTJ; -.
DR PDBsum; 3GV2; -.
DR PDBsum; 3H47; -.
DR PDBsum; 3H4E; -.
DR PDBsum; 3L3U; -.
DR PDBsum; 3L3V; -.
DR PDBsum; 3LPT; -.
DR PDBsum; 3LPU; -.
DR PDBsum; 3LRY; -.
DR PDBsum; 3MGE; -.
DR PDBsum; 3NF6; -.
DR PDBsum; 3NF7; -.
DR PDBsum; 3NF8; -.
DR PDBsum; 3NF9; -.
DR PDBsum; 3NFA; -.
DR PDBsum; 3P05; -.
DR PDBsum; 3P0A; -.
DR PDBsum; 3S85; -.
DR PDBsum; 3WNE; -.
DR PDBsum; 3WNF; -.
DR PDBsum; 3WNG; -.
DR PDBsum; 3WNH; -.
DR PDBsum; 3ZCM; -.
DR PDBsum; 3ZSO; -.
DR PDBsum; 3ZSQ; -.
DR PDBsum; 3ZSR; -.
DR PDBsum; 3ZSV; -.
DR PDBsum; 3ZSW; -.
DR PDBsum; 3ZSX; -.
DR PDBsum; 3ZSY; -.
DR PDBsum; 3ZSZ; -.
DR PDBsum; 3ZT0; -.
DR PDBsum; 3ZT1; -.
DR PDBsum; 3ZT2; -.
DR PDBsum; 3ZT3; -.
DR PDBsum; 3ZT4; -.
DR PDBsum; 4AH9; -.
DR PDBsum; 4AHR; -.
DR PDBsum; 4AHS; -.
DR PDBsum; 4AHT; -.
DR PDBsum; 4AHU; -.
DR PDBsum; 4AHV; -.
DR PDBsum; 4CE9; -.
DR PDBsum; 4CEA; -.
DR PDBsum; 4CEB; -.
DR PDBsum; 4CEC; -.
DR PDBsum; 4CED; -.
DR PDBsum; 4CEE; -.
DR PDBsum; 4CEF; -.
DR PDBsum; 4CEO; -.
DR PDBsum; 4CEQ; -.
DR PDBsum; 4CER; -.
DR PDBsum; 4CES; -.
DR PDBsum; 4CEZ; -.
DR PDBsum; 4CF0; -.
DR PDBsum; 4CF1; -.
DR PDBsum; 4CF2; -.
DR PDBsum; 4CF8; -.
DR PDBsum; 4CF9; -.
DR PDBsum; 4CFA; -.
DR PDBsum; 4CFB; -.
DR PDBsum; 4CFC; -.
DR PDBsum; 4CFD; -.
DR PDBsum; 4CGD; -.
DR PDBsum; 4CGF; -.
DR PDBsum; 4CGG; -.
DR PDBsum; 4CGH; -.
DR PDBsum; 4CGI; -.
DR PDBsum; 4CGJ; -.
DR PDBsum; 4CHN; -.
DR PDBsum; 4CHO; -.
DR PDBsum; 4CHP; -.
DR PDBsum; 4CHQ; -.
DR PDBsum; 4CHY; -.
DR PDBsum; 4CHZ; -.
DR PDBsum; 4CIE; -.
DR PDBsum; 4CIF; -.
DR PDBsum; 4CIG; -.
DR PDBsum; 4CJ3; -.
DR PDBsum; 4CJ4; -.
DR PDBsum; 4CJ5; -.
DR PDBsum; 4CJE; -.
DR PDBsum; 4CJF; -.
DR PDBsum; 4CJK; -.
DR PDBsum; 4CJL; -.
DR PDBsum; 4CJP; -.
DR PDBsum; 4CJQ; -.
DR PDBsum; 4CJR; -.
DR PDBsum; 4CJS; -.
DR PDBsum; 4CJT; -.
DR PDBsum; 4CJU; -.
DR PDBsum; 4CJV; -.
DR PDBsum; 4CJW; -.
DR PDBsum; 4CK1; -.
DR PDBsum; 4CK2; -.
DR PDBsum; 4CK3; -.
DR PDBsum; 4COC; -.
DR PDBsum; 4COP; -.
DR PDBsum; 4DGA; -.
DR PDBsum; 4DGE; -.
DR PDBsum; 4DMN; -.
DR PDBsum; 4E1M; -.
DR PDBsum; 4E1N; -.
DR PDBsum; 4E91; -.
DR PDBsum; 4E92; -.
DR PDBsum; 4GVM; -.
DR PDBsum; 4GW6; -.
DR PDBsum; 4ID1; -.
DR PDBsum; 4IPY; -.
DR PDBsum; 4JLH; -.
DR PDBsum; 4JMU; -.
DR PDBsum; 4LH4; -.
DR PDBsum; 4LH5; -.
DR PDBsum; 4LQW; -.
DR PDBsum; 4NX4; -.
DR PDBsum; 4O0J; -.
DR PDBsum; 4O55; -.
DR PDBsum; 4O5B; -.
DR PDBsum; 4OVL; -.
DR PDBsum; 4PHV; -.
DR PDBsum; 4QNB; -.
DR PDBsum; 4WYM; -.
DR PDBsum; 4Y1C; -.
DR PDBsum; 4Y1D; -.
DR PDBsum; 4ZHR; -.
DR PDBsum; 5HVP; -.
DR PDBsum; 5JL4; -.
DR PDBsum; 5KGW; -.
DR PDBsum; 5KGX; -.
DR PDBsum; 5KRS; -.
DR PDBsum; 5KRT; -.
DR PDBsum; 5TEO; -.
DR PDBsum; 5U1C; -.
DR PDBsum; 5VCK; -.
DR PDBsum; 5VEA; -.
DR PDBsum; 5VJ3; -.
DR PDBsum; 5XN0; -.
DR PDBsum; 5XN1; -.
DR PDBsum; 5XN2; -.
DR PDBsum; 6ES8; -.
DR PDBsum; 6IK9; -.
DR PDBsum; 6IKA; -.
DR PDBsum; 6JCF; -.
DR PDBsum; 6JCG; -.
DR PDBsum; 6KDJ; -.
DR PDBsum; 6KDK; -.
DR PDBsum; 6KDM; -.
DR PDBsum; 6KDN; -.
DR PDBsum; 6KDO; -.
DR PDBsum; 6LMI; -.
DR PDBsum; 6LMQ; -.
DR PDBsum; 6MCR; -.
DR PDBsum; 6MCS; -.
DR PDBsum; 6OOS; -.
DR PDBsum; 6OOT; -.
DR PDBsum; 6OOU; -.
DR PDBsum; 6OPW; -.
DR PDBsum; 6OPY; -.
DR PDBsum; 6OPZ; -.
DR PDBsum; 6OXO; -.
DR PDBsum; 6OXP; -.
DR PDBsum; 6OXQ; -.
DR PDBsum; 6OXR; -.
DR PDBsum; 6OXS; -.
DR PDBsum; 6OXT; -.
DR PDBsum; 6OXU; -.
DR PDBsum; 6OXV; -.
DR PDBsum; 6OXW; -.
DR PDBsum; 6OXX; -.
DR PDBsum; 6OXY; -.
DR PDBsum; 6OXZ; -.
DR PDBsum; 6OY0; -.
DR PDBsum; 6OY1; -.
DR PDBsum; 6OY2; -.
DR PDBsum; 6OYD; -.
DR PDBsum; 6OYR; -.
DR PDBsum; 6PJB; -.
DR PDBsum; 6PJC; -.
DR PDBsum; 6PJD; -.
DR PDBsum; 6PJE; -.
DR PDBsum; 6PJF; -.
DR PDBsum; 6PJG; -.
DR PDBsum; 6PJH; -.
DR PDBsum; 6PJI; -.
DR PDBsum; 6PJK; -.
DR PDBsum; 6PJL; -.
DR PDBsum; 6PJM; -.
DR PDBsum; 6PJN; -.
DR PDBsum; 6PJO; -.
DR PDBsum; 6PUT; -.
DR PDBsum; 6PUW; -.
DR PDBsum; 6PUY; -.
DR PDBsum; 6PUZ; -.
DR PDBsum; 6T6E; -.
DR PDBsum; 6U8Q; -.
DR PDBsum; 6UM8; -.
DR PDBsum; 6V3K; -.
DR PDBsum; 6VDK; -.
DR PDBsum; 6VQS; -.
DR PDBsum; 6VRG; -.
DR PDBsum; 6VX2; -.
DR PDBsum; 6W0U; -.
DR PDBsum; 6W42; -.
DR PDBsum; 6W6T; -.
DR PDBsum; 7D83; -.
DR PDBsum; 7DBM; -.
DR PDBsum; 7DBN; -.
DR PDBsum; 9HVP; -.
DR BMRB; P12497; -.
DR SASBDB; P12497; -.
DR SMR; P12497; -.
DR IntAct; P12497; 5.
DR BindingDB; P12497; -.
DR DrugBank; DB03118; (2Z)-1-(5-Chloro-1H-indol-3-yl)-3-hydroxy-3-(1H-tetrazol-5-yl)-2-propen-1-one.
DR DrugBank; DB02086; (3,4-Dihydroxy-Phenyl)-Triphenyl-Arsonium.
DR DrugBank; DB07575; 2,4-DIAMINO-1,5-DIPHENYL-3-HYDROXYPENTANE.
DR DrugBank; DB02994; Cacodylic acid.
DR DrugBank; DB08027; CAP-1.
DR DrugBank; DB03676; Cystein-S-Yl Cacodylate.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
DR MEROPS; A02.001; -.
DR iPTMnet; P12497; -.
DR ABCD; P12497; 25 sequenced antibodies.
DR SABIO-RK; P12497; -.
DR EvolutionaryTrace; P12497; -.
DR PRO; PR:P12497; -.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA: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 DisProt; DP00410; -.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 3.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR InterPro; IPR000071; Lentvrl_matrix_N.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR010659; RVT_connect.
DR InterPro; IPR010661; RVT_thumb.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00540; Gag_p17; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR PRINTS; PR00234; HIV1MATRIX.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host caspases by virus; AIDS;
KW Aspartyl protease; Capsid protein; DNA integration; DNA recombination;
KW DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Host cell membrane;
KW Host cytoplasm; Host endosome; Host gene expression shutoff by virus;
KW Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
KW Lipid-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Modulation of host cell apoptosis by virus; Multifunctional enzyme;
KW Myristate; Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Viral genome integration; Viral nucleoprotein;
KW Viral penetration into host nucleus; Viral release from host cell; Virion;
KW Virion maturation; Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..1435
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000261276"
FT CHAIN 2..132
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042394"
FT CHAIN 133..363
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042395"
FT PEPTIDE 364..377
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042396"
FT CHAIN 378..432
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042397"
FT PEPTIDE 433..440
FT /note="Transframe peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000246725"
FT CHAIN 441..488
FT /note="p6-pol"
FT /evidence="ECO:0000255"
FT /id="PRO_0000042398"
FT CHAIN 489..587
FT /note="Protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038660"
FT CHAIN 588..1147
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042399"
FT CHAIN 588..1027
FT /note="p51 RT"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042400"
FT CHAIN 1028..1147
FT /note="p15"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042401"
FT CHAIN 1148..1435
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042402"
FT DOMAIN 508..577
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 631..821
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1021..1144
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1201..1351
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 390..407
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 411..428
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1150..1191
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1370..1417
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 7..31
FT /note="Interaction with Gp41"
FT /evidence="ECO:0000269|PubMed:8918455"
FT REGION 8..43
FT /note="Interaction with host CALM1"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 12..19
FT /note="Interaction with host AP3D1"
FT /evidence="ECO:0000269|PubMed:15766529"
FT REGION 14..33
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate and RNA"
FT /evidence="ECO:0000269|PubMed:16840558"
FT REGION 73..77
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate"
FT /evidence="ECO:0000269|PubMed:16840558"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..227
FT /note="Interaction with human PPIA/CYPA and NUP153"
FT /evidence="ECO:0000269|PubMed:19369352,
FT ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:8980234"
FT REGION 277..363
FT /note="Dimerization/Multimerization of capsid protein p24"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 444..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..493
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 537..543
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 576..588
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 814..822
FT /note="RT 'primer grip'"
FT /evidence="ECO:0000250"
FT MOTIF 16..22
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 26..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 985..1001
FT /note="Tryptophan repeat motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 446..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 513
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 697
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 1030
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1065
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1085
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT BINDING 1263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT BINDING 1299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT SITE 132..133
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 221..222
FT /note="Cis/trans isomerization of proline peptide bond; by
FT human PPIA/CYPA"
FT /evidence="ECO:0000250"
FT SITE 363..364
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 377..378
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 432..433
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 440..441
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 488..489
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 587..588
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 988
FT /note="Essential for RT p66/p51 heterodimerization"
FT /evidence="ECO:0000250"
FT SITE 1001
FT /note="Essential for RT p66/p51 heterodimerization"
FT /evidence="ECO:0000250"
FT SITE 1027..1028
FT /note="Cleavage; by viral protease; partial"
FT /evidence="ECO:0000250"
FT SITE 1147..1148
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 148
FT /note="Phosphoserine; by host MAPK1"
FT /evidence="ECO:0000269|PubMed:24509437"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT MUTAGEN 9
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT MUTAGEN 67
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT MUTAGEN 72
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT MUTAGEN 77
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1UPH"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:4JMU"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4JMU"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1UPH"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:4JMU"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:4JMU"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:4JMU"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4JMU"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4JMU"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:4JMU"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:4JMU"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:2H3Q"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2H3F"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2H3F"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2XDE"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4E92"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2XDE"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:2XDE"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:2XDE"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2XDE"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:2XDE"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4E92"
FT HELIX 195..215
FT /evidence="ECO:0007829|PDB:2XDE"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2XDE"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4NX4"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:2XDE"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2XDE"
FT HELIX 258..277
FT /evidence="ECO:0007829|PDB:2XDE"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3DS4"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3DS5"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:3DS4"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:4QNB"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:3DS4"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:3DS4"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:3DS4"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:3DS0"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:4IPY"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:2M3Z"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2M3Z"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2M3Z"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:2M3Z"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:2M3Z"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2M3Z"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2M3Z"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:9HVP"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 540..554
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 557..566
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:6OXU"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:6OYD"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:6OYD"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:5VCK"
FT HELIX 615..630
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:6KDM"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 665..670
FT /evidence="ECO:0007829|PDB:6KDN"
FT TURN 674..678
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 691..697
FT /evidence="ECO:0007829|PDB:6KDN"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:6KDM"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 709..715
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 721..726
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 729..735
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 743..761
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 765..770
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 773..780
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 782..798
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 805..807
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 811..816
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 819..821
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 823..828
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:5XN2"
FT HELIX 841..854
FT /evidence="ECO:0007829|PDB:6KDN"
FT TURN 855..857
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 858..860
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 864..868
FT /evidence="ECO:0007829|PDB:6KDN"
FT TURN 869..872
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 884..898
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 908..910
FT /evidence="ECO:0007829|PDB:4ZHR"
FT STRAND 913..920
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 923..931
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 935..941
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 946..949
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 951..970
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 975..980
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 982..991
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 992..995
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1000..1003
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:4ZHR"
FT STRAND 1017..1019
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1024..1033
FT /evidence="ECO:0007829|PDB:6KDN"
FT TURN 1035..1037
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1040..1046
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1051..1056
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 1061..1074
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1078..1084
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 1087..1094
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1098..1101
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 1103..1114
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1116..1122
FT /evidence="ECO:0007829|PDB:6KDN"
FT STRAND 1125..1127
FT /evidence="ECO:0007829|PDB:7DBM"
FT HELIX 1132..1139
FT /evidence="ECO:0007829|PDB:6KDN"
FT HELIX 1151..1162
FT /evidence="ECO:0007829|PDB:1K6Y"
FT HELIX 1166..1173
FT /evidence="ECO:0007829|PDB:1K6Y"
FT HELIX 1177..1186
FT /evidence="ECO:0007829|PDB:1K6Y"
FT HELIX 1188..1190
FT /evidence="ECO:0007829|PDB:6PUY"
FT HELIX 1204..1206
FT /evidence="ECO:0007829|PDB:3WNE"
FT STRAND 1207..1215
FT /evidence="ECO:0007829|PDB:3WNF"
FT STRAND 1218..1225
FT /evidence="ECO:0007829|PDB:3WNF"
FT TURN 1226..1228
FT /evidence="ECO:0007829|PDB:3WNF"
FT STRAND 1231..1238
FT /evidence="ECO:0007829|PDB:3WNF"
FT HELIX 1241..1254
FT /evidence="ECO:0007829|PDB:3WNF"
FT STRAND 1259..1261
FT /evidence="ECO:0007829|PDB:3WNF"
FT HELIX 1266..1268
FT /evidence="ECO:0007829|PDB:3WNF"
FT HELIX 1271..1280
FT /evidence="ECO:0007829|PDB:3WNF"
FT STRAND 1283..1285
FT /evidence="ECO:0007829|PDB:4CF8"
FT STRAND 1290..1292
FT /evidence="ECO:0007829|PDB:4CJ3"
FT TURN 1293..1296
FT /evidence="ECO:0007829|PDB:4E1M"
FT HELIX 1300..1312
FT /evidence="ECO:0007829|PDB:3WNF"
FT HELIX 1313..1315
FT /evidence="ECO:0007829|PDB:3WNF"
FT STRAND 1316..1318
FT /evidence="ECO:0007829|PDB:1B9D"
FT HELIX 1319..1332
FT /evidence="ECO:0007829|PDB:3WNF"
FT HELIX 1335..1337
FT /evidence="ECO:0007829|PDB:5JL4"
FT STRAND 1338..1340
FT /evidence="ECO:0007829|PDB:5JL4"
FT HELIX 1343..1355
FT /evidence="ECO:0007829|PDB:3WNF"
FT STRAND 1370..1374
FT /evidence="ECO:0007829|PDB:6T6E"
FT STRAND 1383..1391
FT /evidence="ECO:0007829|PDB:6T6E"
FT STRAND 1393..1400
FT /evidence="ECO:0007829|PDB:6T6E"
FT STRAND 1403..1408
FT /evidence="ECO:0007829|PDB:6T6E"
FT HELIX 1409..1411
FT /evidence="ECO:0007829|PDB:6T6E"
FT STRAND 1412..1416
FT /evidence="ECO:0007829|PDB:6T6E"
FT TURN 1420..1422
FT /evidence="ECO:0007829|PDB:6PUZ"
SQ SEQUENCE 1435 AA; 161789 MW; 798E74FD27C21244 CRC64;
MGARASVLSG GELDKWEKIR LRPGGKKQYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TIAVLYCVHQ RIDVKDTKEA LDKIEEEQNK SKKKAQQAAA
DTGNNSQVSQ NYPIVQNLQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT
STLQEQIGWM THNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPG ATLEEMMTAC QGVGGPGHKA
RVLAEAMSQV TNPATIMIQK GNFRNQRKTV KCFNCGKEGH IAKNCRAPRK KGCWKCGKEG
HQMKDCTERQ ANFLREDLAF PQGKAREFSS EQTRANSPTR RELQVWGRDN NSLSEAGADR
QGTVSFSFPQ ITLWQRPLVT IKIGGQLKEA LLDTGADDTV LEEMNLPGRW KPKMIGGIGG
FIKVRQYDQI LIEICGHKAI GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK
PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI KKKDSTKWRK
LVDFRELNKR TQDFWEVQLG IPHPAGLKQK KSVTVLDVGD AYFSVPLDKD FRKYTAFTIP
SINNETPGIR YQYNVLPQGW KGSPAIFQCS MTKILEPFRK QNPDIVIYQY MDDLYVGSDL
EIGQHRTKIE ELRQHLLRWG FTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT
VNDIQKLVGK LNWASQIYAG IKVRQLCKLL RGTKALTEVV PLTEEAELEL AENREILKEP
VHGVYYDPSK DLIAEIQKQG QGQWTYQIYQ EPFKNLKTGK YARMKGAHTN DVKQLTEAVQ
KIATESIVIW GKTPKFKLPI QKETWEAWWT EYWQATWIPE WEFVNTPPLV KLWYQLEKEP
IIGAETFYVD GAANRETKLG KAGYVTDRGR QKVVPLTDTT NQKTELQAIH LALQDSGLEV
NIVTDSQYAL GIIQAQPDKS ESELVSQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDGLVS
AGIRKVLFLD GIDKAQEEHE KYHSNWRAMA SDFNLPPVVA KEIVASCDKC QLKGEAMHGQ
VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK LAGRWPVKTV
HTDNGSNFTS TTVKAACWWA GIKQEFGIPY NPQSQGVIES MNKELKKIIG QVRDQAEHLK
TAVQMAVFIH NFKRKGGIGG YSAGERIVDI IATDIQTKEL QKQITKIQNF RVYYRDSRDP
VWKGPAKLLW KGEGAVVIQD NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED
