TNPA_BPMU
ID TNPA_BPMU Reviewed; 663 AA.
AC P07636; P06021;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DDE-recombinase A;
DE EC=3.1.22.-;
DE EC=6.5.1.-;
DE AltName: Full=DDE-transposase A;
DE AltName: Full=Gene product 03;
DE Short=gp03;
DE AltName: Full=Gene product A;
DE Short=gpA;
DE AltName: Full=MuA;
GN Name=A; OrderedLocusNames=Mup03;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2999776; DOI=10.1073/pnas.82.22.7676;
RA Harshey R.M., Getzoff E.D., Baldwin D.L., Miller J.L., Chaconas G.;
RT "Primary structure of phage mu transposase: homology to mu repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7676-7680(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Priess H., Brauer B., Schmidt C., Kamp D.;
RT "Sequence of the left end of Mu.";
RL (In) Symonds N., Toussaint A., van de Putte P., Howe M.M. (eds.);
RL Phage Mu, pp.277-296, Cold Spring Harbor Laboratory Press, New York (1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
RX PubMed=6214696; DOI=10.1007/bf00729448;
RA Priess H., Kamp D., Kahmann R., Braeuer B., Delius H.;
RT "Nucleotide sequence of the immunity region of bacteriophage Mu.";
RL Mol. Gen. Genet. 186:315-321(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84.
RX PubMed=6222246; DOI=10.1007/bf00330326;
RA Toussaint A., Faelen M., Desmet L., Allet B.;
RT "The products of gene A of the related phages Mu and D108 differ in their
RT specificities.";
RL Mol. Gen. Genet. 190:70-79(1983).
RN [6]
RP FUNCTION.
RX PubMed=2555166; DOI=10.1002/j.1460-2075.1989.tb08513.x;
RA Surette M.G., Lavoie B.D., Chaconas G.;
RT "Action at a distance in Mu DNA transposition: an enhancer-like element is
RT the site of action of supercoiling relief activity by integration host
RT factor (IHF).";
RL EMBO J. 8:3483-3489(1989).
RN [7]
RP INDUCTION.
RX PubMed=2524470; DOI=10.1128/jb.171.6.3440-3448.1989;
RA Stoddard S.F., Howe M.M.;
RT "Localization and regulation of bacteriophage Mu promoters.";
RL J. Bacteriol. 171:3440-3448(1989).
RN [8]
RP SUBUNIT, AND IDENTIFICATION IN THE TRANSPOSOSOME COMPLEX.
RX PubMed=1655409; DOI=10.1002/j.1460-2075.1991.tb07856.x;
RA Lavoie B.D., Chan B.S., Allison R.G., Chaconas G.;
RT "Structural aspects of a higher order nucleoprotein complex: induction of
RT an altered DNA structure at the Mu-host junction of the Mu type 1
RT transpososome.";
RL EMBO J. 10:3051-3059(1991).
RN [9]
RP COFACTOR, AND MUTAGENESIS OF ASP-269; ASP-294; GLU-392; ASP-550; GLU-556;
RP GLU-558; ASP-567; GLU-573; ASP-596; GLU-599 AND GLU-602.
RX PubMed=7912831; DOI=10.1073/pnas.91.14.6654;
RA Baker T.A., Luo L.;
RT "Identification of residues in the Mu transposase essential for
RT catalysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6654-6658(1994).
RN [10]
RP MUTAGENESIS OF ASP-269; ASP-294; GLY-348 AND GLU-392.
RX PubMed=7836417; DOI=10.1074/jbc.270.3.1472;
RA Kim K., Namgoong S.Y., Jayaram M., Harshey R.M.;
RT "Step-arrest mutants of phage Mu transposase. Implications in DNA-protein
RT assembly, Mu end cleavage, and strand transfer.";
RL J. Biol. Chem. 270:1472-1479(1995).
RN [11]
RP FUNCTION OF C-TERMINAL REGION.
RX PubMed=7641701; DOI=10.1002/j.1460-2075.1995.tb00053.x;
RA Wu Z., Chaconas G.;
RT "A novel DNA binding and nuclease activity in domain III of Mu transposase:
RT evidence for a catalytic region involved in donor cleavage.";
RL EMBO J. 14:3835-3843(1995).
RN [12]
RP DNA-BINDING.
RX PubMed=8577730; DOI=10.1073/pnas.93.3.1146;
RA Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H.,
RA Mizuuchi K., Clore G.M., Gronenborn A.M.;
RT "The wing of the enhancer-binding domain of Mu phage transposase is
RT flexible and is essential for efficient transposition.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1146-1150(1996).
RN [13]
RP INTERACTION WITH MUB AND HOST CLPX.
RX PubMed=9203582; DOI=10.1101/gad.11.12.1561;
RA Levchenko I., Yamauchi M., Baker T.A.;
RT "ClpX and MuB interact with overlapping regions of Mu transposase:
RT implications for control of the transposition pathway.";
RL Genes Dev. 11:1561-1572(1997).
RN [14]
RP SUBUNIT.
RX PubMed=9649447; DOI=10.1093/emboj/17.13.3775;
RA Namgoong S.Y., Harshey R.M.;
RT "The same two monomers within a MuA tetramer provide the DDE domains for
RT the strand cleavage and strand transfer steps of transposition.";
RL EMBO J. 17:3775-3785(1998).
RN [15]
RP FUNCTION.
RX PubMed=11298282; DOI=10.1046/j.1365-2958.2001.02364.x;
RA Roldan L.A., Baker T.A.;
RT "Differential role of the Mu B protein in phage Mu integration vs.
RT replication: mechanistic insights into two transposition pathways.";
RL Mol. Microbiol. 40:141-155(2001).
RN [16]
RP FUNCTION.
RX PubMed=11756423; DOI=10.1074/jbc.m110341200;
RA Goldhaber-Gordon I., Williams T.L., Baker T.A.;
RT "DNA recognition sites activate MuA transposase to perform transposition of
RT non-Mu DNA.";
RL J. Biol. Chem. 277:7694-7702(2002).
RN [17]
RP FUNCTION.
RX PubMed=11756424; DOI=10.1074/jbc.m110342200;
RA Goldhaber-Gordon I., Early M.H., Gray M.K., Baker T.A.;
RT "Sequence and positional requirements for DNA sites in a mu
RT transpososome.";
RL J. Biol. Chem. 277:7703-7712(2002).
RN [18]
RP FUNCTION.
RX PubMed=12086600; DOI=10.1016/s0092-8674(02)00728-6;
RA Pathania S., Jayaram M., Harshey R.M.;
RT "Path of DNA within the Mu transpososome. Transposase interactions bridging
RT two Mu ends and the enhancer trap five DNA supercoils.";
RL Cell 109:425-436(2002).
RN [19]
RP CHARACTERIZATION, AND COFACTOR.
RX PubMed=14661976; DOI=10.1021/bi035360o;
RA Goldhaber-Gordon I., Early M.H., Baker T.A.;
RT "MuA transposase separates DNA sequence recognition from catalysis.";
RL Biochemistry 42:14633-14642(2003).
RN [20]
RP REVIEW.
RX PubMed=16046622; DOI=10.1110/ps.051417505;
RA Burton B.M., Baker T.A.;
RT "Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu
RT transposase.";
RL Protein Sci. 14:1945-1954(2005).
RN [21]
RP DNA-BINDING.
RX PubMed=17669422; DOI=10.1016/j.jmb.2007.06.086;
RA Yin Z., Suzuki A., Lou Z., Jayaram M., Harshey R.M.;
RT "Interactions of phage Mu enhancer and termini that specify the assembly of
RT a topologically unique interwrapped transpososome.";
RL J. Mol. Biol. 372:382-396(2007).
RN [22]
RP INTERACTION WITH HOST CLPX.
RX PubMed=18406325; DOI=10.1016/j.molcel.2008.02.013;
RA Abdelhakim A.H., Oakes E.C., Sauer R.T., Baker T.A.;
RT "Unique contacts direct high-priority recognition of the tetrameric Mu
RT transposase-DNA complex by the AAA+ unfoldase ClpX.";
RL Mol. Cell 30:39-50(2008).
RN [23]
RP FUNCTION AS FLAPS ENDONUCLEASE, AND MUTAGENESIS OF 575-ARG--LYS-579.
RX PubMed=20167799; DOI=10.1073/pnas.0912615107;
RA Choi W., Harshey R.M.;
RT "DNA repair by the cryptic endonuclease activity of Mu transposase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10014-10019(2010).
RN [24]
RP FUNCTION.
RX PubMed=20133746; DOI=10.1073/pnas.0910905106;
RA Abdelhakim A.H., Sauer R.T., Baker T.A.;
RT "The AAA+ ClpX machine unfolds a keystone subunit to remodel the Mu
RT transpososome.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2437-2442(2010).
RN [25]
RP FUNCTION.
RX PubMed=22511883; DOI=10.1371/journal.pgen.1002642;
RA Jang S., Sandler S.J., Harshey R.M.;
RT "Mu insertions are repaired by the double-strand break repair pathway of
RT Escherichia coli.";
RL PLoS Genet. 8:E1002642-E1002642(2012).
RN [26]
RP STRUCTURE BY NMR OF 1-76.
RX PubMed=7881904; DOI=10.1016/s0969-2126(94)00107-3;
RA Clubb R.T., Omichinski J.G., Savilahti H., Mizuuchi K., Gronenborn A.M.,
RA Clore G.M.;
RT "A novel class of winged helix-turn-helix protein: the DNA-binding domain
RT of Mu transposase.";
RL Structure 2:1041-1048(1994).
RN [27]
RP STRUCTURE BY NMR OF 76-174.
RX PubMed=9405381; DOI=10.1093/emboj/16.24.7532;
RA Schumacher S., Clubb R.T., Cai M., Mizuuchi K., Clore G.M.,
RA Gronenborn A.M.;
RT "Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu
RT transposase: modular DNA recognition by two tethered domains.";
RL EMBO J. 16:7532-7541(1997).
RN [28]
RP STRUCTURE BY NMR OF 173-247.
RX PubMed=9367742; DOI=10.1006/jmbi.1997.1312;
RA Clubb R.T., Schumacher S., Mizuuchi K., Gronenborn A.M., Clore G.M.;
RT "Solution structure of the I gamma subdomain of the Mu end DNA-binding
RT domain of phage Mu transposase.";
RL J. Mol. Biol. 273:19-25(1997).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 248-574, AND METAL-BINDING.
RX PubMed=7628012; DOI=10.1016/0092-8674(95)90308-9;
RA Rice P., Mizuuchi K.;
RT "Structure of the bacteriophage Mu transposase core: a common structural
RT motif for DNA transposition and retroviral integration.";
RL Cell 82:209-220(1995).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.71 ANGSTROMS) OF 77-605, AND FUNCTION.
RX PubMed=23135398; DOI=10.1038/nature11602;
RA Montano S.P., Pigli Y.Z., Rice P.A.;
RT "The mu transpososome structure sheds light on DDE recombinase evolution.";
RL Nature 491:413-417(2012).
CC -!- FUNCTION: Responsible for viral genome integration into the host
CC chromosome. During integration of the incoming virus, DDE-recombinase A
CC cleaves both viral DNA ends and the resulting 3'-OH perform a
CC nucleophilic attack of the host DNA. The 5' flanking DNA attached to
CC the ends of the viral genome (flaps) are resected by the DDE-
CC recombinase A endonuclease activity, with the help of host chaperone
CC ClpX. The gaps created in the host chromosome by the viral genome
CC insertion are repaired by the host primary machinery for double-strand
CC break repair.
CC -!- FUNCTION: Responsible for replication of the viral genome by
CC replicative transposition. During replicative transposition, DDE-
CC recombinase A is part of the transpososome complex. DDE-recombinase A
CC cleaves the viral DNA and the resulting 3'-OH performs a nucleophilic
CC attack of the host DNA. The 5' flanking DNA is not resected and an
CC intermediary structure is formed. This structure is resolved by target-
CC primed replication leading to two copies of the viral genome (the
CC original one and the copied one). Host ClpX and translation initiation
CC factor IF2 play an essential transpososome-remodeling role by releasing
CC the block between transposition and DNA replication. Successive rounds
CC of replicative transposition can lead up to 100 copies of the viral
CC genome.
CC -!- FUNCTION: Promotes replication and thereby lytic development by
CC competing with repressor c (Repc) for binding to the internal
CC activation sequence (IAS) in the enhancer/operator region. The outcome
CC of this competition determines if the virus enters latency or starts
CC replication.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14661976, ECO:0000269|PubMed:7912831};
CC -!- SUBUNIT: Homotetramer. Part of the transpososome complex composed of a
CC DDE-recombinase A tetramer synapsing the ends of the viral genome and
CC the enhancer element. Interacts with target DNA activator B; this
CC interaction brings DDE-recombinase A to the transposition target site.
CC Interacts with host ClpX; this interaction remodels the transpososome
CC for replication and is required for the flaps endonuclease activity of
CC DDE-recombinase A. Binds (via N-terminus) three distinct recognition
CC sites in the AttR and AttL regions of the viral genome ends: R1, R2,
CC and R3 on the right end and L1, L2, and L3 on the left, not all of
CC which are essential for transposition. The active transpososome is
CC formed by three DDE-recombinase A subunits tightly bound to R1, R2, L1
CC plus a fourth subunit tightly bound in the complex but weakly bound to
CC the L2 recognition site. Only two subunits out of the four involved are
CC responsible for catalysis. Each subunit performs the cleavage and
CC joining reactions for one DNA end and acts in trans, ensuring the
CC reaction is only initiated when both viral genome ends are paired.
CC {ECO:0000269|PubMed:1655409, ECO:0000269|PubMed:18406325,
CC ECO:0000269|PubMed:9203582, ECO:0000269|PubMed:9649447}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC Expression of early genes is repressed by viral Repc (latency) and
CC favored by viral Ner protein. {ECO:0000269|PubMed:2524470}.
CC -!- DOMAIN: The catalytic domain contains two distinct activities, the
CC cleavage and strand transfer activity and the flaps endonuclease
CC activity. The N-terminal HTH Mu-type domain 1-alpha is responsible for
CC sequence-specific DNA binding to the IAS. Two adjacent regions 1-beta
CC and 1-gamma bind to the ends of the viral genome.
CC -!- DOMAIN: Contains a D-x(n)-D-x(35)-E motif, named for the conserved
CC glutamic acid and aspartic acid residues and the invariant 35 amino
CC acid spacing between the second and third acidic residues. These
CC residues coordinate the metal ions required for nucleophile activation.
CC Each acidic residue of the D,D(35)E motif is independently essential
CC for the 3'-processing and strand transfer activities (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: This enzyme is structurally similar to and performs the
CC same endonucleotidic reaction as retroviral integrases, RNase H, RuvC
CC holliday resolvases and RAG proteins.
CC -!- SIMILARITY: Belongs to the mulikevirus repressor c protein family.
CC {ECO:0000305}.
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DR EMBL; M11195; AAA32369.1; -; Genomic_DNA.
DR EMBL; M64097; AAA32379.1; -; Genomic_DNA.
DR EMBL; AF083977; AAF01083.1; -; Genomic_DNA.
DR EMBL; V01464; CAA24713.1; -; Genomic_DNA.
DR EMBL; V00868; CAA24236.1; -; Genomic_DNA.
DR PIR; A24746; TQBPU.
DR RefSeq; NP_050607.1; NC_000929.1.
DR PDB; 1BCM; X-ray; 2.80 A; A/B=248-574.
DR PDB; 1BCO; X-ray; 2.40 A; A=248-574.
DR PDB; 1TNS; NMR; -; A=1-76.
DR PDB; 1TNT; NMR; -; A=1-76.
DR PDB; 2EZH; NMR; -; A=174-247.
DR PDB; 2EZI; NMR; -; A=174-247.
DR PDB; 2EZK; NMR; -; A=77-174.
DR PDB; 2EZL; NMR; -; A=77-174.
DR PDB; 4FCY; X-ray; 3.71 A; A/B=77-605.
DR PDBsum; 1BCM; -.
DR PDBsum; 1BCO; -.
DR PDBsum; 1TNS; -.
DR PDBsum; 1TNT; -.
DR PDBsum; 2EZH; -.
DR PDBsum; 2EZI; -.
DR PDBsum; 2EZK; -.
DR PDBsum; 2EZL; -.
DR PDBsum; 4FCY; -.
DR BMRB; P07636; -.
DR SMR; P07636; -.
DR DIP; DIP-59984N; -.
DR GeneID; 2636292; -.
DR KEGG; vg:2636292; -.
DR EvolutionaryTrace; P07636; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IMP:CACAO.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004803; F:transposase activity; IMP:UniProtKB.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0098689; P:latency-replication decision; IEA:UniProtKB-KW.
DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.30.130; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR003314; Mu-type_HTH.
DR InterPro; IPR015126; Mu_I-gamma.
DR InterPro; IPR004189; Phage_Mu_transposase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015378; Transposase-like_Mu_C.
DR InterPro; IPR009004; Transposase_Mu_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF02914; DDE_2; 1.
DR Pfam; PF02316; HTH_Tnp_Mu_1; 1.
DR Pfam; PF09039; HTH_Tnp_Mu_2; 1.
DR Pfam; PF09299; Mu-transpos_C; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50610; SSF50610; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51702; HTH_MU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA excision; DNA integration; DNA recombination;
KW DNA replication; DNA-binding; Early protein; Host cytoplasm; Hydrolase;
KW Latency-replication decision; Ligase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Transposable element; Transposition;
KW Viral DNA replication.
FT CHAIN 1..663
FT /note="DDE-recombinase A"
FT /id="PRO_0000077584"
FT DOMAIN 1..69
FT /note="HTH Mu-type; 1-alpha, viral IAS binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01039"
FT DNA_BIND 176..196
FT /note="H-T-H motif; viral genome ends binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01039"
FT REGION 77..174
FT /note="1-beta, viral genome ends binding"
FT REGION 175..247
FT /note="1-gamma, viral genome ends binding"
FT REGION 249..490
FT /note="Catalytic"
FT REGION 491..605
FT /note="Target DNA capture and bending"
FT REGION 575..579
FT /note="Involved in flaps endonuclease activity"
FT REGION 605..663
FT /note="Interaction with MuB"
FT REGION 656..663
FT /note="Interaction with and host ClpX"
FT MOTIF 269..392
FT /note="DDE"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT MUTAGEN 269
FT /note="D->N: Complete loss of both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7836417,
FT ECO:0000269|PubMed:7912831"
FT MUTAGEN 269
FT /note="D->V: Loss of DNA-protein assembly."
FT /evidence="ECO:0000269|PubMed:7836417,
FT ECO:0000269|PubMed:7912831"
FT MUTAGEN 294
FT /note="D->N: Almost complete loss of both the DNA cleavage
FT and joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7836417,
FT ECO:0000269|PubMed:7912831"
FT MUTAGEN 348
FT /note="G->D: Loss of DNA-protein assembly."
FT /evidence="ECO:0000269|PubMed:7836417"
FT MUTAGEN 392
FT /note="E->A: Complete loss of both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7836417,
FT ECO:0000269|PubMed:7912831"
FT MUTAGEN 392
FT /note="E->Q: Complete loss of both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7836417,
FT ECO:0000269|PubMed:7912831"
FT MUTAGEN 550
FT /note="D->N: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT MUTAGEN 556
FT /note="E->Q: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT MUTAGEN 558
FT /note="E->Q: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT MUTAGEN 567
FT /note="D->N: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT MUTAGEN 573
FT /note="E->Q: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT MUTAGEN 575..579
FT /note="RRRQK->KKKQR: No effect on DNA-binding and flaps
FT endonuclease activity."
FT /evidence="ECO:0000269|PubMed:20167799"
FT MUTAGEN 575..579
FT /note="RRRQK->LQLQQ: Almost complete loss of flaps
FT endonuclease activity, DNA-binding and transpososome
FT assembly."
FT /evidence="ECO:0000269|PubMed:20167799"
FT MUTAGEN 576..579
FT /note="RRQK->QRQQ: Partial loss of flaps endonuclease
FT activity resulting in delayed flaps removal. Complete loss
FT of DNA-binding."
FT MUTAGEN 596
FT /note="D->N: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT MUTAGEN 599
FT /note="E->Q: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT MUTAGEN 602
FT /note="E->Q: Almost no effect on both the DNA cleavage and
FT joining activities without bloing tetramer assembly."
FT /evidence="ECO:0000269|PubMed:7912831"
FT CONFLICT 66
FT /note="G -> R (in Ref. 5; CAA24236)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="P -> S (in Ref. 2; AAA32379)"
FT /evidence="ECO:0000305"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1TNS"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1TNS"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1TNS"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1TNS"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1TNS"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:1TNS"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1TNS"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2EZK"
FT HELIX 101..122
FT /evidence="ECO:0007829|PDB:2EZK"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:2EZK"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2EZL"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:2EZK"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:2EZK"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:2EZH"
FT HELIX 200..214
FT /evidence="ECO:0007829|PDB:2EZH"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:2EZH"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:2EZH"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:1BCO"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 311..325
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1BCM"
FT TURN 341..346
FT /evidence="ECO:0007829|PDB:1BCO"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1BCO"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:1BCM"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:1BCO"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1BCO"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1BCM"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 433..449
FT /evidence="ECO:0007829|PDB:1BCO"
FT TURN 456..461
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 482..487
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 529..535
FT /evidence="ECO:0007829|PDB:1BCO"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:1BCO"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:1BCO"
FT STRAND 553..559
FT /evidence="ECO:0007829|PDB:1BCO"
SQ SEQUENCE 663 AA; 75003 MW; B882CFDCBFC0B2E3 CRC64;
MELWVSPKEC ANLPGLPKTS AGVIYVAKKQ GWQNRTRAGV KGGKAIEYNA NSLPVEAKAA
LLLRQGEIET SLGYFEIARP TLEAHDYDRE ALWSKWDNAS DSQRRLAEKW LPAVQAADEM
LNQGISTKTA FATVAGHYQV SASTLRDKYY QVQKFAKPDW AAALVDGRGA SRRNVHKSEF
DEDAWQFLIA DYLRPEKPAF RKCYERLELA AREHGWSIPS RATAFRRIQQ LDEAMVVACR
EGEHALMHLI PAQQRTVEHL DAMQWINGDG YLHNVFVRWF NGDVIRPKTW FWQDVKTRKI
LGWRCDVSEN IDSIRLSFMD VVTRYGIPED FHITIDNTRG AANKWLTGGA PNRYRFKVKE
DDPKGLFLLM GAKMHWTSVV AGKGWGQAKP VERAFGVGGL EEYVDKHPAL AGAYTGPNPQ
AKPDNYGDRA VDAELFLKTL AEGVAMFNAR TGRETEMCGG KLSFDDVFER EYARTIVRKP
TEEQKRMLLL PAEAVNVSRK GEFTLKVGGS LKGAKNVYYN MALMNAGVKK VVVRFDPQQL
HSTVYCYTLD GRFICEAECL APVAFNDAAA GREYRRRQKQ LKSATKAAIK AQKQMDALEV
AELLPQIAEP AAPESRIVGI FRPSGNTERV KNQERDDEYE TERDEYLNHS LDILEQNRRK
KAI
