FEN_BPT5
ID FEN_BPT5 Reviewed; 291 AA.
AC P06229; Q5DMH3; Q66LT5;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Flap endonuclease {ECO:0000255|HAMAP-Rule:MF_04140};
DE Short=FEN {ECO:0000255|HAMAP-Rule:MF_04140};
DE EC=3.1.11.- {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:17559871, ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:9874768};
DE AltName: Full=5'-3' exonuclease {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000303|PubMed:8657312};
DE AltName: Full=Exodeoxyribonuclease {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000303|PubMed:2211703};
DE EC=3.1.11.3 {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:17559871, ECO:0000269|PubMed:2211703, ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:9380501, ECO:0000269|PubMed:9874768};
GN Name=D15; Synonyms=exo5 {ECO:0000312|EMBL:AAX12058.1};
GN ORFNames=T5.130 {ECO:0000312|EMBL:AAS77176.1},
GN T5p128 {ECO:0000312|EMBL:AAU05267.1};
OS Escherichia phage T5 (Enterobacteria phage T5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX NCBI_TaxID=2695836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3002857; DOI=10.1016/0014-5793(86)80130-2;
RA Kaliman A.V., Krutilina A.I., Kryukov V.M., Bayev A.A.;
RT "Cloning and DNA sequence of the 5'-exonuclease gene of bacteriophage T5.";
RL FEBS Lett. 195:61-64(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT "Bacteriophage T5 complete genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:AAX12058.1};
RX PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA Hu S.;
RT "Complete genome sequence of bacteriophage T5.";
RL Virology 332:45-65(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St0 deletion mutant;
RX PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA Boulanger P.;
RT "Insights into bacteriophage T5 structure from analysis of its
RT morphogenesis genes and protein components.";
RL J. Virol. 88:1162-1174(2014).
RN [5]
RP PROTEIN SEQUENCE OF 2-20, AND CATALYTIC ACTIVITY.
RX PubMed=2211703; DOI=10.1016/s0021-9258(17)44753-3;
RA Sayers J.R., Eckstein F.;
RT "Properties of overexpressed phage T5 D15 exonuclease. Similarities with
RT Escherichia coli DNA polymerase I 5'-3' exonuclease.";
RL J. Biol. Chem. 265:18311-18317(1990).
RN [6]
RP PROTEIN SEQUENCE OF 18-27, DNA-BINDING, ACTIVITY REGULATION, MUTAGENESIS OF
RP CYS-115, AND CATALYTIC ACTIVITY.
RX PubMed=9380501; DOI=10.1093/nar/25.19.3801;
RA Garforth S.J., Sayers J.R.;
RT "Structure-specific DNA binding by bacteriophage T5 5'-->3' exonuclease.";
RL Nucleic Acids Res. 25:3801-3807(1997).
RN [7]
RP MUTAGENESIS OF LYS-83; LYS-196 AND LYS-215, AND CATALYTIC ACTIVITY.
RX PubMed=9889266; DOI=10.1093/nar/27.3.730;
RA Pickering T.J., Garforth S.J., Thorpe S.J., Sayers J.R., Grasby J.A.;
RT "A single cleavage assay for T5 5'-->3' exonuclease: determination of the
RT catalytic parameters for wild-type and mutant proteins.";
RL Nucleic Acids Res. 27:730-735(1999).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-83.
RX PubMed=10364212; DOI=10.1074/jbc.274.25.17711;
RA Pickering T.J., Garforth S., Sayers J.R., Grasby J.A.;
RT "Variation in the steady state kinetic parameters of wild type and mutant
RT T5 5'-3'-exonuclease with pH. Protonation of Lys-83 is critical for DNA
RT binding.";
RL J. Biol. Chem. 274:17711-17717(1999).
RN [9]
RP MUTAGENESIS OF ARG-33; ARG-172; LYS-215; ARG-216 AND LYS-241, AND
RP DNA-BINDING.
RX PubMed=12084915; DOI=10.1073/pnas.082241699;
RA Dervan J.J., Feng M., Patel D., Grasby J.A., Artymiuk P.J., Ceska T.A.,
RA Sayers J.R.;
RT "Interactions of mutant and wild-type flap endonucleases with
RT oligonucleotide substrates suggest an alternative model of DNA binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8542-8547(2002).
RN [10]
RP MUTAGENESIS OF TYR-82.
RX PubMed=12126622; DOI=10.1016/s0022-2836(02)00547-8;
RA Patel D., Tock M.R., Frary E., Feng M., Pickering T.J., Grasby J.A.,
RA Sayers J.R.;
RT "A conserved tyrosine residue aids ternary complex formation, but not
RT catalysis, in phage T5 flap endonuclease.";
RL J. Mol. Biol. 320:1025-1035(2002).
RN [11]
RP COFACTOR.
RX PubMed=12606565; DOI=10.1093/emboj/cdg098;
RA Tock M.R., Frary E., Sayers J.R., Grasby J.A.;
RT "Dynamic evidence for metal ion catalysis in the reaction mediated by a
RT flap endonuclease.";
RL EMBO J. 22:995-1004(2003).
RN [12]
RP CATALYTIC ACTIVITY.
RX PubMed=17559871; DOI=10.1016/j.jmb.2007.04.063;
RA Williams R., Sengerova B., Osborne S., Syson K., Ault S., Kilgour A.,
RA Chapados B.R., Tainer J.A., Sayers J.R., Grasby J.A.;
RT "Comparison of the catalytic parameters and reaction specificities of a
RT phage and an archaeal flap endonuclease.";
RL J. Mol. Biol. 371:34-48(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND DOMAIN.
RX PubMed=8657312; DOI=10.1038/382090a0;
RA Ceska T.A., Sayers J.R., Stier G., Suck D.;
RT "A helical arch allowing single-stranded DNA to thread through T5 5'-
RT exonuclease.";
RL Nature 382:90-93(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ALA-83, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF LYS-83; LYS-196 AND LYS-215, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9874768; DOI=10.1073/pnas.96.1.38;
RA Garforth S.J., Ceska T.A., Suck D., Sayers J.R.;
RT "Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3'
RT exonuclease suggests separate mechanisms of endo- and exonucleolytic
RT cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:38-43(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 2-290, COFACTOR, MUTAGENESIS OF
RP 128-GLU--ASP-130 AND 201-ASP--ASP-204, AND FUNCTION.
RX PubMed=15077103; DOI=10.1038/nsmb754;
RA Feng M., Patel D., Dervan J.J., Ceska T., Suck D., Haq I., Sayers J.R.;
RT "Roles of divalent metal ions in flap endonuclease-substrate
RT interactions.";
RL Nat. Struct. Mol. Biol. 11:450-456(2004).
RN [16] {ECO:0007744|PDB:5HML, ECO:0007744|PDB:5HMM, ECO:0007744|PDB:5HNK, ECO:0007744|PDB:5HP4}
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 20-291 IN COMPLEX WITH MAGNESIUM,
RP COFACTOR, DOMAIN, MUTAGENESIS OF ASP-153 AND ASP-155, CATALYTIC ACTIVITY,
RP AND REACTION MECHANISM.
RX PubMed=27273516; DOI=10.1038/nsmb.3241;
RA AlMalki F.A., Flemming C.S., Zhang J., Feng M., Sedelnikova S.E., Ceska T.,
RA Rafferty J.B., Sayers J.R., Artymiuk P.J.;
RT "Direct observation of DNA threading in flap endonuclease complexes.";
RL Nat. Struct. Mol. Biol. 23:640-646(2016).
CC -!- FUNCTION: Catalyzes both the 5'-exonucleolytic and structure-specific
CC endonucleolytic hydrolysis of DNA branched nucleic acid molecules and
CC probably plays a role in viral genome replication (PubMed:9874768,
CC PubMed:15077103, PubMed:10364212). Active on flap (branched duplex DNA
CC containing a free single-stranded 5'-end), 5'overhangs and pseudo-Y
CC structures (PubMed:9874768, PubMed:15077103, PubMed:10364212). The
CC substrates require a free, single-stranded 5' end, with endonucleolytic
CC hydrolysis occurring at the junction of double- and single-stranded DNA
CC (PubMed:9874768). This function may be used for example to trim such
CC branched molecules generated by Okazaki fragments synthesis during
CC replication. {ECO:0000255|HAMAP-Rule:MF_04140,
CC ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:15077103,
CC ECO:0000269|PubMed:9874768}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04140, ECO:0000269|PubMed:10364212,
CC ECO:0000269|PubMed:17559871, ECO:0000269|PubMed:2211703,
CC ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:9380501,
CC ECO:0000269|PubMed:9874768, ECO:0000269|PubMed:9889266};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04140,
CC ECO:0000269|PubMed:12606565, ECO:0000269|PubMed:15077103,
CC ECO:0000269|PubMed:27273516};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04140,
CC ECO:0000269|PubMed:27273516};
CC Note=Binds divalent metal cations, probably Mg(2+). In vitro low metal
CC concentrations selectively stimulate the endonuclease reaction.
CC Endonuclease activity is suggested to require only the first cation,
CC whereas exonuclease activity is suggested to require binding of both.
CC High pH favors the exonuclase activity whereas low pH favors the
CC endonuclease activity. Metal ions enhance substrate binding.
CC {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:12606565,
CC ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516};
CC -!- ACTIVITY REGULATION: Inhibited by p-hydroxymercuribenzoate (PHMB).
CC {ECO:0000269|PubMed:9380501}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.3 for the exonuclease activity, 5.5 for endonuclease
CC activity. High pH favors the exonuclase activity whereas low pH
CC favors the endonuclease activity. {ECO:0000269|PubMed:10364212,
CC ECO:0000269|PubMed:9874768};
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305|PubMed:15661140}.
CC -!- DOMAIN: Three alpha-helices form a helical arch which forms a hole in
CC the protein and through which the 5' flap of the scissile ssDNA is
CC threaded. {ECO:0000255|HAMAP-Rule:MF_04140,
CC ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:8657312}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX12058.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY543070; AAS77176.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX12058.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY692264; AAU05267.1; -; Genomic_DNA.
DR PIR; A23610; NCBPT5.
DR RefSeq; YP_006958.1; NC_005859.1.
DR PDB; 1EXN; X-ray; 2.50 A; A/B=2-291.
DR PDB; 1UT5; X-ray; 2.75 A; A/B=2-291.
DR PDB; 1UT8; X-ray; 2.75 A; A/B=2-291.
DR PDB; 1XO1; X-ray; 2.50 A; A/B=1-291.
DR PDB; 5HML; X-ray; 1.48 A; A/B=20-291.
DR PDB; 5HMM; X-ray; 1.50 A; A/B=20-290.
DR PDB; 5HNK; X-ray; 2.22 A; A/B=20-291.
DR PDB; 5HP4; X-ray; 1.86 A; A=20-291.
DR PDBsum; 1EXN; -.
DR PDBsum; 1UT5; -.
DR PDBsum; 1UT8; -.
DR PDBsum; 1XO1; -.
DR PDBsum; 5HML; -.
DR PDBsum; 5HMM; -.
DR PDBsum; 5HNK; -.
DR PDBsum; 5HP4; -.
DR SMR; P06229; -.
DR GeneID; 2777611; -.
DR KEGG; vg:2777611; -.
DR EvolutionaryTrace; P06229; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; Genome.
DR GO; GO:0019034; C:viral replication complex; IMP:CACAO.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IMP:CACAO.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IDA:CACAO.
DR GO; GO:0004529; F:exodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR GO; GO:0019086; P:late viral transcription; IMP:CACAO.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04140; FEN_T5; 1.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR038969; FEN.
DR InterPro; IPR043666; FEN_D15-like.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR PANTHER; PTHR42646; PTHR42646; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication; DNA-binding;
KW Early protein; Endonuclease; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Potassium; Reference proteome;
KW Viral DNA replication.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:2211703"
FT CHAIN 2..291
FT /note="Flap endonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140"
FT /id="PRO_0000165217"
FT DOMAIN 190..263
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140"
FT REGION 82..116
FT /note="Helical arch"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516, ECO:0000305|PubMed:8657312"
FT REGION 188..224
FT /note="DNA-binding; H3TH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516"
FT BINDING 83
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:10364212"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516,
FT ECO:0000269|PubMed:8657312"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516,
FT ECO:0000269|PubMed:8657312"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516"
FT BINDING 209
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516"
FT BINDING 212
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04140,
FT ECO:0000269|PubMed:27273516"
FT MUTAGEN 33
FT /note="R->A: 10 fold increase in the dissociation constant
FT for pseudo-Y binding. 3 fold increase in the dissociation
FT constant for 5'overhangs binding."
FT /evidence="ECO:0000269|PubMed:12084915"
FT MUTAGEN 82
FT /note="Y->F: 3.5-fold decrease in binding affinity for DNA.
FT No effect on endonuclease and exonuclease activities."
FT /evidence="ECO:0000269|PubMed:12126622"
FT MUTAGEN 83
FT /note="K->A: No exonuclease activity, retains full
FT endonuclease activity on a flap structure. Binds DNA
FT pseudo-Y substrates with a dissociation constant of 200
FT nM."
FT /evidence="ECO:0000269|PubMed:10364212,
FT ECO:0000269|PubMed:9874768, ECO:0000269|PubMed:9889266"
FT MUTAGEN 115
FT /note="C->S: Complete loss of inhibition by PHMB; when
FT associated with S-266."
FT /evidence="ECO:0000269|PubMed:9380501"
FT MUTAGEN 128..130
FT /note="EAD->QAN: Loss of both exo- and endonuclease
FT activity, still binds DNA."
FT /evidence="ECO:0000269|PubMed:15077103"
FT MUTAGEN 153
FT /note="D->K: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:27273516"
FT MUTAGEN 155
FT /note="D->K: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:27273516"
FT MUTAGEN 172
FT /note="R->A: 10 fold increase in the dissociation constant
FT for pseudo-Y binding. No effect on 5'overhangs binding."
FT /evidence="ECO:0000269|PubMed:12084915"
FT MUTAGEN 196
FT /note="K->A: 10% exonuclease activity, little change in
FT endonuclease activity. Binds DNA pseudo-Y substrates with a
FT dissociation constant of 200 nM."
FT /evidence="ECO:0000269|PubMed:9874768,
FT ECO:0000269|PubMed:9889266"
FT MUTAGEN 201..204
FT /note="DLGD->ILGS: Retains most endo- but very little
FT exonuclease activity; binds pseudo-Y substrate more tightly
FT than wt."
FT /evidence="ECO:0000269|PubMed:15077103"
FT MUTAGEN 201..204
FT /note="DLGD->RLGP,RLGR: Retains most endonuclease but
FT complete loss of exonuclease activity; binds pseudo-Y
FT substrate more tightly than wt."
FT /evidence="ECO:0000269|PubMed:15077103"
FT MUTAGEN 215
FT /note="K->A: Wild-type exo- and endonuclease activities. 10
FT fold increase in the dissociation constant for pseudo-Y
FT binding. Drastic increase in the dissociation constant for
FT 5'overhangs binding."
FT /evidence="ECO:0000269|PubMed:12084915,
FT ECO:0000269|PubMed:9889266"
FT MUTAGEN 216
FT /note="R->A: 100 fold increase in the dissociation constant
FT for pseudo-Y binding. Drastic increase in the dissociation
FT constant for 5'overhangs binding."
FT /evidence="ECO:0000269|PubMed:12084915"
FT MUTAGEN 241
FT /note="K->A: 10 fold increase in the dissociation constant
FT for pseudo-Y binding. 10 fold increase in the dissociation
FT constant for 5'overhangs binding."
FT /evidence="ECO:0000269|PubMed:12084915"
FT MUTAGEN 266
FT /note="C->S: Complete loss of inhibition by PHMB; when
FT associated with S-115."
FT /evidence="ECO:0000269|PubMed:9380501"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:5HML"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:5HML"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 95..118
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5HML"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:5HML"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5HML"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5HML"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1EXN"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:5HML"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:5HML"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:5HML"
SQ SEQUENCE 291 AA; 33448 MW; 234C9564E491B4E9 CRC64;
MSKSWGKFIE EEEAEMASRR NLMIVDGTNL GFRFKHNNSK KPFASSYVST IQSLAKSYSA
RTTIVLGDKG KSVFRLEHLP EYKGNRDEKY AQRTEEEKAL DEQFFEYLKD AFELCKTTFP
TFTIRGVEAD DMAAYIVKLI GHLYDHVWLI STDGDWDTLL TDKVSRFSFT TRREYHLRDM
YEHHNVDDVE QFISLKAIMG DLGDNIRGVE GIGAKRGYNI IREFGNVLDI IDQLPLPGKQ
KYIQNLNASE ELLFRNLILV DLPTYCVDAI AAVGQDVLDK FTKDILEIAE Q
