##gff-version 3 P06229 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2211703;Dbxref=PMID:2211703 P06229 UniProtKB Chain 2 291 . . . ID=PRO_0000165217;Note=Flap endonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04140 P06229 UniProtKB Domain 190 263 . . . Note=5'-3' exonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04140 P06229 UniProtKB Region 82 116 . . . Note=Helical arch;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516,ECO:0000305|PubMed:8657312;Dbxref=PMID:27273516,PMID:8657312 P06229 UniProtKB Region 188 224 . . . Note=DNA-binding%3B H3TH;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Binding site 83 83 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:10364212;Dbxref=PMID:10364212 P06229 UniProtKB Binding site 130 130 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Binding site 130 130 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Binding site 153 153 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:15077103,ECO:0000269|PubMed:27273516,ECO:0000269|PubMed:8657312;Dbxref=PMID:15077103,PMID:27273516,PMID:8657312 P06229 UniProtKB Binding site 155 155 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:15077103,ECO:0000269|PubMed:27273516,ECO:0000269|PubMed:8657312;Dbxref=PMID:15077103,PMID:27273516,PMID:8657312 P06229 UniProtKB Binding site 155 155 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Binding site 201 201 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Binding site 209 209 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Binding site 212 212 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_04140,ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Mutagenesis 33 33 . . . Note=10 fold increase in the dissociation constant for pseudo-Y binding. 3 fold increase in the dissociation constant for 5'overhangs binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12084915;Dbxref=PMID:12084915 P06229 UniProtKB Mutagenesis 82 82 . . . Note=3.5-fold decrease in binding affinity for DNA. No effect on endonuclease and exonuclease activities. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12126622;Dbxref=PMID:12126622 P06229 UniProtKB Mutagenesis 83 83 . . . Note=No exonuclease activity%2C retains full endonuclease activity on a flap structure. Binds DNA pseudo-Y substrates with a dissociation constant of 200 nM. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10364212,ECO:0000269|PubMed:9874768,ECO:0000269|PubMed:9889266;Dbxref=PMID:10364212,PMID:9874768,PMID:9889266 P06229 UniProtKB Mutagenesis 115 115 . . . Note=Complete loss of inhibition by PHMB%3B when associated with S-266. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9380501;Dbxref=PMID:9380501 P06229 UniProtKB Mutagenesis 128 130 . . . Note=Loss of both exo- and endonuclease activity%2C still binds DNA. EAD->QAN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15077103;Dbxref=PMID:15077103 P06229 UniProtKB Mutagenesis 153 153 . . . Note=Complete loss of enzymatic activity. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Mutagenesis 155 155 . . . Note=Complete loss of enzymatic activity. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27273516;Dbxref=PMID:27273516 P06229 UniProtKB Mutagenesis 172 172 . . . Note=10 fold increase in the dissociation constant for pseudo-Y binding. No effect on 5'overhangs binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12084915;Dbxref=PMID:12084915 P06229 UniProtKB Mutagenesis 196 196 . . . Note=10%25 exonuclease activity%2C little change in endonuclease activity. Binds DNA pseudo-Y substrates with a dissociation constant of 200 nM. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9874768,ECO:0000269|PubMed:9889266;Dbxref=PMID:9874768,PMID:9889266 P06229 UniProtKB Mutagenesis 201 204 . . . Note=Retains most endo- but very little exonuclease activity%3B binds pseudo-Y substrate more tightly than wt. DLGD->ILGS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15077103;Dbxref=PMID:15077103 P06229 UniProtKB Mutagenesis 201 204 . . . Note=Retains most endonuclease but complete loss of exonuclease activity%3B binds pseudo-Y substrate more tightly than wt. DLGD->RLGP%2CRLGR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15077103;Dbxref=PMID:15077103 P06229 UniProtKB Mutagenesis 215 215 . . . Note=Wild-type exo- and endonuclease activities. 10 fold increase in the dissociation constant for pseudo-Y binding. Drastic increase in the dissociation constant for 5'overhangs binding. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12084915,ECO:0000269|PubMed:9889266;Dbxref=PMID:12084915,PMID:9889266 P06229 UniProtKB Mutagenesis 216 216 . . . Note=100 fold increase in the dissociation constant for pseudo-Y binding. Drastic increase in the dissociation constant for 5'overhangs binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12084915;Dbxref=PMID:12084915 P06229 UniProtKB Mutagenesis 241 241 . . . Note=10 fold increase in the dissociation constant for pseudo-Y binding. 10 fold increase in the dissociation constant for 5'overhangs binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12084915;Dbxref=PMID:12084915 P06229 UniProtKB Mutagenesis 266 266 . . . Note=Complete loss of inhibition by PHMB%3B when associated with S-115. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9380501;Dbxref=PMID:9380501 P06229 UniProtKB Beta strand 21 26 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 27 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 32 34 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 35 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 44 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Beta strand 60 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 73 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Turn 80 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 84 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 95 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 129 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 141 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Beta strand 147 150 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 154 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Beta strand 164 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Beta strand 173 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXN P06229 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 180 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Beta strand 185 188 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 189 199 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 202 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 214 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 227 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 241 247 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 250 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 262 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML P06229 UniProtKB Helix 275 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HML