##gff-version 3
P0A814	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1661673,ECO:0000269|PubMed:1758493;Dbxref=PMID:1661673,PMID:1758493	
P0A814	UniProtKB	Chain	2	173	.	.	.	ID=PRO_0000183096;Note=Crossover junction endodeoxyribonuclease RuvC	
P0A814	UniProtKB	Active site	8	8	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_00034	
P0A814	UniProtKB	Active site	67	67	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_00034	
P0A814	UniProtKB	Active site	139	139	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_00034	
P0A814	UniProtKB	Binding site	8	8	.	.	.	Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_00034,ECO:0000305|PubMed:7923356;Dbxref=PMID:7923356	
P0A814	UniProtKB	Binding site	67	67	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_00034	
P0A814	UniProtKB	Binding site	139	139	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_00034	
P0A814	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Does not complement deletion%2C loss of Holliday junction (HJ) cleavage%2C forms dimer%2C binds DNA%2C dominant negative to wild-type (wt). D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638215;Dbxref=PMID:7638215	
P0A814	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Does not complement deletion%2C loss of HJ cleavage%2C forms dimer%2C binds DNA%2C dominant negative to wt. Decreases endonuclease activity%2C forms RuvA-RuvC-DNA complex. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7638215,ECO:0000269|PubMed:9000618;Dbxref=PMID:7638215,PMID:9000618	
P0A814	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Does not complement deletion%2C loss of HJ cleavage%2C forms dimer%2C binds DNA%2C dominant negative to wt. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638215;Dbxref=PMID:7638215	
P0A814	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Does not complement deletion%2C very low HJ cleavage%2C forms dimer%2C binds DNA%2C dominant negative to wt. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638215;Dbxref=PMID:7638215	
P0A814	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Loss of DNA repair activity. R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7923356;Dbxref=PMID:7923356	
P0A814	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Inhibits endonuclease activity%2C loss of some RuvA-RuvC-DNA complexes. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9000618;Dbxref=PMID:9000618	
P0A814	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Inhibits endonuclease activity%2C forms RuvA-RuvC-DNA complex. G->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9000618;Dbxref=PMID:9000618	
P0A814	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Inhibits endonuclease activity%2C forms RuvA-RuvC-DNA complex. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9000618;Dbxref=PMID:9000618	
P0A814	UniProtKB	Mutagenesis	119	119	.	.	.	Note=Loss of DNA repair activity. K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7923356;Dbxref=PMID:7923356	
P0A814	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Does not complement deletion%2C loss of HJ cleavage%2C forms dimer%2C binds DNA%2C dominant negative to wt. D->E%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638215;Dbxref=PMID:7638215	
P0A814	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Loss of HJ cleavage in Mg(2+)%2C poor cleavage with Mn(2+). D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36000732;Dbxref=PMID:36000732	
P0A814	UniProtKB	Mutagenesis	142	142	.	.	.	Note=Does not complement deletion%2C very low HJ cleavage%2C forms dimer%2C binds DNA%2C dominant negative to wt. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638215;Dbxref=PMID:7638215	
P0A814	UniProtKB	Mutagenesis	142	142	.	.	.	Note=Does not complement deletion%2C loss of HJ cleavage%2C forms dimer%2C binds DNA%2C dominant negative to wt. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638215;Dbxref=PMID:7638215	
P0A814	UniProtKB	Beta strand	3	8	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Beta strand	11	22	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Beta strand	25	35	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Helix	41	59	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Beta strand	62	68	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Helix	78	93	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Turn	94	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Beta strand	99	103	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Helix	104	111	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Beta strand	113	116	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Helix	119	129	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Helix	141	152	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR	
P0A814	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HJR