UniProt functional annotation for P58301



	UniProt functional annotation for P58301

UniProt code: P58301.

Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).

Taxonomy: Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus.

Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair (PubMed:11029422, PubMed:18957200). The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA (PubMed:18957200). Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex (PubMed:24493214). The ATP-bound conformation promotes DNA end binding and end tethering, and alters Mre11 nuclease activity (PubMed:24493214). ATP hydrolysis promotes both Mre11 activity as well as HerA/NurA activity (PubMed:24493214). Has also reversible adenylate kinase activity (PubMed:17349953). {ECO:0000269|PubMed:11029422, ECO:0000269|PubMed:17349953, ECO:0000269|PubMed:18957200, ECO:0000269|PubMed:24493214}.

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000269|PubMed:12152085}; Note=Binds 1 zinc ion per homodimer. {ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000269|PubMed:12152085};

Activity regulation: The adenylate kinase inhibitor P(1),P(5)- di(adenosine-5') pentaphosphate (Ap5A) inhibits adenylate kinase activity, but does not affect ATPase activity. {ECO:0000269|PubMed:17349953}.

Subunit: Homodimer (PubMed:10892749, PubMed:14698290). Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits (PubMed:11371344, PubMed:21441914, PubMed:22102415). Homodimerization is promoted by ATP binding (PubMed:10892749). {ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:11371344, ECO:0000269|PubMed:14698290, ECO:0000269|PubMed:21441914, ECO:0000269|PubMed:22102415}.

Domain: Binding of ATP induces a closed, compact conformation of the Rad50/Mre11 complex. ATP hydrolysis opens the complex. {ECO:0000269|PubMed:22102415}.

Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer. {ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000269|PubMed:12152085}.

Similarity: Belongs to the SMC family. RAD50 subfamily. {ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
Taxonomy:		Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus.



Function:		Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair (PubMed:11029422, PubMed:18957200). The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA (PubMed:18957200). Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex (PubMed:24493214). The ATP-bound conformation promotes DNA end binding and end tethering, and alters Mre11 nuclease activity (PubMed:24493214). ATP hydrolysis promotes both Mre11 activity as well as HerA/NurA activity (PubMed:24493214). Has also reversible adenylate kinase activity (PubMed:17349953). {ECO:0000269\|PubMed:11029422, ECO:0000269\|PubMed:17349953, ECO:0000269\|PubMed:18957200, ECO:0000269\|PubMed:24493214}.


Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255\|HAMAP-Rule:MF_00449, ECO:0000269\|PubMed:12152085}; Note=Binds 1 zinc ion per homodimer. {ECO:0000255\|HAMAP-Rule:MF_00449, ECO:0000269\|PubMed:12152085};
Activity regulation:		The adenylate kinase inhibitor P(1),P(5)- di(adenosine-5') pentaphosphate (Ap5A) inhibits adenylate kinase activity, but does not affect ATPase activity. {ECO:0000269\|PubMed:17349953}.
Subunit:		Homodimer (PubMed:10892749, PubMed:14698290). Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits (PubMed:11371344, PubMed:21441914, PubMed:22102415). Homodimerization is promoted by ATP binding (PubMed:10892749). {ECO:0000269\|PubMed:10892749, ECO:0000269\|PubMed:11371344, ECO:0000269\|PubMed:14698290, ECO:0000269\|PubMed:21441914, ECO:0000269\|PubMed:22102415}.
Domain:		Binding of ATP induces a closed, compact conformation of the Rad50/Mre11 complex. ATP hydrolysis opens the complex. {ECO:0000269\|PubMed:22102415}.
Domain:		The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer. {ECO:0000255\|HAMAP-Rule:MF_00449, ECO:0000269\|PubMed:12152085}.
Similarity:		Belongs to the SMC family. RAD50 subfamily. {ECO:0000255\|HAMAP-Rule:MF_00449, ECO:0000305}.