ID F0LKK5_THEBM Unreviewed; 865 AA.
AC F0LKK5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000256|HAMAP-Rule:MF_00449};
GN Name=rad50 {ECO:0000256|HAMAP-Rule:MF_00449};
GN OrderedLocusNames=TERMP_01864 {ECO:0000313|EMBL:ADT84839.1};
OS Thermococcus barophilus (strain DSM 11836 / MP).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT84839.1, ECO:0000313|Proteomes:UP000007478};
RN [1] {ECO:0000313|EMBL:ADT84839.1, ECO:0000313|Proteomes:UP000007478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX PubMed=21217005; DOI=10.1128/JB.01490-10;
RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT "Complete genome sequence of the hyperthermophilic, piezophilic,
RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL J. Bacteriol. 193:1481-1482(2011).
CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the
CC early steps of DNA double-strand break (DSB) repair. The complex may
CC facilitate opening of the processed DNA ends to aid in the recruitment
CC of HerA and NurA. Rad50 controls the balance between DNA end bridging
CC and DNA resection via ATP-dependent structural rearrangements of the
CC Rad50/Mre11 complex. {ECO:0000256|HAMAP-Rule:MF_00449}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00449};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000256|HAMAP-Rule:MF_00449};
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC subunits and two Rad50 subunits. {ECO:0000256|HAMAP-Rule:MF_00449}.
CC -!- DOMAIN: The two conserved Cys that bind zinc constitute the zinc-hook,
CC which separates the large intramolecular coiled coil regions. The 2 Cys
CC residues coordinate one molecule of zinc with the help of the 2 Cys
CC residues of the zinc-hook of another Rad50 molecule, thereby forming a
CC V-shaped homodimer. {ECO:0000256|HAMAP-Rule:MF_00449}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439, ECO:0000256|HAMAP-Rule:MF_00449}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00449}.
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DR EMBL; CP002372; ADT84839.1; -; Genomic_DNA.
DR AlphaFoldDB; F0LKK5; -.
DR KEGG; tba:TERMP_01864; -.
DR PATRIC; fig|391623.17.peg.1863; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR Proteomes; UP000007478; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.510; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF13304; AAA_21; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00449};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00449}; Reference proteome {ECO:0000313|Proteomes:UP000007478};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 398..501
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 168..329
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 368..439
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 465..709
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 25..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 769..774
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
SQ SEQUENCE 865 AA; 101143 MW; 9545499B6C2216CB CRC64;
MKNFLSHKDT KIDFPLGVTV FIGPNGAGKT SIIDAIFVAL FNTLPRGDKF DDIIYRGERE
AKIELEFEEG GIPYKIVWRR KKGKSSPTYE LYRLDKNMLI AHGVKAVKKE VENIIGIEKD
SAVNSILIRQ GEITSLLDQA PAKRKEIIGK LLGLEKLEKA WQFMREVIDH FEQIKNDLEK
EIAEIGGELR SKSEQREKLK QEIQELKEKI KELEQILKKL EHQLGEIKRE LDELNEKEKR
YNELMIELAK KTEGIKSVQE QIKRLEKDLN ESKEAKEKVK KLEEEIKKIP YLEKYIKCLN
ELKELNTEKE QLNADLSKIL EIRNEANEKI TVLCEKYGGN IEDSKEVGEL PSDLAEIAKF
VSRIFTWVES IVQQIEEKHK ELEKLIIKAL EVLPEATIEA KEKKLQELKE EKERLENEIS
RLQNEKGKLE GRINDLQQAL SMLGESDTCP VCKTKLTPEH RDKVKSEMQE EIRGLKEEIR
QKEKMLIEVS RQLLEVEKRI EQVSKVDIER IERLKKEIEE KKKELAEHYK ELQRIITGLN
DIENDIRSKI SDIESKIKEI EEKLNELIKE IGHKLEDPEN ELKELRKKKE EYDRLKPIAD
KYEELLKDLK EKQEELEQLE REKCKLQEEI EKLGYDKKHH EEVRKKHEEL LRQFERTKAE
LEEKNNSLKK KLEELNEVKE KIKELEEKLN NLEAELDKVK KFINDLERIR AAYHKDGVQK
LLRKKFAPAL SELATNYIES FNMDITDIYL SEDFDISVTK NSVEVPISLL SGGEKVAVAL
ALRLAIARVL ARRLSVIIMD EPTTHLDEER RRDLVEILGK FFKAENTVPQ IIIVTHHREL
EDVADTVYIV QKVDGISKVV ESSPL
//
