RAD50_THEKO
ID RAD50_THEKO Reviewed; 883 AA.
AC Q5JHN1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000255|HAMAP-Rule:MF_00449};
GN Name=rad50 {ECO:0000255|HAMAP-Rule:MF_00449}; OrderedLocusNames=TK2211;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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:0000255|HAMAP-Rule:MF_00449}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00449};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000255|HAMAP-Rule:MF_00449};
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC subunits and two Rad50 subunits. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00449}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00449}.
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DR EMBL; AP006878; BAD86400.1; -; Genomic_DNA.
DR RefSeq; WP_011251161.1; NC_006624.1.
DR AlphaFoldDB; Q5JHN1; -.
DR SMR; Q5JHN1; -.
DR STRING; 69014.TK2211; -.
DR EnsemblBacteria; BAD86400; BAD86400; TK2211.
DR GeneID; 3235694; -.
DR KEGG; tko:TK2211; -.
DR PATRIC; fig|69014.16.peg.2166; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR InParanoid; Q5JHN1; -.
DR OMA; ISHVQEM; -.
DR OrthoDB; 1771at2157; -.
DR PhylomeDB; Q5JHN1; -.
DR Proteomes; UP000000536; 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 CDD; cd03240; ABC_Rad50; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045171; ABC_Rad50.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..883
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138663"
FT DOMAIN 395..492
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 218..420
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 452..585
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 620..741
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 32..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 790..795
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 883 AA; 102727 MW; 914DCEE61996F88D CRC64;
MKIEKLIIKD FRSHALTKVN FSSGINLIIG QNGSGKSSIL DALLVGLYWP SKPKDLKKDD
FERINGSGTE ITVFFEKGNV KYQIHRNIGR GLAFVKYHDG SSWKTLETGQ KPVRDWMEKL
VPYDVFLNAI YIRQGEIDAI LESDESREKV VRQVLGLDRY ENSYKNLLDV RKEIDARIKA
IEDYLKSTEN IDELIGNLEK ELTSVLREIN EISPKLPELR GELGGLEKEL KELEKTAEEL
AKARVELKSE EGNLRELEAK KSGIQSMIRE TEKRVEELKE KVKELESLEE KAKEYERLSR
FYRNFTEGIN RIEKLLATYS QQAENLRERI DELSKKEARV KELLKEKEGL QKELGALEED
LKAYQRAKEL MANLERLKKR LTLSEEEIEK LEAEIQKARE RKEEIMKELE EIGSRRGELK
SIAGERNKAL MELKKAKGRC PVCGRELTEE HRKELLEKYT AELKEISAEM KELEKREKKL
RAELVEVEKT LKKERELFAL KEVLEQIRET EEKLKEYDLE KLEEANEKAE ELKKKLAGLE
GEIKSLEDEI KKGELLKKKL ALVEKKLREL EEERASLLGE LKKLGFGDVK ELEERLKELE
PAYKRYIELR PARDELKREE DLLKSLKLDL TAILKEIEKT SKRVEELRKR VEELEKSYDK
DRHEELKGKT RELSNELAGL EARLKSLEER RDEVKASLEK LREEKETRKE KAKELEKLKK
ARERVQRLRE KVKAYKNLLK EGALAKVGEM ASEIFEELTE EKYSGVTVKA EENKVRLGVV
YNGKEYGLGF LSGGERIALG LAFRLALSLY LAGEISLLIL DEPTPYLDEE RRRRLVDIMQ
RYLRKIPQVI VVSHDEELKD AADRVIRVSL ENGVSVVREA EVG
