ID B6YXU9_THEON Unreviewed; 884 AA.
AC B6YXU9;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=TON_1422 {ECO:0000313|EMBL:ACJ16912.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850 {ECO:0000313|EMBL:ACJ16912.1, ECO:0000313|Proteomes:UP000002727};
RN [1] {ECO:0000313|EMBL:ACJ16912.1, ECO:0000313|Proteomes:UP000002727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1 {ECO:0000313|EMBL:ACJ16912.1,
RC ECO:0000313|Proteomes:UP000002727};
RX PubMed=18790866; DOI=10.1128/JB.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.S., Kwon K.K., Kim H.T., Park C.J., Lee H.W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.J., Lee J.H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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}.
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DR EMBL; CP000855; ACJ16912.1; -; Genomic_DNA.
DR RefSeq; WP_012572384.1; NC_011529.1.
DR AlphaFoldDB; B6YXU9; -.
DR STRING; 523850.TON_1422; -.
DR GeneID; 7018456; -.
DR KEGG; ton:TON_1422; -.
DR PATRIC; fig|523850.10.peg.1433; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OrthoDB; 25344at2157; -.
DR Proteomes; UP000002727; 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; 6.10.250.70; -; 1.
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; 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; 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};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 395..492
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 216..288
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 316..429
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 456..738
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 32..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 440
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 443
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 790..795
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
SQ SEQUENCE 884 AA; 103168 MW; B01B55C8F5992E32 CRC64;
MKIEKLIIKD FRSHKLTKVT FTSGINLIIG QNGSGKSSLL DALLIGLYWP SKPKDLKKDD
FLRIGGTTTE ITVFFEKDGV KYQIHRNITR GLSFVKYHDG SSWRGLESGQ KQVRDWMEKL
VPYDVFLNAI YIRQGEIDAI LESDESREKV VRQVLGLDRY ENAYKNLLEV RKEIDARIRA
IEDYLKSTEN IDELIGNMEK ELAETLKVIN ELSPEIPKLI KELEGVEKRL RDLDALAEEI
NALQLETRKR EGNVKALEAK LQELEKRIEE SRSHLRELEE KVRESNKLKG SAELYLKLVE
FRKQYVDEKA NGEKLAENYR AQISGIEERL AELSDMKNRI GELEKKREEL KKKLAELEES
VKAYEEARAL KTNLDRLRKR LKFEPEEIER LAAEIEAAKK RKEEIQRELE EINEKRGELK
NRVSERNKAI IELKKAKGKC PVCNRELTEE HRKGLMERYL AEVKDVSKEI KELDSQERKL
RRELVKVEGV LKGERELITQ RELLEQIKEL EEKLKSYDLK KLEKKAEDYE NLKGKLGKIE
GELKSLKDEL EKAKALEKKK AVLEKKLKSI EEKLAELENE LGELGFSDIK ELDEKLSELE
PAYRRYLELK GAESELEREK KRLKRTEEEL EETREKLQGE FSSLEELRKR LNEKEKLYSP
EEHAGIRERF TSLREELAGK RAQLEALEKK REETMENLKK LKEEKEERKE KIKELENLKK
ARERVQNLRE KVRRYKAMLK EGALAKVGEL ASEIFEELTE EKYSGVTVKA EENKVKLGVI
YNGKEYGLGF LSGGERIALG LAFRLALSLY LAGEISLLIL DEPTPYLDDE RRRRLVDIMQ
RYLRKIPQVI VVSHDEELKD AADRVIRVSL ENGVSSVREV ELSV
//
