ID   RAD50_NANEQ             Reviewed;         786 AA.
AC   P62135;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000250|UniProtKB:P58301};
GN   Name=rad50 {ECO:0000250|UniProtKB:P58301}; OrderedLocusNames=NEQ256;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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:0000250|UniProtKB:P58301}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P58301};
CC       Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:P58301};
CC   -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC       subunits and two Rad50 subunits. {ECO:0000250|UniProtKB:P58301}.
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:0000250|UniProtKB:P58301}.
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR   EMBL; AE017199; AAR39107.1; -; Genomic_DNA.
DR   AlphaFoldDB; P62135; -.
DR   STRING; 228908.NEQ256; -.
DR   EnsemblBacteria; AAR39107; AAR39107; NEQ256.
DR   KEGG; neq:NEQ256; -.
DR   HOGENOM; CLU_004785_0_2_2; -.
DR   OMA; FELPYSH; -.
DR   Proteomes; UP000000578; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..786
FT                   /note="DNA double-strand break repair Rad50 ATPase"
FT                   /id="PRO_0000138659"
FT   DOMAIN          366..459
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000305"
FT   COILED          194..249
FT                   /evidence="ECO:0000255"
FT   COILED          337..455
FT                   /evidence="ECO:0000255"
FT   COILED          551..650
FT                   /evidence="ECO:0000255"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P58301"
FT   BINDING         33..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P58301"
FT   BINDING         138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P58301"
FT   BINDING         411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P58301"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P58301"
SQ   SEQUENCE   786 AA;  93236 MW;  D0B0D91B26DDD186 CRC64;
     MVIVKKVILN NVKTHSKREF DFEKGINLIL GPNGSGKTTL VESIFLALFG GDFARVIDYF
     KKGEKTMAIT LILEDKGKTY RIRRKWVLEN NAKLVESSLE LIDTIPKKLA SDHNKLLQQI
     KHLFGLDKKI IPLIYYKQNE ITKIIEMDPR KRKEWFDEIL GIKDLEEFSE KLKMAIKLIK
     TGKISRIEDR IKLLKAELNK KSLLENKLKN YKEKLVLLSN ELENLEKEYK ILENQYKEYL
     ELKAKLKSIE GQINNINVKE IESKINNIRE ELNNIEELTD YEKDILSKKH EIIRCNEIKN
     RLKELEKEIK DYDKIKKEFL EIESKYKQYE EKRLEYEKAK MLEKEKEKAK REYSYLLKEK
     ESLEKEIAEL QNKINQIKEL EKMEQELLEI QERIGVIKAK LKLLENIKDR CPLCGAKLSS
     DTIEHLQKER EKLQKEYYYL KEKYNQLLIK IRALEKYKGL EKVLEAKTKH LETIENRLKE
     IKPIIELEIP KIELDESIPY KYKQLLNKVS YLEAKIKEYE RYKNIECPYD IAIEELKRIE
     DKYNKYIKKP ALERELNLLL KELERYNSLL KEKEEILSKL NPEIETKYKE LTKKKENLLS
     EISKVKGIIK EIESQIKEIE KHESTIKQLE EKKRKWEKLV EKLNRIVKAL GRDGIPKALR
     EGAINYINDM ANIYLREFTD KYKLKVNNDL SIYAIPIDNP HYEIEAKNLS GGEKVVFSLS
     IALAIISWLS LQNMFMVLDE PTANLDNERT LALRKTFDKL EKMVEQAIIV THNELLDTGE
     NHVVRL