ID   RAD50_AQUAE             Reviewed;         978 AA.
AC   O67124;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Probable DNA double-strand break repair Rad50 ATPase;
GN   Name=rad50; OrderedLocusNames=aq_1006;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). The
CC       Rad50/Mre11 complex possesses single-strand endonuclease activity and
CC       ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50
CC       provides an ATP-dependent control of Mre11 by unwinding and/or
CC       repositioning DNA ends into the Mre11 active site (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Forms a complex with Mre11 (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07092.1; -; Genomic_DNA.
DR   PIR; A70387; A70387.
DR   RefSeq; NP_213687.1; NC_000918.1.
DR   RefSeq; WP_010880625.1; NC_000918.1.
DR   AlphaFoldDB; O67124; -.
DR   SMR; O67124; -.
DR   STRING; 224324.aq_1006; -.
DR   EnsemblBacteria; AAC07092; AAC07092; aq_1006.
DR   KEGG; aae:aq_1006; -.
DR   PATRIC; fig|224324.8.peg.787; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_1_2_0; -.
DR   InParanoid; O67124; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000000798; 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   InterPro; IPR004592; SbcC_gammaproteobac_type.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00618; sbcc; 1.
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..978
FT                   /note="Probable DNA double-strand break repair Rad50
FT                   ATPase"
FT                   /id="PRO_0000138669"
FT   DOMAIN          440..542
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT   COILED          160..421
FT                   /evidence="ECO:0000255"
FT   COILED          440..478
FT                   /evidence="ECO:0000255"
FT   COILED          510..542
FT                   /evidence="ECO:0000255"
FT   COILED          578..826
FT                   /evidence="ECO:0000255"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         486
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT   BINDING         489
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   978 AA;  115898 MW;  9B0F2BF51ADD1151 CRC64;
     MRPLKLEVKG FTVYKKPQVI DFTPLKFFVI QGKTGAGKTS IIDAITYALY GKVPRYGASV
     ATKYVLSRGE KELKVALDFS LRGRNYRVER YYREFPEDSQ VRVYEEGRRL NIKANEVEKW
     LFKISGLDYK TFTKVILLPQ GEFDRFLKES SERKKILINL LGLEELEKVR QLASETFKNL
     EGKREALKKE YELLKDYTPT KKEVLEKTLK NLEEELKELK ETEEKLRQEL KKAEEKDSLE
     RELSQVVTKL KELENLEKEV EKLREKLEFS RKVAPYVPIA KRIEEIDKKL TELKVRKNKL
     TKELAVLKDE LSFAQEELNR IEAEKEKFKE EKEREKELEH RLKKLQEIKE ILKELSQLSS
     SLKEKEREYE QAKQEFEDLS ERVEKGKKLV AETEEKLEKI KELFSEEEYT SLKMKERLLV
     ELQRKLKELK EKEGQLENLT QKYKEKKKVH EKVLNELKEL ERELKERELH YHAHMVASYL
     SPGDTCPVCG GIYRGKALEN VDAEGISELK HAKELKEKEE REIDTTLKLY AQKINSLKEE
     MEKLRNEVEE LRKEIPENLK ERIKKLEELR IEKEKLEHKL NKYRKALEDR QKQKEEAQAK
     LHKAQTELEL LKEKIREKSR LVKEFKELYR VERLEDYEES LKEEINYINS KLQEIEEKEK
     KLRKHFEELS SRKSKLEGEL SALNESINSL EEERKEKLKE LANIYEVAKS PREVVELYLG
     DKEAELERKI KEFEESFQSL KLKKSEIEEK LKEYEGIREL SDIKGEYESV KTQLEEKHKK
     LGEVKRELEH LGERLKRKEE LQKEISELEK KLEVYRVISN DFRGDRFQKY VSEIMLQKVV
     DRASEYFYKF TGNYFFELER ATKGRDKDIV VVESSTSQRR PVSSLSGGET FLASLSFAFA
     VSDLLSGSAN LESLFIDEGF GSLDQDMRER VSEILEAIKT NVNKMIGIVS HIPDFAERFT
     ERIVVEKKGD YSEVRVIY