ID   RAD50_METMP             Reviewed;         993 AA.
AC   P62134;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=MMP1341;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF30897.1; -; Genomic_DNA.
DR   RefSeq; WP_011171285.1; NC_005791.1.
DR   AlphaFoldDB; P62134; -.
DR   SMR; P62134; -.
DR   STRING; 267377.MMP1341; -.
DR   EnsemblBacteria; CAF30897; CAF30897; MMP1341.
DR   GeneID; 2762040; -.
DR   KEGG; mmp:MMP1341; -.
DR   PATRIC; fig|267377.15.peg.1376; -.
DR   eggNOG; arCOG00368; Archaea.
DR   HOGENOM; CLU_004785_0_2_2; -.
DR   OMA; FELPYSH; -.
DR   OrthoDB; 1771at2157; -.
DR   BioCyc; MMAR267377:MMP_RS06920-MON; -.
DR   Proteomes; UP000000590; 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:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
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; 3.40.50.300; -; 2.
DR   HAMAP; MF_00449; RAD50; 1.
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   Pfam; PF13476; AAA_23; 1.
DR   Pfam; PF04423; Rad50_zn_hook; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..993
FT                   /note="DNA double-strand break repair Rad50 ATPase"
FT                   /id="PRO_0000138657"
FT   DOMAIN          452..556
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          192..222
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          402..493
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          570..612
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          646..677
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          702..731
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         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         500
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ   SEQUENCE   993 AA;  116892 MW;  A34EDB49D922AD7E CRC64;
     MIIKNIKMEN FRSHRNTSIN FSKGITSIIG QNGSGKSSIF QAMNFALFAP RGNNFRIENL
     MQQGAASFSV ELEFEMMGNT YLVKRKRFQH KTDDKLYVNG KLNAESASEI NKKIEEILEI
     DNSVFSNAIY IKQGEIANLI QMTPRDRKEV IGKLLGIEKY EKASEKMNIV KKSYEETLLK
     LEGELTQEPE ILENLEKLKN EVSESEILKE EILKKYENLE KLKLEKNSEI LQMEEKFAEN
     NQLKENLKDI ISEIKNINLE IQNFKNSLNL VAEESKNISE NEENYKKYLE LELKIKELNN
     KLIGHKSNYE SYNKLKTIEE SLLKELGVLK ESLKDNKKNP DELKENLKEN DEKILILDKI
     KEKIKELEFI EKQIYEIKIH KKTVETLFDS VKIYDDSIKT FEELKTKKNS YENLLKEKFD
     LEKKLQNETD EKTKLISELT DFEKIEEKIN LENELKEKYE DLSEKIDKLN EIVLKKESKI
     SEYKNSKAEL EKTKDSCHVC QSKITEEKKQ ELLEKYNSEI QNEQLSTESL KKQLEIILNK
     KEKMKVKLNE IDSFKLKYGE LKEKKNYSLK VEESIIETTE KLNELTGKIN EYSSLNDEIS
     LIENKLKNLE NDYKNCNYSS QFLTKNDESE FLTKKLELSK IIGDYDSSKI ENEKKSLENL
     KDELKNTIYN LEREINLKKE LKNIQNDISS KIGIVECYVK WETEKSDFEN KLSECKENYE
     KYMESLAVLK NYSKTYSVEI NNLNEFLNQK IAEKQQFCEK LLETRTEIEK NIQTVNYNPE
     LHENAKRLYE NILNEFNDIL RTLERISSEL KLKNENISYL NEKIQNLSNK KEEKKKIEEF
     KEYLDKIKRE IFSKDGFQKY LREKYIPLIQ RHTNQIFQEF ELPYSHIQLK DDYSLIVDGL
     PVETLSGGEQ IAVSLALRLG ISKAVCNNIE CIILDEPTAY LDEDRRKNLL NIFKNIKTIN
     QMAIITHHQE LEQIADNIVK VRKIGENSKV SLE