ID   RAD50_METMA             Reviewed;        1070 AA.
AC   Q8PUY4;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=MM_2194;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31890.1; -; Genomic_DNA.
DR   RefSeq; WP_011034125.1; NC_003901.1.
DR   AlphaFoldDB; Q8PUY4; -.
DR   SMR; Q8PUY4; -.
DR   STRING; 192952.MM_2194; -.
DR   PRIDE; Q8PUY4; -.
DR   EnsemblBacteria; AAM31890; AAM31890; MM_2194.
DR   GeneID; 24881907; -.
DR   KEGG; mma:MM_2194; -.
DR   PATRIC; fig|192952.21.peg.2512; -.
DR   eggNOG; arCOG00368; Archaea.
DR   HOGENOM; CLU_004785_0_1_2; -.
DR   OMA; ISHVQEM; -.
DR   Proteomes; UP000000595; 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; IPR045171; ABC_Rad50.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022982; Rad50_ATPase_archaeal.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   Pfam; PF02463; SMC_N; 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..1070
FT                   /note="DNA double-strand break repair Rad50 ATPase"
FT                   /id="PRO_0000138656"
FT   DOMAIN          508..607
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          227..257
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          369..403
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          449..478
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          570..614
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          878..908
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         142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         555
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         558
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         969..974
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ   SEQUENCE   1070 AA;  121981 MW;  190783B11349EBA0 CRC64;
     MKLKNLYIEN IRSYKKLDFT FEDGVTVISG VNGSGKSSLL EACFMGLFGS KILSKDFVLA
     DMIFKGAESA KIHLGFEHLG REYLIEQAFR YSLKSENASN SRCVLFADGE NIVDQATRTY
     EEVCALLNMD EEAYRNCAYI RQGEIDVLIN AKPRDRQRMI DDLLQLGKLE EYRERAGYAK
     TAVRRLERDA KNSFLGVKAE IEGIESTEPV AAVNRLRQKV KETDAILEEL NKKKEFAAAR
     KGELDLRIAE YRERLQEIEV LKQAIRKSQE DKAACFKEKE TFSEEVQVQR RVLLELGEEN
     SGMREECGFG DLEIEALLLQ QEKSESSARE KVNSGSKELA LLLKEEETGV QALRELEKDK
     VETERVLVEC RTSIGAANKE IEGYRANIKQ LEEENKRLRE KAGFGAAGEI ASVIKELEEK
     ESLLRDRKNE VSTKLGFALK EKESGDASLR ELDSEMQSCR VAVSKGKSEI EALEKEIRDN
     SKAVLDFQEQ KSEVFAGLKA LGFTEEQLEN LEDFNELLLE NKNRLHGKEK ELEVTLREIE
     NTLRKNRELL AEGKCPTCGQ ELKGSGIACT AEECEEKKEK LSLELADIKL QRAELEKKLN
     RLKEAKKLEK QAYDYDIEIE KLLEKAKASE KLIDTHRTRI EEDSLKLESS GKRKQELEAA
     GSKLLLDIKA LREQEKAAQK VHLESEKALR EAKVFERKLA ENASEIESLN GKIRTSLALI
     ENYGQRLGEL NEKLKAFAEK ETQSKEKLEA LELTLETARK NEEEAKKAHI ESARLLGEAK
     KLQANLLRMQ NIKHKISEFE AGIGNLAEKI GFFDREIVER SDRIRQLEGK LEGNRLEELQ
     QKLARFEEAQ VNITEKIREI TAEKDTLLKE IGMIENSLKR LKELKEELKA LENKRLYLEA
     VYNNADELEN TYMRVRADMR ARNIGALSIL LNEMFSFMYT NNAYSHIELD PEYNLTVYRK
     DGTPLEPKLL SGGERAIFNL VLRCAIYRLL ALGFGGDRPD GLPPMILDEP TVFLDRGHVR
     QLLKLIDMMR SIGVGQIIVV SHDESLIDSA DHVFQVEKDP LTNMSSITKI