ID   RAD50_PYRHO             Reviewed;         879 AA.
AC   O58687;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
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=PH0929;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA30025.1; -; Genomic_DNA.
DR   PIR; C71083; C71083.
DR   RefSeq; WP_010885020.1; NC_000961.1.
DR   AlphaFoldDB; O58687; -.
DR   SMR; O58687; -.
DR   STRING; 70601.3257342; -.
DR   PRIDE; O58687; -.
DR   EnsemblBacteria; BAA30025; BAA30025; BAA30025.
DR   GeneID; 1443255; -.
DR   KEGG; pho:PH0929; -.
DR   eggNOG; arCOG00368; Archaea.
DR   OMA; VNFIYGP; -.
DR   OrthoDB; 1771at2157; -.
DR   Proteomes; UP000000752; 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; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00449; RAD50; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
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; PF04423; Rad50_zn_hook; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; Zinc.
FT   CHAIN           1..879
FT                   /note="DNA double-strand break repair Rad50 ATPase"
FT                   /id="PRO_0000138662"
FT   DOMAIN          396..493
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          241..344
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          390..429
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   COILED          462..727
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         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         444
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT   BINDING         788..793
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ   SEQUENCE   879 AA;  103674 MW;  FD4E30FD1BBCDB29 CRC64;
     MKIERVIVQN FRSHKNSEIE FKPGINLIIG QNGAGKSSLL DAILVGLYWS KRMRLRGLKK
     DEFTRTGTRG AIIEITFEED GTKYKVLRDF ARNVSYLKRL DGREWRHVTE TSMESVSSFI
     DRIIPYNVFL NAIYVRQGQI DAILESDETR DKIVKEILNL DKLEKAYDNL GKIRKYIKYS
     IEEKEKFIMK TENIEDLIRT QEKSFTEVLN EIRNISSNLP RLRRELEGIK EEVKTLEATF
     NSITELKLRL GELNGKKGRL EERIRQLESG IEEKRKKSKE LEEVVKELPE LEKKETEYRR
     LIEFKDEYLV KKNELEKRLG ILSNRLQEVK RKIKDAESKV ARIRWIEERL KEIQEKIMKL
     EPRVREFEDA MRLKAQMESL KSKLGGLEPE KINEKLLYLE NRKKELEEEI DKITRKIGEL
     NQRSKDRRLA IIELKKARGK CPVCGRELTE EHKADLLRKY SLELSSIEKE IQEAKALERQ
     LRAEFRKVEN ELSRLSSLKT IADQIIEIRE RLSKINLEDL KRDKEEYELL KSESNKLKGE
     VESLKKEVNE LNDYKNESTK LEIEIDKAKK ELSEIEDRLL RLGFKTIDEL SGRIRELEKF
     HNKYIEAKNA EKELRDILES LKDEREELDK AFEELAKIET DIEKVTSQLN ELQRKFDQKK
     YEEKREKMMK LSMEIKGLET KLEELERRRD EIKSTIEKLK EERKERESAK MELEKLNIAI
     KRIEELRGKI KEYKALIKEE ALNKIGEIAS EIFSEFTDGK YSGIAIRAED NKVKLFVIYD
     GVERPLTFLS GGERIALGLA FRLAMSMYLI GKVDLLILDE PTPFLDEERR RKLIEIMERH
     LRKISQVIIV SHDEELKDAA DHVIRIRLEG GASKVEVVS