RAD50_ARCFU
ID RAD50_ARCFU Reviewed; 886 AA.
AC O29230;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-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=AF_1032;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB90211.1; -; Genomic_DNA.
DR PIR; H69378; H69378.
DR RefSeq; WP_010878532.1; NC_000917.1.
DR AlphaFoldDB; O29230; -.
DR SMR; O29230; -.
DR STRING; 224325.AF_1032; -.
DR PRIDE; O29230; -.
DR EnsemblBacteria; AAB90211; AAB90211; AF_1032.
DR GeneID; 1484255; -.
DR KEGG; afu:AF_1032; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; ISHVQEM; -.
DR OrthoDB; 1771at2157; -.
DR PhylomeDB; O29230; -.
DR Proteomes; UP000002199; 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 CDD; cd03240; ABC_Rad50; 2.
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; 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; 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; Reference proteome; Zinc.
FT CHAIN 1..886
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138650"
FT DOMAIN 392..489
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 183..360
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 400..433
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 489..518
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 545..713
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 33..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 792..797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 886 AA; 103635 MW; D35641D499AA8B58 CRC64;
MILLKELQIK NFRSHSDSKI EFDTGINLIA GRNGAGKSSI LEAILVAFYG LKPATLRKND
LVRVNSSGYS LSLTFSLNGD DYTISRKSNG ESILTGKEIV EGDSNITEWV ERHLCPAHVF
TGAIYVRQGE IDSIIRDDES RERIIRQITR IEDYENAWKN LGAVIRMLER EKERLKEFLS
QEEQIKRQKE EKKAEIERIS EEIKSIESLR EKLSEEVRNL ESRLKELEEH KSRLESLRKQ
ESSVLQEVRG LEEKLRELEK QLKEVVERIE DLEKKAKEVK ELKPKAERYS ILEKLLSEIN
QALRDVEKRE GDLTREAAGI QAQLKKAEED NSKLEEITKR IEELERELER FEKSHRLLET
LKPKMDRMQG IKAKLEEKNL TPDKVEKMYD LLSKAKEEEK EITEKLKKLI AKKSSLKTRG
AQLKKAVEEL KSAERTCPVC GRELDEEHRK NIMAEYTREM KRIAEELAKA DEIEKKLKER
LEKVEKALEK QETVLKYRQM VDELKALENE LSSHDAEKLS AESEEYRKVK ERLDGLRGQQ
KILLSSASRI KELKSSLREI EEALKNVESE RGELHRKIRE EGFESLEELE REVQSLRPFY
NKWLELKDAE SRLESELKRR EKLEDEISEA IAKLEEANGK AEEIRGQIDE LLRIYSEEEH
RRLSDEHLRK SKELAGLKSR LETLRESLQS AEKDLKFLEE QLAKMDEYRK KVEVFEKIAI
PELTRIREKF RKYRNLVAEN SMREVERYAS QIFEELTEGK YSGVRLKKTT ERGKEKLKVF
VVYQGEEREI GFLSGGEIIA LGLAFRLALS MFMIRGKIPL LILDEPTPFL DEERRRKLVD
ITTNYLRKIP QVIIVSHDEE LKDAADKVIF VESQGGVSRV RYVEAQ
