RAD50_THEVO
ID RAD50_THEVO Reviewed; 895 AA.
AC P58302;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=TV0228;
GN ORFNames=TVG0235331;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000011; BAB59370.1; -; Genomic_DNA.
DR AlphaFoldDB; P58302; -.
DR SMR; P58302; -.
DR STRING; 273116.14324442; -.
DR PRIDE; P58302; -.
DR EnsemblBacteria; BAB59370; BAB59370; BAB59370.
DR KEGG; tvo:TVG0235331; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; FELPYSH; -.
DR PhylomeDB; P58302; -.
DR Proteomes; UP000001017; 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; Zinc.
FT CHAIN 1..895
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138668"
FT DOMAIN 411..507
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 183..253
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 464..510
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 618..647
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 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 895 AA; 103224 MW; 4A47DA9287E82D3A CRC64;
MIIERIRLRN FLSHSDSDIY FDTGINMIIG QNGAGKSSIV DAIRFALFSD KRTRRTEDMI
KKGERYMEVE LYFRSEGHSY RIRRTIERRG KSISTDAEIE RDGSIITRGA SDVSNYVEKN
VLNINKDVFL TSIFVRQGEM DALVSKDPAE RKKILDEILN IDRLEAGYLL LKEVIDDLTA
NVSDYDYLKN ELQSKINEID NNNKQIEELE SKLRLIEPEI KALEEEINIK ENKKDHLNEE
LHRLNAQLET IKKYEMELAE SQSRKASIEM EVVKLPSIEE ELKRLENNAA VVKRNEIIEY
INLKKDLGSL SEIIEGLKSD LSKYDEAHRK LEDLQSFRSE FLEKKKRKED LDKLRSSLKE
DEDNYQSAVR NIENIKKWIE NEEKEIERMS AFISEILKIQ EITPEIINSR RAEINSSLMQ
IEGKIASLNA SIDAMRSHKM EVEENAAMLS GRGVCPVCGT HLGTEKSEDL VKHYGEEASR
LEEDINKTEN EIKKLDEERK HQKKLLDRIN GKDVERLIAS YNLLSSKRAE LKKFMDDEAR
LKEAHLKAEA AISQYNSIDL GDLEAKNEEW LKANAVISSI DIENIRSRFE EKNKQLNDII
KRMNEIEVNI PDVESYNENS LKRIDEELNS LRNKKNELYA KKAAMDEIQK TIEHFKEEIS
KKKGIEDSQA EVNAQLLQIN DDLKQLSSRL DKINVDQYEW KSLHKVLLQD NEKLNIAVAD
IRKRLEKKET IIKAIADLKR VREAFSKDGV PAIIRKSASE FITNQTRQYI QRFELDIDDV
DVDQDFNITV FRGGIAEGID SLSGGERMAV AFALRVAIAQ FLNKDVSLLV MDEPTAFLDE
DRRSDLANII EYSLKDSSGI PQVIMISHHR ELLSASDLAL EVKKRNGSSI VDVIR
