RAD50_METTH
ID RAD50_METTH Reviewed; 837 AA.
AC O26640;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=MTH_540;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(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; AE000666; AAB85046.1; -; Genomic_DNA.
DR PIR; D69171; D69171.
DR RefSeq; WP_010876179.1; NC_000916.1.
DR AlphaFoldDB; O26640; -.
DR SMR; O26640; -.
DR IntAct; O26640; 1.
DR STRING; 187420.MTH_540; -.
DR PRIDE; O26640; -.
DR EnsemblBacteria; AAB85046; AAB85046; MTH_540.
DR GeneID; 1470501; -.
DR KEGG; mth:MTH_540; -.
DR PATRIC; fig|187420.15.peg.520; -.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; VNFIYGP; -.
DR Proteomes; UP000005223; 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 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..837
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138658"
FT DOMAIN 379..478
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 197..419
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 462..551
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 634..673
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 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 837 AA; 97637 MW; A88B2A9D5AFDECF6 CRC64;
MIIRSLELKN IRSYESGRVE FDDGVTLFEG DIGSGKTTLL LAVEFALFGL GDQRGDSLLR
ATSNSGSVKL TFTVDGEEYT VYRELKRGSS GVQQGELYIR KQGVVKKLSA KELKAEVLEI
LGYREPLNPR ARSRIYRYAV FTPQEQMKSI IEAPKNDRLE RLRKAFDLEK YSRAADNANL
VSRRIRRESE SLEDRSYDLE DKKRELEGLL GEKEKLESEK KQLDSDIEGI EAEIAKLKSE
MEVLQREKNR IESAEREIES LQNEIETLRS SSERLMERNR SIEEEYRRSL DELQKCSDIR
EKLQEELNSL GERISALELK RESLMDDSRR FREASIQYRN LVSELENLIK TGRDLEDEIS
GLEDYTDRIK SKIESMESIE DPGYTEDEVE AGIRKLEVEV SDLQQELGGI HGKIEDYESI
GRRGVCPTCD QEVNPDYIND KLSSARERKG SVESRIADLR NEIMNKNELM KRIAEYKRSR
EELRLLREDL EKRIKECHRR RESLDNIRER IRQIEEGKAE SEKLIEELKD AESDFNKVEH
ELKSLREMES GYSSKLAAAS GRMDQLRTRI TELNPETSRE YRDNLKKIDE NESNIAEKRA
KIRENEEALK NRDEVESSIH DLTQSICEME NLRDEKRDRR AAVEGKIEEK QRQIGNLESE
IAKKRELRKR ARELGNYVTW LNEYFIPAMD DIETHVMAQI NHEFNERFQK WFRVLVDDPG
KSVRIDEDFT PIVEQDGYEQ NLEYLSGGER TSIALAYRLA LNMVVQRLTD VRSDILILDE
PTDGFSKEQL YKLRDIFDEL ESRQIILVSH EEELENLADH IYRVEKSDGT SIIEKTG
