RAD50_THEAC
ID RAD50_THEAC Reviewed; 896 AA.
AC Q9HLR8;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=Ta0157;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(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}.
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DR EMBL; AL445063; CAC11304.1; -; Genomic_DNA.
DR RefSeq; WP_010900584.1; NC_002578.1.
DR AlphaFoldDB; Q9HLR8; -.
DR SMR; Q9HLR8; -.
DR STRING; 273075.Ta0157; -.
DR EnsemblBacteria; CAC11304; CAC11304; CAC11304.
DR GeneID; 1455804; -.
DR KEGG; tac:Ta0157; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; FELPYSH; -.
DR OrthoDB; 1771at2157; -.
DR Proteomes; UP000001024; 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; 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 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..896
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138667"
FT DOMAIN 411..507
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 200..274
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 412..505
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 580..611
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 636..669
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 702..731
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 896 AA; 103436 MW; 2C584D700CCD2CB2 CRC64;
MIIDRIRLIN FLSHEDSEIF FDTGVNIIVG HNGAGKSSII DAIRFALFGD KRTKKIEDMI
RKGAKSLEVE MEFRHGGHTY IIRRSITRRS KNPESNAMIM VDGSALSQSV KDANDYIEKN
IITKSKDVFL NSVFSKQGEM DDLISGDPAR RKKLLDEILE IEKLEETYDV LKDVIDSLQA
GISNLDYLIS ENERDRDDLR RYQDDVAELS KQIDQEEAIE SDLLRKKEEA SAEYNAVSKE
LIMLDATLKN MMSLSDEANR YEEEIRKIDG KLQEISGSTE RYNEITSSKV YASRERIRGY
WTDKGQIIDY RKMLKNIDGQ VQSYEDNMKK AAELQADHDQ YEIMQRRMDE IKHELDDLRT
YESKYVSLIN EIEQKKKKRE EYRKKQKDLG DEISRTLGRA FANASELVAI YEEIRRDIDE
INTDLGNLQV KIGALRQKEE EIRRNMNMLE GHNKCPVCGT DLGDEGSRRI REHYSEDLNR
LNEEIDHLER EASAIDEKKR QLISMESYLA KGKIREYETY DRQMKDLEAQ ITDDENSLST
IAYKHTKYEQ LDEEYRSMHL EDLRQKYTDW NNAMAVISNI GDIEALRKQK DEVSKKLKDA
EDRTHEIESE FPDINSYTPS YIGKIEDEVR LLEPQIKLAE DLKRQRETLR EKVKDLRSRS
AGMDEIQKRK NELSVKASES ETRLKYVEGQ IQATLSSLSG KRSKVETLRS HVSEIEQRIS
DRERDIERMK KIEKAINDVK RIREAFGKNG VPAMIRQSVS DYLTAKTRDY LSSFDLDFDD
ISVDQDFNVT VYRGGVPEGI DSLSGGEKTA VAFAIRVAVA QFLNADLSLL ILDEPTAFLD
EERRNSLSDI IEYTLKDSSV IPQVIIISHH RELLASANVA IEVKKIGGRS VVSNAD
