ID A4YET5_METS5 Unreviewed; 858 AA.
AC A4YET5;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000256|HAMAP-Rule:MF_00449};
GN Name=rad50 {ECO:0000256|HAMAP-Rule:MF_00449};
GN OrderedLocusNames=Msed_0762 {ECO:0000313|EMBL:ABP94937.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP94937.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP94937.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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:0000256|HAMAP-Rule:MF_00449}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00449};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000256|HAMAP-Rule:MF_00449};
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC subunits and two Rad50 subunits. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00449}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00449}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00449}.
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DR EMBL; CP000682; ABP94937.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YET5; -.
DR STRING; 399549.Msed_0762; -.
DR KEGG; mse:Msed_0762; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR Proteomes; UP000000242; 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 Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.5.1070; Head and neck region of the ectodomain of NDV fusion glycoprotein; 1.
DR Gene3D; 1.10.287.510; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00449}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_00449};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00449};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00449};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00449};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00449}; Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 374..472
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 164..318
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 436..696
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 32..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 765..770
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
SQ SEQUENCE 858 AA; 99816 MW; 58CAD71A1D1D627D CRC64;
MRLDRVYLKD FLSHEKTTVS FKGDINVIVG QNGAGKSSII EAITFALFRE GKGKQEEMIK
KGKTNAELEL VLRDNNLEVR VLRKIPPGDQ LYVNGKLTAR GTKEVTKKIE ELGLNSKVVT
STMIVRQGEI ETIFDTLTDV LKRVMMIDNL EKLTESGGKI KQLMDKYDQE VRSHEIYLEN
LRRLQEEKSS LEREISSLTE RMEKTREELQ KLESEEAKLK DKIKDLEEKQ REYDVLLSEK
RLAEDELQRV MAELRNLEGL ERRISNLEEK EKELEKIVSL SDTILDLEGK RARLTDRKNE
FERVKRQFEK KSKEFEQKRK LEPRHEEYQR VVSRLKELEE YHERFTSLYS TLRNLMERKN
KIEQEVRMLP RIAVEEIQTR LDSVSKELDE AASLQKERKV EYDQIRKSLD ALLSATEGKC
PVCGGPLDEP HRQELTQKYR QRLTELSKEL KDLEGKLESL KRDKSRLEDE HKRAIRVDAE
RRGKENDLEG LSSDIARLES ELKQLKELEE EFRAMQRRKD ELENDERSYL QVQGVSEAEV
MELEDQMATY SHDISTLEEE IDQLEGRVGN LTKQDVESAK GQLEKVRREL SELQRKRGEK
TNLESRMVEL KRSVDELSRR IQLLGFRRQD LEQMRRDLEV LSKQLREVHG DLGNLEGKLN
QVKGRHQEVE NEIAQLQEKV KEVEKSRRAK ERLEKLRKVL SEGMLQSYLI STLKGRIENN
LNDIVSMFDI SYTRILVNMT QTKTLSGKVE LTALNQSGQQ LSIGMLSGGE KIAVALALRL
AIARALTGEI GFMILDEPTV HLDSMRRAEL LSVIRESMNV VPQIIVVTHD DEVLRIADYV
IRVEKVGESS RVKEEIAQ
//
