ID U1QZT1_9EURY Unreviewed; 896 AA.
AC U1QZT1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ORFNames=J07HB67_00545 {ECO:0000313|EMBL:ERH11537.1};
OS halophilic archaeon J07HB67.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX NCBI_TaxID=1085029 {ECO:0000313|EMBL:ERH11537.1};
RN [1] {ECO:0000313|EMBL:ERH11537.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the
CC early steps of DNA double-strand break (DSB) repair. Rad50 controls the
CC balance between DNA end bridging and DNA resection via ATP-dependent
CC structural rearrangements of the Rad50/Mre11 complex.
CC {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; KE356582; ERH11537.1; -; Genomic_DNA.
DR AlphaFoldDB; U1QZT1; -.
DR STRING; 1085029.J07HB67_00545; -.
DR HOGENOM; CLU_004785_0_1_2; -.
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; 1.10.287.510; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR NCBIfam; NF041035; Rad50_Halo; 1.
DR PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 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}; 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};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 409..508
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT REGION 269..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 456
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 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 896 AA; 100650 MW; D05A5DB43D0561E7 CRC64;
MIFERIVLRN FKPYGDAAVD LSEGVTVVHG LNGSGKSSLL EACFFALYGA RALDGTLSDV
ITNGVEETDV ELWFSHDGRR FHVTREVRTH GDRASTATCT LETDDGGVVR DGATDVRAFV
TDLLRMDAEA FVNCAYVRQG EVNELIEASP SARQDTIDDL LQLGRLEEYR DRAGQARLGV
EDVLEGRRGA LENLDDRIER KEAKDLPERL NQLESTVGEV DDDIDQYETE REKAVATRDD
ARDTLATYED RRGELSAVDA EIDALETEIR ESETERREVE SELAAARDRR SEAETALREA
VAESDVADGD PETVRERRAT LDERESRLRE RLLDARDEVT DATNRAEERT EAATERRERA
AEERERAETL ASKREEDRER LTELRERREQ KAAERDRLQA AFTDAPVEVG GAASLQESIA
EDRSELDEEI EDVRTDLKEA RSAVERGEEL LAAGNCPECG QPVADSPHVD ALDDRRERVD
RLETQLTELR ADREALTDRR ERAEELREVE RDLDAVEDTL SLLDDRITEV EGRIEDRGEQ
IQQHERRAAE LESDAETAAA DAETAAEAAA AARERVAECN RELASVSETT DRLDRIDDCR
TDREQAAAEI DRLEERRDGL ETLNDQRRDS LAAKRARREE LAAAVDDEAV AAARERLDKA
ESYIERADQK LSDLRDRRDD LTNQIGAVTN ELDELEQLRG EREAVAEDVS ALESLREETA
DLADTYASLR AELRQRHVDA LETRLNETFE LVYGNDAYSH IELDDSYELT VYQKNGEPLE
PAQLSGGERA LFNLSLRCGI YRLLAEGVEG AAPTPPLILD EPTVFLDDGH VGRLVDLVEQ
MRGFGVAQIL IVSHDDELVD AADDLVRVEK NPTTNRSSVE RIENASVAEL REPADD
//
