ID J3JGW3_9EURY Unreviewed; 898 AA.
AC J3JGW3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=HSB1_10820 {ECO:0000313|EMBL:EJN60479.1};
OS Halogranum salarium B-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1210908 {ECO:0000313|EMBL:EJN60479.1, ECO:0000313|Proteomes:UP000007813};
RN [1] {ECO:0000313|EMBL:EJN60479.1, ECO:0000313|Proteomes:UP000007813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-1 {ECO:0000313|EMBL:EJN60479.1,
RC ECO:0000313|Proteomes:UP000007813};
RX PubMed=23144405; DOI=10.1128/JB.01815-12;
RA Kim K.K., Lee K.C., Lee J.S.;
RT "Draft Genome Sequence of the Extremely Halophilic Archaeon Halogranum
RT salarium B-1T.";
RL J. Bacteriol. 194:6659-6659(2012).
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|ARBA:ARBA00009439, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJN60479.1}.
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DR EMBL; ALJD01000003; EJN60479.1; -; Genomic_DNA.
DR RefSeq; WP_009366196.1; NZ_ALJD01000003.1.
DR AlphaFoldDB; J3JGW3; -.
DR PATRIC; fig|1210908.3.peg.1030; -.
DR eggNOG; arCOG00368; Archaea.
DR OrthoDB; 25344at2157; -.
DR Proteomes; UP000007813; Unassembled WGS sequence.
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; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
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; PF13476; AAA_23; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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 219..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..572
FT /note="Basic and acidic residues"
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 137
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 898 AA; 101791 MW; 0A19021AE51F336F CRC64;
MRFDRLRLEN FKPYADADLG LDDGVTVIHG LNGSGKSSLL DACFFALYGS KALDGTLDDV
ITNGEEDAEI ELWFTHDGES YHIERRLRRS GERTLTAKCV LEGPDTTVDG SRDVRRFVTE
LLRMDAEAFV NCAYVRQGEV NKLINATPRQ RQDMIDDLLQ LGKLEEYRER AGQARLGVDD
ILANKRGALD ELDTQIQERE EQDLHGRLNE LESKLKSIDD DLERHRENRE RAESSRDEAQ
ATLDSYEEKR ERLDELADEI EELESKIAET ERERDDLRDE IRETQAQKTE LESTTADVLA
ETTLETASES AIESRLDTLD EQETEQSEAL NEARMHAQAL DNQSGNLSEK ADDRRSRADD
KRARADRLDT EVETATEELD SRRETLDEMA DEIAELKTAF DTAEADIELG EASVHLADLR
EERESLRDEI ENVRTELKTV RNSVTEAERL LDEGKCPECG QPVEDSPHVD TLDEDRARVS
ELETELDELQ ADRESLDAAI DRAKDLVETE AEIESLQSNR ENVEQLVEQK AETVDEKRTE
AETLREEADE LATQAENTRE VAEGKAEEAA EARETVEELE TELDAIDAKQ AQLDRLADLR
ERIEEAEERA ERLREKRTDL DERNDERREY LAGKRDQRDD LRGEVDEEQV EQARSQKQNA
VDYLEKVEAE LDRLAERRDE LQNAIGSVNN AIEQLETLRE QRESVATRVA ALESLHEETE
ELEGLYGDLR ADLRQRNVES LERMLNETFD LVYGNDAYST IRLDGEYELT VFQKDGQALD
PEQLSGGERA LFNLSLRCAI YRLLAEGIEG TAPLPPLILD EPTVFLDSGH VSRLVDLVEE
MRALGVRQII IVSHDDELVG AADDLVTVEK NSTTNRSTVG RADAASLAAV ESLAGTND
//
