ID Q18JH7_HALWD Unreviewed; 898 AA.
AC Q18JH7;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 119.
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 ECO:0000313|EMBL:CAJ51829.1};
GN OrderedLocusNames=HQ_1701A {ECO:0000313|EMBL:CAJ51829.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51829.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ51829.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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}.
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DR EMBL; AM180088; CAJ51829.1; -; Genomic_DNA.
DR RefSeq; WP_011570979.1; NC_008212.1.
DR AlphaFoldDB; Q18JH7; -.
DR STRING; 362976.HQ_1701A; -.
DR GeneID; 4194565; -.
DR KEGG; hwa:HQ_1701A; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_1_2; -.
DR Proteomes; UP000001975; 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; 1.10.287.510; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00449};
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}; Reference proteome {ECO:0000313|Proteomes:UP000001975};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 407..506
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT REGION 355..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..273
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 470..737
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COMPBIAS 366..389
FT /note="Polar 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 454
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 457
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; 101694 MW; F7F3692CFD7AD8DA CRC64;
MRFDHITLEH FKPYADASLD LQDGVTIIHG LNGSGKSSLL EACFFALYGA RALDETLDDI
VTTDEDDATI ELTFSHAGSQ YHIKRRLRRS GDRIQTAQCT LDGPDIEIDG ATDVRAFITD
ILRMDAEAFV NCAYVRQGEV NKLINATPTQ RQAIIDDLLQ LGRLEMYRER ASDARLGVED
ILSEQRGAQT EIKAQIERKE DANLHEKLNE YEAARADIDA EIERYEENKI RAQETRDNAK
EILTSHEETQ EELTELEAEI DDLRMTIEED ESTRADFREA IETKTEQVET LLSARTDALS
SAEVTSADAD TLAARRSTLD DKESSIRDSL QTARQQQTMF ENQAERLTER VDELESRADE
LQEQASEAET AVTKAKEQIT TQQNAQADIE EQMTSVREQF NNSPATLGKA TEYLEMLQEE
HDDIRNDLAS TRASLSTVQD RRNEAQTLQE AGKCPTCEQP IEESPHVEAI DEYDVQIETL
TERLSQLETK QNKVNNKIES AESLVESERQ FETLKERKSL ASERIADARE TVNEQTETAA
SLHENAGELE TEADEKRDAA ATQMSNADSE AEKVATLESK LETINNARDQ LDNLAEIQSE
IENIRAEIER LRERREEIAD RNDERREYLQ AKRDRHAELA ADVNEARIEK AQNNHEEAVS
YLEDVSEKLD ELRDKRDNIQ SQIGSVRGEI ENLAELREKH TAINDRVSAL ETLHEQVETL
SSTYRELRAD LRKQNVETLE RMLNEVFMLI YDNDAYSRIQ LDDAYELTIF QKDETALNPE
QLSGGERALF NLSLRCAIYR LLAEGIDGTA PMPPLILDEP TVFLDSGHVG RLVDLIKDMQ
RRGVAQILIV SHDKELIAAA DHLVTVKKDP TSNRSSITRI DDPQRAAISA ASSNKTPQ
//
