RAD50_HALSA
ID RAD50_HALSA Reviewed; 883 AA.
AC Q9HRW3;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=VNG_0514C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=18502851; DOI=10.1128/jb.00292-08;
RA Kish A., DiRuggiero J.;
RT "Rad50 is not essential for the Mre11-dependent repair of DNA double-strand
RT breaks in Halobacterium sp. strain NRC-1.";
RL J. Bacteriol. 190:5210-5216(2008).
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: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 -!- DISRUPTION PHENOTYPE: Mutants show a slight growth defect, but do not
CC show increased sensitivity to ionizing radiation or alkylating agents.
CC Show decreased rates of survival after UV-C irradiation.
CC {ECO:0000269|PubMed:18502851}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00449}.
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DR EMBL; AE004437; AAG19045.1; -; Genomic_DNA.
DR PIR; A84210; A84210.
DR RefSeq; WP_010902341.1; NC_002607.1.
DR AlphaFoldDB; Q9HRW3; -.
DR STRING; 64091.VNG_0514C; -.
DR PaxDb; Q9HRW3; -.
DR PRIDE; Q9HRW3; -.
DR EnsemblBacteria; AAG19045; AAG19045; VNG_0514C.
DR GeneID; 5952569; -.
DR KEGG; hal:VNG_0514C; -.
DR PATRIC; fig|64091.14.peg.392; -.
DR HOGENOM; CLU_004785_0_1_2; -.
DR InParanoid; Q9HRW3; -.
DR OMA; ISHVQEM; -.
DR OrthoDB; 1771at2157; -.
DR Proteomes; UP000000554; 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:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
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; 1.
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; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13476; AAA_23; 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..883
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138651"
FT DOMAIN 407..506
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT REGION 271..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 244..283
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 336..389
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 414..452
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 571..604
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 668..720
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 883 AA; 96970 MW; F8284D3326C92BB9 CRC64;
MRFTRLSLSN FKCYADAAVS LDPGVTVIHG LNGSGKSSLL DACFFALYGT TALDTTLADA
VTIGAETAEI DLHFEHAGGD YHVHRRIRAS GGRAQTAACV LETPTDRIDG VTDVEAHISG
LLRMDAEAFV NCAYVRQGEV NKLINAAPST RQDMIDALLQ LGKLEEYRQR AGDARLGVED
VKSNVEGQLD RLADQIADKE AADPHDRLAS HNTALAEVTA DIEHFEAERE QARQTRDDAA
DVLERYEESR TALADVEETI ADVREAVAEA ERERETLADR VSDHRERASD LDDEAAALAA
DLGLDDPDAE DASAERDAVA DQREAVAERV REVAPAVSRL TEQADSAADD AATLDERAET
LREEAAALDA EADDAAAKRD DAAARIEALD ADIEAAMAAF DDAPVAFGAA EAFLDDATAE
RDELRERVAT LRADRQSAAD RVAEAEALLD EGKCPECGQP VEGAPHVERV TDDRERVAEL
DAELADVEDE LDAVAQRVDR GESLVAAEDR VDDLEQQRER AVERRDEQAD IADAKRDQAA
EKRDRAADLD AEAEDARADA AAKRDAADEK RETLAALNAD QTALKERLDA LADLVDRLEA
AADAREAAQR LAEKRAALAA QNEQRRDRLS ELRERKRTLD SEFDADRIET ARADKDRAED
YLEQVEPKLQ ALREDRDDLQ AKIGAAENAI AELESLREEH ERVQSRHQDL QAVHDEVTAL
ETMYGELRAE LRQQNVSKLE RLLNETFELV YQNDSYARIE LSGEYELTVY QKDGEPLEPA
QLSGGERALF NLSLRTAVYR LLAEGIEGDA PLPPLILDEP TVFLDSGHVS QLVELVESMR
RLGVEQIVVV SHDDELVAAA DDVVRVAKDA TSNRSRVSTP EHI
