RAD50_SULAC
ID RAD50_SULAC Reviewed; 886 AA.
AC O33600; Q4JCJ8;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=Saci_0051;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=9211741; DOI=10.1007/pl00006193;
RA Elie C., Baucher M.F., Fondrat C., Forterre P.;
RT "A protein related to eucaryal and bacterial DNA-motor proteins in the
RT hyperthermophilic archaeon Sulfolobus acidocaldarius.";
RL J. Mol. Evol. 45:107-114(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=12052775; DOI=10.1093/embo-reports/kvf112;
RA Constantinesco F., Forterre P., Elie C.;
RT "NurA, a novel 5'-3' nuclease gene linked to rad50 and mre11 homologs of
RT thermophilic Archaea.";
RL EMBO Rep. 3:537-542(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [4]
RP INTERACTION WITH MRE11 AND HERA.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=18294364; DOI=10.1186/1471-2199-9-25;
RA Quaiser A., Constantinesco F., White M.F., Forterre P., Elie C.;
RT "The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase
RT and is recruited to DNA following gamma irradiation in the archaeon
RT Sulfolobus acidocaldarius.";
RL BMC Mol. Biol. 9:25-25(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: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 (By similarity). Interacts with Mre11
CC and HerA (PubMed:18294364). {ECO:0000255|HAMAP-Rule:MF_00449,
CC ECO:0000269|PubMed:18294364}.
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 -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00449}.
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DR EMBL; Y10687; CAA71688.1; -; Genomic_DNA.
DR EMBL; AJ437617; CAD26845.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79481.1; -; Genomic_DNA.
DR RefSeq; WP_011276982.1; NC_007181.1.
DR AlphaFoldDB; O33600; -.
DR SMR; O33600; -.
DR STRING; 330779.Saci_0051; -.
DR PRIDE; O33600; -.
DR EnsemblBacteria; AAY79481; AAY79481; Saci_0051.
DR GeneID; 3472966; -.
DR KEGG; sai:Saci_0051; -.
DR PATRIC; fig|330779.12.peg.48; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; FELPYSH; -.
DR Proteomes; UP000001018; 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; 3.40.50.300; -; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR041685; AAA_15.
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 Pfam; PF13175; AAA_15; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..886
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138664"
FT DOMAIN 391..489
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 181..240
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 320..416
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 450..657
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 682..718
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 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 886 AA; 103858 MW; 0390AE1403194104 CRC64;
MIIREIRLQN FLSHEDTTVK FEGSINVIIG NNGAGKSSII DGILFGLFKR TNRDIGKNEE
LIKKGKKSGQ VSIKFEINGD TYLIDRNVGE TSRDTISLLK EGKIITLARQ STTVNNKIKE
ILGFDHKILM STTIIGQGSV ESVFSDFPEV MKELLKINKL EMLRESNGPI HSLIKVLTDR
IRSLQSIKDI LKREEAEIDR LKKEIEEIKV KLENIEREAK EKEDELNQYN TEFNRIKEIK
VQYDILSGEL SVVNKKIEEI ALRLKDFEEK EKRYNKIETE VKELDENREK INTISSFKSI
LVQIDSLKSQ INVVENDLKR KKEKLKRKKE LEEKEKQYEE IEKRKKELEE KEKQYEEIEK
RLTYVLKNIE RQKNEIEKLN YVDTQDLENK IKDVSDRINQ IDNELKGLLD RRGDLNGRKE
QTLKIYNNLN SIEDDRCPIC GRPLDSEHKA KIREEIKVQL LELNKQITAL QARINSLIKE
REELEATRNK LQLELQKRSK EKGIYEAKLK ELQRLEEEKN KLQNEILSLL SYHQEFENIA
EKEKELIDYH EEYLKNSDIL EEDIQEQEQR LNELNSKLSE LEKSYNDYKA KYQFLPADLK
SLVSLEERIR RRISELEKLK IEYERLKEEI TRMKGLKEEY EKLKEEEDAL LNRISELGYS
EKRYKQLEEI IDKLSKILSG IEADKGKIKG SLEEKIKNIE EKERNIEELR NKMNEESKLN
LGISKLQKLR EVLDNKHLQS HIMNIVRNQI ENNVNEVIAK FDLSFSAVEI DFVGKSELYV
YTASGQKIHI NALSGGERIS IALALRLAIA KALMNQFSTL ILDEPTVNLD EYRRKELIDV
IRSAIEIVPQ IILVTHDQEL IQAGDYIIRV EKKGDTSKVE VSSYDR
