RAD50_SACS2
ID RAD50_SACS2 Reviewed; 864 AA.
AC Q97WH0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SSO2249;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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. {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 -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00449}.
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DR EMBL; AE006641; AAK42417.1; -; Genomic_DNA.
DR PIR; B90395; B90395.
DR RefSeq; WP_009991542.1; NC_002754.1.
DR AlphaFoldDB; Q97WH0; -.
DR SMR; Q97WH0; -.
DR STRING; 273057.SSO2249; -.
DR EnsemblBacteria; AAK42417; AAK42417; SSO2249.
DR GeneID; 44127983; -.
DR KEGG; sso:SSO2249; -.
DR PATRIC; fig|273057.12.peg.2344; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR InParanoid; Q97WH0; -.
DR OMA; FELPYSH; -.
DR PhylomeDB; Q97WH0; -.
DR Proteomes; UP000001974; 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 Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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..864
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138665"
FT DOMAIN 380..478
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 176..319
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 376..413
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 440..697
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 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 864 AA; 101602 MW; 657076AEA9B709FC CRC64;
MRIDKITLTN FLSHEHSEIQ FMGEINVIVG QNGAGKSSII DGIVFSLFRT HSRGNNDNLI
RKGSNRGSVT LYLSNEKDKI EIIRDIRSTT EDRLIRNQFP IARSATVVSN EIEKILGIDK
DIALSTIIVR QGELDKILEN FQEIMGKILK LELIEKLIDS RGPIVEFRKN LENKLRELDR
IEQDYNNFKK TVEEKRARVL ELKKDKEKLE DEIKNLEKRI KDIKDQFDEY EKKRNQYLKL
TTTLKIKEGE LNELNRSIEE LRKQTENMDQ LEKEINELEN LRNIKLKFEK YEVLAKSHTE
MSANVINLEK EIEEYEKAIR RKEELEPKYL KYKELERKLE ELQPKYQQYL KLKSDLDSKL
NLKERLEKDA SELSNDIDKV NSLEQKVEET RKKQLNLRAQ LAKVESLISE KNEIINNISQ
VEGETCPVCG RPLDEEHKQK IIKEAKSYIL QLELNKNELE EELKKITNEL NKIEREYRRL
SNNKASYDNV MRQLKKLNEE IENLHSEIES LKNIDEEIKK INEEVKELKL YYEEFMRLSK
YTKEELDKKR VKLDEMKKKK EEIEKEMRGL ESELKGLDRK ALESKILDLE NKRVKLDEMK
KKKGILEDYI RQVKLLQEEV KNLREEVNII QFDENRYNEL KTSLDAYNLS LKEKENRKSR
IEGELESLEK DIEEISNRIA NYELQLKDRE KIINAINKLE KIRSALGERK LQSYIIMTTK
QLIENNLNDI ISKFDLSIKN VEMEIMPKTG RGRSSSGDIL VYTNSGDTLP IVSLSGGERI
ALSIALRLAI AKALMSNTNF FILDEPTIHL DDQRKAYLIE IIRAAKESVP QIIVVTHDEE
VVQAADYVIR VEKRGNKSFV REET
