RAD50_SULTO
ID RAD50_SULTO Reviewed; 879 AA.
AC Q96YR5; F9VP88;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=STK_21080;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(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; BA000023; BAK54735.1; -; Genomic_DNA.
DR RefSeq; WP_052846723.1; NC_003106.2.
DR AlphaFoldDB; Q96YR5; -.
DR SMR; Q96YR5; -.
DR STRING; 273063.STK_21080; -.
DR PRIDE; Q96YR5; -.
DR EnsemblBacteria; BAK54735; BAK54735; STK_21080.
DR GeneID; 1460180; -.
DR KEGG; sto:STK_21080; -.
DR PATRIC; fig|273063.9.peg.2400; -.
DR eggNOG; arCOG00368; Archaea.
DR OMA; FELPYSH; -.
DR OrthoDB; 1771at2157; -.
DR Proteomes; UP000001015; 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; IPR003439; ABC_transporter-like_ATP-bd.
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; PF00005; ABC_tran; 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..879
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138666"
FT DOMAIN 394..492
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 184..304
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 342..436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 502..722
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 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 786..791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 879 AA; 103488 MW; E9103B58914F20D7 CRC64;
MIIRRIDIEN FLSHDRSLIE FKGTVNVIIG HNGAGKSSII DAISFSLFRK SLRDAKKQED
LIKRGAGRAT VTLYLENKGK IYVIKRNAPN QYTSEDTISE LTNDTRRTIA RGATTVSQKI
KELLNLDEEV LKSTIIVGQG KIESVFENLP DVTKKILKID KIEKLRDSNG PIKEVMDKIN
NKIIELQSLE KYKNESENQK IQKEKELENI KRELEDLNIK EEKERKKYED IVKLNEEEEK
KEKRYVELIS LLNKLKDDIS ELREEVKDEN RLREEKEKLE KDILEKDKLI EEKEKIIEAQ
NKIKLAQEKE KSLKTIKINL TDLEEKLKRK RELEEDYKKY IEIKGELEEL EEKERKFNSL
SDRLKSLKIK LSEIESKISN RKISINIEEL DKELQKLNED LNNKNQEREK LASQLGEIKG
RIEELNKLLG NLNQVKGNVC PVCGRELSDD HKRKIQNEII EKLKELDELN KKFKLEINKI
NGLISELNQI INKKSKEKDI AIRNLADYNN LLTQQQELRK EIEEIENEIE RLSIYHEKYI
RLKEEEKNLK PKYEEYLKYY DVTEEKIREL ERQKIELEKE IEEIMNKVRE YYNTDLTQKI
RDIEKRIQEI KGKENKLREL DTLLAKIETA KQKIKQNEEE IKKLTDELQL LNFDPNRFQQ
IKREKEVLEK ILGEINSKKG ELLGKKEVLE NDIKRLEEQI KDYEEKLKNK QKLITAYDKL
KKLREHLAED KLQAYLMNTV KSLVEDSLNS ILSRFELSFT RVEVDFNDKN GIYAYTTSGQ
RLPVNLLSGG ERVSIALALR LAIAKSLMNE VGFLILDEPT VNLDEYRKKE LIDIIRSTVE
VVPQIIVVTH DEELLQAGDY IIRLEKRGDS SKVEVINND
