RAD50_METKA
ID RAD50_METKA Reviewed; 876 AA.
AC Q8TXI4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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}; Synonyms=sbcC;
GN OrderedLocusNames=MK0690;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01904.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXI4; -.
DR SMR; Q8TXI4; -.
DR STRING; 190192.MK0690; -.
DR EnsemblBacteria; AAM01904; AAM01904; MK0690.
DR KEGG; mka:MK0690; -.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; FELPYSH; -.
DR Proteomes; UP000001826; 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; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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..876
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138655"
FT DOMAIN 387..484
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 188..528
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 575..710
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 31..37
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 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 876 AA; 103706 MW; D651E682271FD383 CRC64;
MIERVKIENL RSHSSTEIEF REGINVLVGP NGAGKTTVLE AITLALFPRT FRSYDHMIRE
GERRAVVEVV FWGADGHKYK VRREFYRGGG QRNPRLYREE GDGWKVVASG RAEDVDREVM
NALGGVDRDV FREAVYIRQG EIAKLVEATR EERKRIVDRT LGLAEFKKAR EQAHELLRVA
EAKLETFRER VRDLKGSKKE LKRVERELEE LKREVKELEP EVEELKERLN ELREAKREFE
RLEGELRLLE NKIESLKGRR DDLRKLVEEG KEAERELQRL GDVPSKVREL ENEEAELRRR
IEELRNLLDD LRSLRNRLES AEEELEGVKR ELEELKDEAG VDPERLVEFK DKIVEASERL
RDLRREEELK RKLEKVSDEL SELGDREETL QSEYEELQER LDEIQGELKE IRVKEKELLE
RIESLREAEG ECPVCLRKLP RERAEKLLRD AEKELERLQG REEDLRKERR ELKDRLESVR
RELEGTKERM WRLRERREEL ERELEEIEEL KEELADLSRE LGVEEDRLPE LRDLAVRAES
LLRDLERRRG DVLRLEKELE RTLDRCEKVI GRTPSGVEDV EEELRRLEEE RDHVGQKLRE
AEGELERYHN LEEKVKRARE ARKELKRIER DLEDAKGRLE QVERNLEGLR ERYGSEDRLE
EELESVEKKY ERVRDKLSEV KGRLNGMEKR REELKKQVRK YREAKERKER LERVVEVLSL
CKEVFRYSRD VAREKVLPAV EREASKILQD LSDRYGSLRI EDDGAVIRVS VPGGHFIEAD
RMSGGEKIII GLALRLALAM VGSSFAPFIM LDEPTVHLDA EHRERLAQAL RELDLGKGRV
RQAIVVTHDE ELEDAADELW RIENRAGESR VERYSG
