ID D2ZRK4_METSM Unreviewed; 917 AA.
AC D2ZRK4;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000256|HAMAP-Rule:MF_00449};
GN Name=rad50 {ECO:0000256|HAMAP-Rule:MF_00449};
GN ORFNames=METSMIF1_03488 {ECO:0000313|EMBL:EFC92734.1};
OS Methanobrevibacter smithii DSM 2374.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=521002 {ECO:0000313|EMBL:EFC92734.1, ECO:0000313|Proteomes:UP000004028};
RN [1] {ECO:0000313|EMBL:EFC92734.1, ECO:0000313|Proteomes:UP000004028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2374 {ECO:0000313|EMBL:EFC92734.1,
RC ECO:0000313|Proteomes:UP000004028};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00449}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00449};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000256|HAMAP-Rule:MF_00449};
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC subunits and two Rad50 subunits. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00449}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439, ECO:0000256|HAMAP-Rule:MF_00449}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFC92734.1}.
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DR EMBL; ABYV02000009; EFC92734.1; -; Genomic_DNA.
DR RefSeq; WP_004034067.1; NZ_GG704759.1.
DR AlphaFoldDB; D2ZRK4; -.
DR PATRIC; fig|521002.11.peg.1441; -.
DR HOGENOM; CLU_004785_0_2_2; -.
DR Proteomes; UP000004028; Unassembled WGS sequence.
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; 1.10.287.510; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00449};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 424..521
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 194..385
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 499..550
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 32..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 828..833
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
SQ SEQUENCE 917 AA; 105523 MW; 83F93227F5CDE13E CRC64;
MIFTKLTLNN FKSYGHEVIK FGDGITVIVG ENGAGKSTIL EAISFALFKQ HTAKKIDDLV
RNGSDENMYV DLEFVSNGKE YKIHREKTKS GLKSTLLKKT TSKGQFIPSC AGDKEVANEI
QSILDIDSDL FLNAIYIRQG EIAELVDKTS SEKKQLIGKL LGLDSLEKAW KNLQPIISNY
EKTQSELKGK LFSSEELKEE YDHKKALLGS LKEKGLDLEK QIEEVKEMKA EKQNEKTNME
REKEIFDNFN NNLDAEKKRL ESLENDKRTL QDNLDEIKKA EEQIARLEKF VKKLPLYLDF
EKSVTSIQQL ELDKQKIEKD LNSIATQEEL LATKKEGYNK FLAADEQIEK LNNQKINLEK
ELATLTQLEK DKKQLLKSIE GNRNEIERFF SVTKDNLYDN GLSQDILTDV DNFTQLEEVT
DNFSEEVSNK VKDLSLEIIS KNEEIVKFKQ AIETAQKPLD ELGDVENKCP VCQSDINPQK
KNELIDYYNN EIKINEKSIE ENNENIRLLN KNKDSFEEKY NRLQELSKDI IGYKNKFDNL
EKDLVRLNEI DDGLESKEYT NTKLGELILD ISKEKVGREE NKEDYDAYIK SKGALDVLSS
KTELQYKLNQ VNNEVDVHVK NIKLAIDQDP HLSGDMSTAD LQARITDLKN KEEEFNQLKG
FVQNKKALES QLISKKDDIG VSLNQIEILK NKIEASVYDK EKYEKVIYFY EVYERRYDEF
AGELSEIKGQ AKELIANVNV LAEKILTNYK FQQEYKNTTD YIDLLNHIRT LYSKNGIQKE
LRNRSRPVIQ KYTKDFFDEF NFNYSDLTLD EDYEVTVFGP EGEASMSMVS GGEKIAIALA
LRLGITQAMA KGDLDTILLD EPTIHLDSFR RHELINLLKD MTVLPQMIIV THESQLENAA
DNLVKVEKNN GISKVSN
//
