ID A0A125RCV6_9EURY Unreviewed; 915 AA.
AC A0A125RCV6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=TL18_05630 {ECO:0000313|EMBL:AMD17546.1};
OS Methanobrevibacter sp. YE315.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=1609968 {ECO:0000313|EMBL:AMD17546.1, ECO:0000313|Proteomes:UP000057992};
RN [1] {ECO:0000313|EMBL:AMD17546.1, ECO:0000313|Proteomes:UP000057992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE315 {ECO:0000313|EMBL:AMD17546.1,
RC ECO:0000313|Proteomes:UP000057992};
RA Ouwerkerk D., Gilbert R.A., Klieve A.V., Martinez E.;
RT "Genome sequence of Methanobrevibacter sp. YE315.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; CP010834; AMD17546.1; -; Genomic_DNA.
DR RefSeq; WP_067042638.1; NZ_CP010834.1.
DR AlphaFoldDB; A0A125RCV6; -.
DR STRING; 1609968.TL18_05630; -.
DR GeneID; 28487321; -.
DR KEGG; meye:TL18_05630; -.
DR PATRIC; fig|1609968.3.peg.1161; -.
DR OrthoDB; 25344at2157; -.
DR Proteomes; UP000057992; 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; 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 Pfam; PF04423; Rad50_zn_hook; 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.
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_00449}.
FT DOMAIN 22..908
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 182..383
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 497..541
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 636..663
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 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 826..831
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
SQ SEQUENCE 915 AA; 106001 MW; FD1EBFEC8429DA7E CRC64;
MIFTKLKLIN FKSHENTIIK FDKGISVIVG ENGAGKSTIL EGISFALFKQ HTGKKIDDLV
RNNAQSMLVE LGFTSNGRQY KIIREKKSNL TSSIYKKTSA DGDYVHICSG DKEVANEIRQ
ILDIDSDLFL NAIYIRQGEI SELVDKTPAE KKKLIGKLLG IDSLEKAWNN LLPLITDYEN
ELSELKGKLY NSDELKENLE KKKDELNSLK ERGHELEKNI EEVNELRDEI SESKRNMERE
KEIYEAQSNN LISEEKTLSK LENDKRTVQD DLDKINNAEE EIERLEKYVS KLDTYLDFEK
SVTSIQNLKE KEKEINEKID SINRQKEIIA DNKENYNKFL VSDEEISKLD EQKLSLEKEL
ATMAKLEKDK KDFLKQIEDE RNDIDNFFSR AKEKLHDNGL DQDIVAGIDN FTQIENATND
FLDETSTKIK DLGKDIISKN EDIVVFKQNI KACERPLEEL GEIDNKCPVC QSDIDENKKK
ELVDQYSNDI ETNKRLISEN EEAVRLLTKN KESFEEKYDI LLDLSKNIIE YKQKFNHLQS
EIYKLNEIDE KLESKEYISN KLGEIILLIA NKKSERESCQ ESYDLYNQAQ GALEVLGSVT
ELQYQLNQIN NEIDNHVSSI KWVIEQDPHL SGDISEEELQ DRINDLKQKN EEFNQLKGFV
KNKQSYLTQL DSIKEDIGMS INQIDIIKNK INASVYDEEK YEQIIYRSDM YERRYNTFNN
ELSEIKGRAR ETIVYVKDLT EKIEKADKFQ QEYNDVSDYI NLLNHIRSLY SKNGIQKDLR
NISRPLIQKY TKEFFNEFNF NYSDLTLDEE YDVTVYGPEG KSSMSMVSGG EKIAIALALR
LGITQAMSNG ELDTILLDEP TIHLDNSRKH ELINLLKEMS LLPQMIIVTH EAQLENAADN
LIKVEKVNGI SNVIV
//
