ID W0JKT4_9EURY Unreviewed; 921 AA.
AC W0JKT4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HALLA_10480 {ECO:0000313|EMBL:AHF99213.1};
OS Halostagnicola larsenii XH-48.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF99213.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHF99213.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHF99213.1,
RC ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) 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. Rad50 controls the
CC balance between DNA end bridging and DNA resection via ATP-dependent
CC structural rearrangements of the Rad50/Mre11 complex.
CC {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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00449}.
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DR EMBL; CP007055; AHF99213.1; -; Genomic_DNA.
DR RefSeq; WP_049952424.1; NZ_CP007055.1.
DR AlphaFoldDB; W0JKT4; -.
DR STRING; 797299.HALLA_10480; -.
DR GeneID; 25144887; -.
DR KEGG; hlr:HALLA_10480; -.
DR PATRIC; fig|797299.3.peg.1125; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_1_2; -.
DR OrthoDB; 25344at2157; -.
DR Proteomes; UP000019024; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR NCBIfam; NF041035; Rad50_Halo; 1.
DR PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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}; Reference proteome {ECO:0000313|Proteomes:UP000019024};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 437..536
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT REGION 268..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 484
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 487
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 921 AA; 105222 MW; 60BAF78E0F4AEE42 CRC64;
MKVERIRLRN FKCYGEADLG LERGVTIVHG VNGSGKSTLL EGVFFALYGS KALDNRTLDD
VITTGEEEAE IELAFRHDDV DYRIERRLKL RGDRATTTKC VLETPEGTVE GATDVRQKVT
NLLRMDAEAF VNCAYVRQGE VNKLIHASPS DRQDMIDDLL QLGALEEYRE RASDARLGVK
TVLDGQQDVL EDVRTQVEQK EEKDLHERLN ELESRRAELA DDIENFESQR ENASDTLEAS
TEILERHEET REEIETLEEE IETIRSKINE TERKREDAGE TIDDRKTRRD DLEDERETIL
EEIDHVSESG DDTVDTDGDG DAGDDGLELP EPPQALESTA AVEARIDALE RADEQLRDDL
ETLRVEINER SNETDRLESQ AAEFESEAAD KRERAGDLES KIDDDEDAIE QREEKLSTLE
ERIEAARERF DAAPIDFGEA TDHRETIAED REAIVSELGD VTAGIKAVRG SIEEGEALLE
EGKCPECGQP VEDSPHVDVL DEKRERLAEL EAERDALEDE RDEIGERIDR AETLREAERE
VDRLADNRDN VAQLLAEKRE TLADRRERCE QLREDADELE AEAEQHRDAA TDLDAQIDDA
RSDLGKINGT RGEIRTELEE LHRLLEIDDE REEIEREIEN ARERRADWQT MNDERREQLS
AKRDRKRELT DEFDEQRIEQ AREQKRSAED YLEKVDEKLS TLREKRTEIQ NAIGGVENEL
EELERLRERL EAIETRCGDL ESLYDEAETL QATYGDLRAE LRQRNVETLE RLLNETFELV
YQNDSYASID LDGQYRLTVY QKDGEPLEPE QLSGGERALF NLSLRCAIYR LLAEGVEGTA
PMPPLILDEP TVFLDSGHVT QLVSLVESMR DLGVEQIIVV SHDEELVGAA DELVRVEKDA
TSNRSQLERG EPPEIALLSS D
//
