RAD50_HALVD
ID RAD50_HALVD Reviewed; 893 AA.
AC D4GUK1; P62133;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=HVO_0854;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN POLYPLOID ORGANISMS, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=19593371; DOI=10.1371/journal.pgen.1000552;
RA Delmas S., Shunburne L., Ngo H.P., Allers T.;
RT "Mre11-Rad50 promotes rapid repair of DNA damage in the polyploid archaeon
RT Haloferax volcanii by restraining homologous recombination.";
RL PLoS Genet. 5:E1000552-E1000552(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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 (By similarity).
CC In polyploid organisms, the Rad50/Mre11 complex appears to restrain the
CC repair of double-strand breaks by homologous recombination, allowing
CC another pathway to act as the primary mode of repair (PubMed:19593371).
CC {ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000269|PubMed:19593371}.
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 -!- DISRUPTION PHENOTYPE: Mutants are more resistant to DNA damage, but
CC recover more slowly than the wild-type. {ECO:0000269|PubMed:19593371}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00449}.
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DR EMBL; AJ635369; CAG25775.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03902.1; -; Genomic_DNA.
DR RefSeq; WP_013035478.1; NC_013967.1.
DR AlphaFoldDB; D4GUK1; -.
DR SMR; D4GUK1; -.
DR IntAct; D4GUK1; 10.
DR STRING; 309800.C498_14468; -.
DR PRIDE; D4GUK1; -.
DR EnsemblBacteria; ADE03902; ADE03902; HVO_0854.
DR GeneID; 8925664; -.
DR KEGG; hvo:HVO_0854; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_1_2; -.
DR OMA; ISHVQEM; -.
DR Proteomes; UP000008243; 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; 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 SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..893
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000410349"
FT DOMAIN 404..506
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT REGION 345..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 198..451
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 477..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 564..594
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 688..721
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COMPBIAS 508..573
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: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 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 893 AA; 100087 MW; 0E5C5672CDCD524D CRC64;
MRFTRIAIRN FKPYEDAELD LRDGVTVIHG VNGSGKSSLL EACFFALYGS KALAGTLEDV
VTTGADDAEI TLEFVHDGGE YRIDRRVRVS GDRATTAKCV LDGPEGTVEG ARDVRRHVAS
LLRMDAEAFV NCAYVQQGEV NKLINATPSQ RQDMIDDLLQ LGKLETYRER AGNARLGVED
VLTKKRSVLE DVESQIEAKE DADLHATLNA LESELDSLDE EISNYESQRD KAKSALDAAE
ATLDEHAEKR ERLDEIESAI EDLTAKISAD ETKRDDLSER VRELDAAADE LESDIDDALA
RADLDDASDE AIADAREALS ARESELRDDL SEARTRAQAF ETQAERLRER ADDLESRAEE
KREAAEVDAE TAAEAERELE SFRETRAELR SALDDAEARF EDAPVELGEA ADLLEERREA
RSEARESLAE TETELKNARE RLAEAERLRD AGKCPECGQP VEGSPHVDAI SEREAAVESL
EADRESLESA VESRSAAVEA AEALVEVETR ASSRRDRLDL VDERIADREE TVESRREAAE
EKREAAAELD SEAEEKREAA TTQAERAEEV AETVDSLESD LDTLDDRRDR LDRVESLVDT
RAEKIDARDR LREKRETLAE VNRERREHLR ERRERRDELR ETVDEEAVEG AKQRKKNAAA
YLERVEDEVL PELREKRDDL QSRVGGVEAE LEQLDDLRER RDHLAERVDA LESVHDEVST
LESTYGDLRA ELRQRNVEVL ERMLNETFDL VYANDAYSRI RLDGEYGLTV FQKDGTALEP
EQLSGGERAL FNLSLRCAIY RLLAEGIDGA APLPPLILDE PTVFLDGGHV SRLVDLVEDM
QSRGVKQILI VSHDEDLVGA ADDLVRVEKN PTTNRSTVER TDAPIVEGAL ADD
