RAD50_METJA
ID RAD50_METJA Reviewed; 1005 AA.
AC Q58718;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=MJ1322;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2] {ECO:0007744|PDB:3AUX, ECO:0007744|PDB:3AUY, ECO:0007744|PDB:3AV0}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ADP.
RA Lim H.S., Kim J.S., Park Y.B., Gwon G.H., Cho Y.;
RT "Crystal structure of the Mre11-Rad50-ATP S complex: understanding the
RT interplay between Mre11 and Rad50.";
RL Submitted (FEB-2011) to the PDB data bank.
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; L77117; AAB99331.1; -; Genomic_DNA.
DR PIR; A64465; A64465.
DR PDB; 3AUX; X-ray; 2.80 A; A=1-190, A=825-1005.
DR PDB; 3AUY; X-ray; 2.70 A; A/B=11-190, A/B=825-1005.
DR PDB; 3AV0; X-ray; 3.10 A; B=1-190, B=825-1005.
DR PDB; 5DNY; X-ray; 3.11 A; B/D=1-190, B/D=825-1005.
DR PDB; 5F3W; X-ray; 3.11 A; B/D=1-190, B/D=825-1005.
DR PDBsum; 3AUX; -.
DR PDBsum; 3AUY; -.
DR PDBsum; 3AV0; -.
DR PDBsum; 5DNY; -.
DR PDBsum; 5F3W; -.
DR AlphaFoldDB; Q58718; -.
DR SMR; Q58718; -.
DR STRING; 243232.MJ_1322; -.
DR PRIDE; Q58718; -.
DR EnsemblBacteria; AAB99331; AAB99331; MJ_1322.
DR KEGG; mja:MJ_1322; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR InParanoid; Q58718; -.
DR OMA; FELPYSH; -.
DR PhylomeDB; Q58718; -.
DR EvolutionaryTrace; Q58718; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..1005
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138654"
FT DOMAIN 457..554
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 189..230
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 292..321
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 346..379
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 404..498
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 523..600
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 656..692
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 800..834
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449,
FT ECO:0007744|PDB:3AUY"
FT BINDING 35..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:3AUX, ECO:0007744|PDB:3AUY"
FT BINDING 62..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:3AUX, ECO:0007744|PDB:3AUY"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5DNY"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 158..185
FT /evidence="ECO:0007829|PDB:3AUY"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3AV0"
FT HELIX 193..224
FT /evidence="ECO:0007829|PDB:3AUY"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 231..247
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 278..296
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:3AUY"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:3AUY"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:3AUY"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:3AUY"
SQ SEQUENCE 1005 AA; 119388 MW; 9BBBB48173E788F3 CRC64;
MSMILKEIRM NNFKSHVNSR IKFEKGIVAI IGENGSGKSS IFEAVFFALF GAGSNFNYDT
IITKGKKSVY VELDFEVNGN NYKIIREYDS GRGGAKLYKN GKPYATTISA VNKAVNEILG
VDRNMFLNSI YIKQGEIAKF LSLKPSEKLE TVAKLLGIDE FEKCYQKMGE IVKEYEKRLE
RIEGELNYKE NYEKELKNKM SQLEEKNKKL MEINDKLNKI KKEFEDIEKL FNEWENKKLL
YEKFINKLEE RKRALELKNQ ELKILEYDLN TVVEARETLN RHKDEYEKYK SLVDEIRKIE
SRLRELKSHY EDYLKLTKQL EIIKGDIEKL KEFINKSKYR DDIDNLDTLL NKIKDEIERV
ETIKDLLEEL KNLNEEIEKI EKYKRICEEC KEYYEKYLEL EEKAVEYNKL TLEYITLLQE
KKSIEKNIND LETRINKLLE ETKNIDIESI ENSLKEIEEK KKVLENLQKE KIELNKKLGE
INSEIKRLKK ILDELKEVEG KCPLCKTPID ENKKMELINQ HKTQLNNKYT ELEEINKKIR
EIEKDIEKLK KEIDKEENLK TLKTLYLEKQ SQIEELELKL KNYKEQLDEI NKKISNYVIN
GKPVDEILED IKSQLNKFKN FYNQYLSAVS YLNSVDEEGI RNRIKEIENI VSGWNKEKCR
EELNKLREDE REINRLKDKL NELKNKEKEL IEIENRRSLK FDKYKEYLGL TEKLEELKNI
KDGLEEIYNI CNSKILAIDN IKRKYNKEDI EIYLNNKILE VNKEINDIEE RISYINQKLD
EINYNEEEHK KIKELYENKR QELDNVREQK TEIETGIEYL KKDVESLKAR LKEMSNLEKE
KEKLTKFVEY LDKVRRIFGR NGFQAYLREK YVPLIQKYLN EAFSEFDLPY SFVELTKDFE
VRVHAPNGVL TIDNLSGGEQ IAVALSLRLA IANALIGNRV ECIILDEPTV YLDENRRAKL
AEIFRKVKSI PQMIIITHHR ELEDVADVII NVKKDGNVSK VKING
