RAD50_THEMA
ID RAD50_THEMA Reviewed; 852 AA.
AC Q9X1X1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable DNA double-strand break repair Rad50 ATPase;
GN Name=rad50; OrderedLocusNames=TM_1636;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). The
CC Rad50/Mre11 complex possesses single-strand endonuclease activity and
CC ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50
CC provides an ATP-dependent control of Mre11 by unwinding and/or
CC repositioning DNA ends into the Mre11 active site (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Forms a complex with Mre11 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9X1X1; Q9X1X0: sbcD; NbExp=3; IntAct=EBI-3954207, EBI-3954204;
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD36703.1; -; Genomic_DNA.
DR PIR; D72230; D72230.
DR RefSeq; NP_229436.1; NC_000853.1.
DR RefSeq; WP_004082116.1; NZ_CP011107.1.
DR PDB; 3QF7; X-ray; 1.90 A; A/B=1-190, A/B=686-852.
DR PDB; 3QG5; X-ray; 3.40 A; A/B=1-190, A/B=686-852.
DR PDB; 3THO; X-ray; 2.61 A; A=1-190, A=686-852.
DR PDB; 4W9M; X-ray; 2.70 A; C/E/I/K=1-188, C/E/I/K=687-852.
DR PDBsum; 3QF7; -.
DR PDBsum; 3QG5; -.
DR PDBsum; 3THO; -.
DR PDBsum; 4W9M; -.
DR AlphaFoldDB; Q9X1X1; -.
DR SMR; Q9X1X1; -.
DR IntAct; Q9X1X1; 1.
DR STRING; 243274.THEMA_06065; -.
DR PRIDE; Q9X1X1; -.
DR EnsemblBacteria; AAD36703; AAD36703; TM_1636.
DR KEGG; tma:TM1636; -.
DR eggNOG; COG0419; Bacteria.
DR InParanoid; Q9X1X1; -.
DR OMA; ISHVQEM; -.
DR OrthoDB; 1143316at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.660; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13476; AAA_23; 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..852
FT /note="Probable DNA double-strand break repair Rad50
FT ATPase"
FT /id="PRO_0000138670"
FT DOMAIN 389..488
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT COILED 155..345
FT /evidence="ECO:0000255"
FT COILED 389..427
FT /evidence="ECO:0000255"
FT COILED 460..488
FT /evidence="ECO:0000255"
FT COILED 534..711
FT /evidence="ECO:0000255"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3THO"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:3QF7"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3THO"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3QG5"
FT TURN 145..150
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 167..189
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 686..709
FT /evidence="ECO:0007829|PDB:3QF7"
FT TURN 711..713
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 714..738
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 742..747
FT /evidence="ECO:0007829|PDB:3QF7"
FT TURN 748..751
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 752..757
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 760..763
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 769..786
FT /evidence="ECO:0007829|PDB:3QF7"
FT TURN 787..790
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 793..798
FT /evidence="ECO:0007829|PDB:3QF7"
FT TURN 799..802
FT /evidence="ECO:0007829|PDB:3THO"
FT HELIX 805..816
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 817..820
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 821..830
FT /evidence="ECO:0007829|PDB:3QF7"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 841..845
FT /evidence="ECO:0007829|PDB:3QF7"
FT STRAND 848..850
FT /evidence="ECO:0007829|PDB:3QF7"
SQ SEQUENCE 852 AA; 100002 MW; 31BA9F72A4EC5CD2 CRC64;
MRPERLTVRN FLGLKNVDIE FQSGITVVEG PNGAGKSSLF EAISFALFGN GIRYPNSYDY
VNRNAVDGTA RLVFQFERGG KRYEIIREIN ALQRKHNAKL SEILENGKKA AIAAKPTSVK
QEVEKILGIE HRTFIRTVFL PQGEIDKLLI SPPSEITEII SDVFQSKETL EKLEKLLKEK
MKKLENEISS LQALYTAIWK YLEENDLEVL KSELKTVSEK KKELLKKREE LQKEEEQLKR
LLEKYRELVK KKERLRVLSL RRNELQKEVI YEQKVKKAKE LEPLFREIYL RQREFERFSQ
ELNSREKRYK ELESEKEAIS KEIPVHRERL SKLEEIGEKI KEELDLLEKV LKASRPLLEQ
RIRLKENLTR LEEEFRRLVG EKEKREKELL SIEKTENETK NELEKLLDEL SILKKDHMKW
LAYQIASSLN EGDTCPVCGG VFHGKVEAVE FNIDEFEKLD QKRSELENTL NVLKERKKSL
SSLIEDLLMK IEEGKKNLKS IRNQIEKIEE ELHRLGYSED LEEKLDEKRK KLRKIEEERH
SISQKITAAD VQISQIENQL KEIKGEIEAK RETLKEQREE MDQLKSDFFD RLRKIGIGFE
EFRILVKEEV KDAEKELGVV ETEIRLLEES LKELESENVR DVSEDYEKVR NQLEALSQEI
SDLERKEGRL NHLIEETLRR ERELKSLEKK LKEMSDEYNN LDLLRKYLFD KSNFSRYFTG
RVLEAVLKRT KAYLDILTNG RFDIDFDDEK GGFIIKDWGI ERPARGLSGG ERALISISLA
MSLAEVASGR LDAFFIDEGF SSLDTENKEK IASVLKELER LNKVIVFITH DREFSEAFDR
KLRITGGVVV NE
