RAD50_PYRAB
ID RAD50_PYRAB Reviewed; 880 AA.
AC Q9UZC8; G8ZKL3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=PYRAB12200;
GN ORFNames=PAB0812;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB50131.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70656.1; -; Genomic_DNA.
DR PIR; F75103; F75103.
DR RefSeq; WP_010868338.1; NC_000868.1.
DR AlphaFoldDB; Q9UZC8; -.
DR SMR; Q9UZC8; -.
DR STRING; 272844.PAB0812; -.
DR PRIDE; Q9UZC8; -.
DR EnsemblBacteria; CAB50131; CAB50131; PAB0812.
DR GeneID; 1496602; -.
DR KEGG; pab:PAB0812; -.
DR PATRIC; fig|272844.11.peg.1300; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; ISHVQEM; -.
DR OrthoDB; 1771at2157; -.
DR PhylomeDB; Q9UZC8; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 CDD; cd03240; ABC_Rad50; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041685; AAA_15.
DR InterPro; IPR045171; ABC_Rad50.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13175; AAA_15; 1.
DR Pfam; PF13304; AAA_21; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase; Metal-binding;
KW Nucleotide-binding; Zinc.
FT CHAIN 1..880
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138660"
FT DOMAIN 397..494
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 225..336
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 391..744
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
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 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 789..794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 880 AA; 103971 MW; FDB177EC7E026479 CRC64;
MKIEEVKVYN FRSHEETVVR FRKGINLIIG QNGSGKSSLL DAILVGLYWS KKLRLRGLKK
DEFRRIGGKG GTRIEIKFEN DDSKYVLFRD FSRNVAYLKV QENGKWRHAS EPSMESVSSY
IERILPYNVF LNAIYIRQGQ IDAILESDET RDKVVREILN LDKLESAYEN LKRIKTNINL
LIESKKSFIA RTENIEELIK ANEDELTKKL SEINEISSKL PPIRGELEKV RENVKELESI
KGKISELKIQ VEKLKGRKKG LEEKIVQIER SIEEKKAKIS ELEEIVKDIP KLQEKEKEYR
KLKGFRDEYE SKLRRLEKEL SKWESELKAI EEVIKEGEKK KERAEEIREK LSEIEKRLEE
LKPYVEELED AKQVQKQIER LKARLKGLSP GEVIEKLESL EKERTEIEEA IKEITTRIGQ
MEQEKNERMK AIEELRKAKG KCPVCGRELT EEHKKELMER YTLEIKKIEE ELKRTTEEER
KLRVNLRKLE IKLREFSVMR DIAEQIKELE SKLKGFNLEE LEQKEREFEG LNEEFNKLKG
ELLGLERDLK RIKALEGRRK LIEEKVRKAK EELENLHRQL RELGFESVEE LNLRIQELEE
FHDKYVEAKK SESELRELKN KLEKEKTELD QAFEMLADVE NEIEEKEAKL KDLESKFNEE
EYEEKRERLV KLEREVSSLT ARLEELKKSV EQIKATLRKL KEEKEEREKA KLEIKKLEKA
LSKVEDLRKK IKDYKTLAKE QALNRISEIA SEIFSEFTDG KYSNVIVRAE ENKTKLFVVY
EGKEVPLTFL SGGERIALGL AFRLALSMYL VGRIDLLILD EPTPFLDEER RRKLLDIMER
HLRRISQVIM VSHDEELKDA ADYVIRLRLE GGKSKVEVVS
