RAD50_AERPE
ID RAD50_AERPE Reviewed; 919 AA.
AC Q9YFZ1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=APE_0110;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA79020.1; -; Genomic_DNA.
DR PIR; B72765; B72765.
DR AlphaFoldDB; Q9YFZ1; -.
DR SMR; Q9YFZ1; -.
DR STRING; 272557.APE_0110; -.
DR PRIDE; Q9YFZ1; -.
DR EnsemblBacteria; BAA79020; BAA79020; APE_0110.
DR KEGG; ape:APE_0110; -.
DR eggNOG; arCOG00368; Archaea.
DR OMA; FELPYSH; -.
DR Proteomes; UP000002518; 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; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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; Reference proteome; Zinc.
FT CHAIN 1..919
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138649"
FT DOMAIN 417..516
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 208..268
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 315..379
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 414..458
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 486..515
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 541..595
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 635..749
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 33..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 919 AA; 104139 MW; 7BF4A80EB601B9DD CRC64;
MYVLKRLELR NIMSHFNTSI DFREGFTAIV GRNGAGKSTI LEAILFSITP HQAPRRSSMI
SENSSRGEIY LALQSSEGRL LELRNKLIRR GGGTNTEAAI ITLEGRRIAS KPTGYKEEIH
KILGLRGLPN PASYIEKAII ISQGGLQTLA EILSEPKELR DLLDAALGYA LLKQAISNIG
DVVLGVSPDG SPVKLGSKSI TRLQSGYMTL RNEVLGVDRE IREASKRLEE LEREREELER
RARDLESEAK ALQSEIGKLE TMEEMLVNVT SMIRSERSKL DTINTRLRYA ESKISSIDDL
EKRRAELRAK ASLAHEVAEL ARLQSRLDKL GRDLEMIRDA VEKLEVSRRL KEIESARREA
ENRLLEARSS IKEEQRRYTL LDYRVTRGRS IVTNIRRVLS ECRSKDLCGS EKPESVLERL
DAVINDLESK ARALDQEASA LEAEARRLVQ ALSMLEESGG SARCPVCGAE LPPGRAEAIA
RHYRHEAERL RKAAKEKAAE AEKARAEASR LQDKRRRIEL LLSRLNQLEE GLRELGFQTP
EDLAKAEQKL RMLRERLEEL RKLENSLEEK VRNLSREEVA LREAKTRALE VLQRLGIKEE
EAREKLKTLS SESKKLERML VSKAEDLATR LGITAYRSLD DLLEKAREAL EGVDKELSAI
ERRLEEARRL KEEAAKLKWE AEQVMKRLEE LEAEEKKLRK EVSRKSEIEA RLKEVQNTLA
ELDDRISRID REMGELQTRI REMKSRKASG EEALKLYLPA AASRRIMEEI GEIAYRRLLA
VLEDEMNDIL SRFNLDVAGV EIREKAAREI EVKAIGGNGA YRPLEAVSGG ERTVLALSFV
LALNKAVGGK LGFLALDEPT ANLDEDRRRS LVEVLRGISV EGLVRQLVVV THHEDVRDYA
DTICLVTRTQ QGSRVECTY
