RAD50_METAC
ID RAD50_METAC Reviewed; 1074 AA.
AC Q8TRL1;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=MA_1164;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM04585.1; -; Genomic_DNA.
DR RefSeq; WP_011021188.1; NC_003552.1.
DR AlphaFoldDB; Q8TRL1; -.
DR STRING; 188937.MA_1164; -.
DR PRIDE; Q8TRL1; -.
DR EnsemblBacteria; AAM04585; AAM04585; MA_1164.
DR GeneID; 1473052; -.
DR KEGG; mac:MA_1164; -.
DR HOGENOM; CLU_004785_0_1_2; -.
DR InParanoid; Q8TRL1; -.
DR OMA; ISHVQEM; -.
DR OrthoDB; 1771at2157; -.
DR PhylomeDB; Q8TRL1; -.
DR Proteomes; UP000002487; 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; IPR045171; ABC_Rad50.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF02463; SMC_N; 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; Reference proteome; Zinc.
FT CHAIN 1..1074
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138653"
FT DOMAIN 512..611
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 355..402
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 452..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 574..611
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 649..678
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 749..823
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 865..895
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 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 973..978
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
SQ SEQUENCE 1074 AA; 121649 MW; 5234F068593C8684 CRC64;
MKLKNLYIEN IRSYRKLDFT FEDGVTVISG VNGSGKSSLL EACFMGLFGS KILSKDFVLA
DMIFKGAETA KINLGFEHLG KEYLIEQAFR YSSKSENASS SKCVLYADGE NIIDQATRTY
EEVRTLLNMD EEAYRNCAYI RQGEIDVLIN AKPKDRQRMI DDLLQLGKLE EYRERTGYAK
TAVRRLERDT KNSLVGVKAE IEGIESTEPV KALNGLKQKA KETDGSLKEL NEKKDYAAAR
KGELDLRIAE YRERLQEIEV LKEAIRKTQE DKAGCFKEKE AFSGEVQGQR RILLELGEEN
TGLRDDCGFG DLEIEALLLH QEKEESSARE KVNAVSKDLA LLLKEGETGS QALCELEKEK
TQAERTLLEC RTSIGAANKE IEGYRENIRK LEEESKGLRE KAGFKAASGA ADEIALLIKE
FEEKESLLRD RKNEASTKLG LSLKEKETCD LNLVELEKEL QNAGAAVRKG STEIEALEKE
LRENSKAVLD IQEQKSEVLA ELKGLGFAAD QLENLEDFSE LLLENKSRLH GKEKELEATL
RELENNIRKN RELFAAGKCP TCGQELKGSE IACTAEECED KKEKLASELA DIKVQHAELE
KKITRLKDAK KLEKRISDYD IEIEKLQEKA KASGKLIETH RARIEEDALK LESLDKRKQE
LETSGRQLLS DIKTLQVQEA EARKAHIEGE KTLIEVKTLD RKLAENTAEI ESLNGKIRTS
LALIENYGER LGELNDKLKA LAEKENLSKE KLKALELALE AAQKKENEAK KAHSESEKLL
GQAKKLQANL LSMENIKHKI SELEAAIRNL AEKVGFLDRE ILERSERIRQ LGEKLEGNRL
SELQQKRAQF EQAQAKITEN IREKTEEKDS LLKEIGMLEN SLKRLRELRK ELKALENRQL
YLEAVYSNAE ELENTYIRVR ADMRARNIGA LSVLLNEMFA FMYTNNAYSH IELDPEYNLT
VYRKDGTPLE PKLLSGGERA IFNLVLRCAI YRLLALGFGG DKADGLPPMI LDEPTVFLDR
GHIRQLLKLI DMMRSIGVGQ IIVVSHDDSL IDSADHVFQV EKDPLTNMSS ITRL
