ID A6UPY6_METVS Unreviewed; 1019 AA.
AC A6UPY6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000256|HAMAP-Rule:MF_00449};
GN Name=rad50 {ECO:0000256|HAMAP-Rule:MF_00449};
GN OrderedLocusNames=Mevan_0652 {ECO:0000313|EMBL:ABR54558.1};
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327 {ECO:0000313|EMBL:ABR54558.1, ECO:0000313|Proteomes:UP000001107};
RN [1] {ECO:0000313|EMBL:ABR54558.1, ECO:0000313|Proteomes:UP000001107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB
RC {ECO:0000313|Proteomes:UP000001107};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00449}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00449};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000256|HAMAP-Rule:MF_00449};
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC subunits and two Rad50 subunits. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00449}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00449}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00449}.
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DR EMBL; CP000742; ABR54558.1; -; Genomic_DNA.
DR RefSeq; WP_011972461.1; NC_009634.1.
DR AlphaFoldDB; A6UPY6; -.
DR STRING; 406327.Mevan_0652; -.
DR GeneID; 5324544; -.
DR KEGG; mvn:Mevan_0652; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OrthoDB; 25344at2157; -.
DR Proteomes; UP000001107; 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 Gene3D; 1.10.287.510; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00449};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00449}; DNA damage {ECO:0000256|HAMAP-Rule:MF_00449};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00449};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00449};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00449};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00449};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449}.
FT DOMAIN 5..218
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT COILED 157..315
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 430..464
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 532..638
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 676..703
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT COILED 836..876
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 32..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 523
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
SQ SEQUENCE 1019 AA; 120144 MW; 030B066E89A0E889 CRC64;
MIIKSIKIEN FKSHRNTKLQ LNKGITTIIG HNGSGKSSIF QAMNFALFSP RGANFKIDNM
MQKGSKSFSI ELEFEIRGNS YLVKRKRYQN KTEDKLYING ILNVESSSEV NKKIEEILEL
DNSIFSNAVY IKQGEIANLI QMTSGDRKEV IGKLLGIERY EKVYEKINII KKAYEERLFE
INGELKQEIE VTNLLEKLNL EILRLETLKK EINNEIINLE NIKVEKNNEL TEFNQKFIKI
TKLREDLQEN ISEIKNISLE LQNLENSLKS VDYESLKLEN NQENYFKYLK VESRIKELSE
KIKSHKLEYD AFQKLKLKEE SLSMEILEIG KKINEYSFQE SFKDLNLNEV QILKNINNKD
LKSHSIEDLK KYLVILNEEI LKLDFIKEKI SELEFVEKQI LEINNQKKLK KEFEIDSKNY
DIAVEKISEL NLKKNQYANS LKEKIELEKR LNIENNEKMQ LNKSLKEFMD IELKINLEKN
TKDKYDQICE KISKLTEVIA GNEIVLKNSL VSKAELEKTV DECNICKSKI TNDKKQELLL
AYELEQENLE KVIESLKNQV EILNRKKEIL NSELKIINGL KPKYGELLEK KNSILKVENS
INELELKLTD MKKNLCEYEV IKSELSNYEL QKSRLKEINN KYQYCIQFLN NIDENNVLTT
QSELLKVIGD YDVLKIQLMK KDLETLKDNL KEILQNLERE KVLNFELTNV KNNIYSKLGL
VEQYLEWETE KSNLEVELSM HKKYYEEFME SMAVLKSHSK AYSIEITKLN DYLREKTFEK
YSVLTKKNTL RNKLINDIQE INYNEERHKE LNIYFENILK ELHEFSKKFE RISSELTVKK
ENSESLNKKI KELALKKEEK QKIESFKEYL EKIRREVFSK DGFQKYLREK YIPLIQRHAN
QIFQEFELPY SHIQLKEDYS LIVDGLPVET LSGGEQIAVS LALRLGISKA VCNNIECIIL
DEPTAYLDEE RRKNLLNIFR NIKTISQMAI ITHHQELEQI ADNILTVRKI GEISKVTLE
//
