ID A0A0F7P930_9EURY Unreviewed; 887 AA.
AC A0A0F7P930;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000256|HAMAP-Rule:MF_00449};
GN Name=smc2 {ECO:0000313|EMBL:AKH97262.1};
GN Synonyms=rad50 {ECO:0000256|HAMAP-Rule:MF_00449};
GN ORFNames=HLASA_0763 {ECO:0000313|EMBL:ALG81664.1}, HLASF_0766
GN {ECO:0000313|EMBL:AKH97262.1};
OS Halanaeroarchaeum sulfurireducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halanaeroarchaeum.
OX NCBI_TaxID=1604004 {ECO:0000313|EMBL:AKH97262.1, ECO:0000313|Proteomes:UP000069906};
RN [1] {ECO:0000313|EMBL:AKH97262.1, ECO:0000313|Proteomes:UP000069906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR2 {ECO:0000313|EMBL:AKH97262.1,
RC ECO:0000313|Proteomes:UP000069906};
RX PubMed=25978546;
RA Sorokin D.Y., Kublanov I.V., Gavrilov S.N., Rojo D., Roman P.,
RA Golyshin P.N., Slepak V.Z., Smedile F., Ferrer M., Messina E., La Cono V.,
RA Yakimov M.M.;
RT "Elemental sulfur and acetate can support life of a novel strictly
RT anaerobic haloarchaeon.";
RL ISME J. 0:0-0(2015).
RN [2] {ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|Proteomes:UP000060390};
RA Messina E., Kublanov I.V., Toshchakov S., Arcadi E., La Spada G.,
RA La Cono V., Yakimov M.M.;
RT "Complete genome sequence of Halanaeroarchaeum sulfurireducens type strain
RT M27-SA2, a sulfate-reducer haloarchaeon from marine anoxic lake Medee.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALG81664.1, ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|EMBL:ALG81664.1,
RC ECO:0000313|Proteomes:UP000060390};
RX PubMed=27182430; DOI=10.1186/s40793-016-0155-9;
RA Messina E., Sorokin D.Y., Kublanov I.V., Toshchakov S., Lopatina A.,
RA Arcadi E., Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Complete genome sequence of 'Halanaeroarchaeum sulfurireducens' M27-SA2, a
RT sulfur-reducing and acetate-oxidizing haloarchaeon from the deep-sea
RT hypersaline anoxic lake Medee.";
RL Stand. Genomic Sci. 11:35-35(2016).
CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the
CC early steps of DNA double-strand break (DSB) repair. Rad50 controls the
CC balance between DNA end bridging and DNA resection via ATP-dependent
CC structural rearrangements of the Rad50/Mre11 complex.
CC {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|ARBA:ARBA00009439, 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; CP008874; AKH97262.1; -; Genomic_DNA.
DR EMBL; CP011564; ALG81664.1; -; Genomic_DNA.
DR RefSeq; WP_050048048.1; NZ_CP011564.1.
DR AlphaFoldDB; A0A0F7P930; -.
DR STRING; 1604004.HLASA_0763; -.
DR GeneID; 26010126; -.
DR KEGG; hsf:HLASA_0763; -.
DR KEGG; hsu:HLASF_0766; -.
DR PATRIC; fig|1604004.4.peg.804; -.
DR HOGENOM; CLU_004785_0_1_2; -.
DR OrthoDB; 25344at2157; -.
DR Proteomes; UP000060390; Chromosome.
DR Proteomes; UP000069906; 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 InterPro; IPR013134; Zn_hook_RAD50.
DR NCBIfam; NF041035; Rad50_Halo; 1.
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.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00449};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00449};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00449}; Reference proteome {ECO:0000313|Proteomes:UP000069906};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW ProRule:PRU00471}.
FT DOMAIN 407..506
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT REGION 349..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 470..559
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 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00449,
FT ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 887 AA; 100285 MW; 44CC7B6570F2C765 CRC64;
MRFERLRLHN FKCYEDADVS LGRGVTVIHG LNGSGKSSLL EAIFFALYGT TGLDRTLEEV
VTIGQDEAEI ELWFTHDGDD YHLRRRVRAT GERATTADCV LDGPAETFDG VRDVEDAVTG
MLRMDAEAFV NSAFVRQGEI NKLINATPRS RQEMIDRLLQ LGTLETYRER AAEARLGVES
VLDHWTGRLE SLDDQIDEKE DRDLFEVRSR LQSELNEVQA EIERLETNRS EAESTLTEAE
SVLESYEDAQ SDLEEVKERI TSIREAIAET EAERDDLSEA IAEHREAIAD LDERIESLTG
TTILEEATET AVADRRASLV RERESLQEEI ATIRETVTAN EQTIERLREK ADDHEERAEA
KLEEASALES EAEEAAARVD ELESRLSSIR EDIAALRERF EDAPVDVGEA DELVTSAEAE
LETLEAERSE IRESLASARS RVDDARALIE EGKCPECGQP VEGSPHVESL SEYETTVAEL
EADLSDVESE IEDAEERLDT AESLVEAERT LDRLEGERED VESLLEERRA AVEEKRERAA
SLRETADELA ISAAEARDEA AAARGDMMEA RECIGLMNDR RERIQSTIET LDEIDQALER
RSDHEEAIER ARDERESLAD RNDERRDHLA AARDRKQELE ESFDDTRIEA AREKRERATD
YLEEVEGELE ELTERRDSLQ GQVGAVENAI QELESLREER TSVAERVEAL ESLLQEGRDL
EEVYGDLRAE LRQQNVARLE RLLNETFELV YQNDSYDRIE LNGQYELTVY QKDGEPLEPE
QLSGGERALF NLSLRTAIYR LLAEGIDGAA PMPPLILDEP TVFLDSGHVS QLVSLVESMR
RIGVEQIIVV SHDEELVGAA DDVIRVEKDA TTNRSYVERG RQPTDGT
//
