ID U1MTE4_9EURY Unreviewed; 353 AA.
AC U1MTE4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA repair and recombination protein RadA {ECO:0000256|ARBA:ARBA00018144, ECO:0000256|HAMAP-Rule:MF_00348};
GN Name=radA {ECO:0000256|HAMAP-Rule:MF_00348};
GN ORFNames=J07HQW1_03593 {ECO:0000313|EMBL:ERG93529.1};
OS Haloquadratum walsbyi J07HQW1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=1238424 {ECO:0000313|EMBL:ERG93529.1, ECO:0000313|Proteomes:UP000030649};
RN [1] {ECO:0000313|EMBL:ERG93529.1, ECO:0000313|Proteomes:UP000030649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HQW1 {ECO:0000313|Proteomes:UP000030649};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
CC -!- FUNCTION: Involved in DNA repair and in homologous recombination. Binds
CC and assemble on single-stranded DNA to form a nucleoprotein filament.
CC Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand
CC exchange between homologous DNA molecules. {ECO:0000256|HAMAP-
CC Rule:MF_00348, ECO:0000256|PIRNR:PIRNR005856}.
CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000256|ARBA:ARBA00008050, ECO:0000256|HAMAP-Rule:MF_00348,
CC ECO:0000256|PIRNR:PIRNR005856}.
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DR EMBL; KE356560; ERG93529.1; -; Genomic_DNA.
DR AlphaFoldDB; U1MTE4; -.
DR STRING; 1238424.J07HQW1_03593; -.
DR HOGENOM; CLU_041732_0_0_2; -.
DR Proteomes; UP000030649; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00348; RadA_arch; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR011938; DNA_recomb/repair_RadA.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR NCBIfam; TIGR02236; recomb_radA; 1.
DR PANTHER; PTHR22942:SF39; DNA REPAIR PROTEIN RAD51 HOMOLOG 1; 1.
DR PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF08423; Rad51; 2.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00348};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00348,
KW ECO:0000256|PIRNR:PIRNR005856};
KW DNA recombination {ECO:0000256|HAMAP-Rule:MF_00348,
KW ECO:0000256|PIRNR:PIRNR005856};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00348,
KW ECO:0000256|PIRNR:PIRNR005856};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00348}.
FT DOMAIN 88..288
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 293..353
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00348"
SQ SEQUENCE 353 AA; 38606 MW; 6A73BFF7B0D6A99C CRC64;
MWQWSVYVCT MPEDELEDLP GVGPATSDKL IDAGFESYQA IAVASPSEMS NTADVGESTA
SDIINAARDA ADIGGFETGA AVLQRREQIG KLSWKIPEVD ELLGGGIETQ SITEVYGEFG
AGKSQVTHQM AVNVQLPPEH GGLGGAAIFV DSEDTFRPER IDDMLRGLDD EIIADLLERR
EIEGTPGDDE AMEALLDSFL DHIHVAKAFN SNHQILLAEK AKDLARDNED SDFPIRLLCV
DSLTAHFRAE YVGRGSLAER QQKLNKHLHD LMRIGDLYNT AVLVTNQVAS NPDSYFGDPT
QPIGGNILGH TSTFRMYLRK SKNDKRIVRL VDAPNLADGE AVMRVKDAGL KPE
//
