ID   A0A524FHE6_9ARCH        Unreviewed;       411 AA.
AC   A0A524FHE6;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   02-JUN-2021, entry version 5.
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   ECO:0000313|EMBL:TFG24789.1};
GN   ORFNames=EU529_03110 {ECO:0000313|EMBL:TFG24789.1};
OS   Candidatus Lokiarchaeota archaeon.
OC   Archaea; Asgard group; Candidatus Lokiarchaeota;
OC   unclassified Lokiarchaeota.
OX   NCBI_TaxID=2053489 {ECO:0000313|EMBL:TFG24789.1, ECO:0000313|Proteomes:UP000319889};
RN   [1] {ECO:0000313|EMBL:TFG24789.1, ECO:0000313|Proteomes:UP000319889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMARA_1S {ECO:0000313|EMBL:TFG24789.1};
RA   Bulzu P.-A., Andrei S.-A., Salcher M., Mehrshad M., Inoue K., Kandori H.,
RA   Beja O., Ghai R., Banciu H.L.;
RT   "Elucidating Asgardaeota metabolism in a sunlit microoxic niche using
RT   comparative genomics.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC       {ECO:0000256|ARBA:ARBA00008050, ECO:0000256|HAMAP-Rule:MF_00348}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00348}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TFG24789.1}.
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DR   EMBL; SDNY01000011; TFG24789.1; -; Genomic_DNA.
DR   Proteomes; UP000319889; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008094; F:ATPase activity, acting on DNA; IEA:UniProtKB-UniRule.
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   CDD; cd01123; Rad51_DMC1_radA; 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; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033925; Rad51_DMC1_RadA.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   Pfam; PF08423; Rad51; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47794; SSF47794; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02236; recomb_radA; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00348};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00348};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00348};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00348}.
FT   DOMAIN          174..346
FT                   /note="RECA_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          351..411
FT                   /note="RECA_3"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   COILED          70..97
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   411 AA;  46117 MW;  383C346F5CEC4287 CRC64;
     MAKAVEIKNG GYFCAECNRT HIKGKIYKDH LKYAQDDDAE DANIEEKDDD EVEEENIEDY
     IEDYDDDQEL IEAFDELEQL NEEEDLEEEI YASKDREECI KAVKSLPGVG EATLNKLIKS
     GFNSLESIAY TPPNIIINDS GLGEKTTAKL IKASMERLGI GFKSAEDIWE RRKNIARITT
     TSQELDDLLG SGIETGSVIE FFGEFRTGKT QICHQLCVNV QLPKEQGGLE GNALYIDTEG
     TFRPERIIQM SEAKDLDYQK VLKNIVFGRA YNSDHQILLI KEAANIIKEK NIKLIIVDSL
     IGHFRSEYIG RGTLANRQQL INQHLHDLLR LCDIYPELAI VVTNQVQSKP DVFYGNPLRA
     AGGNVVAHGS TIRVYLRKGK GEQRVAKIVD SPSLPESEAV FAITEDGIKD G
//