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Database: UniProt
Entry: C6A058_THESM
LinkDB: C6A058_THESM
Original site: C6A058_THESM 
ID   C6A058_THESM            Unreviewed;       526 AA.
AC   C6A058;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
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   OrderedLocusNames=TSIB_1992 {ECO:0000313|EMBL:ACS91039.1};
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS91039.1, ECO:0000313|Proteomes:UP000009079};
RN   [1] {ECO:0000313|EMBL:ACS91039.1, ECO:0000313|Proteomes:UP000009079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX   PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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}.
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DR   EMBL; CP001463; ACS91039.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6A058; -.
DR   STRING; 604354.TSIB_1992; -.
DR   KEGG; tsi:TSIB_1992; -.
DR   eggNOG; arCOG00415; Archaea.
DR   HOGENOM; CLU_528557_0_0_2; -.
DR   Proteomes; UP000009079; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd00081; Hint; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_00348; RadA_arch; 1.
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; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   NCBIfam; TIGR01445; intein_Nterm; 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; PF14890; Intein_splicing; 1.
DR   Pfam; PF08423; Rad51; 2.
DR   SMART; SM00278; HhH1; 2.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 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}; Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00348};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00348};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00348};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00348}; Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009079}.
FT   DOMAIN          299..322
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
FT   DOMAIN          322..462
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          467..526
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
SQ   SEQUENCE   526 AA;  58357 MW;  8A43E9221DDB372E CRC64;
     MIQMARKKKI EDEVKELDEF EELDALDELS VEEPTKGSNK KEIKSIEDLP GVGPATAEKL
     REAGYDSLEA IAVASPLELK ELAGVSEGAA LKIIQAAREA ANIGTFMRAD EYFQKRAVVG
     KITTGSKSLD KLLGGGIETQ AVSEVFGEFG SGKCFAKDTT VYYENDDVAH VESIEEMYNK
     YATKNGEIPF DNGFAVPLEV VSVYTFNIKT RKVEKTKVSY IYKEKVSTLV KLKLSTGIEL
     KVTQSHPVLV FKDGLKWIKA SEVQIGDRVV GIGEVPPKSE VNLRFHQVES VEIFDYNDYV
     YDLVVPETHN FIAPNGLILH NTQLAHTLAV IVQKPPEEGG LNGSVVWIDT ENTFRPERIK
     QIAESRGMDP DEVLKNIYVA RAFNSNHQML LVEKAEEIIK EKLPSEKPVK LLVVDSLTGH
     FRSEYVGRGT LAERQQKLAK HLADLHRLAN LYDIAVFVTN QVQARPDAFF GDPTRPIGGH
     ILAHSATVRV YLRKGKAGKR VARLIDSPHL PEGEAAFAIT EKGVED
//
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