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Database: UniProt
Entry: D9QSZ5_ACEAZ
LinkDB: D9QSZ5_ACEAZ
Original site: D9QSZ5_ACEAZ 
ID   D9QSZ5_ACEAZ            Unreviewed;       462 AA.
AC   D9QSZ5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
GN   Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN   OrderedLocusNames=Acear_0132 {ECO:0000313|EMBL:ADL11683.1};
OS   Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL11683.1, ECO:0000313|Proteomes:UP000001661};
RN   [1] {ECO:0000313|EMBL:ADL11683.1, ECO:0000313|Proteomes:UP000001661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC   {ECO:0000313|Proteomes:UP000001661};
RX   PubMed=21304692;
RA   Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA   Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT   7288).";
RL   Stand. Genomic Sci. 3:57-65(2010).
CC   -!- FUNCTION: DNA-dependent ATPase involved in processing of recombination
CC       intermediates, plays a role in repairing DNA breaks. Stimulates the
CC       branch migration of RecA-mediated strand transfer reactions, allowing
CC       the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA
CC       in the presence of ADP but not other nucleotides, has ATPase activity
CC       that is stimulated by ssDNA and various branched DNA structures, but
CC       inhibited by SSB. Does not have RecA's homology-searching function.
CC       {ECO:0000256|RuleBase:RU003555}.
CC   -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, probably
CC       involving stabilizing or processing branched DNA or blocked replication
CC       forks. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- DOMAIN: The middle region has homology to RecA with ATPase motifs
CC       including the RadA KNRFG motif, while the C-terminus is homologous to
CC       Lon protease. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555}.
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DR   EMBL; CP002105; ADL11683.1; -; Genomic_DNA.
DR   RefSeq; WP_013277130.1; NC_014378.1.
DR   AlphaFoldDB; D9QSZ5; -.
DR   STRING; 574087.Acear_0132; -.
DR   MEROPS; S16.A04; -.
DR   KEGG; aar:Acear_0132; -.
DR   eggNOG; COG1066; Bacteria.
DR   HOGENOM; CLU_018264_0_1_9; -.
DR   OMA; FELMRLA; -.
DR   OrthoDB; 9803906at2; -.
DR   Proteomes; UP000001661; Chromosome.
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:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR   CDD; cd01121; RadA_SMS_N; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01498; RadA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004504; DNA_repair_RadA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR041166; Rubredoxin_2.
DR   NCBIfam; TIGR00416; sms; 1.
DR   PANTHER; PTHR32472; DNA REPAIR PROTEIN RADA; 1.
DR   PANTHER; PTHR32472:SF10; DNA REPAIR PROTEIN RADA-LIKE PROTEIN; 1.
DR   Pfam; PF13481; AAA_25; 1.
DR   Pfam; PF13541; ChlI; 1.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   PRINTS; PR01874; DNAREPAIRADA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01498};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001661};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_01498}; Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN          69..218
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   REGION          39..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..462
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   MOTIF           255..259
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   COMPBIAS        39..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         98..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   462 AA;  50913 MW;  844BAB4E1BBD7249 CRC64;
     MAKKKVRYVC EECGHEALKW NGQCAGCGSW NTLVKKIHDK QEKKKQEEKK KKAEKGNPPQ
     QIDQITTATA NRLKTELSEL NRVLGGGIVP GSLILIGGAP GIGKSTLLLQ LAYQISCKYG
     KVLYVSAEES KHQVKLRADR LQVNSSELYV LTETNYFTIE EEVKNLAPEL VIIDSIQTIY
     DPDYDSVPGS IKQVRECTGK LMRLAKTEDI PIFLVGHVTK KGSIAGPKML EHMVDVVLYF
     DSEQQQLYRI LRSAKNRYGS TDEIGIFEMK QQGLIEVLNP SRHFISERPS GVSGSVIVPC
     LEGTRPILVE VQALTSTANY GSPTRMTSGV DHRRVSLILA VLEKRLGLYL QGEDVNINIA
     GGMQIEEPGI DLGIAVAIIS SFRELPLPED LLVLGEIGLS GEVRAVSRME SRIQEAIKLG
     FKQFIIPDGN LSSLELDVSD LEIEVCGVKQ VSEVLDLILG GE
//
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