ID A5WDN8_PSYWF Unreviewed; 482 AA. AC A5WDN8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-NOV-2024, entry version 107. DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|NCBIfam:TIGR00416}; GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498}; GN OrderedLocusNames=PsycPRwf_0827 {ECO:0000313|EMBL:ABQ93779.1}; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93779.1}; RN [1] {ECO:0000313|EMBL:ABQ93779.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93779.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000713; ABQ93779.1; -; Genomic_DNA. DR AlphaFoldDB; A5WDN8; -. DR STRING; 349106.PsycPRwf_0827; -. DR KEGG; prw:PsycPRwf_0827; -. DR eggNOG; COG1066; Bacteria. DR HOGENOM; CLU_018264_0_1_6; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule. DR CDD; cd01121; RadA_SMS_N; 1. DR FunFam; 3.40.50.300:FF:000050; DNA repair protein RadA; 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|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_01498}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_01498}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01498}; Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01498}; Methyltransferase {ECO:0000313|EMBL:ABQ93779.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498, KW ECO:0000256|RuleBase:RU003555}; KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP- KW Rule:MF_01498}; Transferase {ECO:0000313|EMBL:ABQ93779.1}; KW Zinc {ECO:0000256|RuleBase:RU003555}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}. FT DOMAIN 89..241 FT /note="RecA family profile 1" FT /evidence="ECO:0000259|PROSITE:PS50162" FT REGION 376..482 FT /note="Lon-protease-like" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498" FT MOTIF 278..282 FT /note="RadA KNRFG motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498" FT BINDING 118..125 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498" SQ SEQUENCE 482 AA; 51001 MW; 89D978B655E06657 CRC64; MAKSKSSYVC QNCGAYFGKW AGQCSDCGEW NTLVEAPNVS LPHHNKSAAK GAMAAHTGPK MLAGAKSDRM NYSGSQSGVV TLGSVNVTFD TRLPTGISEF DRVLGGGLVA GSVVLIGGDP GIGKSTILLQ TAANMADPES LSGSALYVTG EESLSQVAMR AQRLGLSSDH LKVMTETNVE TICAALTQEQ PAVAIIDSIQ TIYTDAINSA PGGVSQIRES AAMLTRYAKQ TGTALFLVGH VTKEGTLAGP RVLEHMVDTV LYFEGQSDSR FRMIRAVKNR FGAVNELGIF GMTDTGLKEV ANPSAIFLSR YDKPISGSIV MVSREGTRPL LVEVQALVDD SAGQPRRMAL GLDPQRLAML LAVMHRHGGI HTSGQDVYVN VVGGVKVMET GSDLAVLLAC ASSIKERPLP SSLAVFGEVG LSGEIRPVPN GQERLKEAMK HGFTHAIVPK ANAPKNLMGQ FKGITVITAD RLDDAIDRAF EI //