ID A5WDN8_PSYWF Unreviewed; 482 AA. AC A5WDN8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 16-JAN-2019, entry version 81. 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=PsycPRwf_0827 {ECO:0000313|EMBL:ABQ93779.1}; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93779.1, ECO:0000313|Proteomes:UP000001993}; RN [1] {ECO:0000313|EMBL:ABQ93779.1, ECO:0000313|Proteomes:UP000001993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93779.1, RC ECO:0000313|Proteomes:UP000001993}; 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., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., RA 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 CC recombination intermediates, plays a role in repairing DNA breaks. CC Stimulates the branch migration of RecA-mediated strand transfer CC reactions, allowing the 3' invading strand to extend heteroduplex CC DNA faster. Binds ssDNA in the presence of ADP but not other CC nucleotides, has ATPase activity that is stimulated by ssDNA and CC various branched DNA structures, but inhibited by SSB. Does not CC have RecA's homology-searching function. CC {ECO:0000256|RuleBase:RU003555}. CC -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, CC probably involving stabilizing or processing branched DNA or CC blocked replication 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 CC to 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 RefSeq; WP_011960100.1; NC_009524.1. DR ProteinModelPortal; A5WDN8; -. DR STRING; 349106.PsycPRwf_0827; -. DR EnsemblBacteria; ABQ93779; ABQ93779; PsycPRwf_0827. DR KEGG; prw:PsycPRwf_0827; -. DR eggNOG; ENOG4105DNJ; Bacteria. DR eggNOG; COG1066; LUCA. DR HOGENOM; HOG000218329; -. DR KO; K04485; -. DR OMA; SQVREIT; -. DR OrthoDB; 505485at2; -. DR Proteomes; UP000001993; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; 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:0000725; P:recombinational repair; IEA:UniProtKB-UniRule. DR CDD; cd01121; Sms; 1. DR Gene3D; 3.30.230.10; -; 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_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00416; sms; 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 Complete proteome {ECO:0000313|Proteomes:UP000001993}; 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}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01498, KW ECO:0000256|RuleBase:RU003555}; KW 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|HAMAP-Rule:MF_01498}; KW Transferase {ECO:0000313|EMBL:ABQ93779.1}; KW Zinc {ECO:0000256|RuleBase:RU003555}; KW Zinc-finger {ECO:0000256|RuleBase:RU003555}. FT DOMAIN 89 241 RECA_2. {ECO:0000259|PROSITE:PS50162}. FT NP_BIND 118 125 ATP. {ECO:0000256|HAMAP-Rule:MF_01498}. FT REGION 376 482 Lon-protease-like. {ECO:0000256|HAMAP- FT Rule:MF_01498}. FT MOTIF 278 282 RadA KNRFG motif. {ECO:0000256|HAMAP- FT 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 //