ID   A5WDN8_PSYWF            Unreviewed;       482 AA.
AC   A5WDN8;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   06-JUL-2016, entry version 65.
DE   RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498};
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: Has a putative N-terminal zinc-finger, a middle region
CC       with homology to RecA with ATPase motifs including the RadA KNRFG
CC       motif, while the C-terminus is homologous to Lon protease.
CC       {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; 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; FEGERGH; -.
DR   OrthoDB; EOG6DRPHC; -.
DR   BioCyc; PPRW349106:GHZF-846-MONOMER; -.
DR   Proteomes; UP000001993; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000001993};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01498};
KW   Transferase {ECO:0000313|EMBL:ABQ93779.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN       89    241       RECA_2. {ECO:0000259|PROSITE:PS50162}.
FT   ZN_FING      10     27       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_01498}.
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
//