(data stored in SCRATCH zone)

SWISSPROT: E3J8M0_FRAIE

ID   E3J8M0_FRAIE            Unreviewed;       507 AA.
AC   E3J8M0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
DE   Flags: Precursor;
GN   Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN   OrderedLocusNames=FraEuI1c_0377 {ECO:0000313|EMBL:ADP78463.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78463.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78463.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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}.
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DR   EMBL; CP002299; ADP78463.1; -; Genomic_DNA.
DR   STRING; 298654.FraEuI1c_0377; -.
DR   MEROPS; S16.A04; -.
DR   EnsemblBacteria; ADP78463; ADP78463; FraEuI1c_0377.
DR   KEGG; fri:FraEuI1c_0377; -.
DR   eggNOG; ENOG4105DNJ; Bacteria.
DR   eggNOG; COG1066; LUCA.
DR   HOGENOM; HOG000218329; -.
DR   KO; K04485; -.
DR   OMA; SQVREIT; -.
DR   BioCyc; FSP298654:G1GOT-378-MONOMER; -.
DR   Proteomes; UP000002484; 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:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
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   InterPro; IPR041166; Rubredoxin_2.
DR   Pfam; PF18073; Rubredoxin_2; 1.
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;
DR   PRODOM; E3J8M0.
DR   SWISS-2DPAGE; E3J8M0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01498};
KW   Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN      108    257       RECA_2. {ECO:0000259|PROSITE:PS50162}.
FT   NP_BIND     137    144       ATP. {ECO:0000256|HAMAP-Rule:MF_01498}.
FT   REGION      406    507       Lon-protease-like. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
FT   MOTIF       294    298       RadA KNRFG motif. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
SQ   SEQUENCE   507 AA;  51254 MW;  9DB30CACF3C09ACF CRC64;
     MSDPTATVSG MAVVGSSGNA SASGSGSASR RAAGGASGRS RADGGFRCSE CGAESIRWAG
     RCPRCQAWST LEAQKAPPRR AAVAGSGATA PATVTTPAKP VTEVDPSPAA RRSTGVDELD
     RVLGGGVVPG AVILLAGEPG VGKSTLLLEV AARSAQAGHR ALVVTGEESV AQVRLRAGRT
     GTLHADLWLA AETDLGALLG HVEEVQPTLL VVDSVQTISA AGVDGVAGGV TQVREVAAAL
     IRAAKALGLA TILVGHVTKD GSVAGPRLLE HLVDVVLHFE GDQQTALRMI RSVKNRYGPT
     DEVGCFEMNE NGIWGIADPS GLFLSRGATA SAVPGVCVTV MVEGRRPLVA EVQALVAPQS
     YGRGGAGAPA PPPPRRAVSG LDGSRVAMIT AVLQKRSGFG MLGGADIFTA SVGGVKLHEP
     AADLAVALAM VSSAQDRGVP SDLIALGEVG LTGEIRSVSG IERRLAAAAR LGFRRALVPR
     LSGLVPEGMT VTEATDLNAA IANMYDG
//

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