(data stored in SCRATCH zone)

SWISSPROT: A4F6W0_SACEN

ID   A4F6W0_SACEN            Unreviewed;       460 AA.
AC   A4F6W0;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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   ECO:0000313|EMBL:CAL99784.1};
GN   OrderedLocusNames=SACE_0436 {ECO:0000313|EMBL:CAL99784.1};
GN   ORFNames=A8924_0833 {ECO:0000313|EMBL:PFG93586.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99784.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99784.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99784.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93586.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93586.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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; AM420293; CAL99784.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93586.1; -; Genomic_DNA.
DR   RefSeq; WP_009947451.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0436; -.
DR   MEROPS; S16.A04; -.
DR   EnsemblBacteria; CAL99784; CAL99784; SACE_0436.
DR   KEGG; sen:SACE_0436; -.
DR   eggNOG; ENOG4105DNJ; Bacteria.
DR   eggNOG; COG1066; LUCA.
DR   HOGENOM; HOG000218329; -.
DR   KO; K04485; -.
DR   OMA; SQVREIT; -.
DR   OrthoDB; 505485at2; -.
DR   BioCyc; SERY405948:SACE_RS02145-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F6W0.
DR   SWISS-2DPAGE; A4F6W0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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:UP000006728};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01498};
KW   Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN       70    221       RECA_2. {ECO:0000259|PROSITE:PS50162}.
FT   NP_BIND      99    106       ATP. {ECO:0000256|HAMAP-Rule:MF_01498}.
FT   REGION      357    460       Lon-protease-like. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
FT   MOTIF       258    262       RadA KNRFG motif. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
SQ   SEQUENCE   460 AA;  47640 MW;  7847EC9CB4D1B3E8 CRC64;
     MPAKNARTAR PGFRCADCGH EVAKWVGRCP SCQAWGTIDE AAAARPALAK VAAGAPATPA
     RPIAEVDLDS ARAVSTGIGE LDRVLGGGIV PGAVVLMAGE PGVGKSTLLL EVAHRWAATG
     GGGPSLYVTG EESAGQVRLR AERTDSVHPQ LYLGAESDLG SVLGHVDSVK PGLLIVDSVQ
     TVQSPEAEGS PGGVTQVRAV TSALVALAKE RGLPVLLVGH VTKDGAVAGP RVLEHLVDVV
     LHFEGDRHSS LRMLRGVKNR FGPSDEVGCF EQRDDGIAEV ADPSGLFVNR QETQVEGTAV
     TVMVEGKRPL LAEVQALVTP TQMTMPRRAV SGLDSARVSM MLAVLDKHGG VKTGDQEVFA
     ATVGGMKVSE PAADLAVALA VASSRRGVPL PSNVIAVGEV GLAGEIRRVN AVGRRLAEAA
     RLGFDHALVP PDSGPLPRGV RTTVVPDIRA ALRVLKRART
//

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