(data stored in SCRATCH zone)

SWISSPROT: C1D2C5_DEIDV

ID   C1D2C5_DEIDV            Unreviewed;       344 AA.
AC   C1D2C5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=Protein RecA {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526, ECO:0000256|SAAS:SAAS00013832};
DE   AltName: Full=Recombinase A {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526};
GN   Name=recA {ECO:0000256|HAMAP-Rule:MF_00268,
GN   ECO:0000313|EMBL:ACO47564.1};
GN   OrderedLocusNames=Deide_1p01260 {ECO:0000313|EMBL:ACO47564.1},
GN   Deide_3p00210 {ECO:0000313|EMBL:ACO47925.1};
OS   Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923).
OG   Plasmid 1 {ECO:0000313|EMBL:ACO47564.1},
OG   Plasmid 3 {ECO:0000313|EMBL:ACO47925.1},
OG   Plasmid pDeide1 {ECO:0000313|Proteomes:UP000002208}, and
OG   Plasmid pDeide3 {ECO:0000313|Proteomes:UP000002208}.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47564.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO47564.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1 {ECO:0000313|EMBL:ACO47564.1}, 3
RC   {ECO:0000313|EMBL:ACO47925.1}, Plasmid pDeide1, Plasmid pDeide3,
RC   VCD115 {ECO:0000313|EMBL:ACO47564.1}, and VCD115 / DSM 17065 / LMG
RC   22923 {ECO:0000313|Proteomes:UP000002208};
RC   PLASMID=1 {ECO:0000313|EMBL:ACO47564.1}, 3
RC   {ECO:0000313|EMBL:ACO47925.1}, Plasmid pDeide1
RC   {ECO:0000313|Proteomes:UP000002208}, and Plasmid pDeide3
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
RN   [2] {ECO:0000313|EMBL:ACO47564.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VCD115 {ECO:0000313|EMBL:ACO47564.1};
RC   PLASMID=1 {ECO:0000313|EMBL:ACO47564.1}, and 3
RC   {ECO:0000313|EMBL:ACO47925.1};
RX   PubMed=19875382; DOI=10.1074/mcp.M900359-MCP200;
RA   Baudet M., Ortet P., Gaillard J.C., Fernandez B., Guerin P., Enjalbal C.,
RA   Subra G., de Groot A., Barakat M., Dedieu A., Armengaud J.;
RT   "Proteomics-based refinement of Deinococcus deserti genome annotation
RT   reveals an unwonted use of non-canonical translation initiation codons.";
RL   Mol. Cell. Proteomics 9:415-426(2010).
RN   [3] {ECO:0000313|EMBL:ACO47564.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VCD115 {ECO:0000313|EMBL:ACO47564.1};
RC   PLASMID=1 {ECO:0000313|EMBL:ACO47564.1}, and 3
RC   {ECO:0000313|EMBL:ACO47925.1};
RA   De Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Jean A.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ACO47564.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VCD115; PLASMID=1, and 3;
RX   PubMed=24723731; DOI=10.1093/gbe/evu069;
RA   de Groot A., Roche D., Fernandez B., Ludanyi M., Cruveiller S., Pignol D.,
RA   Vallenet D., Armengaud J., Blanchard L.;
RT   "RNA Sequencing and Proteogenomics Reveal the Importance of Leaderless
RT   mRNAs in the Radiation-Tolerant Bacterium Deinococcus deserti.";
RL   Genome Biol. Evol. 6:932-948(2014).
CC   -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC       stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC       DNA, and the ATP-dependent hybridization of homologous single-stranded
CC       DNAs. It interacts with LexA causing its activation and leading to its
CC       autocatalytic cleavage. {ECO:0000256|HAMAP-Rule:MF_00268,
CC       ECO:0000256|SAAS:SAAS00013905}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268,
CC       ECO:0000256|SAAS:SAAS00013840}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00268, ECO:0000256|RuleBase:RU004527,
CC       ECO:0000256|SAAS:SAAS00540280}.
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DR   EMBL; CP001115; ACO47564.1; -; Genomic_DNA.
DR   EMBL; CP001117; ACO47925.1; -; Genomic_DNA.
DR   RefSeq; WP_012694687.1; NC_012528.1.
DR   EnsemblBacteria; ACO47564; ACO47564; Deide_1p01260.
DR   EnsemblBacteria; ACO47925; ACO47925; Deide_3p00210.
DR   KEGG; ddr:Deide_1p01260; -.
DR   KEGG; ddr:Deide_3p00210; -.
DR   HOGENOM; HOG000264120; -.
DR   KO; K03553; -.
DR   OMA; VMRMGDQ; -.
DR   OrthoDB; 1080436at2; -.
DR   BioCyc; DDES546414:G1GCG-2885-MONOMER; -.
DR   BioCyc; DDES546414:G1GCG-3257-MONOMER; -.
DR   Proteomes; UP000002208; Plasmid pDeide1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   CDD; cd00983; recA; 1.
DR   Gene3D; 3.30.250.10; -; 1.
DR   HAMAP; MF_00268; RecA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013765; DNA_recomb/repair_RecA.
DR   InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   PANTHER; PTHR45900:SF1; PTHR45900:SF1; 1.
DR   Pfam; PF00154; RecA; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54752; SSF54752; 1.
DR   TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR   PROSITE; PS00321; RECA_1; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1D2C5.
DR   SWISS-2DPAGE; C1D2C5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00048155};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|SAAS:SAAS00013838};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU004527,
KW   ECO:0000256|SAAS:SAAS01081725};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00289108};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526,
KW   ECO:0000256|SAAS:SAAS00013903};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00422436};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00503978};
KW   Plasmid {ECO:0000313|EMBL:ACO47564.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526, ECO:0000256|SAAS:SAAS00013834}.
FT   DOMAIN          35..194
FT                   /note="RECA_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          199..274
FT                   /note="RECA_3"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   NP_BIND         65..72
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   344 AA;  36579 MW;  E5DE7D21134C372F CRC64;
     MDTDQHKALQ TAMSQIEKQF GKGSIMKLGA DSKLDVQAIS TGSLSLDVAL GVGGIPKGRV
     TEIYGPESGG KTTLALSIIA QSQKAGGTCA FIDAEHALDP VYARALGVNT DDLLVSQPDN
     GEQALEIMEL LIRSGAIDVV VVDSVAALTP RAEIEGEMGD SLPGLQARLM SQALRKLTSI
     VSKTGTAAIF INQVREKIGV MYGNPETTTG GKALKFYASV RLDVRKMGGK STMVDNVAVS
     HSVKVKTVKN KVAPPFKEVE LTLRYGHGFD AMDDLVTLAT TFEVIKKAGS FYSYGDERIG
     QGKEKAIAFL SERPDLLADI RERVLAQMRG TPVAPLPEPA LSAD
//

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