ID   SBCD_RHOCB              Reviewed;         405 AA.
AC   O68033; D5AV81;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=RCAP_rcc02133;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA   Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT   "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT   SB1003.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
CC   -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can
CC       inhibit DNA replication and are intermediates in certain DNA
CC       recombination reactions. The complex acts as a 3'->5' double strand
CC       exonuclease that can open hairpins. It also has a 5' single-strand
CC       endonuclease activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SbcD family. {ECO:0000305}.
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DR   EMBL; AF010496; AAC16119.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE85863.1; -; Genomic_DNA.
DR   PIR; T03466; T03466.
DR   RefSeq; WP_013067842.1; NC_014034.1.
DR   AlphaFoldDB; O68033; -.
DR   SMR; O68033; -.
DR   STRING; 272942.RCAP_rcc02133; -.
DR   EnsemblBacteria; ADE85863; ADE85863; RCAP_rcc02133.
DR   GeneID; 31490984; -.
DR   KEGG; rcp:RCAP_rcc02133; -.
DR   eggNOG; COG0420; Bacteria.
DR   HOGENOM; CLU_038045_2_1_5; -.
DR   OMA; TSGNHDS; -.
DR   OrthoDB; 1831911at2; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041796; Mre11_N.
DR   InterPro; IPR004593; SbcD.
DR   InterPro; IPR026843; SbcD_C.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF12320; SbcD_C; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   TIGRFAMs; TIGR00619; sbcd; 1.
PE   3: Inferred from homology;
KW   Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..405
FT                   /note="Nuclease SbcCD subunit D"
FT                   /id="PRO_0000182197"
SQ   SEQUENCE   405 AA;  42908 MW;  3CAFE4DAF6A676EE CRC64;
     MRILHTADWH IGQTLNGWSR EAEHRAFLAD LGEILLAEQV DALLVAGDVF DGLNPSGEAQ
     RLLYAALAGY VRANPRLQIV LTSGNHDPAQ RLEAPEAVLR ELGVHVLGTL SRGPGGMDLD
     RHLIPLRDRA GQIRAQVLAL PFLRQADLPG LRLGAEEGTE GAVTAALRAL LAETVARAAA
     IAGTLPLIAM AHLTCAGGLE SAGAERRILI GGDHAVPPDV FPPALAHVAL GHLHRPQSLD
     GGRVRYSGAP FPLSASEIGY DHGVTLLDLA GGAAPRHIPL PRPVPMLRLP AQGTAPLPEI
     LAALDRLALP DRPRAEGPFL YLALRADRPV TEITAALDAA LEALPLRLAG LTITRPETAR
     PAAAPPQDLT RTTPEALFAA AFRDLHGTEP ETRHLSAFRD ALSEV