ID   SBCD_STAHJ              Reviewed;         374 AA.
AC   Q4L654;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=SH1562;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006716; BAE04871.1; -; Genomic_DNA.
DR   RefSeq; WP_011275853.1; NC_007168.1.
DR   AlphaFoldDB; Q4L654; -.
DR   SMR; Q4L654; -.
DR   STRING; 279808.SH1562; -.
DR   EnsemblBacteria; BAE04871; BAE04871; SH1562.
DR   GeneID; 58062241; -.
DR   KEGG; sha:SH1562; -.
DR   eggNOG; COG0420; Bacteria.
DR   HOGENOM; CLU_038045_0_1_9; -.
DR   OMA; TSGNHDS; -.
DR   OrthoDB; 1831911at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   TIGRFAMs; TIGR00619; sbcd; 1.
PE   3: Inferred from homology;
KW   DNA recombination; DNA replication; Endonuclease; Exonuclease; Hydrolase;
KW   Nuclease.
FT   CHAIN           1..374
FT                   /note="Nuclease SbcCD subunit D"
FT                   /id="PRO_0000338494"
SQ   SEQUENCE   374 AA;  43199 MW;  1E69983DC5086603 CRC64;
     MKVIHTADWH LGKILNGKQF LEDQHYILNK LIDNLKEEKP DVLVISGDIY DTSYPSKETI
     RLFEETIKII NVNMKIPTII TNGNHDGRER LNYGSTWFEF SQLYIRTQLE LMSTPITINN
     INFYTLPFAT ISEIKAYFDD DDIKTYEQAT QKCINHISKI IDPNQINILI GHLTIKGGKT
     SESERPLTIG TVESVESANF NIFDKVLLGH LHHPFSITDN IVDYSGSLLQ YSFSEVNQAK
     GYKKLMINSK GDINTKFVQL KPLRELEEIE GDYSAVIQGD VPVKNKDNYF HFKLKNMSHV
     TDPIIHLKQI YPNTLSLSNI TFENHNKSTY ADFKTTDDPT IIKNFYKTIT DEDLTNYQEK
     KIHQLLNQVI NRED