ID   SBCD_STAAS              Reviewed;         373 AA.
AC   Q6G9L3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=SAS1285;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG43063.1; -; Genomic_DNA.
DR   RefSeq; WP_000691284.1; NC_002953.3.
DR   AlphaFoldDB; Q6G9L3; -.
DR   SMR; Q6G9L3; -.
DR   KEGG; sas:SAS1285; -.
DR   HOGENOM; CLU_038045_0_1_9; -.
DR   OMA; TSGNHDS; -.
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   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   DNA recombination; DNA replication; Endonuclease; Exonuclease; Hydrolase;
KW   Nuclease.
FT   CHAIN           1..373
FT                   /note="Nuclease SbcCD subunit D"
FT                   /id="PRO_0000338483"
SQ   SEQUENCE   373 AA;  42936 MW;  2473F7EBD76CC5BE CRC64;
     MKIIHTADWH LGKILNGKQL LEDQAYILDM FVEKMKEEEP DIIVIAGDLY DTTYPSKDAI
     MLLEQAIGKL NLELRIPIII ISGNHDGKER LNYGASWFEH NQLFIRTDFT SINSPIEING
     VNFYTLPYAT VSEMKHYFED DTIETHQQGI TRCIETIAPE IDEDAVNILI SHLTVQGGKT
     SDSERPLTIG TVESVQKGVF DIFDYVMLGH LHHPFSIEDD KIKYSGSLLQ YSFSEAGQAK
     GYRRVTINDG IINDVFIPLK PLRQLEIISG EYNDVINEKV HVKNKDNYLH FKLKNMSHIT
     DPMMSLKQIY PNTLALTNET FNYNEENNAI EISEKDDMSI IEMFYKHITD KELSDIQSKK
     IKNILENELR KED