ID   SBCD_STAAN              Reviewed;         373 AA.
AC   Q7A5S7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=SA1180;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB42438.1; -; Genomic_DNA.
DR   PIR; B89910; B89910.
DR   RefSeq; WP_000691301.1; NC_002745.2.
DR   AlphaFoldDB; Q7A5S7; -.
DR   SMR; Q7A5S7; -.
DR   EnsemblBacteria; BAB42438; BAB42438; BAB42438.
DR   KEGG; sau:SA1180; -.
DR   HOGENOM; CLU_038045_0_1_9; -.
DR   OMA; TSGNHDS; -.
DR   Proteomes; UP000000751; 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   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_0000338487"
SQ   SEQUENCE   373 AA;  42968 MW;  6D67BC7232AD6759 CRC64;
     MKIIHTADWH LGKILNGKQL LEDQAYILDM FVEKMKEEEP DIIVIAGDLY DTTYPSKDAI
     MLLEQAIGKL NLELRIPIIM ISGNHDGKER LNYGASWFEH NQLFIRTDFT SINSPIEING
     VNFYTLPYAT VSEMKHYFED DTIETHQQGI TRCIETIAPE IDEDAVNILI SHLTVQGGKT
     SDSERPLTIG TVESVQKGVF DIFDYVMLGH LHHPFSIEDD KIKYSGSLLQ YSFSEAGQAK
     GYRRLTINDG IINDVFIPLK PLRQLEIISG EYNDVINEKV HVKNKDNYLH FKLKNMSHIT
     DPMMSLKQIY PNTLALTNET FNYNEENNAI EISEKDDMSI IEMFYKHITD KELSDIQSKK
     IKNILENELR KED