ID   SBCD_STAEQ              Reviewed;         374 AA.
AC   Q5HPJ4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=SERP0917;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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}.
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DR   EMBL; CP000029; AAW54292.1; -; Genomic_DNA.
DR   RefSeq; WP_001830960.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPJ4; -.
DR   SMR; Q5HPJ4; -.
DR   STRING; 176279.SERP0917; -.
DR   EnsemblBacteria; AAW54292; AAW54292; SERP0917.
DR   GeneID; 50018845; -.
DR   KEGG; ser:SERP0917; -.
DR   eggNOG; COG0420; Bacteria.
DR   HOGENOM; CLU_038045_0_1_9; -.
DR   OMA; TSGNHDS; -.
DR   OrthoDB; 1831911at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome.
FT   CHAIN           1..374
FT                   /note="Nuclease SbcCD subunit D"
FT                   /id="PRO_0000338493"
SQ   SEQUENCE   374 AA;  43553 MW;  7AC26496A4E063C9 CRC64;
     MKIVHTADWH LGKILNGKQL LEDQKYILTQ FKQHMEKEQP DLIVIAGDLY DTSYPSKEAI
     GLLEETIEYL NIELKIPIIM ISGNHDGRER LNYGSKWFEN NQLYIRTQLE NIDDPIELSG
     VQFFTLPFAT VSEVQNYFKD KQIETYQQAL NECLEQMSSS IDNNKVNILI GHLTIEGGKT
     SDSERPLTIG TVESVDMHSF RLFDYVMLGH LHHPFSINNS FIKYSGSILQ YSFSEVNQSK
     GYRVLDIENN QLLNETFVPL KPLRELEVIE GDYEDIIQER IKVKNKNNYF HFKLTNVSHI
     TDPMMKLKQI YPNILALSNV VFDHSENFSH VEIKKQDDQT IIENFYKNMT DQHLSQVQSD
     KIKHLLSFIL DREG