ID   SBCD_BORBU              Reviewed;         413 AA.
AC   O51769;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=BB_0829;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAC67182.1; -; Genomic_DNA.
DR   PIR; D70203; D70203.
DR   RefSeq; NP_212963.1; NC_001318.1.
DR   RefSeq; WP_010889831.1; NC_001318.1.
DR   AlphaFoldDB; O51769; -.
DR   SMR; O51769; -.
DR   STRING; 224326.BB_0829; -.
DR   EnsemblBacteria; AAC67182; AAC67182; BB_0829.
DR   KEGG; bbu:BB_0829; -.
DR   PATRIC; fig|224326.49.peg.1221; -.
DR   HOGENOM; CLU_038045_2_0_12; -.
DR   OMA; TSGNHDS; -.
DR   Proteomes; UP000001807; 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   Pfam; PF00149; Metallophos; 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..413
FT                   /note="Nuclease SbcCD subunit D"
FT                   /id="PRO_0000182194"
SQ   SEQUENCE   413 AA;  48240 MW;  9860378F60214B1A CRC64;
     MSNYKILHTS DWHIGKKIEN FSILKEQKNF LYFLLEFIKK ENIDLLLVAG DVYDSKRPGF
     EEQRLVNNFF YELSFTSCKW CVVISGNHDK KDYLSINKKL LSRFNFFLIT EYDSDEQIVL
     LKDNGNLKFI VVCLPHINER LILGQNFDNI FGLEDQYSSK LFLENLENAY REKISNLSNF
     LENKYKGIPK ILMAHSFFGS SKKIDTLGGS YIIPFNVFGN GFSYVALGHI HKFMKLRDNI
     VYSGSPMQYS FNETCDKYIN VLHFNDNKLI LQEAFPVPIF NKLIFAKGSL NEVLDFLANS
     KKEESFTIYL KIELNEAVDT SAEESIYDLA RLNFMNLVSI SYSLPSSQDL QDDSNFIGEL
     EVLEMDEKYF FEKKLRWDFE NGVIRDIKFK EEELISLFNE VLANGYLGEY EDK