SBCD_STAA3
ID SBCD_STAA3 Reviewed; 373 AA.
AC Q2FH89;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Nuclease SbcCD subunit D;
GN Name=sbcD; OrderedLocusNames=SAUSA300_1242;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD21096.1; -; Genomic_DNA.
DR RefSeq; WP_000691284.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FH89; -.
DR SMR; Q2FH89; -.
DR EnsemblBacteria; ABD21096; ABD21096; SAUSA300_1242.
DR KEGG; saa:SAUSA300_1242; -.
DR HOGENOM; CLU_038045_0_1_9; -.
DR OMA; TSGNHDS; -.
DR Proteomes; UP000001939; 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_0000338491"
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