ID A0A2C1KYM2_9BACI Unreviewed; 393 AA.
AC A0A2C1KYM2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN ORFNames=COD11_00680 {ECO:0000313|EMBL:PGT91386.1};
OS Bacillus sp. AFS040349.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT91386.1, ECO:0000313|Proteomes:UP000222674};
RN [1] {ECO:0000313|EMBL:PGT91386.1, ECO:0000313|Proteomes:UP000222674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS040349 {ECO:0000313|EMBL:PGT91386.1,
RC ECO:0000313|Proteomes:UP000222674};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU363069}.
CC -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000256|ARBA:ARBA00011322,
CC ECO:0000256|RuleBase:RU363069}.
CC -!- SIMILARITY: Belongs to the SbcD family. {ECO:0000256|ARBA:ARBA00010555,
CC ECO:0000256|RuleBase:RU363069}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGT91386.1}.
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DR EMBL; NUMC01000006; PGT91386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1KYM2; -.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000222674; Unassembled WGS sequence.
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 NCBIfam; TIGR00619; sbcd; 1.
DR PANTHER; PTHR30337; COMPONENT OF ATP-DEPENDENT DSDNA EXONUCLEASE; 1.
DR PANTHER; PTHR30337:SF0; NUCLEASE SBCCD SUBUNIT D; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF12320; SbcD_C; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU363069};
KW DNA replication {ECO:0000256|RuleBase:RU363069};
KW Endonuclease {ECO:0000256|RuleBase:RU363069};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|RuleBase:RU363069};
KW Hydrolase {ECO:0000256|RuleBase:RU363069};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU363069};
KW Reference proteome {ECO:0000313|Proteomes:UP000222674}.
FT DOMAIN 1..224
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 276..364
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 393 AA; 43854 MW; 9FF6A39FE1271E68 CRC64;
MRILHTADWH LGRALEGRSR LAEQADFIDE LVRIVEEEKV DAILMAGDAF DTVNPPAAAE
QLFYEGLSRL SDHGKRPIVV IAGNHDNPDR LSAASPLAGN HSIHLIGYPT TELITLDIPS
AGEQMMVAAL AYPSEARLEQ VLSQEHDEVL LRNKYDERIR DLFSIMSKQF QKNTVNIAMS
HIHVAGGSST DSERPIEVGG AYTVAATSMP EAAQYVALGH LHRPQNIKRA STLTRYSGSP
LAYSFSEIGY AKSVTILDAE PNQPVVMKEI PLSSGKPLVK WKATEGISQV HSWLDEGKDH
HAWIDLEIHL TSTLSIEEIH RLRKWHPGFI HIRPVFQAEL EVAATRQSNL PIDQLFSQFY
EKQTGGAKPE EELVRLFLEL VQQDEEQEEG DEA
//
