ID I0R8B6_9FIRM Unreviewed; 378 AA.
AC I0R8B6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN ORFNames=HMPREF9970_2660 {ECO:0000313|EMBL:EIC95924.1};
OS Lachnoanaerobaculum saburreum F0468.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=1095750 {ECO:0000313|EMBL:EIC95924.1, ECO:0000313|Proteomes:UP000005039};
RN [1] {ECO:0000313|EMBL:EIC95924.1, ECO:0000313|Proteomes:UP000005039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0468 {ECO:0000313|EMBL:EIC95924.1,
RC ECO:0000313|Proteomes:UP000005039};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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:EIC95924.1}.
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DR EMBL; AJGH01000060; EIC95924.1; -; Genomic_DNA.
DR RefSeq; WP_008753809.1; NZ_AJGH01000060.1.
DR AlphaFoldDB; I0R8B6; -.
DR PATRIC; fig|1095750.3.peg.1216; -.
DR eggNOG; COG0420; Bacteria.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000005039; 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:0005975; P:carbohydrate metabolic process; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW DNA recombination {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}.
FT DOMAIN 1..213
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 262..355
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 378 AA; 43791 MW; 223381474CB4A954 CRC64;
MKIMHLSDLH LGKRVNEFSM LEDQIYILNE IINIIDEQKP KVIILAGDIY DKPIPPAEAV
EIFDDFLYKL SKRNLYVFII SGNHDSAERI AFGSRLFDKS GIYLSPVYNG KISPICIDDK
YGKVNFYMLP FIKPVHVRRF FPDAEIYTYT DALSTVISDM HIDTAQKNIL ITHQFVTGSS
RTESEDVSVG GSDNVDSDIF KDFDYVALGH IHRSQCCDSE YIRYCGTPLK YSFSESKDIK
SITMLDIKEK GNIKLDFIPL TPLRDMVEIK GSYNELMLKS FYENTSLTDD YVHITLTDEE
DIPDVITKLR VVYKNIMKLD YDNQRTKKSS EINPINDMDS KSPLELFDTF YELQNGKHLS
DTQRVFLKNI IEEIWEYK
//