ID D3LVC8_9FIRM Unreviewed; 382 AA.
AC D3LVC8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069,
GN ECO:0000313|EMBL:EFD93855.1};
GN ORFNames=HMPREF0889_0250 {ECO:0000313|EMBL:EFD93855.1};
OS Megasphaera genomosp. type_1 str. 28L.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=699218 {ECO:0000313|EMBL:EFD93855.1, ECO:0000313|Proteomes:UP000003242};
RN [1] {ECO:0000313|Proteomes:UP000003242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28L {ECO:0000313|Proteomes:UP000003242};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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:EFD93855.1}.
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DR EMBL; ADGP01000020; EFD93855.1; -; Genomic_DNA.
DR RefSeq; WP_007391259.1; NZ_ADGP01000020.1.
DR AlphaFoldDB; D3LVC8; -.
DR STRING; 699218.HMPREF0889_0250; -.
DR eggNOG; COG0420; Bacteria.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000003242; 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|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..99
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 266..348
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 382 AA; 42991 MW; 67618C1542239DBC CRC64;
MRILHTADWH LGKMFYGEYL TEEQAHVLTQ QLLPLIKEER IEALIIAGDI YDRSLPPVGA
VALFDEILTK IAVEAHVPCF IISGNHDSAT RLSFGNALME KEGIFIGGEL ATLHSPIVLE
DRYGAVSFYL LPFAEPAVVR QYYSEETVKD HETALRCLRS AQKIVQDTRS VCVAHAFVTG
GVPCDSERPL AIGGSECVDV SCFDGFSYTA LGHLHGPQKA GGRDNVRYAG SLLKYSFGEA
KQKKGVSIVE IDAKGHVAWE QIPLVPQHDV RIIQGRFADI MTRPEANKED FLLVRLEDEE
PILDGLAKLR KKYPHVLALE TPNRMIQGAP ERKFDVRHTN ERELFLNFTM AMRDGRTLSE
HEKEWTETLW RRLWQEGGDG LL
//
