ID A0Y2U0_9GAMM Unreviewed; 415 AA.
AC A0Y2U0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN ORFNames=ATW7_00945 {ECO:0000313|EMBL:EAW27441.1};
OS Alteromonadales bacterium TW-7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=156578 {ECO:0000313|EMBL:EAW27441.1, ECO:0000313|Proteomes:UP000004833};
RN [1] {ECO:0000313|EMBL:EAW27441.1, ECO:0000313|Proteomes:UP000004833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-7 {ECO:0000313|EMBL:EAW27441.1,
RC ECO:0000313|Proteomes:UP000004833};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (DEC-2006) 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:EAW27441.1}.
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DR EMBL; AAVS01000015; EAW27441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Y2U0; -.
DR eggNOG; COG0420; Bacteria.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000004833; 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..227
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 295..385
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 415 AA; 46263 MW; 3EC6C7F46F360D14 CRC64;
MKVLHTSDWH LGQQFYEHDR RVEHQAFFTW LLATLVKQQI DLLLVAGDIY HTATPSASAE
NQLYQFIKDA KKHCPHMHVV IIAGNHDSAN RILAAQPLLA QFDTHVVGRF DVSAPGDIII
EINTNNKRAV IAAMPFLRSS DVSSLSQTKN GPSYAQGVAN AYELALEHAY KINEQKSPLI
VMGHLHAKGG DISSDSERNL VIGGEESISA NVFGNKANYV ALGHLHKAQQ VAKNEAIRYS
GTPIPMSFSE RNYTHQVNVI EFKSDKKQSI STTVNPLYIP RSADVIILPK GECVPLNDLC
EQIKALDTSQ HAIAPYLRVK LKSSDTDTTF REQIEQALEG KHVKFCGIER VREQTAQTDN
DTVFEHLSEV EMLNPLNLLE QAFANDKDMA GQNVPDELKV LLNDVISELT EQEQL
//
