ID Q5L262_GEOKA Unreviewed; 392 AA.
AC Q5L262;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN OrderedLocusNames=GK0683 {ECO:0000313|EMBL:BAD74968.1};
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD74968.1, ECO:0000313|Proteomes:UP000001172};
RN [1] {ECO:0000313|EMBL:BAD74968.1, ECO:0000313|Proteomes:UP000001172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD74968.1,
RC ECO:0000313|Proteomes:UP000001172};
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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}.
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DR EMBL; BA000043; BAD74968.1; -; Genomic_DNA.
DR RefSeq; WP_011230186.1; NC_006510.1.
DR AlphaFoldDB; Q5L262; -.
DR STRING; 235909.GK0683; -.
DR KEGG; gka:GK0683; -.
DR eggNOG; COG0420; Bacteria.
DR HOGENOM; CLU_038045_3_0_9; -.
DR Proteomes; UP000001172; 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 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:UP000001172}.
FT DOMAIN 1..90
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 276..365
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 392 AA; 43671 MW; EA919C2984E56814 CRC64;
MRILHTADWH FGRTLEGRSR MAEQEAFVDE LVEIVKKEQI DIILVAGDVF DSVNPPAAAE
QLFYESLARL SDKGRRPVAV ISGNHDHPDR ISAARTLMCA HNIFLFGRPQ AAVCRIDVPS
CGETMMLAPL AYPSESRLAE LLSSDCKETT MRDRYDDRIR ALLAAMAASF TAETVNIAMS
HLYVAGGRTS DSERPIEVGG AYTVAAESLP KAAQYVALGH LHRPQDVKQA KTAARYSGSP
LAYSFSEAGQ AKSVTVVDVH PGGAAKVAEI PLVAGKPLIR WKATEGLAQV YRWCEEGRDR
SSWIDLEIHV TESLTMEEID RLRKLHPGFV HIRPVLPNRV EEMMEMSREP LSLEEMFHRF
YERQTGGQTP DEELVRLFLE LAAEEEKEGE GE
//
