ID A0A143HC01_9BACL Unreviewed; 389 AA.
AC A0A143HC01;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN ORFNames=ATY39_05395 {ECO:0000313|EMBL:AMW98939.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMW98939.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMW98939.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMW98939.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014806; AMW98939.1; -; Genomic_DNA.
DR RefSeq; WP_066786903.1; NZ_CP014806.1.
DR AlphaFoldDB; A0A143HC01; -.
DR STRING; 241244.ATY39_05395; -.
DR KEGG; rst:ATY39_05395; -.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000076021; 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:UP000076021}.
FT DOMAIN 1..222
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 271..355
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 389 AA; 44602 MW; 5DF26E258B500610 CRC64;
MKIFHTADWH LGKYVQGVSM IEDQAYILQQ FIAEIDKEKP DVIIIAGDLY DRAVPPTEAV
QLLDNIFFEI VIKREIPVLA IAGNHDSPNR IHFGARFMAS RGLHLIGNLT LDQTPVILKD
DTGEVHFHLV PYTDPTQVRY LFQDPAIRTQ QQAMEKIIDS IIPNMDPKAR HIFIGHAFVT
KNGAEEQNPS DAERPLSIGG SECIDAKLFE PFHYTALGHL HQAHFVDSEK IRYSGSPLKY
SISEENHKKS YLIVEIDGAG QITTTKKPLM PKRDMRTIEN TMEQILVSPT CEDYLFIKLL
DESPIISPME KIRSVYPNAM HVERISLLDY RNKPLEENIS KRKMDDVTLF ESFYYEITGQ
EPDSDTLDLF KEVLQEELLH KQEIEVESK
//
