ID W1N8A1_9GAMM Unreviewed; 435 AA.
AC W1N8A1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN ORFNames=BJB45_13385 {ECO:0000313|EMBL:ERL51406.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL51406.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL51406.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL51406.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL Submitted (AUG-2013) 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:ERL51406.1}.
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DR EMBL; AVBC01000025; ERL51406.1; -; Genomic_DNA.
DR RefSeq; WP_021818792.1; NZ_CP013106.1.
DR AlphaFoldDB; W1N8A1; -.
DR STRING; 1178482.AR456_13765; -.
DR KEGG; hhu:AR456_13765; -.
DR PATRIC; fig|1178482.3.peg.1836; -.
DR eggNOG; COG0420; Bacteria.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000019113; 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; 3.30.160.720; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019113}.
FT DOMAIN 2..246
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 297..398
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 435 AA; 48777 MW; 8A576496DB34236A CRC64;
MLRLIHTADW HLGQSFHGQE RTTEHRAFLR WLLDTLEQQQ ADVLLVAGDI FDVVNPSLRA
QQLLYDFIVE THQRCPDLHM VLIAGNHDSG ARIELPAPLM QRLHAHALGR VSWLDDGSLD
SQRLLVPLSD ANGDTQAWCM ALPFLRPAEI TGRGGQQSAI PSEDDRPDNS FNYVSSVEHV
HQQLINAARE QRQPGQALIA MSHAHLHGAA VSEASERPIV IGGEESISAS VFPADISYVA
LGHLHRAQRV GEERIRYSGS PLPLDFSEVG YPNQVLILEL DGERLGEVQS LPVPRAVTMQ
RIGPCDLNEA LEQIAQLPSR EQSRDTEYWA WLEITIRLDA PMADLRSRID EGLADRAARL
LRLRRELPGG DQQQQPRSGE RLEDIGPRQL FERVWQEQWG APAEQDVLSD FDRLCQDVLD
ADEDGLEQDR KGADA
//
