ID A0A220UBD2_9MICO Unreviewed; 387 AA.
AC A0A220UBD2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN ORFNames=CFK39_06135 {ECO:0000313|EMBL:ASK65479.1};
OS Brachybacterium avium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=2017485 {ECO:0000313|EMBL:ASK65479.1, ECO:0000313|Proteomes:UP000198398};
RN [1] {ECO:0000313|Proteomes:UP000198398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VR2415 {ECO:0000313|Proteomes:UP000198398};
RA Tak E.J., Bae J.-W.;
RT "Brachybacterium sp. VR2415.";
RL Submitted (JUL-2017) 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; CP022316; ASK65479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220UBD2; -.
DR KEGG; brv:CFK39_06135; -.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000198398; 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|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..97
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 275..360
FT /note="Nuclease SbcCD subunit D C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12320"
SQ SEQUENCE 387 AA; 41751 MW; BFE5BDB18483FFEE CRC64;
MKILHTSDWH LGRTLHKVDL HAHQAAFLDW LVALVETERV DVVVIPGDVY DRAVPAVSSV
TLLDSALARL ADTGATVVLT SGNHDSPERL GFGRSLMRAG IHLLTDVPGI EHPVSVADEH
GEVLFFGLPY LEPDRARTEL VAEGEPPLAR SHEAVTRAAL ERVHERAAAH PGARTVVLAH
TFVTGGDASD SERDLSVGGV DSVPAGVLGG LDYLALGHLH GCQDLTRLVG APAWYSGSPL
AFSFSEKNHR KSVLLVELGA PGTAAEVRRI HTPVPRPLTE LRGSLEEILA RAPEHGGDWI
KAVVTDPARP AHLQEQLREA FPQLLLTEYA PEGREARAGT PVVRREQNPL DVMDDFLAHV
TGAAPTAAEH EVLDRAYTAV RRQQEAS
//
