ID D6RWH6_BORVA Unreviewed; 413 AA.
AC D6RWH6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN ORFNames=BVAVS116_0850 {ECO:0000313|EMBL:EEF81552.1};
OS Borreliella valaisiana VS116.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=445987 {ECO:0000313|EMBL:EEF81552.1, ECO:0000313|Proteomes:UP000006163};
RN [1] {ECO:0000313|EMBL:EEF81552.1, ECO:0000313|Proteomes:UP000006163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS116 {ECO:0000313|EMBL:EEF81552.1,
RC ECO:0000313|Proteomes:UP000006163};
RA Fraser-Liggett C.M., Mongodin E.F., Casjens B., Dunn J., Luft B., Qiu W.,
RA Schutzer S., Sebastian Y.;
RL Submitted (JAN-2009) 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:EEF81552.1}.
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DR EMBL; ABCY02000001; EEF81552.1; -; Genomic_DNA.
DR RefSeq; WP_006068365.1; NZ_ABCY02000001.1.
DR AlphaFoldDB; D6RWH6; -.
DR GeneID; 63641607; -.
DR eggNOG; COG0420; Bacteria.
DR HOGENOM; CLU_038045_2_0_12; -.
DR OrthoDB; 9773856at2; -.
DR Proteomes; UP000006163; 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 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 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 5..232
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 413 AA; 48373 MW; BC5E88BE87272854 CRC64;
MNNYKILHTS DWHIGKKIEN FSILKEQKNF LSFLLEFLKK EKIDLLLVAG DVYDSKRPGF
EEQRLVNNFF YELSFTSCKW CVVISGNHDK KDYLSINKKL LSRFNFFLIT EYDSDEQIVF
LKDNGDLKFI VVCLPHINER LVLGQNFDNV FELEDQSSSK LFLENLENAY RKKISSLYNL
LENKYKGIPK ILMAHSFFGS SKKIDTLGGS YIVPFNVFGN GFSYVALGHV HKFMKLRENI
VYSGSPMQYS FNETHDKYVN VLHFNDNKLI LQEAFSVPVF NKLIFVKGSL NEVLDFLTNV
KKEESFTIYL KIELNEAIDT SAEETIYNLA RLNFMNLVSI SYSLLSSQHF QEDSSFIGEL
EVLEMDEKYF FEKKLRRDFE NGVIKDIKFK EEELISLFNE VLKKGYLGEY EDK
//
