GenomeNet

Database: UniProt
Entry: D7AXK0_NOCDD
LinkDB: D7AXK0_NOCDD
Original site: D7AXK0_NOCDD 
ID   D7AXK0_NOCDD            Unreviewed;       385 AA.
AC   D7AXK0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN   Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN   OrderedLocusNames=Ndas_0628 {ECO:0000313|EMBL:ADH66074.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS   7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS   (Actinomadura dassonvillei).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH66074.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH66074.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA   Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT   509).";
RL   Stand. Genomic Sci. 3:325-336(2010).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002040; ADH66074.1; -; Genomic_DNA.
DR   RefSeq; WP_013151681.1; NC_014210.1.
DR   AlphaFoldDB; D7AXK0; -.
DR   STRING; 446468.Ndas_0628; -.
DR   KEGG; nda:Ndas_0628; -.
DR   eggNOG; COG0420; Bacteria.
DR   HOGENOM; CLU_038045_0_1_11; -.
DR   OrthoDB; 9773856at2; -.
DR   Proteomes; UP000002219; Chromosome 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT   DOMAIN          5..221
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          270..355
FT                   /note="Nuclease SbcCD subunit D C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12320"
SQ   SEQUENCE   385 AA;  42272 MW;  A463599A2AD6921A CRC64;
     MSSAMRLLHT SDWHLGRSFH RENLIDAQAA FLDHLVDTIR EHRVDVVVVA GDLYDRALPS
     VDAVRLFDRA LGRIRETGAR AVLISGNHDS MARMSFATGL IDASGVHLRS SLDGVGTPVV
     IEDEHGPVAF YGIPYLEPEI ARHHWDLPER GHAAALGHAM DLVRADLAER PGTRSVVLSH
     AFVTGGEPSD SERDISVGGA SHVPVPVYDG VDYVALGHLH GRQTITPSVR YSGSPLAYSF
     SEEHHVKGYW LVDLDADGLA GAEFAAAPVP RPLARIRGRI EDLLTRPEWE SRTGHWLQIT
     LTDPRRPAHP MDRLRERFPH VLVLDFAPEG GAPDTRPIAA SVADRSERQV VGDFVEWARG
     TPATPEEEAL VNTAVEQVRL QEGTR
//
DBGET integrated database retrieval system