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Database: UniProt
Entry: D0MDI6_RHOM4
LinkDB: D0MDI6_RHOM4
Original site: D0MDI6_RHOM4 
ID   D0MDI6_RHOM4            Unreviewed;       412 AA.
AC   D0MDI6;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN   Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN   OrderedLocusNames=Rmar_0273 {ECO:0000313|EMBL:ACY47179.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY47179.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY47179.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
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; CP001807; ACY47179.1; -; Genomic_DNA.
DR   RefSeq; WP_012842791.1; NC_013501.1.
DR   AlphaFoldDB; D0MDI6; -.
DR   STRING; 518766.Rmar_0273; -.
DR   KEGG; rmr:Rmar_0273; -.
DR   eggNOG; COG0420; Bacteria.
DR   HOGENOM; CLU_038682_0_0_10; -.
DR   OrthoDB; 9773856at2; -.
DR   Proteomes; UP000002221; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002221}.
FT   DOMAIN          1..232
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
SQ   SEQUENCE   412 AA;  46698 MW;  F904830BA473D842 CRC64;
     MKILHTADIH LGITTYGRVD PSTGLNTRLQ DFRRAFEFMV EQALAEDVDL FLFCGDAFRN
     PDPSPTEQTI FAECLQPLTE RGIPIVLLVG NHDHPVTFGR ASSIDIFRYL EGQARVFRRP
     EVATIQTKSG PLQLIALPWP VRSLLLSREE FRQKSASEVR EVIEQLYVEY VQKAVERLDP
     SLPTVLAGHF SVQGAELSGS ERTSLIAHEP KFTVGQLALP PIDYVALGHI HRHQNLNPDG
     IPVVYSSSIE RVTFRETDDP KGFVLVEIQS DGPRKQTRYR FVETPARRFV DLHIDARDSD
     DPTERILNAI ARAPVADAIV RVRYQVDEDQ VARVDVRRIR EALRTAAHIA GVERTVTPVV
     RERRTIVERD SSLREALSRY IDQHEKLHPL REQLIEAALA LEARLEAGRL PE
//
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