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Database: UniProt
Entry: F4VAH7_ECOLX
LinkDB: F4VAH7_ECOLX
Original site: F4VAH7_ECOLX 
ID   F4VAH7_ECOLX            Unreviewed;       408 AA.
AC   F4VAH7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN   Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN   ORFNames=ECPG_03209 {ECO:0000313|EMBL:EGI47403.1};
OS   Escherichia coli H591.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=656408 {ECO:0000313|EMBL:EGI47403.1, ECO:0000313|Proteomes:UP000004681};
RN   [1] {ECO:0000313|EMBL:EGI47403.1, ECO:0000313|Proteomes:UP000004681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H591 {ECO:0000313|EMBL:EGI47403.1,
RC   ECO:0000313|Proteomes:UP000004681};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli H591.";
RL   Submitted (JAN-2010) 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; GL884418; EGI47403.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4VAH7; -.
DR   HOGENOM; CLU_038045_2_0_6; -.
DR   Proteomes; UP000004681; 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}.
FT   DOMAIN          9..233
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          284..381
FT                   /note="Nuclease SbcCD subunit D C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12320"
SQ   SEQUENCE   408 AA;  45659 MW;  3204E0F45B9C5EB0 CRC64;
     MLFRQGIVMR ILHTSDWHLG QNFYSKSREA EHQAFLDWLL ETAQTHQVDA IIVAGDVFDT
     GSPPSYARTL YNRFVVNLQQ TGCHLVVLAG NHDSVATLNE SRDIMAFLNT TVVASAGHAP
     QILPRRDGTP GAVLCPIPFL RPRDIITSQA GLNGIEKQQH LLAAITDYYQ QHYADACKLR
     GDQPLPIIAT GHLTTVGASK SDAVRDIYIG TLDAFPAQNF PPADYIALGH IHRAQIIGGM
     EHVRYCGSPI PLSFDECGKS KYVHLVTFSN GKLESVENLN VPVTQPMAVL KGDLASITAQ
     LEQWRDVSQE PPVWLDIEIT TDEYLHDIQR KIQALTESLP VEVLLVRRSR EQRERVLASQ
     QRETLSELSV EEVFNRRLAL EELDESQQQR LQHLFTTTLH TLAGEHEA
//
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