(data stored in ACNUC10821 zone)

SWISSPROT: C8U282_ECO10

ID   C8U282_ECO10            Unreviewed;       400 AA.
AC   C8U282;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|RuleBase:RU363069};
GN   Name=sbcD {ECO:0000256|RuleBase:RU363069,
GN   ECO:0000313|EMBL:BAI29240.1};
GN   OrderedLocusNames=ECO103_0372 {ECO:0000313|EMBL:BAI29240.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29240.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29240.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures
CC       can inhibit DNA replication and are intermediates in certain DNA
CC       recombination reactions. The complex acts as a 3'->5' double
CC       strand exonuclease that can open hairpins. It also has a 5'
CC       single-strand endonuclease activity.
CC       {ECO:0000256|RuleBase:RU363069}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD.
CC       {ECO:0000256|RuleBase:RU363069}.
CC   -!- SIMILARITY: Belongs to the SbcD family.
CC       {ECO:0000256|RuleBase:RU363069}.
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DR   EMBL; AP010958; BAI29240.1; -; Genomic_DNA.
DR   RefSeq; WP_001221316.1; NC_013353.1.
DR   EnsemblBacteria; BAI29240; BAI29240; ECO103_0372.
DR   KEGG; eoh:ECO103_0372; -.
DR   HOGENOM; HOG000026261; -.
DR   KO; K03547; -.
DR   OMA; TSGNHDS; -.
DR   BioCyc; ECOL585395:ECO103_RS01950-MONOMER; -.
DR   Proteomes; UP000000959; 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   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF12320; SbcD_C; 1.
DR   TIGRFAMs; TIGR00619; sbcd; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U282.
DR   SWISS-2DPAGE; C8U282.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   DNA recombination {ECO:0000256|RuleBase:RU363069};
KW   DNA replication {ECO:0000256|RuleBase:RU363069};
KW   Endonuclease {ECO:0000256|RuleBase:RU363069};
KW   Exonuclease {ECO:0000256|RuleBase:RU363069,
KW   ECO:0000313|EMBL:BAI29240.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU363069};
KW   Nuclease {ECO:0000256|RuleBase:RU363069}.
FT   DOMAIN        1    225       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   DOMAIN      276    373       SbcD_C. {ECO:0000259|Pfam:PF12320}.
SQ   SEQUENCE   400 AA;  44683 MW;  FD9D11CC0DC96D40 CRC64;
     MRILHTSDWH LGQNFYSKSR EAEHQAFLDW LLETAQTHQV DAIIVAGDVF DTGSPPSYAR
     TLYNRFVVNL QQTGCHLVVL AGNHDSVATL NESRDIMAFL NTTVVASAGH APQILPRRDG
     TPGAVLCPIP FLRPRDIITS QAGLNGIEKQ QHLLAAITDY YQQHYADACK LRGDQPLPII
     ATGHLTTVGA SKSDAVRDIY IGTLDAFPAQ NFPPADYIAL GHIHRAQIIG GMEHVRYCGS
     PIPLSFDECG KSKYVHLVTF SNGKLESVEN LNVPVTQPMA VLKGDLASIT AQLEQWRDVS
     QEPPVWLDIE ITADEYLHDI QRKIQALTES LPVEVLLVRR SREQRERVLA SQQRETLSEL
     SVEEVFNRRL ALEELDESQQ QRLQHLFTTT LHTLAGEHEA
//

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