(data stored in SCRATCH zone)

SWISSPROT: B7UJM1_ECO27

ID   B7UJM1_ECO27            Unreviewed;       400 AA.
AC   B7UJM1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|RuleBase:RU363069};
GN   Name=sbcD {ECO:0000256|RuleBase:RU363069,
GN   ECO:0000313|EMBL:CAS07881.1};
GN   OrderedLocusNames=E2348C_0333 {ECO:0000313|EMBL:CAS07881.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07881.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07881.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07881.1; -; Genomic_DNA.
DR   RefSeq; WP_001221284.1; NC_011601.1.
DR   EnsemblBacteria; CAS07881; CAS07881; E2348C_0333.
DR   KEGG; ecg:E2348C_0333; -.
DR   HOGENOM; HOG000026261; -.
DR   KO; K03547; -.
DR   OMA; TSGNHDS; -.
DR   BioCyc; ECOL574521:E2348C_RS01755-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UJM1.
DR   SWISS-2DPAGE; B7UJM1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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:CAS07881.1};
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;  44712 MW;  63573DFD195287A0 CRC64;
     MRILHTSDWH LGQNFYSKSR EAEHQAFLDW LLETAQAHQV 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 EQLEQWRDVS
     QEPPVWLDIE ITTDEYLHDI QRKIQALTES LPVEVLLVRR SREQRERVLA SQQRETLSEL
     SVEEVFNRRL ALEELEESQQ QRLQHLFATT LHSLAGEHEA
//

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