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Database: UniProt/SWISS-PROT
Entry: EX7L_BACC3
LinkDB: EX7L_BACC3
Original site: EX7L_BACC3 
ID   EX7L_BACC3              Reviewed;         452 AA.
AC   C1ERQ3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   29-MAY-2013, entry version 33.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit;
DE            EC=3.1.11.6;
DE   AltName: Full=Exodeoxyribonuclease VII large subunit;
DE            Short=Exonuclease VII large subunit;
GN   Name=xseA; OrderedLocusNames=BCA_4289;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large
CC       acid-insoluble oligonucleotides, which are then degraded further
CC       into small acid-soluble oligonucleotides (By similarity).
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'-
CC       or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the XseA family.
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DR   EMBL; CP001407; ACO27045.1; -; Genomic_DNA.
DR   RefSeq; YP_002751540.1; NC_012472.1.
DR   STRING; 572264.BCA_4289; -.
DR   EnsemblBacteria; ACO27045; ACO27045; BCA_4289.
DR   GeneID; 7688199; -.
DR   KEGG; bcx:BCA_4289; -.
DR   PATRIC; 18821737; VBIBacCer84800_4184.
DR   eggNOG; COG1570; -.
DR   HOGENOM; HOG000229265; -.
DR   KO; K03601; -.
DR   OMA; ENAQVRC; -.
DR   ProtClustDB; PRK00286; -.
DR   BioCyc; BCER572264:GH22-4225-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
DR   GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:HAMAP.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR   HAMAP; MF_00378; Exonuc_7_L; 1; -.
DR   InterPro; IPR003753; Exonuc_VII_L.
DR   InterPro; IPR020579; Exonuc_VII_lsu_C.
DR   InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR   Pfam; PF02601; Exonuc_VII_L; 1.
DR   Pfam; PF13742; tRNA_anti_2; 1.
DR   TIGRFAMs; TIGR00237; xseA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN         1    452       Exodeoxyribonuclease 7 large subunit.
FT                                /FTId=PRO_1000200659.
SQ   SEQUENCE   452 AA;  51440 MW;  8C706930F60B724A CRC64;
     MEKQYLTVTA LTRYIKTKIE YDPHLQSVWL KGEISNFKNH SRGHMYFTLK DENARIAAVM
     FAGHNRNIKF RPENGMKVLV KGKISVYEAS GSYQIYIQDM QPDGIGNLHL AYEQLKVRLE
     EEGLFSQVYK KTIPPYAKTI GVITSPTGAA IRDIITTIKR RYPIGNVIVF PVLVQGESAA
     PSIVQAIRTA NEMEEIDVLI VGRGGGSIEE LWAFNEEMVA RAIFKSEIPI ISAVGHETDF
     TVADFVADLR APTPTAAAEL AAPNIIELQE KVLQRTLRLQ RAMRELVHKK EEKLQVLQKS
     YAFRYPRQVY EQKEEQLDRA LEQLVLAKER YIDKKVNQLK QLSFYLEKHH PSQKIMQTKV
     AVETLQKQLQ REMQTLLQTK EFAFVRAAQK LEALSPLKVM MRGYGLVYDE EKQVLKSVKD
     VSLGDAVSVQ LQDGILDCSV SGIEERELNN GK
//
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