ID   EX7L_CLOBL              Reviewed;         401 AA.
AC   A7GEJ7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=CLI_1949;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC       insoluble oligonucleotides, which are then degraded further into small
CC       acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC         direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00378};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00378}.
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DR   EMBL; CP000728; ABS42702.1; -; Genomic_DNA.
DR   RefSeq; WP_012099922.1; NC_009699.1.
DR   AlphaFoldDB; A7GEJ7; -.
DR   EnsemblBacteria; ABS42702; ABS42702; CLI_1949.
DR   KEGG; cbf:CLI_1949; -.
DR   HOGENOM; CLU_023625_2_0_9; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000002410; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04489; ExoVII_LU_OBF; 1.
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   PANTHER; PTHR30008; PTHR30008; 2.
DR   Pfam; PF02601; Exonuc_VII_L; 2.
DR   Pfam; PF13742; tRNA_anti_2; 1.
DR   TIGRFAMs; TIGR00237; xseA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN           1..401
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000048770"
SQ   SEQUENCE   401 AA;  45539 MW;  542E8825473A529F CRC64;
     MHIKTLTVSQ LNRYVKNTLD ADFILNNASV KGEISNLKIH SSGHIYFSLK DGGSKINCVM
     FKSYAYNLKF APENGMDVVA LGNVSVYEKE GSYQLYVKDM KREGIGDLYV AFEKLKEKLK
     EEELFDDVHK KEIPKFSKKV GVITSPTGAA LKDIINVTKR RNKGIELLIY PALVQGTDAS
     RTLIEGIKIL NKVEDVDIII LARGGGSIEE LWAFNNEELA YAVYNSKKPI ITGVGHETDF
     TIVDFVSDRR APTPSAAAEI AVFDREVLIN EILNYKYNIK NYMENIIKEK RNYLNLYKQK
     IEANSPTNII VNEYKNIDNL KELLNMKIEG KLNKEKNNLS RLSSLLEAHN PLNVLKKGYT
     LIEDEGNNLI TEKEALKKLN KINIIFKDGR AKLSIEYIEE F