EX7L_CLOBJ
ID EX7L_CLOBJ Reviewed; 401 AA.
AC C1FPB2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=CLM_2102;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) 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; CP001581; ACO85866.1; -; Genomic_DNA.
DR RefSeq; WP_012704993.1; NC_012563.1.
DR AlphaFoldDB; C1FPB2; -.
DR STRING; 536232.CLM_2102; -.
DR EnsemblBacteria; ACO85866; ACO85866; CLM_2102.
DR KEGG; cby:CLM_2102; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_9; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000001374; 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_1000200665"
SQ SEQUENCE 401 AA; 45407 MW; D5FC3BDF81183771 CRC64;
MHIKTLTVSQ LNRYVKNTLD ADFILNNASV KGEISNLKIH SSGHIYFSLK DGGSKINCVM
FKSYAYNLKF VPENGMDVVA LGNVSVYEKE GSYQLYVKDM KREGIGDLYV AFEKLKEKLK
EEGLFDDVHK KEIPKFSKKV GVITSPTGAA LKDIINVTKR RNKGIELLIY PALVQGTDAS
RTLIEGIKIL NKVEDVDIII LARGGGSIEE LWAFNNEELA YAVYNSKKPI ITGVGHETDF
TIVDFVSDRR APTPSAAAEI AVFDREVLIN EILNYKYNIK NSMENIIKEK RSYLNLYKQK
IEANSPTNII VNEYKNIDNL KELLNMKIEG KLNKEKNNLS RLSSLLEAHN PLNVLKKGYT
LIEDEGNNLI TEKESLKKLN KINIIFKDGR AKLSIEYIEE F
