EX7L_CLOB6
ID EX7L_CLOB6 Reviewed; 401 AA.
AC C3KXC6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=CLJ_B2072;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-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; CP001083; ACQ53328.1; -; Genomic_DNA.
DR RefSeq; WP_003362519.1; NC_012658.1.
DR AlphaFoldDB; C3KXC6; -.
DR SMR; C3KXC6; -.
DR EnsemblBacteria; ACQ53328; ACQ53328; CLJ_B2072.
DR KEGG; cbi:CLJ_B2072; -.
DR HOGENOM; CLU_023625_2_0_9; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000002333; 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_1000205669"
SQ SEQUENCE 401 AA; 45384 MW; 48651DB72CBC5E9A CRC64;
MHIKTLTVSQ LNRYVKNTLD ADFILNNASV KGEISNLKIH SSGHIYFSLK DGGSKINCVM
FKSYAYNLKF APENGMDVVA LGNVSVYEKE GSYQLYVKDM KREGIGDLYV AFEKLKEKLK
EEGLFDDVHK KEIPKFSKKV GVITSPTGAA LKDIINVTKR RNKGIELLIY PALVQGTDSS
KTLIEGIKTL NKVEDVDIII LARGGGSIEE LWAFNNEELA YSVYNSKKPI ITGVGHETDF
TIVDFVSDRR APTPSAAAEI AVFDREVLIN EILNYKYNIK NSMENIIKEK RNYLNLYKQK
IEANSPTNII VNEYKNIDNL KELLNMKIEG KLNKEKNDLS RLSSLLEAHN PLNVLKKGYT
LIEDEGNNLI TEKEALKELN KINIIFKDGR AKLSIEYIEE F
