ID   EX7L_CLOK1              Reviewed;         400 AA.
AC   B9E101;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=CKR_1125;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) 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; AP009049; BAH06176.1; -; Genomic_DNA.
DR   RefSeq; WP_012101611.1; NC_011837.1.
DR   AlphaFoldDB; B9E101; -.
DR   SMR; B9E101; -.
DR   EnsemblBacteria; BAH06176; BAH06176; CKR_1125.
DR   KEGG; ckr:CKR_1125; -.
DR   HOGENOM; CLU_023625_2_0_9; -.
DR   Proteomes; UP000007969; 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; 1.
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..400
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000200667"
SQ   SEQUENCE   400 AA;  45366 MW;  0EC035B3B4A03829 CRC64;
     MYIKTLTVSD INRYIKKTLD NDFILGNCSV KGEVSNFKFH SSGHMYFSLK DKFSKINCIM
     FKSSVEKLNF MPGDGMKVIV KGRISLYEKE GVYQLYCSEM KPDGMGELYL AFEKLKIELE
     KKGLFDISHK KKIPLYAKKI GVITSPTGAA VKDIINVTRR RNKKIELLIY PSLVQGTGAS
     DNIIKGIETF NSMEDVELII IARGGGSIEE LWCFNDEKLA EAVYSSKKPI ITGVGHEIDY
     TIVDFVSDMR APTPSAAAEI GVFSLEEYVQ KILNYKNKLY NSVKNTVNDK KNRLAFVKKT
     LEVNNPLTYI ANEYENIDKI KESLNFKIKV IINGKKEKLG KINALLSAHN PLNILNKGYC
     IIEDEQKNVI SSIEELNKKY KVDIIMKDGT SKVELIHYKK