ID   EX7L_LEGPL              Reviewed;         443 AA.
AC   Q5WY82;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=lpl0857;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH15091.1; -; Genomic_DNA.
DR   RefSeq; WP_011215014.1; NC_006369.1.
DR   AlphaFoldDB; Q5WY82; -.
DR   SMR; Q5WY82; -.
DR   EnsemblBacteria; CAH15091; CAH15091; lpl0857.
DR   KEGG; lpf:lpl0857; -.
DR   LegioList; lpl0857; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000002517; 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   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00378; Exonuc_7_L; 1.
DR   InterPro; IPR003753; Exonuc_VII_L.
DR   InterPro; IPR020579; Exonuc_VII_lsu_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR   PANTHER; PTHR30008; PTHR30008; 1.
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..443
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000273667"
SQ   SEQUENCE   443 AA;  49654 MW;  14EC09F7088C7A16 CRC64;
     MSSQLPILTV SQLNRQVKGF LENEIGLVHV EGEISNLSKP SSGHYYFTLK DSTAQIRCAF
     FKNRHSSSLL RNFNDGQQIV ASGKLSLYEA RGEYQLIVEE IVEAGMGILY QRFEELKIKL
     AREGLFNPER KKTLPRIPET IGIITSPTGA AIQDILSTLA RRFPIARIII YPSEVQGQAA
     PQQLVNALKL ANTHKRCQVL ILARGGGSIE DLWAFNDEYL ARQIAISEIP VVSGIGHETD
     FTIADFVADY RAETPTAAAT AVTPNCIELF NILDTAIYRL HDAIIRLVKG LQLKLNHLID
     KIASPRQTIS TYWQTLDYLE RQLISAMTQF INLNINKMNL FSTRLQANNP KTQIERTKIQ
     LRQLILQLTQ EIRIKVNQLK HQLSTNLSTL HAVSPLATLD RGYAIVSKNQ RILFAAQQAQ
     IGDTIDVRLA KGSLACEVTQ IKD