ID   EX7L_LEGPA              Reviewed;         443 AA.
AC   Q5X6S7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=lpp0888;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
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; CR628336; CAH12039.1; -; Genomic_DNA.
DR   RefSeq; WP_010946562.1; NC_006368.1.
DR   AlphaFoldDB; Q5X6S7; -.
DR   GeneID; 66490007; -.
DR   KEGG; lpp:lpp0888; -.
DR   LegioList; lpp0888; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; DFTIIDY; -.
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_0000273668"
SQ   SEQUENCE   443 AA;  49571 MW;  B26DAC411495415D CRC64;
     MSSQLPILTV SQLNRQVKGF LENEIGLVHV EGEISNLSKP SSGHYYFTLK DSTAQIRCAF
     FKNRHSNSLL RNFNDGQQIV ATGKLSLYEA RGEYQLIVEE IVKAGMGILY QRFEELKIKL
     ASEGLFNPER KKPLPRIPET IGIITSPTGA AIQDILSTLA RRFPIARIII YPSEVQGQTA
     PQQLVKALKL ANAHKRCQVL ILARGGGSIE DLWAFNDEYL ARQIAISEIP VVSGIGHETD
     FTIADFVADY RAETPTAAAT AVTPNCIELF NILDTAIYRL HDAIIRLVKG LQLKLNHLID
     KIASPRQTIS TYWQTLDYLE RQLISAMTQF INLNINKVNI FSTQLQANNP KTQIERTKTQ
     LRQLIMQLNQ EIRIQVNQLK NQLSTNLSTL HAVSPLATLD RGYAIVSKNQ RILFAAQQAQ
     IGDTIDVRLA KGSLACEVTQ IKD