ID   EX7L_LEGPC              Reviewed;         443 AA.
AC   A5IG90;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=LPC_2470;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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; CP000675; ABQ56390.1; -; Genomic_DNA.
DR   RefSeq; WP_011945942.1; NC_009494.2.
DR   AlphaFoldDB; A5IG90; -.
DR   SMR; A5IG90; -.
DR   KEGG; lpc:LPC_2470; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   BioCyc; LPNE400673:LPC_RS04545-MON; -.
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_1000048776"
SQ   SEQUENCE   443 AA;  49446 MW;  A0259330BCF783C0 CRC64;
     MSSQLPILTV SQLNRQVKGF LENEIGLVHV EGEISNLSKP SSGHYYFTLK DSTAQIRCAF
     FKNRHSSSLL RNFNDGQQIV ASGKLSLYEA RGEYQLIVEE IVEAGMGVLY QRFEELKIKL
     ASEGLFNPER KKTLPRIPET IGIITSPTGA AIQDILSTLA RRFPIARVII YPSEVQGQTA
     PQQLVNALKL ANAHKRCQVL ILARGGGSIE DLWAFNDEYL ARQIAISEIP VVSGIGHETD
     FTIADFVADY RAETPTAAAT AVTPNCIELF NILDTAIYRL HDAIIRLIKG LQLKLNHLID
     KIASPRQAIS TYWQTLDYLE RQLISAMTQF INLNINKVNI FSTQLQASNP KIQIERTKIQ
     LQQLIMQLTQ EIRIKVNQLK NQLSTNLSTL HAVSPLATLD RGYAIVSKNQ RILFAAQQAQ
     IGDTINIRLA KGSLACEVTQ IKD