ID   EX7L_RICB8              Reviewed;         442 AA.
AC   A8GXS3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=A1I_06785;
OS   Rickettsia bellii (strain OSU 85-389).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=391896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU 85-389;
RA   Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT   "Complete genome sequencing of Rickettsia bellii.";
RL   Submitted (SEP-2007) 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; CP000849; ABV79673.1; -; Genomic_DNA.
DR   RefSeq; WP_011476902.1; NC_009883.1.
DR   AlphaFoldDB; A8GXS3; -.
DR   SMR; A8GXS3; -.
DR   KEGG; rbo:A1I_06785; -.
DR   HOGENOM; CLU_023625_2_0_5; -.
DR   OMA; WPAVRFE; -.
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; 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..442
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000048781"
SQ   SEQUENCE   442 AA;  49474 MW;  0B31507C46A20525 CRC64;
     MLDNFTSSQT TKEFSVSEIS NKIKELLENN FGYIKVKGEI SGLKIASSGH AYFNLKENTA
     ILACTCWRPI LAKIKFPLND GMEVVISGKL SSYAGNSRYQ LSVENLQPAG LGAMVQILNE
     RKARLEKEGL FNKIRKPIPF LPNKIGVITS ITGAVIQDII HRIRERFPTH VIIWPVSVQG
     ENSGNEIAEA IDGFNKLEEA NKPDVIIVAR GGGSIEDLWS FNDEVLVRAT YNSKIPIISA
     VGHEVDYTLI DLAADKRAPT PTAAAEFAVP VRSILNSTLQ SYEKVLVTNT KQLVKNHEQA
     ITNYDKINRY LAHYINHKQQ LLDETGFNLL DSLPCLISLK ETKLKSFSKE RIHPHKIITY
     KTLELTHKAA YIIKSANNTL KNFEYKLELN SLLLLSLDYH NVLKRGFAIV KGESGNFVSS
     KTTTEKVLNI QFFDGNIKAV RD