ID   EX7L_BRUA2              Reviewed;         511 AA.
AC   Q2YL15;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=BAB2_0475;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ12641.1; -; Genomic_DNA.
DR   RefSeq; WP_002968954.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YL15; -.
DR   SMR; Q2YL15; -.
DR   STRING; 359391.BAB2_0475; -.
DR   EnsemblBacteria; CAJ12641; CAJ12641; BAB2_0475.
DR   GeneID; 3827916; -.
DR   KEGG; bmf:BAB2_0475; -.
DR   PATRIC; fig|359391.11.peg.2667; -.
DR   HOGENOM; CLU_023625_3_1_5; -.
DR   OMA; LVWPVKV; -.
DR   PhylomeDB; Q2YL15; -.
DR   PRO; PR:Q2YL15; -.
DR   Proteomes; UP000002719; Chromosome II.
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; Reference proteome.
FT   CHAIN           1..511
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000273649"
SQ   SEQUENCE   511 AA;  56363 MW;  6765E8983A45DB42 CRC64;
     MASDSSFPGA SSNVAEYSVS EISGALKRTV EDTFGHVRVR GEISGYRGPH SSGHAYFALK
     DDRARLEAVI WRGSMSRLRF RPEEGMEVIA TGKLTTYPGS SKYQIVIEQM EPAGAGALMA
     LLEERKQRLA AEGLFDPTLK QLLPFMPRVI GVVTSPTGAV IRDIIHRISD RYPLRVIVWP
     VRVQGDTCGP EVATAVNGFN TLPDDGPIPR PDVLIVARGG GSLEDLWGFN DEIVVRAVAA
     SHIPVISAVG HETDWTLIDL AADMRAPTPT GAAEMAVPVK ADLQASLASQ SARLSSAMSR
     FFDQKRQAHR AAARAMPSAD QLLALPRRRF DEAASRLTRA LFVNTQKKRV HFDGHARQLS
     PRLLQRRLVE LERGVTMLGQ RLPRALEAFL RERRTAFTHR ANRLSPEPIL RRTRLTGSTL
     EQLDRRRDQA VRLLIERVKR RSQELDRLMR TLSYESVLER GFAVVFDAQG KPVKQAAAVS
     PGDALSVRFR DGDVGVVARA GLTIPDPTKG Q