ID   EX7L_TROW8              Reviewed;         404 AA.
AC   Q83HE6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 108.
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=TW665;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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; BX251412; CAD67324.1; -; Genomic_DNA.
DR   RefSeq; WP_011096602.1; NC_004551.1.
DR   AlphaFoldDB; Q83HE6; -.
DR   GeneID; 67388442; -.
DR   KEGG; tws:TW665; -.
DR   HOGENOM; CLU_023625_2_1_11; -.
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; 2.
DR   Pfam; PF02601; Exonuc_VII_L; 2.
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..404
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000273698"
SQ   SEQUENCE   404 AA;  44985 MW;  BCE7C0E22BCC8B30 CRC64;
     MDMQADEMYR QDPLGSCGNP RQVSHITGRL SSLLGELPAT WIEGEVTQLS PRRIGVFLTL
     KDMNESKHLE FFLPFDAFKD EVEVGNRVKI HGKLEFWATS GQIKVKGFEI QSVGIGELIE
     RIARLRVQLA LEGLYEHKRP LPFIPKLIGL VTGQNSDAEK DVVTNVLLRW PAAKFCTIYA
     SMQGASCVSE TISAIQKLDA NNDVDVIIVA RGGGSFHDLI GFSDEQMIRA VFAIKTPLIS
     AIGHEADRPI LDEVADLRAS TPTDAAKRVV PDIADEKRLI KSAMSFLKKS YEPVIDKIKC
     DTLSWSQAFS NPFETFIAPR RREIDLFYQQ MLTVVWANFS KTETEIAAIK KHLLAISPQN
     TLVRGYAMIE DETGRIISSA DKLSAGDTVT LRLHDGLVRA EITQ