ID   EX7L_THEFY              Reviewed;         406 AA.
AC   Q47SR1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=Tfu_0468;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54506.1; -; Genomic_DNA.
DR   RefSeq; WP_011290915.1; NC_007333.1.
DR   AlphaFoldDB; Q47SR1; -.
DR   STRING; 269800.Tfu_0468; -.
DR   EnsemblBacteria; AAZ54506; AAZ54506; Tfu_0468.
DR   KEGG; tfu:Tfu_0468; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_1_11; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
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; 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..406
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000303832"
SQ   SEQUENCE   406 AA;  44638 MW;  C710E06BEB088A5A CRC64;
     MGMESSPESP QPVRVVLQAV GGWIGRLGRI WIEGQVAELH RRGGMAYITL RDPVANVSAR
     VTCSIRVLRA ADPPPEQGAR VVVYAKPDFY VPRGTFSFQA LEIRHVGLGE LLARLERLRQ
     ALAAEGLFAE SRKRKLPFLP GVVGLICGRD SAAERDVLEN ARRRWPAVRF EVREVAVQGD
     RAVPEVMAAL EELDAHPEVD VIIIARGGGS LEDLLPFSDE ALVRAVAAAR TPVVSAIGHE
     QDTPLLDYVA DLRASTPTDA AKKVVPDVGE QWELIRQLRD RARRVLEGGI AREEAWLASM
     RSRPVLANPV QEVERKIEQV FDLRDRGRRA LTAALDRAGD NLAHIRARLH ALSPATTLAR
     GYAIVRRADG TVVRSAAEVA PGEELRLRFA EDGLVAIAQN REEDEL