ID   EX7L_STRGG              Reviewed;         403 AA.
AC   B1W2D9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-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=SGR_2474;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG19303.1; -; Genomic_DNA.
DR   RefSeq; WP_012379226.1; NC_010572.1.
DR   AlphaFoldDB; B1W2D9; -.
DR   STRING; 455632.SGR_2474; -.
DR   EnsemblBacteria; BAG19303; BAG19303; SGR_2474.
DR   GeneID; 6214877; -.
DR   KEGG; sgr:SGR_2474; -.
DR   PATRIC; fig|455632.4.peg.2518; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_1_11; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000001685; Chromosome.
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; 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..403
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000122091"
SQ   SEQUENCE   403 AA;  43854 MW;  336AEB27E1860C86 CRC64;
     MALNTSAEAP LPVGEVSRLI GGWIDRLGAI WVEGQITQLS RRPGAGVVFL TLRDPSHDIS
     VSVTCFRQVF DRIADVVTEG ARVVVLAKPE WYAPRGQLSL RATDIRPVGI GELLVRLEQL
     KKSLAAEGLF ALDRKKPLPF LPQLVGLVCG RASAAERDVL ENARRRWPAV RFEVRNTAVQ
     GVNAVAQVVQ AVEELDALQE VDVIVVARGG GSVEDLLPFS DEQLIRTVAA CRTPVVSAIG
     HEPDSPLLDL VADLRASTPT DAAKKVVPDV GEELERVQQL RDRALRTVRG LLDREERGLA
     HALGRPAMER PHRLVDEREA EVDALLGRAR RVLGHLLDRA DSELSHTLAR VVSLSPAATL
     ERGYAVLQRP DGHVVRSPEE AGAPGEPLRA RVSEGEFTVR VDG