ID   EX7L_SYNS9              Reviewed;         387 AA.
AC   Q3AZZ0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
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};
GN   OrderedLocusNames=Syncc9902_0367;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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; CP000097; ABB25337.1; -; Genomic_DNA.
DR   RefSeq; WP_011359194.1; NC_007513.1.
DR   AlphaFoldDB; Q3AZZ0; -.
DR   STRING; 316279.Syncc9902_0367; -.
DR   EnsemblBacteria; ABB25337; ABB25337; Syncc9902_0367.
DR   KEGG; sye:Syncc9902_0367; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_1_3; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000002712; 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; Reference proteome.
FT   CHAIN           1..387
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000303830"
SQ   SEQUENCE   387 AA;  42793 MW;  DD6AD159BC212C6B CRC64;
     MSADRVPTYS VGELNTAIGS LLERGFAPRF LLEATVSRPQ VKKGHLWLTL TDGTASISGV
     VWASRLAQLS YRPTDGDGVT VVGKLNFWAA RASITVQALD IRPSLSTVLR QFEQVRQRLE
     DEGVINPGRQ RSLPSQPATL ALLTSVPSSA LADMLRTGRE RWPMTRLLVI PIPVQGAVAD
     QIIKVLNRLA ERCEALAVDG LVLARGGGSR EDLAVFDDEA LCRCLAQFPR PVVTGIGHED
     DLTIADLVAD HRAATPTAAM VACLPDRDSA KRNLQDRRQR MKDVVGWRIE RDRQRLNDRR
     AFLRQQSPLR RLQQLQDDLN RKRDLLRALS PSRWLQRGLA LLSNDAGETL SGVTSIKVGD
     RVVIQMNDGE LDTDVKVVRP SSHQSMS