ID   EX7L_YERPG              Reviewed;         459 AA.
AC   A9R7Z4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=YpAngola_A0410;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX86881.1; -; Genomic_DNA.
DR   RefSeq; WP_002209810.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R7Z4; -.
DR   GeneID; 57975829; -.
DR   KEGG; ypg:YpAngola_A0410; -.
DR   PATRIC; fig|349746.12.peg.1365; -.
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; 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.
FT   CHAIN           1..459
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000122105"
SQ   SEQUENCE   459 AA;  52098 MW;  547EEFFBA10BA6D4 CRC64;
     MSQSSASSIF TVSRLNQTVR ELLEREMGQI WLTAEISNFS QPASGHWYFT LKDDRAQVRC
     AMFRNSNRRT TFRPQNGQQV LVRASITLYE PRGDYQLIAE SMQPAGDGLL QQQFEQLKQQ
     LAAEGLFDQS HKQPLPHPAK QVGVITSASG AALHDVLHVL QRRDPSLPVI IYPTSVQGVD
     APLQIVRAIQ LANLRAECDV LIVGRGGGSL EDLWSFNDER VARAIFNSHI PIVSAVGHET
     DVTIADFVAD LRAPTPSAAA ELVSRNQIEL VRQIQGQQQR MEMAMDYYLA QRNQQFTRLE
     HRLQQQHPHL RLARQQTLLL KLQRRLEESA QTQIRLLSKR TERLQQRLQQ VQPQGQIHRY
     NQRVQQQEYR LRQAVERQLN GYRQRFGIAC SQLEAVSPLA TLARGYSVTQ TPAGALLKTT
     KQVQAGDKLT TRLQDGWVES EITQVTVAKK SRQKKVVTQ