ID   EX7L_YERPB              Reviewed;         459 AA.
AC   B2K9P2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=YPTS_2942;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-2008) 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; CP001048; ACC89899.1; -; Genomic_DNA.
DR   RefSeq; WP_011192797.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K9P2; -.
DR   GeneID; 66844743; -.
DR   KEGG; ypb:YPTS_2942; -.
DR   PATRIC; fig|502801.10.peg.2372; -.
DR   OMA; WPAVRFE; -.
DR   BioCyc; YPSE502801:YPTS_RS14815-MON; -.
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_1000122104"
SQ   SEQUENCE   459 AA;  52048 MW;  C9625009F01EFB7B CRC64;
     MSQSSASSIF TVSRLNQTVR ELLEREMGQI WLTAEISNFS QPASGHWYFT LKDDRAQVRC
     AMFRNSNRRT TFRPQNGQQV LVRASITLYE PRGDYQLIAE SMQPAGDGLL QQQFEQLKQQ
     LAAEGLFDQS HKQPLPSPAK 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