ID   EX7L_PASMU              Reviewed;         445 AA.
AC   Q9CP86;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 117.
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=PM0168;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004439; AAK02252.1; -; Genomic_DNA.
DR   RefSeq; WP_010906514.1; NC_002663.1.
DR   AlphaFoldDB; Q9CP86; -.
DR   SMR; Q9CP86; -.
DR   STRING; 747.DR93_1898; -.
DR   EnsemblBacteria; AAK02252; AAK02252; PM0168.
DR   KEGG; pmu:PM0168; -.
DR   PATRIC; fig|272843.6.peg.173; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000000809; 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; 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; Reference proteome.
FT   CHAIN           1..445
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000197865"
SQ   SEQUENCE   445 AA;  50596 MW;  63A126F53E439218 CRC64;
     MSEHIYSVSQ LNQTVRVMLE NQLRQVWLTG EISNFTQPVS GHWYLTLKDE NAQVRCAMFR
     MKNMRVSFRP QNGMQVLVHA SVSLYEPRGD YQLIIESMHP AGEGLLQQQF EALKMQLAAE
     GLFAQHLKKS LPPFCKSVGI VTSQTGAALQ DILQILRRRD PSLQVVIYPT AVQGKEASAE
     IVQMIELANR RQEVDALIVG RGGGSLEDLW CFNEEMVARA IFHSQLPIIS AVGHETDVTI
     ADFVADLRAP TPSAAAELVS RDQQALLQQL VYQRQRLEMA LDRLFKQKDD RLQRLRLRLH
     NQHPQRQLSA QKQLMQQLAH RLDWSMQAVL QQKQAQLRVL WARVEKNPLP FTLQKQKQDL
     AQLKVRLDVA LKRELTFKHH QFAALCTKLD SISPLKVFAR GYSIAQNAQG VAITQLKQVS
     VGERVITRLA DGEIVSQVTD LRPRS