ID   EX7L_VIBVU              Reviewed;         443 AA.
AC   Q8DF05;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=VV1_0420;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016795; AAO08943.1; -; Genomic_DNA.
DR   RefSeq; WP_011078518.1; NC_004459.3.
DR   AlphaFoldDB; Q8DF05; -.
DR   SMR; Q8DF05; -.
DR   EnsemblBacteria; AAO08943; AAO08943; VV1_0420.
DR   KEGG; vvu:VV1_0420; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000002275; Chromosome 1.
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..443
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000197901"
SQ   SEQUENCE   443 AA;  49727 MW;  F4CBE1D257C06779 CRC64;
     MSSLTNPNIF TVSRLNSEVR LLLENQLGIV WLVGEISNFS APVSGHWYFT LKDSMAQVKC
     AMFRGNNRLV SFKPTNGNQV LVKARLSLYE PRGDYQLIIE SMQPEGDGRL QQQFDALKMK
     LASEGLFAQS SKQAIPEHPK CVGIITSKTG AALYDILDVL KRRDPSLPVV IYPTLVQGEE
     AAIQIAQAIG RANSRNECDV LIVGRGGGSL EDLWCFNNEI VARTIAASQI PIISAVGHEI
     DVTIADFVAD LRAPTPSAAA ELVSRDNSHK DQALMSREQK LRAAWRHYLT EQNRTIVSLS
     HRLEKQHPRY RLMRQTQQAD ELQIRLQRAM EKYLAQREQK VSRVQHKLQL LSPVRQISEQ
     KNALARVEQK MMDAMDRKLL RLRHQIAIAA EKLDTVSPLA TLKRGYSITQ SESGDVITRQ
     SQIKTGDTLV TRLSDGEIRS TVN