ID   EX7L_NEIG1              Reviewed;         451 AA.
AC   Q5F8V5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=NGO0655;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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; AE004969; AAW89382.1; -; Genomic_DNA.
DR   RefSeq; WP_003688847.1; NC_002946.2.
DR   RefSeq; YP_207794.1; NC_002946.2.
DR   AlphaFoldDB; Q5F8V5; -.
DR   STRING; 242231.NGO_0655; -.
DR   PRIDE; Q5F8V5; -.
DR   EnsemblBacteria; AAW89382; AAW89382; NGO_0655.
DR   GeneID; 66752994; -.
DR   KEGG; ngo:NGO_0655; -.
DR   PATRIC; fig|242231.10.peg.772; -.
DR   HOGENOM; CLU_023625_3_1_4; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000000535; 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..451
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000273671"
SQ   SEQUENCE   451 AA;  49798 MW;  4040CED8CE88A526 CRC64;
     MSDFFHSDVL SVSELNAFAK SILENHLAGL WIAGEVSNLT RAASGHYYFS LKDSRAQVRC
     AMFKGAAARL AQPLKEGDHI EVAGKISIYE ARGEFQITVN EVRLKGLGQL YEAYERLKAQ
     LQAEGAFAAE RKKPLPVRPQ CIGIVTSLAA AALRDVVTTL KRRAPEIPVI VYPAAVQGAG
     SGFQIAQAIK TASQRAECDV LIVCRGGGSI EDLRAFNEEP VVRAIEACTI PVVSGVGHET
     DFTLADFVAD VRAPTPTGAA ELVSPNRQES LHRLVQAQGR LKTVLEQRYF DASQKLDWLA
     RQIRHPRQKL DEQRASIGKL AQTLSYSMTQ NLRAHTARFE RQTQALQHCR PDVSVYRQDI
     VRLQTALPAA FSRLLARRRQ SLTAQAALLE AVSPQHILER GFSVVKNTRG QVIRNADVLK
     QGQKLHITFS DGETDVRVSK EQGQQDLFDC I