ID   EX7L_STRM5              Reviewed;         443 AA.
AC   B4SQC8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Smal_2759;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-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; CP001111; ACF52459.1; -; Genomic_DNA.
DR   RefSeq; WP_012511662.1; NC_011071.1.
DR   AlphaFoldDB; B4SQC8; -.
DR   STRING; 391008.Smal_2759; -.
DR   EnsemblBacteria; ACF52459; ACF52459; Smal_2759.
DR   KEGG; smt:Smal_2759; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   BioCyc; SMAL391008:SMAL_RS14030-MON; -.
DR   Proteomes; UP000001867; 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.
FT   CHAIN           1..443
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000122092"
SQ   SEQUENCE   443 AA;  49326 MW;  3DF3D0E4823F677B CRC64;
     MQPRNNDILT PSQLNTLARD LLEGSFPAIW VEAELGSVAR PSSGHLYFTL KDARAQLRAA
     MFRMKAQYLK FVPREGMRVL VRGKVTLYDA RGEYQMVLDH MEEAGEGALR RAFEELKARL
     EAEGLFDQAR KRPMPAHVQR LAVITSPTGA AVRDVLSVLG RRFPLLEVDL LPTLVQGNSA
     AAQITRLLQA ADASGRYDVI LLTRGGGSLE DLWAFNDEAL ARAIAASRTP VVSAVGHETD
     FSLSDFAADL RAPTPSVAAE LLVPDQRELA LRLRRNAARM VQLQRHTMQQ AMQRADRALL
     RLNAQSPQAR LDLLRRRQLD LGRRLHAAFN QQQERRAARL RHAAAILRGH HPQRQLDAMQ
     RRLAALRGRP QIAMQRLLER DALRLRGLAR SLEAVSPLAT VARGYSILTR SDDGTLVRQV
     DQVQPGDALQ ARVGDGVIDV QVK