EX7L_LIMRJ
ID EX7L_LIMRJ Reviewed; 445 AA.
AC B2G849;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-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=LAR_1115;
OS Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557433;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 1112;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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; AP007281; BAG25631.1; -; Genomic_DNA.
DR RefSeq; WP_003668406.1; NC_010609.1.
DR AlphaFoldDB; B2G849; -.
DR GeneID; 66471254; -.
DR KEGG; lrf:LAR_1115; -.
DR HOGENOM; CLU_023625_2_0_9; -.
DR OMA; WPAVRFE; -.
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..445
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122071"
SQ SEQUENCE 445 AA; 50628 MW; D34EDE00A7A8859E CRC64;
MDRSQYLTVS ELTKYLKMKF DRDPYLHTVY LTGELSNFRL RQKHQYFSLK DDNAVIDAVM
FEHQFRKIKF TPEQGMKVCV VGHVSLYEKS GRYQIYIDRM EPDGLGSLYL AFEQLKKKLS
AEGLFNLPKK QIPMFPKRIA VVTSIDGAVI RDINTTVRRR YPIAQVVLYP TVVQGDKAAA
DIARQINRAN DRGDFDTLII GRGGGSMEDL WPFNEEVVAR AIANSKIPVI SSVGHETDTT
IADLVADQRA ATPTAAAELA TPVKLNDALM TLKDDQNRLL NTMRTKINFD RQQLNKQLQS
YIFQQPTRLY ENYAQKVDQL TQQLGQAAQN KMQELQMNVE RLSGRLTAAS PLHRVQQQEQ
LVDQLKKQLV TASLASQNEK KQQVTTLIKQ LDSLSPLKIM SRGYTYVTSD EKVVNHASQL
TVGQNVHLHF DDGEVQAEIK KVKEH
