EX7L_STRU0
ID EX7L_STRU0 Reviewed; 442 AA.
AC B9DUT9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=SUB1276;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR42780.1; -; Genomic_DNA.
DR RefSeq; WP_012658750.1; NC_012004.1.
DR AlphaFoldDB; B9DUT9; -.
DR SMR; B9DUT9; -.
DR STRING; 218495.SUB1276; -.
DR EnsemblBacteria; CAR42780; CAR42780; SUB1276.
DR KEGG; sub:SUB1276; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000000449; 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..442
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200686"
SQ SEQUENCE 442 AA; 50209 MW; 5F4262F44517DB87 CRC64;
MSDYLSVSHL TKYLKMKFDR DPYLERVYLT GQVSNFRKRP NHQYFSLKDE NAVIQATMWA
SAYKRLAFDL EEGMKINVIG RVQIYEPSGS YSIIIEEAVP DGIGALAIQF EQLKKKLTNE
GFFDDKHKQD LPQFVQKVGV ITSPSGAVIR DIITTISRRF PGVEILLFPT KVQGEGAAEE
IVANISKANQ REDLDLLIVG RGGGSIEDLW AFNEEIVVHA IFASQLPIIS SVGHETDVTL
SDFVADRRAA TPTAAAELAT PVTKADIISW ISERQNRSYQ ATLRLLHQKR DQVMVLGQSV
IFRQPERLYD AYLQKIDRLH NSLLNSIKSK LSDSRQAEMT VSHRLQTMNL LSTINRYQER
LMTLNQWLNV DMQKQFDQLR TRFEKAQDAL LTLDTKRIVA RGYSIVRQED KIISSVKDVS
TGDLLAIEMR DGQIEVEVKN GN
