EX7L_BACC2
ID EX7L_BACC2 Reviewed; 452 AA.
AC B7IXH1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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};
GN OrderedLocusNames=BCG9842_B0944;
OS Bacillus cereus (strain G9842).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
RL Submitted (OCT-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; CP001186; ACK96888.1; -; Genomic_DNA.
DR RefSeq; WP_000415249.1; NC_011772.1.
DR AlphaFoldDB; B7IXH1; -.
DR SMR; B7IXH1; -.
DR EnsemblBacteria; ACK96888; ACK96888; BCG9842_B0944.
DR GeneID; 67508817; -.
DR KEGG; bcg:BCG9842_B0944; -.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000006744; 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..452
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122039"
SQ SEQUENCE 452 AA; 51310 MW; 37BC17866A191476 CRC64;
MEKQYLTVTA LTRYIKTKIE YDPHLQSVWL KGEISNFKNH SRGHMYFTLK DENARIAAVM
FAGHNRNIKF KPENGMKVLV KGKISVYEAS GSYQIYIQDM QPDGVGNLHL AYEQLKVRLE
EEGLFSQVYK KAIPPYAKTI GVITSPTGAA IRDIITTIKR RYPIGNVIVF PVLVQGESAA
PSIVQAIRTA NEMGEIDVLI VGRGGGSIEE LWAFNEEMVA RAIFKSEIPI ISAVGHETDF
TIADFVADLR APTPTAAAEL AAPNIIELQE KVLQRTLRLQ RAMRELVHKK EEKLQVLQKS
YAFRYPRQVY EQKEEQLDRA LEQLVLAKER YIDKKVNQLK QLSFYLEKHH PSQKIMQTKV
AVETLQKQLQ REMQTLLQTK EFAFVRAAQK LEALSPLKVM MRGYGLVYDE EKQVLKSVKD
VSLGDAVSVQ LQDGILDCSV SGIEERELNN GK