ID EX7L_BEII9 Reviewed; 549 AA.
AC B2IJK8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=Bind_1238;
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712;
RX PubMed=20601475; DOI=10.1128/jb.00656-10;
RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA Dunfield P.F.;
RT "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL J. Bacteriol. 192:4532-4533(2010).
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; CP001016; ACB94880.1; -; Genomic_DNA.
DR RefSeq; WP_012384237.1; NC_010581.1.
DR AlphaFoldDB; B2IJK8; -.
DR SMR; B2IJK8; -.
DR STRING; 395963.Bind_1238; -.
DR KEGG; bid:Bind_1238; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_5; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000001695; 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 NCBIfam; TIGR00237; xseA; 1.
DR PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..549
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000205668"
FT REGION 511..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 60338 MW; AE394D2CA4F52C86 CRC64;
MIGHLAAMLP PPSTNSPELT VSELSAALKR TLEDRFGIVR LRGEISNYRG PHSSGHAYFC
LKDQNARIDA VIWKTTFMRL KVKPEEGLEV IATGKITTYA GKSSYQIVVE AIEPAGLGAL
MALFEARRRQ LASEGLFDEE RKRALPFLPA VIGVITSPTG AVIRDILHRI TERFPRPVLL
WPVRVQGETA AAEVSAAIEG FNALPVTGQG PLHRPDLLIV ARGGGSLEDL WGFNEENVVR
AAAASSIPLI AAIGHETDWT LIDYAADLRA PTPTGAAEKA VPVRADLLTS LNDLQRRHAG
AAYRLLERRR SDLRALARAL PQADSLLATP RQRLDRTATR LATACLRAQD QRGLVLGRLA
HRLSRQAPHA SLARLGQKLE AFGRGLGRAC EIAQERRRQS LLHLGIRLTQ NFTQGIRVER
ERVHGRRQKL ASLDNRLRQA MSLTLSQRQA RLANLAQLTR SLSYHAVLAR GFALVRDETG
QPLRRAADII ENHVLTLEFS DGCRQAVAGA LVATDPPVDP KPTRKPVQKS SSPKPSSRKP
KKSQQEDLF
//
