EX7L_BORA1
ID EX7L_BORA1 Reviewed; 452 AA.
AC Q2KZF3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=BAV2097;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49707.1; -; Genomic_DNA.
DR RefSeq; WP_012417763.1; NC_010645.1.
DR AlphaFoldDB; Q2KZF3; -.
DR STRING; 360910.BAV2097; -.
DR EnsemblBacteria; CAJ49707; CAJ49707; BAV2097.
DR GeneID; 41393933; -.
DR KEGG; bav:BAV2097; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_4; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001977; 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..452
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303776"
SQ SEQUENCE 452 AA; 48854 MW; A5020D96F6DCD9CA CRC64;
MTTGFAAKDD VFARDILSVA QLNQAVGQLM ERSIPPLWVR GEVSNFTQAA SGHWYFTLKD
AGAAVRTVMF RGRASMVGFV PRPGDEVEIR GRVSLYEPRG DYQLQADAMR RAGVGNLFEA
FSRLKDKLAS EGLFDASRKR VPLRLPRAIG VVTSLQAAAL RDVLSALARR APQVEIVIYP
APVQGADAAS RLAAQVRQAS ARREVDTLLL VRGGGSIEDL WSFNDEDLAR AVADCAIPVI
SGVGHETDFT IADFVADLRA PTPTAAAELA CVPRAELLSA LGHAASRLSR AQQRRLDLAA
QRLDRASAQL VSPAQRLAHQ CERLNTLRHR LAASAQRPLA ASAARLTGLA QRLARRAPQT
ARVQDRVQSL AQRLLRGQQA GLAERGVRLQ ALAAQLRALD PEHTLARGYA VLRDAQGRVV
SNASALVVGE GVRIDLAQGR VQADITDVQP RR