EX7L_BRUAB
ID EX7L_BRUAB Reviewed; 511 AA.
AC Q578P4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-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=BruAb2_0468;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; AE017224; AAX75890.1; -; Genomic_DNA.
DR RefSeq; WP_002968954.1; NC_006933.1.
DR AlphaFoldDB; Q578P4; -.
DR SMR; Q578P4; -.
DR EnsemblBacteria; AAX75890; AAX75890; BruAb2_0468.
DR GeneID; 3827916; -.
DR KEGG; bmb:BruAb2_0468; -.
DR HOGENOM; CLU_023625_3_1_5; -.
DR OMA; LVWPVKV; -.
DR PRO; PR:Q578P4; -.
DR Proteomes; UP000000540; Chromosome II.
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..511
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000273648"
SQ SEQUENCE 511 AA; 56363 MW; 6765E8983A45DB42 CRC64;
MASDSSFPGA SSNVAEYSVS EISGALKRTV EDTFGHVRVR GEISGYRGPH SSGHAYFALK
DDRARLEAVI WRGSMSRLRF RPEEGMEVIA TGKLTTYPGS SKYQIVIEQM EPAGAGALMA
LLEERKQRLA AEGLFDPTLK QLLPFMPRVI GVVTSPTGAV IRDIIHRISD RYPLRVIVWP
VRVQGDTCGP EVATAVNGFN TLPDDGPIPR PDVLIVARGG GSLEDLWGFN DEIVVRAVAA
SHIPVISAVG HETDWTLIDL AADMRAPTPT GAAEMAVPVK ADLQASLASQ SARLSSAMSR
FFDQKRQAHR AAARAMPSAD QLLALPRRRF DEAASRLTRA LFVNTQKKRV HFDGHARQLS
PRLLQRRLVE LERGVTMLGQ RLPRALEAFL RERRTAFTHR ANRLSPEPIL RRTRLTGSTL
EQLDRRRDQA VRLLIERVKR RSQELDRLMR TLSYESVLER GFAVVFDAQG KPVKQAAAVS
PGDALSVRFR DGDVGVVARA GLTIPDPTKG Q
