EX7L_BRUMB
ID EX7L_BRUMB Reviewed; 511 AA.
AC C0RLR7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=BMEA_B0742;
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457;
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-2009) 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; CP001489; ACO02550.1; -; Genomic_DNA.
DR RefSeq; WP_004686015.1; NC_012442.1.
DR AlphaFoldDB; C0RLR7; -.
DR SMR; C0RLR7; -.
DR EnsemblBacteria; ACO02550; ACO02550; BMEA_B0742.
DR KEGG; bmi:BMEA_B0742; -.
DR HOGENOM; CLU_023625_3_1_5; -.
DR OMA; LVWPVKV; -.
DR PRO; PR:C0RLR7; -.
DR Proteomes; UP000001748; 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_1000200662"
SQ SEQUENCE 511 AA; 56347 MW; 799106944B4600E7 CRC64;
MASDSSFPGA SSNVAEYSVS EISGALKRTV EDTFGHVRVR GEISGYRGPH SSGHAYFALK
DDRARLEAVI WRGSMSRLRF RPEEGMEVIA TGKLTTYPGS SKYQIVIEQM EPAGAGALMA
LLEERKQRLA AEGLFDPALK 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
PGDALSIRFR DGDVGVVARA GLTIPDPTKG Q
