EX7S_AERS4
ID EX7S_AERS4 Reviewed; 83 AA.
AC A4SJQ1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Exodeoxyribonuclease 7 small subunit {ECO:0000255|HAMAP-Rule:MF_00337};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00337};
DE AltName: Full=Exodeoxyribonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337};
DE Short=Exonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337};
GN Name=xseB {ECO:0000255|HAMAP-Rule:MF_00337}; OrderedLocusNames=ASA_0992;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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_00337}.
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_00337};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00337}.
CC -!- SIMILARITY: Belongs to the XseB family. {ECO:0000255|HAMAP-
CC Rule:MF_00337}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000644; ABO89123.1; -; Genomic_DNA.
DR RefSeq; WP_005317577.1; NC_009348.1.
DR AlphaFoldDB; A4SJQ1; -.
DR SMR; A4SJQ1; -.
DR STRING; 382245.ASA_0992; -.
DR EnsemblBacteria; ABO89123; ABO89123; ASA_0992.
DR GeneID; 60851483; -.
DR KEGG; asa:ASA_0992; -.
DR eggNOG; COG1722; Bacteria.
DR HOGENOM; CLU_145918_3_3_6; -.
DR OMA; PLNDYKG; -.
DR OrthoDB; 2057189at2; -.
DR Proteomes; UP000000225; 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:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.1040; -; 1.
DR HAMAP; MF_00337; Exonuc_7_S; 1.
DR InterPro; IPR003761; Exonuc_VII_S.
DR InterPro; IPR037004; Exonuc_VII_ssu_sf.
DR PANTHER; PTHR34137; PTHR34137; 1.
DR Pfam; PF02609; Exonuc_VII_S; 1.
DR PIRSF; PIRSF006488; Exonuc_VII_S; 1.
DR SUPFAM; SSF116842; SSF116842; 1.
DR TIGRFAMs; TIGR01280; xseB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT CHAIN 1..83
FT /note="Exodeoxyribonuclease 7 small subunit"
FT /id="PRO_0000303684"
SQ SEQUENCE 83 AA; 9341 MW; 8FDD8F360BC6D323 CRC64;
MASKKIDRLS FDATLEELET IVHQLEQGSL PLEEALKQFE QGVHLVRAGQ QKLEQAEQKI
QILLTQADGT EQAVPFQPEQ GEE