GenomeNet

Database: UniProt
Entry: A0A150N0Y7_9BACI
LinkDB: A0A150N0Y7_9BACI
Original site: A0A150N0Y7_9BACI 
ID   A0A150N0Y7_9BACI        Unreviewed;       449 AA.
AC   A0A150N0Y7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378};
GN   ORFNames=B4113_0296 {ECO:0000313|EMBL:KYD30262.1};
OS   Geobacillus sp. B4113_201601.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1586290 {ECO:0000313|EMBL:KYD30262.1, ECO:0000313|Proteomes:UP000075654};
RN   [1] {ECO:0000313|EMBL:KYD30262.1, ECO:0000313|Proteomes:UP000075654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4113_201601 {ECO:0000313|EMBL:KYD30262.1,
RC   ECO:0000313|Proteomes:UP000075654};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_00378,
CC         ECO:0000256|RuleBase:RU004355};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC       ECO:0000256|RuleBase:RU004355}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYD30262.1}.
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; LQYX01000014; KYD30262.1; -; Genomic_DNA.
DR   RefSeq; WP_033019353.1; NZ_LQYX01000014.1.
DR   AlphaFoldDB; A0A150N0Y7; -.
DR   PATRIC; fig|1586290.3.peg.444; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000075654; Unassembled WGS sequence.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00378};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378}.
FT   DOMAIN          7..101
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          124..439
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   COILED          280..330
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   449 AA;  51178 MW;  F8959B55AFA166BB CRC64;
     MEVKYVTVGA LTKYIKRKFD VDPHLRDLWV KGEISNFKQH SRGHMYFTLK DSQGRIAAVM
     FAGYNQHLPF RPEDGMNVLA RGEISVYEPN GNYQLYVKEM QPEGVGSLYL AYEQLKQRLE
     AEGLFASAHK KPLPAFPRCI GVVTSPTGAA VRDIMTTIRR RYPLAKVILF PALVQGEGAA
     SSIARAIERA NELGAVDVLI VGRGGGSIEE LWAFNEEMVA RAIFASRVPI ISAVGHETDF
     TIADFVADLR APTPTAAAEL AVPHVGELAE RLAERKWRLI RAMKERLAAG RERLDRLQAS
     YAFRYPKRLY EQKEQQFDAL LERLHRQRRS YVDEKHRQLR ELGLRLWRHH PAAELERVKE
     RQIAAATALK KAMRSALERH AFRFRSHLAR LEALSPLRVM ERGYSLVYNE RGELVKRLSQ
     LAVGERLSVR VQDGRVNCQV MGVEEKRDE
//
DBGET integrated database retrieval system