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Database: UniProt
Entry: A0A0S8JTB4_9BACE
LinkDB: A0A0S8JTB4_9BACE
Original site: A0A0S8JTB4_9BACE 
ID   A0A0S8JTB4_9BACE        Unreviewed;       466 AA.
AC   A0A0S8JTB4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|RuleBase:RU004355};
DE            EC=3.1.11.6 {ECO:0000256|RuleBase:RU004355};
GN   ORFNames=AMS26_18810 {ECO:0000313|EMBL:KPL12069.1};
OS   Bacteroides sp. SM23_62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL12069.1, ECO:0000313|Proteomes:UP000050819};
RN   [1] {ECO:0000313|EMBL:KPL12069.1, ECO:0000313|Proteomes:UP000050819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_62 {ECO:0000313|EMBL:KPL12069.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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|RuleBase:RU004355};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004355}.
CC   -!- SIMILARITY: Belongs to the XseA family.
CC       {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:KPL12069.1}.
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DR   EMBL; LJUP01000227; KPL12069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8JTB4; -.
DR   PATRIC; fig|1703352.3.peg.1460; -.
DR   Proteomes; UP000050819; 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-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR   CDD; cd04489; ExoVII_LU_OBF; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|RuleBase:RU004355};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004355};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU004355}.
FT   DOMAIN          10..117
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          142..455
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   466 AA;  53423 MW;  8224900644D5FAF4 CRC64;
     MEAGNRHTMK LSDLQEEIRE VIQSSFETPR WIICEIMDIT QNYSGHCYLD LIEKDEKSDK
     ILARARATIW ASSYRMLKPY FETSTGYELS SGIKILVLAR VEFHPVYGLS LNIQDIDPSY
     TLGDVERKKR EIILRLENEG VLDMNKEIPL PIVPQRIAVV SSMSAAGYED FMDQLRGNPY
     GYQFYTRLFP AVMQGENAAQ SIIESLERIF EYESHFDAVV IIRGGGSKSD LACFDSYDLA
     YHVSQFPLPV ITGIGHEQDD TITDLVAHTR LKTPTAVAGF FIDKLASFEG ELEEFQAVLI
     NATLTILNEQ KLRLQLYQQK YVSGSIAMVR ARQEYLLKLT GNARFQIQQQ LRFYDQLILR
     FMEQLRSTAK YIPQRIAIES LHVMQRFKQL INNKMEGEAK RLEEYHRLVA YAEPGQILKM
     GFSISRMDGK ALKDVKNTSP GSIVETELYS GKFKSKVIDI QKKNIL
//
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