ID   I2F4X6_9BACT            Unreviewed;       513 AA.
AC   I2F4X6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|RuleBase:RU004355};
DE            EC=3.1.11.6 {ECO:0000256|RuleBase:RU004355};
GN   ORFNames=Theba_1291 {ECO:0000313|EMBL:AFK06979.1};
OS   Mesotoga prima MesG1.Ag.4.2.
OC   Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX   NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK06979.1, ECO:0000313|Proteomes:UP000002881};
RN   [1] {ECO:0000313|EMBL:AFK06979.1, ECO:0000313|Proteomes:UP000002881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX   PubMed=22798451;
RA   Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA   Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA   Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT   "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT   MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL   Genome Biol. Evol. 4:700-708(2012).
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}.
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DR   EMBL; CP003532; AFK06979.1; -; Genomic_DNA.
DR   RefSeq; WP_014730955.1; NC_017934.1.
DR   AlphaFoldDB; I2F4X6; -.
DR   STRING; 660470.Theba_1291; -.
DR   KEGG; mpg:Theba_1291; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_4_2_0; -.
DR   Proteomes; UP000002881; 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-EC.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR   InterPro; IPR003753; Exonuc_VII_L.
DR   InterPro; IPR020579; Exonuc_VII_lsu_C.
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.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000256|RuleBase:RU004355, ECO:0000313|EMBL:AFK06979.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU004355};
KW   Nuclease {ECO:0000256|RuleBase:RU004355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002881}.
FT   DOMAIN          155..504
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   513 AA;  57735 MW;  0077A99E94BB026C CRC64;
     MEEETLEFKD LDNMLEHIRT ILTDAGLNNL RVKFPADVTN INVRGSYVYI NVSQDYVERG
     TKRRIDLSMI SGTSAFARMG RQLALKSSSD LKGKKWLFEG TLSFYKPRAS FSIWIDTIAP
     IGESDIAARR REIYLALKAR NALRTEEHDL AELPPIKRIA VISSSTAAGL GDFFSNLSLQ
     YPYKPIVHLF ESYMQGNRTV PGILSALRKI ASCPVKYDVV VLTRGGGSAS DLMYFDNLDL
     GSAISDFNKT YCPVLSAIGH ERDFTIPDFV AWKRFDTPTA VARGITEQVN EYVASLEEFA
     NHLDDEMNWL FQRACDETDP KRLGIMLDRI EDNMNRTEHF FEDEIRVLSG TILHRIGQAV
     NELGSFNPTR YVLSIERTMN EILAVTEGLI NRAETTIQRS FHYSESQLDY AGLRNQLDRH
     LMNANGQVEL LDKGILRLFD DKINEAGNDL DDLFNDLTLH GGYAASLLFG GVVLKKADRI
     VNSVRIISPG DEVDCIFKDG EAKATIDEVK SEV
//