ID Q5NFP1_FRATT Unreviewed; 461 AA.
AC Q5NFP1; A0A0G2RP00;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|RuleBase:RU004355};
DE EC=3.1.11.6 {ECO:0000256|RuleBase:RU004355};
GN Name=xseA {ECO:0000313|EMBL:CAG45823.1};
GN OrderedLocusNames=FTT_1190c {ECO:0000313|EMBL:CAG45823.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45823.1, ECO:0000313|Proteomes:UP000001174};
RN [1] {ECO:0000313|EMBL:CAG45823.1, ECO:0000313|Proteomes:UP000001174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG45823.1; -; Genomic_DNA.
DR RefSeq; WP_003021434.1; NZ_CP010290.1.
DR RefSeq; YP_170151.1; NC_006570.2.
DR AlphaFoldDB; Q5NFP1; -.
DR DNASU; 3192120; -.
DR EnsemblBacteria; CAG45823; CAG45823; FTT_1190c.
DR KEGG; ftu:FTT_1190c; -.
DR PATRIC; fig|177416.36.peg.1616; -.
DR OrthoDB; 7235451at2; -.
DR Proteomes; UP000001174; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001174}.
FT DOMAIN 6..113
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 138..452
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 461 AA; 52236 MW; DED844D379EA9FFC CRC64;
MQQSLKLSEF LELMKSTIEM SFGYEGFWIV AELSEWRKSG KHYYGELIEH DGISKYPIAK
IRCNCWANKA DYIHNKFSLV TGEKLSSDMK VLMKVTVSYH ISFGLSLNIV DIDPAFTLGD
RQARKIGILE KLAKKGILEK NKSLAMPYDF TSIAVITSIT AAGKGDFFEE ADKLQDLGLC
NFDIYEAKMQ GAECSESVST AFAKIEAKAF DYDAIVVIRG GGSQADLDWF NNITPAESIC
NSKIPVMIGI GHERDTTVLD EICTKRFDTP SKVINFIANI IITNAKNAKY NYADILKITN
NSVKQNKHQL DSLYHNFKTK IEHYLYQTNQ NIEHNYKATI SIARGLVKLY GKSMDMQYDN
IISNSQNLIK NSQHNLEESY NHSLSIAKNV IKYYNQASEY LYKQILSISI EPTLRRGFSI
TKTKDGKYIT SQKQAQKYLN LEIIYADGQV QVEVKNNGNA N
//