EX7L_NITSB
ID EX7L_NITSB Reviewed; 416 AA.
AC A6Q232;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=NIS_0427;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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_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:0000255|HAMAP-Rule:MF_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
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DR EMBL; AP009178; BAF69541.1; -; Genomic_DNA.
DR RefSeq; WP_012081804.1; NC_009662.1.
DR AlphaFoldDB; A6Q232; -.
DR STRING; 387092.NIS_0427; -.
DR EnsemblBacteria; BAF69541; BAF69541; NIS_0427.
DR KEGG; nis:NIS_0427; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; DFTIIDY; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001118; 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: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 PANTHER; PTHR30008; PTHR30008; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..416
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000048777"
SQ SEQUENCE 416 AA; 47011 MW; C25206ED5C3376DC CRC64;
MNVYTVSQLN EQIKNLLESH FVEVYVEGEV SRPTYHTSGH LYFSLKDEKS VIRCVMFRSA
LAKVPFRVED GQKLIVAGKI GVYKPRGEYQ LYATELHPSG VGSLQLAFEQ LKAKLEKKGY
FASELKKPLP DFIQTIALVT SQTGAALQDM LRIIQNRWPL VKVYVVDTLV QGSDAAPMIA
RSIAYADGLG VDVIVVGRGG GSLEDLWPFN EEIVADAIFE AKTPIVSAVG HEIDFLISDF
VADLRAPTPS AAMEMILPDR QEMLMHLDLL MQRLTKRMQT ILQLKTQELG HLQNSLFQLS
PQKRLEFYEK EITIMNERMN ETITAILKNS SHEIPHLKAL FDQKIEWIWK QKKQDLTSLQ
QKLTMTMEAK KIPKNSAQMV KNGKPVSLED IDVGDEVELQ DVHYKALAKI LSKDAL
