EX7L_NITEC
ID EX7L_NITEC Reviewed; 448 AA.
AC Q0AFX7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=Neut_1510;
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57;
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(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; CP000450; ABI59755.1; -; Genomic_DNA.
DR RefSeq; WP_011634561.1; NC_008344.1.
DR AlphaFoldDB; Q0AFX7; -.
DR STRING; 335283.Neut_1510; -.
DR PRIDE; Q0AFX7; -.
DR EnsemblBacteria; ABI59755; ABI59755; Neut_1510.
DR KEGG; net:Neut_1510; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_4; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001966; 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.
FT CHAIN 1..448
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000060029"
SQ SEQUENCE 448 AA; 51541 MW; B7EEB80DD018F8CE CRC64;
MTDNNLFPEP KKIVWRVSEL NRHVRVILEQ TFPLLWVSGE ISNLKRYPSG HWYFSLKDDN
AQVRCVMFRH KNMYLDWMPQ DGAQVEAQAL ITLYEARGEF QLTIERLRRA GLGVLFETFE
RLKTRLQQEG LFNPEYKQLI PPYPQQIGII TSTNTAALRD VLTTLQRRLP SLPVVIYPAP
VQGKEAASAI VTALQIATQR SECDVLILCR GGGSIEDLWA FNEEIVARAI AACPIPIVTG
IGHETDFTIA DFVADMRAPT PTGAAQLAAP DRQDILHRLQ YWQHRLQQAI ERNIERRMQT
TDLLAHRLVH PGERIRYQLI HLSQLHNRLL HAWSRQLEVC KWRIEAFRRR IQFTKPDINT
GKRYQQELAA RLQRAMVYRL ESLQVQLIRQ QQHLAHLDPK AVLERGYSIT YTAGGEILQD
SQQIHTGDNV QIVFAKGSAK ANITETNK
