EX7L_CUPPJ
ID EX7L_CUPPJ Reviewed; 448 AA.
AC Q475F5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=Reut_A0596;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ59978.1; -; Genomic_DNA.
DR AlphaFoldDB; Q475F5; -.
DR STRING; 264198.Reut_A0596; -.
DR EnsemblBacteria; AAZ59978; AAZ59978; Reut_A0596.
DR KEGG; reu:Reut_A0596; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_4; -.
DR OMA; WPAVRFE; -.
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_0000273680"
SQ SEQUENCE 448 AA; 49213 MW; 9BA5FB953B7A2EDC CRC64;
MPARNPREAI PVGELNHAIA TMLERGFPLT WVRGEISNFT RAASGHWYFS LKDARAQIRC
VMFRGRNQHV DFTPREGEAV EVRAVVTLYE ARGDLQLGVE AMRRAGLGNL YEAFLRLKEK
LAQAGLFAPE RKRPVPSHPR SIGIVTSLQA AALRDVLTTL RRRAPHVPVT VYPVPVQGAG
AAQKIADMLD QASARRECDV IILCRGGGSI EDLWSFNEEA VAHAIARSAV PVVSGVGHET
DFTIADFVAD VRAPTPTGAA ELVSPDRGHL LGLTRRAGDA LVQSMRRELD RRAQHLDWLA
RRVRSPLAQL QERRARVDNL ARHLRSALRE TVVAQRHRQQ LLAIRWTACR PDMAAASADV
ARLSQRMQAA ATRTHERQTQ RLARVAGALE LLAPQRTLER GYAVLLDQRG RALRSPAELR
AGSVVEAHLA DGVADIAIAG VQAKLGGI
