ID G2GXI2_9ENTR Unreviewed; 451 AA.
AC G2GXI2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378};
GN ORFNames=Rin_00004740 {ECO:0000313|EMBL:EGY29544.1};
OS Candidatus Regiella insecticola 5.15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY29544.1, ECO:0000313|Proteomes:UP000004116};
RN [1] {ECO:0000313|EMBL:EGY29544.1, ECO:0000313|Proteomes:UP000004116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5.15 {ECO:0000313|Proteomes:UP000004116};
RX PubMed=21948522; DOI=10.1101/gr.125351.111;
RA Hansen A.K., Vorburger C., Moran N.A.;
RT "Genomic basis of endosymbiont-conferred protection against an insect
RT parasitoid.";
RL Genome Res. 22:106-114(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_00378,
CC ECO:0000256|RuleBase:RU004355};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC ECO:0000256|RuleBase:RU004355}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGY29544.1}.
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DR EMBL; AGCA01000103; EGY29544.1; -; Genomic_DNA.
DR RefSeq; WP_006706176.1; NZ_AGCA01000103.1.
DR AlphaFoldDB; G2GXI2; -.
DR PATRIC; fig|1005043.3.peg.436; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000004116; Unassembled WGS sequence.
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 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, ECO:0000256|HAMAP-Rule:MF_00378};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00378};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378};
KW Reference proteome {ECO:0000313|Proteomes:UP000004116}.
FT DOMAIN 10..103
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 126..440
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 451 AA; 51471 MW; 52EA45083C9AC2EE CRC64;
MPSISAPSIF TVSQLNQNVR QLLEREMRQI RLSAEISNFS QPSSGHWYFT LKDDQAQVRC
VMFRNSNRFV TFKPGNGQQV LIRASITLYE SRGDYQLIAE NMQPAGDGLL QQQFEQLKQQ
LTAEGLFKQD HKKPLPHSAK QIGVITSIHG AVLHDVLQVL QRRDPSLPVV IYPTSVQGVD
APWQIIKAIE IANQRAECDV LIVCRGGGAL EDLWSFNDER VVRAIFNSRL PIVSAVGHET
DVTLADFVAD LRAPTPSAAA ELLSRDQLEL MRQIAVQQQR MAMALDYYLA RCQRQFSQFK
HRLQQRHPQL QLANQQTELV RLQNRLEQAI STQMAEQLQQ LHFLQQRLTK LPLLEYLYGY
HQRIQQQAYC LKQALERQCN QYRQRFSVVC SRLEAVSPLA ILARGYNVTH TSAGTVLNSI
RQGHRGEKII TRLQDGSIES EITQINAVKN R
//
