ID A0A1X6WM85_9ENTE Unreviewed; 446 AA.
AC A0A1X6WM85;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=FM121_04715 {ECO:0000313|EMBL:SLM85377.1};
OS Vagococcus fluvialis bH819.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1255619 {ECO:0000313|EMBL:SLM85377.1, ECO:0000313|Proteomes:UP000195918};
RN [1] {ECO:0000313|Proteomes:UP000195918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bH819 {ECO:0000313|Proteomes:UP000195918};
RA Dridi B.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FWFD01000008; SLM85377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6WM85; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000195918; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000195918}.
FT DOMAIN 6..101
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 124..437
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT COILED 321..386
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 446 AA; 51034 MW; 58B9D23A801B9E87 CRC64;
MTEKYLTVTA LTKYLKRKFE ADPYLERIFL TGEISNFRMR PNAHQYFSLK DDQAKISAIM
FKGAFGKLKF QPEEGMKVLV IGRISLYEPG GSYQIYVEHM EPDGVGALYQ ALEERKKAFH
KEGLFNPNFK QPLVKYPKKI AVVTSPSGAV VRDIMTTVKR RYPIAQLVVF PTLVQGDKAA
ADITRRIKEV DQSGEYDTMI VARGGGSIED LWPFNEENVA RAIFEARTPI VSSVGHETDT
TIADLVADVR AATPTAAAEI ATPVLREELL RIKEKENRLF QAMSAQLKHK KQKHEHAVNS
FVFKQPKRLY EAFSVQLDTL NRKLEQSLSQ EINQKEKKFE QMKQRLYFRN PQEKVKISRQ
QIEFLNDKLE KNMERLVESK KIAVSQQIAN LDLLSPLKTM LRGYSYVTID EKIIKSVNEI
DKEQILSVHL SDGVVDTTVT DVVRKD
//
