ID A0A371AZ40_9FIRM Unreviewed; 403 AA.
AC A0A371AZ40;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ECO:0000313|EMBL:RDU24868.1};
GN ORFNames=DWV06_02515 {ECO:0000313|EMBL:RDU24868.1};
OS Anaerosacchariphilus polymeriproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerosacchariphilus.
OX NCBI_TaxID=1812858 {ECO:0000313|EMBL:RDU24868.1, ECO:0000313|Proteomes:UP000255036};
RN [1] {ECO:0000313|EMBL:RDU24868.1, ECO:0000313|Proteomes:UP000255036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCWD5 {ECO:0000313|EMBL:RDU24868.1,
RC ECO:0000313|Proteomes:UP000255036};
RA Kim W., Yang S.-H., Oh J., Lee J.-H., Kwon K.K.;
RT "Anaerosacharophilus polymeroproducens gen. nov. sp. nov., an anaerobic
RT bacterium isolated from salt field.";
RL Submitted (JUL-2018) 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}.
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:RDU24868.1}.
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DR EMBL; QRCT01000010; RDU24868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371AZ40; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000255036; 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 Gene3D; 2.40.50.1010; -; 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; 2.
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:UP000255036}.
FT DOMAIN 5..99
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 123..300
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT DOMAIN 272..391
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 403 AA; 46253 MW; 95CCCB277FFEA198 CRC64;
MQNVYSVGQV NKYIKTMFEQ DFFLKRIYIK GEVSNCKYHS TGHIYFTLKD ETGSMAVVMF
AGQRKGLAFR LTEGQKIIVL GSVSVYERDG KYQLYAQEIV LDGIGALYQR FEQLKQELEE
MGMFSVEYKR PIPRFIKKLG VVTAPTGAVI HDISNVAYRR NPYIQIILYP AFVQGEGAKE
SIVKGIQKLD QMGLDCIIVG RGGGSIEDLW AFNEECVARA IFECTTPVIS AVGHETDVTI
ADYVADLRAP TPSAAAELAV YDLQLLQQFL IEKSFEFKRA LQDKIKMERK RIEKYEMQFK
HLSPQSKIRD KRQYLMNQEE KINICFQKIL QNKKHRLQIY IEKFKGLSPL DKLQQGYSFV
ENHEHHAISR IGQVQIGDSL QIHVSDGTIK TQVEQIEAVR REL
//
