ID A0A1I5W361_9LACT Unreviewed; 446 AA.
AC A0A1I5W361;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN04488506_0741 {ECO:0000313|EMBL:SFQ14194.1};
OS Desemzia incerta.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae; Desemzia.
OX NCBI_TaxID=82801 {ECO:0000313|EMBL:SFQ14194.1, ECO:0000313|Proteomes:UP000199136};
RN [1] {ECO:0000313|EMBL:SFQ14194.1, ECO:0000313|Proteomes:UP000199136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20581 {ECO:0000313|EMBL:SFQ14194.1,
RC ECO:0000313|Proteomes:UP000199136};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOXW01000002; SFQ14194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5W361; -.
DR STRING; 82801.SAMN04488506_0741; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000199136; 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:UP000199136}.
FT DOMAIN 6..100
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 126..435
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT COILED 278..328
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 353..380
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 446 AA; 51017 MW; 4A7AE893A45E87E4 CRC64;
MSNEYLTVST LTKYIKRKFD VDPYLERVYL TGEISNFRNR PGHQYFSLKD NNAVISATMF
KSAYQRLKFT PEEGMKVLVI GRVSVYSDQG KYQIYIEHME PDGVGALYQA LEEMKKKLKN
EGLFDAPKKL LPTFPKRIAV VTSPSGAVIR DIMTTVKRRF PIAELVLFPT KVQGKQAADT
IVESIRQVEE KGDFDTLIIA RGGGSIEDLW PFNEEKVARA IFAAQTPVIS SVGHETDTTI
ADLVADVRAA TPTAAAELAV PQLTEEILKI DQVHLRLLKS YQRKVERAEE RLKHSLNSYV
FRQPQRLYEG YTQNLDLLTE RLEREMSEKI TSYQQDLRVY NMQLQSHNPL NLVRQKEDNL
QQVTAQLKVQ INRYMEAQQQ RLDYGIQSLD YLSPLKIMHR GYSYALKDDT IIKSTNDVNI
GETIDIHLSD GKLTAKVTEK MEDTHG
//
