ID A0A0W8JII0_9VIBR Unreviewed; 446 AA.
AC A0A0W8JII0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=VRK_07050 {ECO:0000313|EMBL:KUI99992.1};
OS Vibrio sp. MEBiC08052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI99992.1, ECO:0000313|Proteomes:UP000054473};
RN [1] {ECO:0000313|EMBL:KUI99992.1, ECO:0000313|Proteomes:UP000054473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI99992.1,
RC ECO:0000313|Proteomes:UP000054473};
RA Kim Y.J., Lee J.-H., Kwon K.K.;
RT "Genome sequence of Vibrio sp. MEBiC08052.";
RL Submitted (DEC-2015) 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:KUI99992.1}.
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DR EMBL; LQIY01000004; KUI99992.1; -; Genomic_DNA.
DR RefSeq; WP_059120098.1; NZ_KQ947475.1.
DR AlphaFoldDB; A0A0W8JII0; -.
DR STRING; 1761910.VRK_07050; -.
DR PATRIC; fig|1761910.3.peg.709; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000054473; 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}.
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 446 AA; 50760 MW; 976E7078CC4D40DB CRC64;
MLSANNQNIY TVSRLNAEVR LLLENEMGII WLLGEVSNFS MPVSGHWYLS LKDARAQVKC
AMFKGNNRFV SFKPQNGQQV LVRARLSLYE PRGDYQLIIE SMQAEGDGRL QQEFEQLKQK
LTAEGLFAPD NKKPLPEHPQ CIGIITSKTG AALFDILDVL KRRDPTLPVI IYPTIVQGED
AAIRIAQAIG RANARQECDV LIVGRGGGSL EDLWCFNHEI VARTIAASQI PIVSAVGHEI
DITIADFVAD VRAPTPSAAA ELVSRDSSYK RTGLLNYHHR LSQAIRYYLA AQRQKSQTHQ
YALEKQHPTY RLERQIQQMD ELSIRLQQAI QRYLDRHSQM MERTAYQLRY HSPEQQIRQQ
HYLLTKYEQR YIDAMERKLL NSRHQLALAA ETLEAVSPLS TLRRGYSVTQ NQAGQIIRRL
RDVKPGECIT TRLTDGTIHS TVTQSD
//
