ID A0A1G6AVT2_9FIRM Unreviewed; 403 AA.
AC A0A1G6AVT2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN02910298_00644 {ECO:0000313|EMBL:SDB12516.1};
OS Pseudobutyrivibrio sp. YE44.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520802 {ECO:0000313|EMBL:SDB12516.1, ECO:0000313|Proteomes:UP000198713};
RN [1] {ECO:0000313|Proteomes:UP000198713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE44 {ECO:0000313|Proteomes:UP000198713};
RA Varghese N., Submissions S.;
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; FMXT01000001; SDB12516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6AVT2; -.
DR STRING; 1520802.SAMN02910298_00644; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000198713; 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; 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}.
FT DOMAIN 6..102
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 125..320
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT DOMAIN 266..393
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 403 AA; 44785 MW; 4608197B7772ECF1 CRC64;
MNKNVYSVSQ INTYIERMFA DDFMLGNLSL SGEVSNCKYN HTGHIYFTLK DEKSAISCVM
FAGKRAKGLK FQMKDGDQVV VTGYVGVYSP HGKYQVYANE IELAGVGDLY QRFEALKAEL
EESGMFDPMY KKPLPSHAMR IGVVTASTGA AVHDIIRVSK TRNPFVSIIL YPAQVQGEGA
VPSIISGIQR LDEMNLDVLI VGRGGGSIED LWAFNEEAVA RAIFKANTPI ISAVGHETDF
TIADFVADKR AATPSQAAEL ANFVYQDFAG KLERYSDKLN RDLDFKITAY EERLMSMKQR
LQLLRPENKI KANEERFKHL SLLINNLMDS KLDRYSNRLV ALSGRLDGLS PAKKLATGFG
YVTDDSGTRV DSIDQLSVGN GLSIRIKDGQ INTEITELIP YKD
//
