ID A0A0W0W0D0_9GAMM Unreviewed; 443 AA.
AC A0A0W0W0D0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:KTD25682.1};
GN ORFNames=Llan_0072 {ECO:0000313|EMBL:KTD25682.1};
OS Legionella lansingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD25682.1, ECO:0000313|Proteomes:UP000054869};
RN [1] {ECO:0000313|EMBL:KTD25682.1, ECO:0000313|Proteomes:UP000054869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD25682.1,
RC ECO:0000313|Proteomes:UP000054869};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTD25682.1}.
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DR EMBL; LNYI01000003; KTD25682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0W0D0; -.
DR STRING; 45067.Llan_0072; -.
DR PATRIC; fig|45067.4.peg.75; -.
DR eggNOG; COG1570; Bacteria.
DR Proteomes; UP000054869; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054869}.
FT DOMAIN 9..100
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 125..437
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 443 AA; 49693 MW; 5BA34AC7CAC4D950 CRC64;
MMQHDKPALS ISQLNRQIRL WLENEIGEVT VVGELSNLTK PNSGHFYFTL KDPGAQLRCV
YFRNHHSLNS KHFKDGQQVL ATGRLSVYEA RGDYQLIVYS LTEAGLGELY RQFEELKAKL
QVQGLFDSNR KKIIPRFPSV IGVITSPTGA ALHDILTTLA RRYPLARVKI YTSEVQGKDA
AQQLIKALSK ANEDKDAEVL ILARGGGSIE DLWAFNNEQL ALAISQSSIP IVSGIGHETD
FTIADFVADL RAATPTAAAE AVTPNRIDLA ASLKDLEQRA LSSITRYTQH KQLLLSNRIA
KILSPQQLIA RHWQTLDFLE RQLYQCMQSL LYQKKNTLHL FITKLQGKNP KALLQHSEIK
IRGIEQQLIQ HIKNKLSELK QTFTTRLATL HAVSPLATLE RGYAIATINN NIIFSSTQVE
KGNIINVRLA QGRLDCEVSD IKE
//
