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Database: UniProt
Entry: A0A165KT78_9BURK
LinkDB: A0A165KT78_9BURK
Original site: A0A165KT78_9BURK 
ID   A0A165KT78_9BURK        Unreviewed;       442 AA.
AC   A0A165KT78;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=A1D30_11050 {ECO:0000313|EMBL:KZT16053.1};
OS   Acidovorax sp. GW101-3H11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT16053.1, ECO:0000313|Proteomes:UP000077219};
RN   [1] {ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA   Ray J., Price M., Deutschbauer A.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KZT16053.1, ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT16053.1,
RC   ECO:0000313|Proteomes:UP000077219};
RX   PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA   Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA   Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA   Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA   Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT   "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL   Nature 557:503-509(2018).
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:KZT16053.1}.
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DR   EMBL; LUKZ01000009; KZT16053.1; -; Genomic_DNA.
DR   RefSeq; WP_063460382.1; NZ_LUKZ01000009.1.
DR   AlphaFoldDB; A0A165KT78; -.
DR   STRING; 1813946.A1D30_11050; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000077219; 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          15..107
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          130..433
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   442 AA;  47715 MW;  356F2C25CAD28A35 CRC64;
     MFERTNPGVA PRVWEVGALC RAIADALEAR FNPVAVRGEI TGFSRASSGH CYFSIKDANG
     QLRCAMFRRA ASLLDFSPRD GELVEVRGRL GVYEARGDLQ FIVESMQRAG QGALFEQFLR
     LKAQLDAEGL FDTARKRPLP LLPRAIGLVT SPGAAALHDV VTALRRRVPH IPVVLVPALV
     QGAAAPASLV AALSKMYLLA QAGRAQGADL AQNPPVDVIL LVRGGGSIED LWAFNDEQLA
     RTIVQSPVPL ISGVGHETDF TIADFCADLR APTPTAAAEL VAQPREVWLG ALGLLAGRLA
     DGVERQLDAR HQRLDQAAAR LGRPSGLVAR EQLQLARLAQ RMRHGVLLKL QRLSQSQQAM
     EANLPQKMQR CVAQHTQRLD RAALRLDLLD PRLVLQRGYA LLTDTGGRAV TSVQQAHPGD
     ALRATLADGV VDVTVAAQPR LL
//
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