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Entry: A0A1N7S3A1_9BURK
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ID   A0A1N7S3A1_9BURK        Unreviewed;       459 AA.
AC   A0A1N7S3A1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-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   ECO:0000313|EMBL:SIT41847.1};
GN   ORFNames=BN2475_320058 {ECO:0000313|EMBL:SIT41847.1};
OS   Paraburkholderia ribeironis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT41847.1, ECO:0000313|Proteomes:UP000187012};
RN   [1] {ECO:0000313|EMBL:SIT41847.1, ECO:0000313|Proteomes:UP000187012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM7296 {ECO:0000313|EMBL:SIT41847.1,
RC   ECO:0000313|Proteomes:UP000187012};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-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; CYGX02000032; SIT41847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7S3A1; -.
DR   STRING; 1247936.BN2475_320058; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000187012; 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   Gene3D; 2.40.50.1010; -; 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:UP000187012}.
FT   DOMAIN          20..111
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          135..445
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   459 AA;  50569 MW;  571E57EB2A05E852 CRC64;
     MNSDNPFASP ATPGGEVVVP VSALNRAIGA MLERSFPLVW VAGEVSNFTR AASGHWYFSI
     KDAQAQMRCV MFRGRAQYAE FTPREGDRIE VRALVTMYEP RGELQLNVEA VRRTGQGRLY
     EAFLRLKAQL EAEGLFAAER KRALPAHPRA IGIVTSLQAA ALRDVLTTLS RRAPHIPVIV
     YPAPVQGAGV SSKLAAMVDA ASARREVDVL IVCRGGGSIE DLWAFNEEVL ARAIAQSAIP
     VVSGVGHETD FTIADFAADM RAPTPTGAAE LVSPQRVLLL RELDHRHATL ARGFGRMMER
     RAQQLDWLAR RLVSPTERLA RQRIHLQQLS VRLASAGARP LRDARARFVL LQMRWQRWRP
     DLAAHRARLG NLAQRLDAAL LRQHERQVAR IGTLAARLEV LSPQRTLERG YAAMLDAQSG
     RAVRAPSSLK PGRRFTVHLA EGSADIALAD VQTRLADGF
//
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