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Database: UniProt
Entry: I8U348_9ALTE
LinkDB: I8U348_9ALTE
Original site: I8U348_9ALTE 
ID   I8U348_9ALTE            Unreviewed;       445 AA.
AC   I8U348;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
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:EIW87731.1};
GN   ORFNames=AGRI_14460 {ECO:0000313|EMBL:EIW87731.1};
OS   Alishewanella agri BL06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alishewanella.
OX   NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW87731.1, ECO:0000313|Proteomes:UP000035062};
RN   [1] {ECO:0000313|EMBL:EIW87731.1, ECO:0000313|Proteomes:UP000035062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL06 {ECO:0000313|EMBL:EIW87731.1,
RC   ECO:0000313|Proteomes:UP000035062};
RX   PubMed=22933763; DOI=10.1128/JB.01129-12;
RA   Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT   "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT   Landfill Soil.";
RL   J. Bacteriol. 194:5135-5136(2012).
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:EIW87731.1}.
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DR   EMBL; AKKU01000026; EIW87731.1; -; Genomic_DNA.
DR   RefSeq; WP_008985650.1; NZ_AKKU01000026.1.
DR   AlphaFoldDB; I8U348; -.
DR   STRING; 1195246.AGRI_14460; -.
DR   PATRIC; fig|1195246.3.peg.2870; -.
DR   eggNOG; COG1570; Bacteria.
DR   Proteomes; UP000035062; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000035062}.
FT   DOMAIN          7..99
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          123..437
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   COILED          309..374
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   445 AA;  50108 MW;  FE8BFE451D34CA94 CRC64;
     MQNPDIYTVS RLNSEVRLTL ELQFQQLWLV GEVSNFVAAA SGHWYFSLKD QAAQVKVAMF
     KQANRYATVR PQNGQQVLIR ARISVYEPRG EYQLLAEFIE PAGAGLLKQQ FEQLKAKLAA
     EGLFAPERKR PLPANPRRVG VITSPTGAAV RDIITVLARR APGIELIIYP CQVQGETAAA
     QLRNMLSTAI RRNEVDVLII GRGGGSIEDL WCFNDEALAR AVADCPIPIV SAVGHEIDFA
     LTDFVADVRA ATPSAAAELV SPDQSQYLTA LTQLQQRLSR AVRRQLAQQQ PRLMQLQQRL
     QQLHPQRRLE QQQQRLDELQ LRLQRRMQQQ LQTARRQHSY LQQSLQHLSP AKAIKQQQLQ
     LQQLAKRLQQ AQLQQLKQHK FNLIQLSKQL HTVSPLATLA RGYSIAFDAQ QQVVTRNSQL
     APGDKVTVKL AEGAFEAEVK KLTTQ
//
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