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Database: UniProt
Entry: A0A1E1F5C4_9SPHN
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ID   A0A1E1F5C4_9SPHN        Unreviewed;       497 AA.
AC   A0A1E1F5C4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SCLO_1026800 {ECO:0000313|EMBL:BAV65720.1};
OS   Sphingobium cloacae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=120107 {ECO:0000313|EMBL:BAV65720.1, ECO:0000313|Proteomes:UP000218272};
RN   [1] {ECO:0000313|EMBL:BAV65720.1, ECO:0000313|Proteomes:UP000218272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10874 {ECO:0000313|EMBL:BAV65720.1,
RC   ECO:0000313|Proteomes:UP000218272};
RA   Ootsuka M., Nishizawa T., Ohta H.;
RT   "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT   Sphingobium cloacae JCM 10874T.";
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; AP017655; BAV65720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E1F5C4; -.
DR   KEGG; sclo:SCLO_1026800; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000218272; Chromosome.
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:UP000218272}.
FT   DOMAIN          27..120
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          143..458
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   REGION          459..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  54188 MW;  7563DA1D60F2C857 CRC64;
     MSPDYDAYDN SGRLLAEERA GDNAPPLTVS ELSGLLKRTV EDRFGHVRLR GEISGFKRAA
     SGHLYLCLKD DNAVIDGVMW KGSAARIAFA AQDGVEVIAT GKLTTYPGRS KYQIVIDRME
     LAGEGALMAL LEKLKAKLAA EGLFDRDRKR PLPFMPRTIG VVTSPTGAVI RDILHRLSDR
     CPTDVLLWPV LVQGDGAAAQ VARAVRGFSA MPADGPLPRP DLVIVARGGG SIEDLWSFNE
     EIVVRAVAEC SIPVISAVGH ETDTTLCDYA ADMRAPTPTA AAEMAVPVRA ELLAMLREQG
     VRMDRAVRRG AAQARERLEM QARLMPTPDT LLAPQRQRLD QLSDALASGL RHRLADARTH
     LSQAGGALRP ALLQQYVSRA RERVDRLRLR PDYLTRALAD RATAFDRLSR LFVSLDPDRP
     LQRGFARVMA GGHLVRDTAA ARAAGQVTLH FRDGEVDATV EGAPPLEKPA PPAISNPSRP
     AHKKREEGEI RQQDLFS
//
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