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Database: UniProt
Entry: F2F927_SOLSS
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Original site: F2F927_SOLSS 
ID   F2F927_SOLSS            Unreviewed;       452 AA.
AC   F2F927;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   25-OCT-2017, entry version 42.
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   OrderedLocusNames=SSIL_1699 {ECO:0000313|EMBL:BAK16122.1};
OS   Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae;
OC   Solibacillus.
OX   NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK16122.1, ECO:0000313|Proteomes:UP000006691};
RN   [1] {ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA   Morohoshi T., Someya N., Ikeda T.;
RT   "Genome sequence of Solibacillus silvestris StLB046.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAK16122.1, ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|EMBL:BAK16122.1,
RC   ECO:0000313|Proteomes:UP000006691};
RX   PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA   Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT   "Complete genome sequence and characterization of the N-acylhomoserine
RT   lactone-degrading gene of the potato leaf-associated Solibacillus
RT   silvestris.";
RL   J. Biosci. Bioeng. 113:20-25(2012).
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large
CC       acid-insoluble oligonucleotides, which are then degraded further
CC       into small acid-soluble oligonucleotides. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|SAAS:SAAS00723532}.
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to
CC       3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
CC       {ECO:0000256|HAMAP-Rule:MF_00378, ECO:0000256|RuleBase:RU004355,
CC       ECO:0000256|SAAS:SAAS00723505}.
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, ECO:0000256|SAAS:SAAS00723552}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355,
CC       ECO:0000256|SAAS:SAAS00723548}.
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DR   EMBL; AP012157; BAK16122.1; -; Genomic_DNA.
DR   RefSeq; WP_014823480.1; NC_018065.1.
DR   EnsemblBacteria; BAK16122; BAK16122; SSIL_1699.
DR   KEGG; siv:SSIL_1699; -.
DR   PATRIC; fig|1002809.3.peg.1719; -.
DR   KO; K03601; -.
DR   OMA; NARRRWP; -.
DR   OrthoDB; POG091H02EK; -.
DR   Proteomes; UP000006691; 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   PANTHER; PTHR30008; PTHR30008; 1.
DR   Pfam; PF02601; Exonuc_VII_L; 1.
DR   Pfam; PF13742; tRNA_anti_2; 1.
DR   TIGRFAMs; TIGR00237; xseA; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006691};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|SAAS:SAAS00723549};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723511,
KW   ECO:0000313|EMBL:BAK16122.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723558};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006691}.
FT   DOMAIN        7    102       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      125    438       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
SQ   SEQUENCE   452 AA;  50981 MW;  BE30A6BEB86006F4 CRC64;
     MTSNSYLSVK ALTKYIKRKF DADPHLRDVY VTGELSNVKV HSSGHIYFTL KDDSSRINAT
     MFRSQASKLS FKPEEGMKVF IRGDVNVYEA SGAYQLYAQT MEPDGIGGLF VAFNQLKERL
     QNEGLFNPNF KQPIPQFPKT IGVLTATTGA AIRDICTTIN RRYPQAEILI YPTLVQGAGA
     APNITENIYL ANRHGFCDVL IVGRGGGSIE DLWAFNEEIV ARAIFESRIP VISAVGHETD
     TTIADFVADL RAPTPTAAAE LAVPNQQQLY QQILHYQSIL HQMMTSKLNF ERNRLTKLQN
     SYPLATPERL YRPFIERLVQ VDLSLQNATK LYMMNEKSKL QSIDSKMKLY SPVHQLIAAK
     QQLEHRTQTL TNRMQQQLAQ NKVAFTNQLR MLEALNPLAL MSKGFSVAYK EENVVKSVHE
     LEKGDVIQVT FQDGYAEAKI EKKHVQKEGE AK
//
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