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Database: UniProt/SWISS-PROT
Entry: EX7L_SALAR
LinkDB: EX7L_SALAR
Original site: EX7L_SALAR 
ID   EX7L_SALAR              Reviewed;         454 AA.
AC   A9MHM3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   01-MAY-2013, entry version 37.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit;
DE            EC=3.1.11.6;
DE   AltName: Full=Exodeoxyribonuclease VII large subunit;
DE            Short=Exonuclease VII large subunit;
GN   Name=xseA; OrderedLocusNames=SARI_00364;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V.,
RA   Nash W., Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large
CC       acid-insoluble oligonucleotides, which are then degraded further
CC       into small acid-soluble oligonucleotides (By similarity).
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'-
CC       or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the XseA family.
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DR   EMBL; CP000880; ABX20301.1; -; Genomic_DNA.
DR   RefSeq; YP_001569443.1; NC_010067.1.
DR   STRING; 41514.SARI_00364; -.
DR   EnsemblBacteria; ABX20301; ABX20301; SARI_00364.
DR   GeneID; 5764383; -.
DR   KEGG; ses:SARI_00364; -.
DR   PATRIC; 18469881; VBISalEnt13497_0338.
DR   eggNOG; COG1570; -.
DR   HOGENOM; HOG000229265; -.
DR   KO; K03601; -.
DR   OMA; ENAQVRC; -.
DR   ProtClustDB; PRK00286; -.
DR   BioCyc; SENT882884:GJ8H-364-MONOMER; -.
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:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:HAMAP.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
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   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; Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN         1    454       Exodeoxyribonuclease 7 large subunit.
FT                                /FTId=PRO_1000079989.
SQ   SEQUENCE   454 AA;  51566 MW;  639A4BEAFE48FA12 CRC64;
     MLSSQTSSIF TVSRLNQTVR LLLEQEMGQV WISGEISNFT QPASGHWYFT LKDDTAQVRC
     AMFRNSNRRV TFRPQHGQQV LVRANITLYE PRGDYQIIVE SMQPAGEGLL QQKYEQLKAK
     LQAEGLFDQQ YKHPLPSPAY CVGVITSKTG AALHDILHVL KRRDPSLPVI IYPAAVQGED
     APGQIVRAIT LANARKECDV LIVGRGGGSL EDLWSFNDER VARAIFASTI PVVSAVGHET
     DVTIADFVAD LRAPTPSAAA EVVSRNQQEL LRQMQTACQR LEMAMDYYLA NRQRRFSQLY
     HRLQQQHPQL RLARQQTTLE RLRQRMHLAL ENQLKQANQR QQRASQRLRQ QNPQPRIHRA
     QSRIQQLEYR LAENFRARLS EQRERFGNTV THLEAVSPLA TLARGYSVST ATDGNVLKKV
     KQLKVGDMMT TRLKDGWVTS EVTAIKPVKK IRLG
//
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