EX7L_SHEDO
ID EX7L_SHEDO Reviewed; 446 AA.
AC Q12PS2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=Sden_1268;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
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DR EMBL; CP000302; ABE54554.1; -; Genomic_DNA.
DR RefSeq; WP_011495713.1; NC_007954.1.
DR AlphaFoldDB; Q12PS2; -.
DR STRING; 318161.Sden_1268; -.
DR EnsemblBacteria; ABE54554; ABE54554; Sden_1268.
DR KEGG; sdn:Sden_1268; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001982; 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 Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..446
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000273684"
SQ SEQUENCE 446 AA; 49538 MW; 9F8C4757BCB0D835 CRC64;
MKAAKNNVYT VSRLNGEVRQ ILEGQIGKIW LNGEISNFSS PSSGHWYLTL KDTHSQIRCA
MFKGRNQSVN FRPVNGQQVL VKGAISVYEP RGDYQLLLES MLPAGDGLLA QEYEALKMKL
AAEGLFASET KRALPSNIQR IGIITSATGA ALRDVLHVLQ RRDASIEVVV YPTQVQGTSA
SDNICRAIEL ANKRLEVDVL LLTRGGGSLE DLWCFNNEML AHSIYNSALP VVSAVGHEVD
TTISDYVADV RAPTPSAGAE LLSQDKGNKA QKLALMLSRL AQGMRHYQLS QDKHFVNLQH
RLNQQDPKRR LQQLEQQFDE FQLRLDNAFK HRLSRLTLRH ERLSAQLQRQ SPEHKLRLAH
QALTHVSGRF DDAIKDTLGS AEQRLKQAVH QLEAMSPLAT LSRGYSISSN ANGKVITDAS
KVKVGDSLHT RLAKGQLVST VIDVEM
