EX7L_SHEB8
ID EX7L_SHEB8 Reviewed; 448 AA.
AC A6WQP2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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};
GN OrderedLocusNames=Shew185_3000;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-2007) 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; CP000753; ABS09131.1; -; Genomic_DNA.
DR RefSeq; WP_012089731.1; NC_009665.1.
DR AlphaFoldDB; A6WQP2; -.
DR SMR; A6WQP2; -.
DR KEGG; sbm:Shew185_3000; -.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
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.
FT CHAIN 1..448
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000048785"
SQ SEQUENCE 448 AA; 49949 MW; B80C0B6C69C8FA57 CRC64;
MQGTKNNIYT VSRLNGEVRQ ILEGQLGKIW LNGEISNFSS PSSGHWYLTL KDHSSQIRCA
MFKGRNQTVS FKPINGQQVL VKGAISVYEP RGDYQLLIES MLPAGDGLLA QQFDALKMKL
AAEGLFAADT KRPLPKNIQR IGVITSPTGA AIRDVLHVLA RRDPSIEVII YPTQVQGETA
AQSICQAINI ANQRLEVDVL LLTRGGGSLE DLWCFNSEAL AHTIYNSALP VVSAVGHEVD
TTISDYVADI RAPTPSAGAE LLSQDSDNKA QKLATALSRL QQSAKHYQLK QERRLSLLEH
RLQRQDPKRT LQQFEQRFDE MQLRLESALS NRLHILSRRQ QLLASRLEQQ SPKHKLAIEG
NRLSYLASRL QDALQDKLSQ SEQRIKYAAH QLETVSPLAT LSRGYSITTD IHNQVVDSTD
KLTIGDSLQT RLRHGQVIST VTQIKPLE
