EX7L_ALIFM
ID EX7L_ALIFM Reviewed; 449 AA.
AC B5FAX9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=VFMJ11_0650;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) 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; CP001139; ACH65762.1; -; Genomic_DNA.
DR RefSeq; WP_012533268.1; NC_011184.1.
DR AlphaFoldDB; B5FAX9; -.
DR SMR; B5FAX9; -.
DR PRIDE; B5FAX9; -.
DR EnsemblBacteria; ACH65762; ACH65762; VFMJ11_0650.
DR KEGG; vfm:VFMJ11_0650; -.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000001857; Chromosome I.
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..449
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122100"
SQ SEQUENCE 449 AA; 50464 MW; C4FED5B29045EE19 CRC64;
MSLDSNPRIF TVSRLNAEVR LLLENEMGIV WLVGEISNLT VPVSGHWYLT LKDSQAQVKC
AMFKGNNRRV TFKPQNGKQV LVKARLSLYE PRGDYQLIIE SMQPEGDGRL QQEFDQLKMS
LAAEGLFAQT AKKTLPEQPK RVGIITSQTG AALFDILHVL KRRDPNLPVV IYPTMVQGSG
AAIQIAQAIG RANSRNECDI LIVGRGGGSL EDLWCFNEEI VARTIAASEI PIVSAVGHEI
DVTIADFVAD VRAPTPSAAA ELVSRDLSAQ LQTVAHQKRR LNSAMERYLS HQQRSLSAYQ
HRIEKQHPQM QLNNQSQRLD DLNQRLMNHI QQRLQRQQYR VENLTLRLNN LSPTKRISQD
KLHIEELKRR LLDSMDRNLL MQRHQLALAA EKLDTVSPLA TLMRGYSITH NQDGKVITST
KQVELGDNIT TRFADGDITS TVTKASELS
