EX7L_ALIF1
ID EX7L_ALIF1 Reviewed; 449 AA.
AC Q5E765;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=VF_0636;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85131.1; -; Genomic_DNA.
DR RefSeq; WP_011261371.1; NC_006840.2.
DR RefSeq; YP_204019.1; NC_006840.2.
DR AlphaFoldDB; Q5E765; -.
DR SMR; Q5E765; -.
DR STRING; 312309.VF_0636; -.
DR EnsemblBacteria; AAW85131; AAW85131; VF_0636.
DR KEGG; vfi:VF_0636; -.
DR PATRIC; fig|312309.11.peg.628; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000000537; 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; Reference proteome.
FT CHAIN 1..449
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000273700"
SQ SEQUENCE 449 AA; 50518 MW; 6777411A73373DA2 CRC64;
MSLDSNPRIF TVSRLNAEVR LLLENEMGIV WLVGEISNLT VPVSGHWYLT LKDSQAQVKC
AMFKGNNRRV NFKPQNGKQV LVKARLSLYE PRGDYQLIIE SMQPEGDGRL QQEFDQLKMS
LAAEGLFAQT AKKSLPEQPK RVGIITSQTG AALFDILHVL KRRDPNLPIV IYPTMVQGSG
AAIQIAQAIG RANSRNECDI LIVGRGGGSL EDLWCFNEEI VARTIAASEI PIVSAVGHEI
DVTIADFVAD VRAPTPSAAA ELVSRDLSAQ LQTVAHQKRR LNSAMERYLS HQQRSLSAYQ
HRIEKQHPQM QLNNQSQRLD DLNQRLMNHI QQRLQRQQYR VENLTLRLNN LSPTKRISQD
KLHIEELKRR LLDSMDRNLL MQRHQLALAA EKLDTVSPLA TLMRGYSITH NQDGKIITST
KQVELGDNIT TRFADGDITS TVTKASELN
