EX7L_VIBC1
ID EX7L_VIBC1 Reviewed; 443 AA.
AC A7MU31;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-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};
GN OrderedLocusNames=VIBHAR_01075;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-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; CP000789; ABU70068.1; -; Genomic_DNA.
DR RefSeq; WP_012127095.1; NC_022269.1.
DR AlphaFoldDB; A7MU31; -.
DR SMR; A7MU31; -.
DR EnsemblBacteria; ABU70068; ABU70068; VIBHAR_01075.
DR KEGG; vha:VIBHAR_01075; -.
DR PATRIC; fig|338187.25.peg.1552; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000008152; 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..443
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000048791"
SQ SEQUENCE 443 AA; 49854 MW; 38CA4E6116D1F298 CRC64;
MLSQTNQNIF TVSRLNAEVR LLLENEMGIV WLVGEISNFS APVSGHWYLT LKDSRAQVKC
AMFRGNNRRV TFKPANGNQV LVKARLSLYE PRGDYQLIIE SMQPEGDGRL QQEFEALKMK
LAAEGLFAQT NKQPLPEHPK RVGVITSKTG AALYDILDVL KRRDPSLPVV VYPTMVQGEE
AAIQMAQAIG RANSRDECDV LIVGRGGGSL EDLWCFNNEI LARTIAASQI PIISAVGHEV
DVTIADFVAD IRAPTPSAAA ELVSRDNSHK DQALVTHQHK LASAMRYYLA QQKQQSAQLM
HRLERQHPSY QLQRQTQQLD ELEMRLQRAM QRFITTRQQA VERKHHRLQL NSPVKRLAEQ
KSKLDRVEQK LLDAMDRKLL TMRHQLAIAA EKLDTVSPLA TLKRGYSITQ TEQGQVVTQA
KDVKTGDVLV TRLSDGELRS TVN
