EX7L_VIBPA
ID EX7L_VIBPA Reviewed; 443 AA.
AC Q87S09;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=VP0615;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC58878.1; -; Genomic_DNA.
DR RefSeq; NP_796994.1; NC_004603.1.
DR RefSeq; WP_005460216.1; NC_004603.1.
DR AlphaFoldDB; Q87S09; -.
DR STRING; 223926.28805601; -.
DR EnsemblBacteria; BAC58878; BAC58878; BAC58878.
DR GeneID; 1188090; -.
DR KEGG; vpa:VP0615; -.
DR PATRIC; fig|223926.6.peg.583; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000002493; Chromosome 1.
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..443
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000197900"
SQ SEQUENCE 443 AA; 49843 MW; 120645C1DD8FE70E CRC64;
MLSKTNQNIF TVSRLNAEVR LLLENEMGIV WLVGEISNFS APVSGHWYLT LKDSRAQVKC
AMFRGNNRRV TFKPANGNQV LVKARLSLYE PRGDYQLIIE SMQPEGDGRL QQEFEELKMK
LAAEGLFAQT NKLPLPEHPK RVGIITSKTG AALYDILDVL KRRDPSLPVV IYPTMVQGDD
AAIQIAQAIG RANSRNECDV LIVGRGGGSL EDLWCFNNEI LARTIAASQI PIISAVGHEV
DMTIADFVAD VRAPTPSAAA ELVSRDNSHK DQSLVAKQHK LASAMRYYLS QQKQQSAQLL
HRLERQHPSY QLQRQSQQLD ELDMRLRRAM QRFIDTRQQA VERKHHRLQL NSPVKHLAQQ
KSRLERVEHK LLDTMDRKLL TMRHQLAIAA EKLDTVSPLA TLKRGYSITQ TEQGKVVTSA
DDVKTGDLLV TRLANGEIHS TVS
