EX7L_HELP2
ID EX7L_HELP2 Reviewed; 420 AA.
AC B6JKI8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=HPP12_0258;
OS Helicobacter pylori (strain P12).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12;
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-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; CP001217; ACJ07416.1; -; Genomic_DNA.
DR RefSeq; WP_000382851.1; NC_011498.1.
DR AlphaFoldDB; B6JKI8; -.
DR EnsemblBacteria; ACJ07416; ACJ07416; HPP12_0258.
DR KEGG; hpp:HPP12_0258; -.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000008198; Chromosome.
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..420
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122065"
SQ SEQUENCE 420 AA; 47170 MW; 2C3F59C5EAA9DCC5 CRC64;
MDVLSVSEIN AQIKALLEAT FLQVRVQGEV SNLTIHKVSG HAYFSLKDSQ SVIRCVLFKG
NANRLKFALK EGQEMVVFGG ISVYVPRGDY QINCFEIEPK EIGSLTLALE QLKEKLRLKG
YFDEANKLPK PHFPKRVAVI TSQNSAAWAD MKKIASKRWP MCELVCINTL MQGEGCVQSV
VESIAYADSL HDTKNAFDAI VVARGGGSME DLYSFNDEKI ADALYLAKTF SMSAIGHESD
FLLSDLVADL RASTPSNAME ILLPNSDEWL QKLDGFNVKL HRSFKILLHQ KKAYLEHLAD
FLKRLSFENK HHLNALKLEK LKIALENKTL EFLRFKKTLL EKISTQTLTS PFLQTKTERL
NALENALKLA HANLKLPQFG AFLSKNNQAI ELEALKRGDK IELSNEKARA SAEILSVDRV
