EX7L_HELAH
ID EX7L_HELAH Reviewed; 420 AA.
AC Q17W89;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Hac_1349;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM260522; CAK00087.1; -; Genomic_DNA.
DR RefSeq; WP_011578177.1; NC_008229.1.
DR AlphaFoldDB; Q17W89; -.
DR SMR; Q17W89; -.
DR STRING; 382638.Hac_1349; -.
DR EnsemblBacteria; CAK00087; CAK00087; Hac_1349.
DR KEGG; hac:Hac_1349; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR BioCyc; HACI382638:HAC_RS05795-MON; -.
DR Proteomes; UP000000775; 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_0000303790"
SQ SEQUENCE 420 AA; 47037 MW; 7A1AA9987EB11B76 CRC64;
MDALSVSEIN AKIKALLEAT FLQVRVQGEV SNLTIHKVSG HAYFSLKDSQ SVIRCTLFRG
NASKLKFALK EGQEVAVFGA ISVYPPRGDY QINCFEIEPK DWGSLALALE QLKEKLRLKG
YFDKENKLPK PSFPKRVAII TSQNSAAWAD MQKIAFKRWP MCELVCINTL MQGEGCVQSV
VESIAYADSF YNTRNAFDAI VVARGGGSME DLYSFNDERI ADALHLAKTF SMSAIGHESD
FLLSDSVADL RASTPSNAME ILLPSSEEWQ QKLDGFNLKL QRSFKILLHQ KKVHLEHLAA
SLKRLSFENK HHLNSLKLEK LKIALENKTL EFLRLKKTLL EKISTQLSTS PFLQTKTERL
NALDNALKLA HAHLKLPKFG AFVSKNNQAI ELEELKIGDK IELNNEKARA SAAILSVDKA