EX7L_CAMLR
ID EX7L_CAMLR Reviewed; 387 AA.
AC B9KDM8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Cla_1351;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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; CP000932; ACM64666.1; -; Genomic_DNA.
DR RefSeq; WP_012662049.1; NC_012039.1.
DR AlphaFoldDB; B9KDM8; -.
DR SMR; B9KDM8; -.
DR STRING; 306263.Cla_1351; -.
DR EnsemblBacteria; ACM64666; ACM64666; CLA_1351.
DR GeneID; 7409857; -.
DR KEGG; cla:CLA_1351; -.
DR PATRIC; fig|306263.5.peg.1337; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000007727; 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..387
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200663"
SQ SEQUENCE 387 AA; 43898 MW; 8F4E7CE265C1BABE CRC64;
MKVSELNLKA KSLLEFHLDD IELSGEISKI TIHGSGHWYF DLKDEKSSIA CVMFKGFNQF
VQTQPKVGDM LDLRGYVSLY EASGRYQFIA KSMQKTSLGD LEAKFLALKE KLEKEGLFDI
NAKKSIVKFP KKIGIITSFT SAALQDMLKL ISQKEYNLCK ITIFNALTQG QSAPNSLINA
LKKANEYDLD AIILARGGGS REDLFCFNDE ELARCIFSLK TPVVSAIGHE IDYVISDFVA
DLRAPTPSAA IDMIFPNKLS LEQGLDELTM RFKSQMLNHL KFYQNKIDHL QNLAKAKSLE
NAFFLRKQKL DFLQSQLKSV LNLKLLNYEN KLNNFEELLA QHKNFFDKSK NLINLQKDGK
NISLEKLKKG DIIKLCSINE SKEAQIL
