EX7L_JANMA
ID EX7L_JANMA Reviewed; 453 AA.
AC A6T178;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=mma_2585;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88515.1; -; Genomic_DNA.
DR RefSeq; WP_012080437.1; NC_009659.1.
DR AlphaFoldDB; A6T178; -.
DR STRING; 375286.mma_2585; -.
DR EnsemblBacteria; ABR88515; ABR88515; mma_2585.
DR KEGG; mms:mma_2585; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_4; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR BioCyc; JSP375286:MMA_RS13420-MON; -.
DR Proteomes; UP000006388; 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; Reference proteome.
FT CHAIN 1..453
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000079987"
SQ SEQUENCE 453 AA; 49882 MW; 18D39B036FCF4A50 CRC64;
MISDRSPSPP SSAPAVLSVS ALNQAVSRML ERNFPLSWVS GEISNFTCAA SGHWYFTLKD
SAAQVRAVMF RGRAQYADFM PREGDKVEVR ALVTLYAPRG DYQLSVEAIR RAGVGNLYEA
FLQLKEKLNA EGLFDPARKR AIPSFARTIG IVTSPQAAAL RDILTTLQRR APHVRVILYP
TPVQGEGSAN KIAQAIATAS ARAECDVLLV CRGGGSIEDL WSFNHELVAR TIVGCDIPVI
VGVGHETDFT IADFAADLRA PTPTAAAELA ATPRADWLAR LEAQADDMRY VLKRQLSDTA
QTLDWLSRRL ISPAAYIAHE RMKLQNLQAR LGHATRIPLS KAQFALAQLR NRWLSQLPDT
QAQRLHVINH ARRMSNQINN HIASQRQSLA ALSAQLEMLN PQRTLERGYA MITDEKGKIV
RAPKELQPRQ SVTVRLADGT AQVGIASVQE TLE
