EX7L_CORGB
ID EX7L_CORGB Reviewed; 417 AA.
AC A4QCY8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=cgR_1108;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(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; AP009044; BAF54085.1; -; Genomic_DNA.
DR RefSeq; WP_011897006.1; NC_009342.1.
DR AlphaFoldDB; A4QCY8; -.
DR EnsemblBacteria; BAF54085; BAF54085; cgR_1108.
DR KEGG; cgt:cgR_1108; -.
DR HOGENOM; CLU_023625_2_1_11; -.
DR OMA; WPAVRFE; -.
DR PhylomeDB; A4QCY8; -.
DR Proteomes; UP000006698; 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; 2.
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..417
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303784"
SQ SEQUENCE 417 AA; 45522 MW; 065FFB755FA768C2 CRC64;
MSSEKASSKS TPEAPWPVRE VNTQVKQWIE RLGHLWVEGQ LAQINVKPNW KLSYLTLRDV
EQEVSVQLTC PTDIIRNRPT PLKDGDRVIV YGKPAFYAGR GTFSLWVTDI RPVGIGELLA
RIEELRKRLA AEGLFDPARK KRLPFLPNRV GLITGRGSAA ERDVLSVAKD RWPEVQFEVI
NTAVQGASAV PEIIEALRAL DQDPRVDVII IARGGGSVED LLPFSEEALQ RAVAAAQTPV
VSAIGHEPDT PVLDNVADLR AATPTDAAKR VVPDVAEERM LINQLRSRSA AALRGWVQRE
QQALAAIRTR PVLADPMTPI NRRRDEIAQA VGLIRRDVTH LVRTEQALVA SLRAQVSALG
PSATLARGYS VVQVIPRDGS APEVVTTIEQ SPPGSQLRIR VADGSITAAS MGTQQAN
