EX7L_SODGM
ID EX7L_SODGM Reviewed; 458 AA.
AC Q2NS50;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SG1750;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(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}.
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DR EMBL; AP008232; BAE75025.1; -; Genomic_DNA.
DR RefSeq; WP_011411574.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NS50; -.
DR SMR; Q2NS50; -.
DR STRING; 343509.SG1750; -.
DR PRIDE; Q2NS50; -.
DR EnsemblBacteria; BAE75025; BAE75025; SG1750.
DR KEGG; sgl:SG1750; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR BioCyc; SGLO343509:SGP1_RS15935-MON; -.
DR Proteomes; UP000001932; 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..458
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000273694"
SQ SEQUENCE 458 AA; 51766 MW; E6C2C8869A74784B CRC64;
MSTPPSSLIF TVSRLNKTVR ELLEGEMGQI WLTGEISNFS QPASGHWYFT LKDDRAQVRC
AMFRNTNRRT TFAPRNGQQV LVRASLTLYE PRGDYQLIAE SMQPAGDGLL QQQFEQLKQQ
LSDEGLFSQQ FKQPLPSPAR RVGVITSASG AALHDILQVL QRRDPSLPVV IYPTAVQGQE
APAQILRALE AANRRAECDV LIVGRGGGSL EDLASFNDER VARAIFASRL PVVSAVGHET
DVTIADFVAD LRAPTPSAAA ELVSRNQLEL LRQLQSQQQR LEMAMDYFLA QRQQRYSRLQ
HRLQQQHPQL RLARQHTALM TLRRRLDDGV QGQLRQAQRR HDYVRQRMVQ QAPAARINRA
QQRLQALRYQ LSQGISLRVN RQNNAFVALC SRLEGMSPLK TLARGFSVTT DSHGAVVKQT
RQLSAGDRLT TRLRDGWVES QVTEITRQPA RRPRRSQD
