EX7L_SYNWW
ID EX7L_SYNWW Reviewed; 405 AA.
AC Q0AZF4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Swol_0567;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI67900.1; -; Genomic_DNA.
DR RefSeq; WP_011640005.1; NC_008346.1.
DR AlphaFoldDB; Q0AZF4; -.
DR STRING; 335541.Swol_0567; -.
DR DNASU; 4281408; -.
DR EnsemblBacteria; ABI67900; ABI67900; Swol_0567.
DR KEGG; swo:Swol_0567; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_9; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001968; 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; Reference proteome.
FT CHAIN 1..405
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000048788"
SQ SEQUENCE 405 AA; 46034 MW; 019F00553203E718 CRC64;
MKEILTVTEL NSYIANLLDS DPFLGQLWLR GEISGFRLYQ QSGHMYFTLK DEDSTISAVM
FKSRARGLKF KPKDGMEVLL RASVSVFARQ GKYQLYVEEM QPYGIGGLFL YLEELKKKLA
AKGYFAPERK KAIPAFVQRV GIVTSQDGAA LRDICRILKQ RHPGVEVVLA HSSVQGSEAP
GELAEGLRLL NSYAEVELII IGRGGGSYED LMAFNSELVV QAIYESNIPV ISAVGHEVDF
TLADLVADLR AATPSQAASL AVADMQALSR QLDNYQQRLL RAMQRKLLYY TEIIDRLMMK
RIWKQPRSLL HMREELLSQL EKSLSRGMAE IFREKKMKLS MNMAALDSLS PLKIMERGYV
LLQKEGRIIR DEQQVQIGDR LEVAMRHADL EIEVIKKERV KRWKS