EX7L_SYNC1
ID EX7L_SYNC1 Reviewed; 401 AA.
AC Q3A3Z3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=Pcar_1670;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000142; ABA88914.1; -; Genomic_DNA.
DR RefSeq; WP_011341404.1; NC_007498.2.
DR AlphaFoldDB; Q3A3Z3; -.
DR SMR; Q3A3Z3; -.
DR STRING; 338963.Pcar_1670; -.
DR PRIDE; Q3A3Z3; -.
DR EnsemblBacteria; ABA88914; ABA88914; Pcar_1670.
DR KEGG; pca:Pcar_1670; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_7; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000002534; 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; 2.
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..401
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303808"
SQ SEQUENCE 401 AA; 44213 MW; 8B12330ED3C6CA18 CRC64;
MNISEGTVSV SRLVYLLKEV VEDNFVQVLV TGEIANFSAP SSGHYYFAVK DDQAQLRGVM
FRSSNRLLKF TPENGMQVLC GGRVSLYPQR GELQLVVDRM EPLGVGSWQL AFEKLKTKLD
AEGLFEVGRK RRLPSFPRTI GVVTSPTGAA IHDILNVLRR RGAGLHVLLS PVRVQGDGAA
DEIARAIADF NRHGQADVLI VGRGGGSPED LWAFNEEVVA RAVFASRIPV ISAVGHEVDV
TISDLVADLR APTPSAAAEL VVQGRQELER HVDHLVMRLS GQMQGRLSLL KERLDGLRRR
LRSPVDDLRR QYRDLEQLRK RLFSAMEKTM QRAANRLGLA GSRLHALSPL ATLDRGYAIV
FSAKTSTIVR DARTLTPGDR VQIRFAKGSV EATVDEVDHG D
