EX7L_SYNSC
ID EX7L_SYNSC Reviewed; 387 AA.
AC Q3AH76;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 90.
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};
GN OrderedLocusNames=Syncc9605_2324;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB36056.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000110; ABB36056.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041435211.1; NC_007516.1.
DR AlphaFoldDB; Q3AH76; -.
DR SMR; Q3AH76; -.
DR STRING; 110662.Syncc9605_2324; -.
DR EnsemblBacteria; ABB36056; ABB36056; Syncc9605_2324.
DR KEGG; syd:Syncc9605_2324; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_1_3; -.
DR OrthoDB; 1371775at2; -.
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.
FT CHAIN 1..387
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303829"
SQ SEQUENCE 387 AA; 42184 MW; A90382BCAD617C2D CRC64;
MSADRLPSYS VAELNTAIGS LLERGFAPRF LLEATVSRPQ LKKGHLWLTL TDGSASISGV
VWASKLAQLS YQPKDGDGVT VVGKLNFWAA RASLTVQALD IRPSLSTVLR DFERVRQVLE
QEGVIDPSRL RPLPSQPASI AVLTSVPSSA LADMLRTAAE RWPLTQLIVV PIPVQGSVAP
TIINTLEAIA ERTAELGLQA LVLARGGGSR EDLAVFDNEA LCRLLANYPI PVVTGLGHED
DLTVADLVAD HRAATPTAAI VALLPDREAE RQGLTQRQSR LKDTLLGRIL RERQRLQDRA
VALQQQSPRE KIMRKRQELI QKHQLLKALS PERWLKRGLA LISNKAGDPI PGLESVKIGD
QLNIRMSDGS LEARVDQIQP SAPNTTS
