EXO_LAMBD
ID EXO_LAMBD Reviewed; 226 AA.
AC P03697;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Exonuclease;
DE EC=3.1.11.3;
GN Name=exo; Synonyms=red-alpha, redX;
OS Escherichia phage lambda (Bacteriophage lambda).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage lambda DNA.";
RL J. Mol. Biol. 162:729-773(1982).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9295273; DOI=10.1126/science.277.5333.1824;
RA Kovall R., Matthews B.W.;
RT "Toroidal structure of lambda-exonuclease.";
RL Science 277:1824-1827(1997).
CC -!- FUNCTION: Facilitates phage DNA recombination through the double-strand
CC break repair (DSBR) and single-strand annealing pathways. Also
CC important for the late, rolling-circle mode of lambda DNA replication.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Trimer of three subunits that form a toroid, with a tapered
CC channel passing through the middle.
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DR EMBL; J02459; AAA96569.1; -; Genomic_DNA.
DR PIR; H94614; NDBPXL.
DR RefSeq; NP_040616.1; NC_001416.1.
DR PDB; 1AVQ; X-ray; 2.40 A; A/B/C=1-226.
DR PDB; 3SLP; X-ray; 2.30 A; A/B/C=1-226.
DR PDB; 3SM4; X-ray; 1.88 A; A/B/C=1-226.
DR PDB; 4WUZ; X-ray; 2.38 A; A/B/C=1-226.
DR PDB; 6M9K; X-ray; 2.30 A; A/B/C=1-226.
DR PDBsum; 1AVQ; -.
DR PDBsum; 3SLP; -.
DR PDBsum; 3SM4; -.
DR PDBsum; 4WUZ; -.
DR PDBsum; 6M9K; -.
DR SMR; P03697; -.
DR DIP; DIP-59695N; -.
DR GeneID; 2703469; -.
DR GeneID; 2703502; -.
DR KEGG; vg:2703522; -.
DR EvolutionaryTrace; P03697; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR019080; YqaJ_viral_recombinase.
DR Pfam; PF09588; YqaJ; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..226
FT /note="Exonuclease"
FT /id="PRO_0000077574"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3SLP"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:3SM4"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 75..96
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3SM4"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 193..216
FT /evidence="ECO:0007829|PDB:3SM4"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3SM4"
SQ SEQUENCE 226 AA; 25909 MW; 7D93AABA17F9AE26 CRC64;
MTPDIILQRT GIDVRAVEQG DDAWHKLRLG VITASEVHNV IAKPRSGKKW PDMKMSYFHT
LLAEVCTGVA PEVNAKALAW GKQYENDART LFEFTSGVNV TESPIIYRDE SMRTACSPDG
LCSDGNGLEL KCPFTSRDFM KFRLGGFEAI KSAYMAQVQY SMWVTRKNAW YFANYDPRMK
REGLHYVVIE RDEKYMASFD EIVPEFIEKM DEALAEIGFV FGEQWR