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   08-NOV-2023, entry version 127.
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   Lambdavirus; Lambdavirus lambda.
OX   NCBI_TaxID=2681611;
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; 2703468; -.
DR   KEGG; vg:2703522; -.
DR   OrthoDB; 6547at10239; -.
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   CDD; cd22343; PDDEXK_lambda_exonuclease-like; 1.
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   PANTHER; PTHR46609; EXONUCLEASE, PHAGE-TYPE/RECB, C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46609:SF6; YQAJ DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF09588; YqaJ; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 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
//