DNE1_CHLMO
ID DNE1_CHLMO Reviewed; 218 AA.
AC P32761;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=DNA endonuclease I-CeuI;
DE EC=3.1.-.-;
DE AltName: Full=23S rRNA intron 1 protein;
OS Chlamydomonas moewusii (Chlamydomonas eugametos).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3054;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2036685; DOI=10.1007/bf00362086;
RA Gauthier A., Turmel M., Lemieux C.;
RT "A group I intron in the chloroplast large subunit rRNA gene of
RT Chlamydomonas eugametos encodes a double-strand endonuclease that cleaves
RT the homing site of this intron.";
RL Curr. Genet. 19:43-47(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1849178; DOI=10.1016/0022-2836(91)90713-g;
RA Turmel M., Boulanger J., Schnare M.N., Gray M.W., Lemieux C.;
RT "Six group I introns and three internal transcribed spacers in the
RT chloroplast large subunit ribosomal RNA gene of the green alga
RT Chlamydomonas eugametos.";
RL J. Mol. Biol. 218:293-311(1991).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9185572; DOI=10.1093/nar/25.13.2610;
RA Turmel M., Otis C., Cote V., Lemieux C.;
RT "Evolutionarily conserved and functionally important residues in the I-CeuI
RT homing endonuclease.";
RL Nucleic Acids Res. 25:2610-2619(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 5-211 IN COMPLEX WITH DNA AND
RP CALCIUM IONS, MUTAGENESIS OF GLN-93, AND SUBUNIT.
RX PubMed=16698548; DOI=10.1016/j.str.2006.03.009;
RA Spiegel P.C., Chevalier B., Sussman D., Turmel M., Lemieux C.,
RA Stoddard B.L.;
RT "The structure of I-CeuI homing endonuclease: evolving asymmetric DNA
RT recognition from a symmetric protein scaffold.";
RL Structure 14:869-880(2006).
CC -!- FUNCTION: Endonuclease involved in intron homing. Recognizes a
CC degenerate sequence of 17-19 bp to produce a staggered cut 5 bp
CC downstream from the CeLSU.5 intron insertion site.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. A third magnesium ion may be
CC bound between subunits. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16698548}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the LAGLIDADG endonuclease family.
CC {ECO:0000305}.
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DR EMBL; Z17234; CAA78934.1; -; Genomic_DNA.
DR PIR; S14133; S14133.
DR PDB; 2EX5; X-ray; 2.20 A; A/B=5-211.
DR PDBsum; 2EX5; -.
DR AlphaFoldDB; P32761; -.
DR SMR; P32761; -.
DR DIP; DIP-29110N; -.
DR REBASE; 2614; I-CeuI.
DR EvolutionaryTrace; P32761; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 1.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004860; LAGLIDADG_2.
DR Pfam; PF00961; LAGLIDADG_1; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; DNA-binding; Endonuclease; Hydrolase;
KW Intron homing; Magnesium; Metal-binding; Nuclease; Plastid.
FT CHAIN 1..218
FT /note="DNA endonuclease I-CeuI"
FT /id="PRO_0000192781"
FT REGION 71..75
FT /note="Interaction with DNA"
FT REGION 90..94
FT /note="Interaction with DNA"
FT REGION 114..116
FT /note="Interaction with DNA"
FT REGION 191..199
FT /note="Interaction with DNA"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT SITE 21
FT /note="Interaction with DNA"
FT SITE 80
FT /note="Interaction with DNA"
FT SITE 130
FT /note="Interaction with DNA"
FT SITE 172
FT /note="Interaction with DNA"
FT MUTAGEN 93
FT /note="Q->R: Impaired DNA cleavage activity."
FT /evidence="ECO:0000269|PubMed:16698548"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:2EX5"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:2EX5"
FT STRAND 82..94
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2EX5"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2EX5"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:2EX5"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2EX5"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:2EX5"
SQ SEQUENCE 218 AA; 24891 MW; A1748116D5AA48CD CRC64;
MSNFILKPGE KLPQDKLEEL KKINDAVKKT KNFSKYLIDL RKLFQIDEVQ VTSESKLFLA
GFLEGEASLN ISTKKLATSK FGLVVDPEFN VTQHVNGVKV LYLALEVFKT GRIRHKSGSN
ATLVLTIDNR QSLEEKVIPF YEQYVVAFSS PEKVKRVANF KALLELFNND AHQDLEQLVN
KILPIWDQMR KQQGQSNEGF PNLEAAQDFA RNYKKGIK
