SCE1_YEAST
ID SCE1_YEAST Reviewed; 235 AA.
AC P03882; A0A0A7NYJ1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Intron-encoded endonuclease I-SceI;
DE EC=3.1.-.-;
DE AltName: Full=21S rRNA intron maturase;
DE AltName: Full=Homing endonuclease omega;
GN Name=SCEI; Synonyms=OMEGA, SECY; OrderedLocusNames=Q0160;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IL8-8C/R53;
RX PubMed=6156002; DOI=10.1016/0092-8674(80)90246-9;
RA Dujon B.;
RT "Sequence of the intron and flanking exons of the mitochondrial 21S rRNA
RT gene of yeast strains having different alleles at the omega and rib-1
RT loci.";
RL Cell 20:185-197(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTRON HOMING.
RX PubMed=3886163; DOI=10.1016/s0092-8674(85)80011-8;
RA Jacquier A., Dujon B.;
RT "An intron-encoded protein is active in a gene conversion process that
RT spreads an intron into a mitochondrial gene.";
RL Cell 41:383-394(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9872396; DOI=10.1016/s0014-5793(98)01467-7;
RA Foury F., Roganti T., Lecrenier N., Purnelle B.;
RT "The complete sequence of the mitochondrial genome of Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 440:325-331(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, ENDONUCLEASE ACTIVITY, COFACTOR, PH OPTIMUM, CLEAVAGE SITE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=2183191; DOI=10.1093/nar/18.6.1407;
RA Monteilhet C., Perrin A., Thierry A., Colleaux L., Dujon B.;
RT "Purification and characterization of the in vitro activity of I-Sce I, a
RT novel and highly specific endonuclease encoded by a group I intron.";
RL Nucleic Acids Res. 18:1407-1413(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=14636596; DOI=10.1016/j.jmb.2003.09.068;
RA Moure C.M., Gimble F.S., Quiocho F.A.;
RT "The crystal structure of the gene targeting homing endonuclease I-SceI
RT reveals the origins of its target site specificity.";
RL J. Mol. Biol. 334:685-695(2003).
CC -!- FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. It
CC introduces a specific double-strand break in the DNA of the 21S rRNA
CC gene and thus mediates the insertion of an intron, containing its own
CC coding sequence (group I intron), into an intronless gene. Specifically
CC recognizes and cleaves the sequence 5'-TAGGGATAACAGGGTAAT-3'.
CC {ECO:0000269|PubMed:2183191}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:2183191};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9-10. {ECO:0000269|PubMed:2183191};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2183191}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the LAGLIDADG endonuclease family.
CC {ECO:0000305}.
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DR EMBL; M11280; AAA32168.2; -; Genomic_DNA.
DR EMBL; V00684; CAA24055.1; -; Genomic_DNA.
DR EMBL; KP263414; AIZ98896.1; -; Genomic_DNA.
DR PIR; A23170; QQBY1M.
DR RefSeq; NP_009324.1; NC_001224.1.
DR PDB; 1R7M; X-ray; 2.25 A; A/B=1-235.
DR PDB; 3C0W; X-ray; 2.20 A; A=1-235.
DR PDB; 3C0X; X-ray; 2.30 A; A=1-235.
DR PDB; 3OOL; X-ray; 2.30 A; A=1-235.
DR PDB; 3OOR; X-ray; 2.50 A; A=1-235.
DR PDB; 5A0M; X-ray; 2.90 A; A/B=1-235.
DR PDBsum; 1R7M; -.
DR PDBsum; 3C0W; -.
DR PDBsum; 3C0X; -.
DR PDBsum; 3OOL; -.
DR PDBsum; 3OOR; -.
DR PDBsum; 5A0M; -.
DR AlphaFoldDB; P03882; -.
DR SMR; P03882; -.
DR BioGRID; 34783; 2.
DR STRING; 4932.Q0160; -.
DR REBASE; 2594; I-SceI.
DR PaxDb; P03882; -.
DR PRIDE; P03882; -.
DR EnsemblFungi; Q0160_mRNA; Q0160; Q0160.
DR GeneID; 854590; -.
DR KEGG; sce:Q0160; -.
DR SGD; S000007279; SCEI.
DR VEuPathDB; FungiDB:Q0160; -.
DR eggNOG; ENOG502TAHD; Eukaryota.
DR HOGENOM; CLU_1355297_0_0_1; -.
DR InParanoid; P03882; -.
DR OMA; LAWWYQD; -.
DR BioCyc; YEAST:G3O-34385-MON; -.
DR EvolutionaryTrace; P03882; -.
DR PRO; PR:P03882; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P03882; protein.
DR GO; GO:0005739; C:mitochondrion; TAS:SGD.
DR GO; GO:0004519; F:endonuclease activity; IDA:SGD.
DR GO; GO:0006314; P:intron homing; TAS:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 2.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004860; LAGLIDADG_2.
DR Pfam; PF03161; LAGLIDADG_2; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Intron homing; Mitochondrion;
KW mRNA processing; mRNA splicing; Nuclease; Reference proteome.
FT CHAIN 1..235
FT /note="Intron-encoded endonuclease I-SceI"
FT /id="PRO_0000192785"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3OOR"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1R7M"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3C0X"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3OOR"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3C0W"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3C0W"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:3C0W"
SQ SEQUENCE 235 AA; 27683 MW; 551B6EF3BC8E3D4C CRC64;
MKNIKKNQVM NLGPNSKLLK EYKSQLIELN IEQFEAGIGL ILGDAYIRSR DEGKTYCMQF
EWKNKAYMDH VCLLYDQWVL SPPHKKERVN HLGNLVITWG AQTFKHQAFN KLANLFIVNN
KKTIPNNLVE NYLTPMSLAY WFMDDGGKWD YNKNSTNKSI VLNTQSFTFE EVEYLVKGLR
NKFQLNCYVK INKNKPIIYI DSMSYLIFYN LIKPYLIPQM MYKLPNTISS ETFLK
