ID   ENS2_YEASX              Reviewed;         476 AA.
AC   P12294; E9P9W9; P05512;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Endonuclease SceI small subunit;
DE            EC=3.1.21.-;
DE   AltName: Full=Endo.SceI 50 kDa subunit;
DE   AltName: Full=Maturase-like RF3 protein;
GN   Name=ENS2; Synonyms=RF3;
OS   Saccharomyces cerevisiae (Baker's yeast).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D273-10B/A;
RX   PubMed=2987871; DOI=10.1093/nar/13.8.3005;
RA   Seraphin B., Simon M., Faye G.;
RT   "A mitochondrial reading frame which may code for a maturase-like protein
RT   in Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 13:3005-3014(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=4228 / ATCC 9080 / CBS 2354 / DSM 70424 / NBRC 0565 / NCYC 74 / NRRL
RC   Y-1089;
RX   PubMed=2440860; DOI=10.1016/s0021-9258(18)61090-7;
RA   Seraphin B., Simon M., Faye G.;
RT   "The mitochondrial reading frame RF3 is a functional gene in Saccharomyces
RT   uvarum.";
RL   J. Biol. Chem. 262:10146-10153(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-39; 110-118;
RP   140-154; 191-199; 248-251; 274-281; 288-299 AND 458-461, AND FUNCTION.
RC   STRAIN=ATCC 46276 / IAM 4274 / NCYC 1408 / OC-2;
RX   PubMed=1988456; DOI=10.1016/s0021-9258(18)52388-7;
RA   Nakagawa K., Morishima N., Shibata T.;
RT   "A maturase-like subunit of the sequence-specific endonuclease endo.SceI
RT   from yeast mitochondria.";
RL   J. Biol. Chem. 266:1977-1984(1991).
RN   [4]
RP   ERRATUM OF PUBMED:1988456.
RA   Nakagawa K., Morishima N., Shibata T.;
RL   J. Biol. Chem. 266:10018-10018(1991).
RN   [5]
RP   IDENTIFICATION IN ENDONUCLEASE SCEI, AND FUNCTION.
RX   PubMed=2828049; DOI=10.1111/j.1432-1033.1988.tb13753.x;
RA   Nakagawa K., Hashikawa J., Makino O., Ando T., Shibata T.;
RT   "Subunit structure of a yeast site-specific endodeoxyribonuclease, endo
RT   SceI. A study using monoclonal antibodies.";
RL   Eur. J. Biochem. 171:23-29(1988).
RN   [6]
RP   FUNCTION.
RX   PubMed=7625280; DOI=10.1016/0065-227x(95)99384-2;
RA   Shibata T., Nakagawa K., Morishima N.;
RT   "Multi-site-specific endonucleases and the initiation of homologous genetic
RT   recombination in yeast.";
RL   Adv. Biophys. 31:77-91(1995).
RN   [7]
RP   FUNCTION.
RX   PubMed=10464305; DOI=10.1074/jbc.274.36.25682;
RA   Mizumura H., Shibata T., Morishima N.;
RT   "Stable association of 70-kDa heat shock protein induces latent multisite
RT   specificity of a unisite-specific endonuclease in yeast mitochondria.";
RL   J. Biol. Chem. 274:25682-25690(1999).
CC   -!- FUNCTION: Catalytic component of endonuclease SceI (Endo.SceI), which
CC       cleaves specifically at multiple sites on mitochondrial DNA and
CC       produces double-stranded breaks. {ECO:0000269|PubMed:10464305,
CC       ECO:0000269|PubMed:1988456, ECO:0000269|PubMed:2828049,
CC       ECO:0000269|PubMed:7625280}.
CC   -!- SUBUNIT: Endonuclease SceI (Endo.SceI) is a heterodimer of ENS2 and
CC       SSC1. {ECO:0000269|PubMed:2828049}.
CC   -!- INTERACTION:
CC       P12294; P0CS90: SSC1; Xeno; NbExp=2; IntAct=EBI-6490, EBI-8637;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the LAGLIDADG endonuclease family.
CC       {ECO:0000305}.
CC   -!- CAUTION: S.cerevisiae displays strain polymorphism with regard to
CC       Endo.SceI endouclease activity. This is due to the mitochondrion-
CC       encoded, catalytic subunit ENS2, which exhibits strain polymorphism. It
CC       can be either present as continuous ORF in the mitochondrial genome
CC       (e.g. strain IAM 4274), present but disrupted by the insertion of GC
CC       clusters (e.g. strain D273-10B/A), or completely absent in the
CC       mitochondrial genome (e.g. strain S288c). {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26271.1; Type=Miscellaneous discrepancy; Note=In strain D273-10B/A, RF3 is interrupted by GC clusters, which introduce a shift of +1 base und thus break the frame, producing 4 overlapping ORFs.; Evidence={ECO:0000305};
CC       Sequence=CAA26272.1; Type=Miscellaneous discrepancy; Note=In strain D273-10B/A, RF3 is interrupted by GC clusters, which introduce a shift of +1 base und thus break the frame, producing 4 overlapping ORFs.; Evidence={ECO:0000305};
CC       Sequence=CAA26273.1; Type=Miscellaneous discrepancy; Note=In strain D273-10B/A, RF3 is interrupted by GC clusters, which introduce a shift of +1 base und thus break the frame, producing 4 overlapping ORFs.; Evidence={ECO:0000305};
CC       Sequence=CAA26274.1; Type=Miscellaneous discrepancy; Note=In strain D273-10B/A, RF3 is interrupted by GC clusters, which introduce a shift of +1 base und thus break the frame, producing 4 overlapping ORFs.; Evidence={ECO:0000305};
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DR   EMBL; X02421; CAA26271.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X02421; CAA26272.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X02421; CAA26273.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X02421; CAA26274.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; J03300; AAA32166.2; -; Genomic_DNA.
DR   EMBL; M63839; AAA32160.2; -; Genomic_DNA.
DR   PIR; A23003; A23003.
DR   PIR; A28439; A28439.
DR   AlphaFoldDB; P12294; -.
DR   SMR; P12294; -.
DR   ComplexPortal; CPX-1741; Endonuclease SceI.
DR   DIP; DIP-2N; -.
DR   IntAct; P12294; 1.
DR   REBASE; 2773; F-SceI.
DR   PRIDE; P12294; -.
DR   SGD; S000029698; ENS2.
DR   GO; GO:1905347; C:endodeoxyribonuclease complex; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0032042; P:mitochondrial DNA metabolic process; IDA:ComplexPortal.
DR   GO; GO:0000018; P:regulation of DNA recombination; IDA:ComplexPortal.
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   Direct protein sequencing; Endonuclease; Hydrolase; Mitochondrion;
KW   Nuclease.
FT   CHAIN           1..476
FT                   /note="Endonuclease SceI small subunit"
FT                   /id="PRO_0000086979"
FT   VARIANT         36
FT                   /note="E -> G (in strain: D273-10B/A)"
FT   VARIANT         217
FT                   /note="G -> K (in strain: D273-10B/A and NCYC 74)"
FT   VARIANT         346
FT                   /note="N -> D (in strain: D273-10B/A and NCYC 74)"
SQ   SEQUENCE   476 AA;  57791 MW;  AE561085E55FDA69 CRC64;
     MKKQNLNSIL LMYINYIINY FNNIHKNQLK KDWIMEYEYM YKFLMNNMTC FIKWDNNKIL
     LLLDMYYNVL YNYHKQRTPM SNKRLMNSKN IMDYKLLYTY FYILNKMKME MDNYNNNNNN
     ISLKYNELLK NIMNNLNYKT SNIETNLSNN FYLMDKYLIN KYMKYLDMLN MIPNNYMFNN
     INYKGKLNIK TVLDLNNNEF YDYLSGLIEG DGYIGPGGIT ITNHANDVLN TIFINKRIKN
     SILVEKWMDT LKDNPYFVNA FSINIKTNLA KEKIFTNIYN KLYSDYKINQ INNHIPYYNY
     LKINNKLPIK NIMDIKNNYW LAGFTAADGS FLSSMYNPKD TLLFKNMRPS YVISQVETRK
     ELIYLIQESF DLSISNVKKV GNRKLKDFKL FTRTTDELMK FIYYFDKFLP LHDNKQFNYI
     KFRFNTFIKS YNWNNRVFGL VLSEYINNIK IDNYDYYYYN KYINMHNARK PKGYIK