ID   LCL3_YEAS8              Reviewed;         274 AA.
AC   C8Z8G3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; ORFNames=EC1118_1G1_2036g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000250}; Single-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LCL3 family. {ECO:0000305}.
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DR   EMBL; FN393070; CAY79679.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z8G3; -.
DR   EnsemblFungi; CAY79679; CAY79679; EC1118_1G1_2036g.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   Proteomes; UP000000286; Chromosome VII, Scaffold EC1118_1G1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.90; -; 1.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR   Pfam; PF00565; SNase; 1.
DR   SMART; SM00318; SNc; 1.
DR   SUPFAM; SSF50199; SSF50199; 1.
DR   PROSITE; PS50830; TNASE_3; 1.
PE   3: Inferred from homology;
KW   Calcium; Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW   Nuclease; Transmembrane; Transmembrane helix.
FT   CHAIN           1..274
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408692"
FT   TRANSMEM        15..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          53..261
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         156
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   274 AA;  32054 MW;  A912B01CEE03545C CRC64;
     MREGDSNSKK SADVAVLSII LTGSTLTLIY TYKRYLTQFK RTNDIPRRIF RKHWLYGKVT
     SVGDGDNFHF FHMPGGIRGG WGWLRPVPQM IKNGSTAEKL VGDSRNMRFF NFNWITHGRS
     TKSKIQKAKS QFLKLNVPYK NRKNLPTIPI RLCGIDAPER AHFGNPAQPF GNEALIWLQN
     RILGKKVWVK PLSIDQYNRC VARVSYWDWF GGWKDLSLEM LKDGLAVVYE GKVNTEFDDR
     EDKYRYYEFL ARSRKKGLWI QNKFETPGEY KKRI