ID   LCL3_YEAS1              Reviewed;         274 AA.
AC   B3LHF1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; ORFNames=SCRG_01084;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408044; EDV10309.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LHF1; -.
DR   EnsemblFungi; EDV10309; EDV10309; SCRG_01084.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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_0000408688"
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;  32112 MW;  38C1B01FEF4838A0 CRC64;
     MREGDSNSKK SADVAVLSII LTGSTLTLIY TYKRYLTQFK RTNDIPRRIF RKHWLYGKVT
     SVGDGDNFHF FHMPGGIRGG WGWLRPVPQM IKNDSTAEKL VGDSRNMRFF NFNWITHGRS
     TKSKIQKAKS QFLKLNVPYK NRKNLPTIPI RLCGIDAPER AHFGNPAQPF GNEALIWLQN
     RILGKKVWVK PLSIDQYNRC VARVSYWDWF GGWKDLSLEM LKDGLAVVYE GKVNTEFDDR
     EDKYRYYEFL ARSRKKGLWI QNKFETPGEY KKRI