ID   LCL3_CLAL4              Reviewed;         233 AA.
AC   C4Y4X4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; ORFNames=CLUG_03208;
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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; CH408079; EEQ39080.1; -; Genomic_DNA.
DR   RefSeq; XP_002615967.1; XM_002615921.1.
DR   AlphaFoldDB; C4Y4X4; -.
DR   SMR; C4Y4X4; -.
DR   STRING; 306902.C4Y4X4; -.
DR   EnsemblFungi; EEQ39080; EEQ39080; CLUG_03208.
DR   GeneID; 8497101; -.
DR   KEGG; clu:CLUG_03208; -.
DR   VEuPathDB; FungiDB:CLUG_03208; -.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   InParanoid; C4Y4X4; -.
DR   OMA; IYHTPGG; -.
DR   Proteomes; UP000007703; 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; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..233
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408655"
FT   TRANSMEM        22..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          62..220
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   233 AA;  26267 MW;  3B51C5ADB5404836 CRC64;
     MSDEPLSSSE ESPSVSVLHP KVLLLSAGFT GAAAASYFLY GRYVRRVKTY LDLTPAILDG
     QRKLYGKVTR VGDGDNFRFF HTPGGVLLGW GWLRKIPDTR SGLKDQTLMV RLCGVDAPER
     SHFGKPAQPF SEEALQWLQS YVGGRSVTIT PYSIDQYKRV VARAQVWRWT GKRDVSAEML
     RNGLGVVYEA NSGAEFGENE GWYRRLEEKA KRRRRGMWSL GSKLVTPGNF KRQ