ID   LCL3_VANPO              Reviewed;         278 AA.
AC   A7TE94;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; ORFNames=Kpol_1002p63;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480379; EDO19416.1; -; Genomic_DNA.
DR   RefSeq; XP_001647274.1; XM_001647224.1.
DR   AlphaFoldDB; A7TE94; -.
DR   STRING; 436907.A7TE94; -.
DR   EnsemblFungi; EDO19416; EDO19416; Kpol_1002p63.
DR   GeneID; 5547766; -.
DR   KEGG; vpo:Kpol_1002p63; -.
DR   eggNOG; ENOG502S1U4; Eukaryota.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   InParanoid; A7TE94; -.
DR   OMA; IYHTPGG; -.
DR   OrthoDB; 1333771at2759; -.
DR   PhylomeDB; A7TE94; -.
DR   Proteomes; UP000000267; 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..278
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408685"
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          58..263
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   278 AA;  32246 MW;  8A20A5AE49BA1CAE CRC64;
     MSDIDEKNDT KESSFSSDVV LLSLLISGST LGAIAGYNRY LKQVTKATDI PNYMFRKRWM
     YGKVTAVGDG DNFHLFHTPG GIFGGWGWLR KVPKLPKSDS NGLIVSRKKT SNFYSGLKNS
     YHKFTGSYRY SSEYFLDLKV PYKNLRNLPT VPIRLCAIDA PERAHFGNTS QPYGDEALIW
     LRNRLLGKYV WVKPLSVDQY NRCVSKVVCW NWLGWQNISL QMVRQGLAVV YEGKTSAEFD
     REEFLYRFYE RRSKAKKRGL WRQRVIETPG EYKKKIKK