ID   LCL3_KOMPG              Reviewed;         228 AA.
AC   C4QW04;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; OrderedLocusNames=PAS_chr1-1_0068;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(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; FN392319; CAY67427.1; -; Genomic_DNA.
DR   RefSeq; XP_002489708.1; XM_002489663.1.
DR   AlphaFoldDB; C4QW04; -.
DR   SMR; C4QW04; -.
DR   STRING; 644223.C4QW04; -.
DR   EnsemblFungi; CAY67427; CAY67427; PAS_chr1-1_0068.
DR   GeneID; 8197196; -.
DR   KEGG; ppa:PAS_chr1-1_0068; -.
DR   eggNOG; ENOG502S1U4; Eukaryota.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   InParanoid; C4QW04; -.
DR   OMA; IYHTPGG; -.
DR   Proteomes; UP000000314; Chromosome 1.
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..228
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408677"
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..214
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         110
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   228 AA;  26379 MW;  5EFA8A974915C29C CRC64;
     MAQSNQHVSI YNPKVIVYSI GLTTAILASM SIYRSHFVRF STSLDVPKTL FRTKHLHGKV
     TSVGDGDNFH FYHLPGGIFA GWGWIRETPE INKFRKLKNK TIHVRLCGVD APERSHFGKP
     SQPYSEEALQ WLRQFILGKK VKVKPLSVDQ YNRIVGRVFI FRWNGWNDVS EEMLRNGVAI
     VYENKSSAEF DGMKERYLKV ENKAKKKKKG LWGIERGLTP GEYKRLYK