ID   LCL3_ARTOC              Reviewed;         282 AA.
AC   C5FTB4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; ORFNames=MCYG_05936;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995705; EEQ33117.1; -; Genomic_DNA.
DR   RefSeq; XP_002846067.1; XM_002846021.1.
DR   AlphaFoldDB; C5FTB4; -.
DR   SMR; C5FTB4; -.
DR   STRING; 63405.XP_002846067.1; -.
DR   EnsemblFungi; EEQ33117; EEQ33117; MCYG_05936.
DR   GeneID; 9224356; -.
DR   eggNOG; ENOG502S1U4; Eukaryota.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   OMA; IYHTPGG; -.
DR   OrthoDB; 1333771at2759; -.
DR   Proteomes; UP000002035; 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..282
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408640"
FT   TRANSMEM        55..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          95..256
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         149
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   282 AA;  32123 MW;  769AB086E4A9497F CRC64;
     MRWLFWTSEN DKDECKCNNK PSSNSDEKPS IILNSSKDWN ALSNATNWSH FLEPSNLIPT
     VLLTSGILFA VRIHRRYLRR IPEATNISPS YLRQRSILGK VTSVGDGDNF RIYHTPGGML
     AGWGWLRKVP TSKKELKNNT IHIRIAGVDA PELAHFGRPS QPFGEEAHTW LTNRLIGRRI
     RAYVYRPDQY SRVVATVYAY RFLFFPQDIG LQMLREGLAT IYEAKSGAEF GGPKQEKKYR
     DAEALAKKKG KGLWKAKASS DWESPRDFKS RMNAIDQGKG ST