ID   LCL3_PYRTR              Reviewed;         271 AA.
AC   B2WC78;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-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=PTRG_07587;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231622; EDU50506.1; -; Genomic_DNA.
DR   RefSeq; XP_001937919.1; XM_001937884.1.
DR   AlphaFoldDB; B2WC78; -.
DR   SMR; B2WC78; -.
DR   STRING; 426418.B2WC78; -.
DR   EnsemblFungi; EDU50506; EDU50506; PTRG_07587.
DR   GeneID; 6345859; -.
DR   eggNOG; ENOG502RZZQ; Eukaryota.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   InParanoid; B2WC78; -.
DR   OMA; IYHTPGG; -.
DR   OrthoDB; 1333771at2759; -.
DR   Proteomes; UP000001471; 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..271
FT                   /note="Probable endonuclease lcl3"
FT                   /id="PRO_0000408680"
FT   TRANSMEM        38..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          76..236
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   271 AA;  31295 MW;  1238F1DF509120E8 CRC64;
     MRWPWSGDDH EQNKSSRLWA TSPKSSDWPS TLVEPRTLIA TLALTVSTVA GVRLYKTYLR
     RIPTVNHIKP NYFRRKSLFG QVTSVGDADN FRLYHTPGGR IAGWGLLPWK RIPTKREDLT
     KQTLHIRIAG VDAPELAHWG REAQPFSKEA HDWLINLIHN RRVRAYIYRR DQYDRVVAQV
     YVRRWLFRKD VGLEMLRAGL ATVYEAKTGA EFGTVEDKYR AAEQKARDSK VGMWAKPTLR
     QRLGGAPTQP PESPREYKNR HNAAEKLKKP G