ID   LCL3_PODAN              Reviewed;         277 AA.
AC   B2AU25; A0A090CFP3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; OrderedLocusNames=Pa_1_17740; ORFNames=PODANS_1_17740;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000250}; Single-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LCL3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU633899; CAP67898.1; -; Genomic_DNA.
DR   EMBL; FO904936; CDP24157.1; -; Genomic_DNA.
DR   RefSeq; XP_001907227.1; XM_001907192.1.
DR   AlphaFoldDB; B2AU25; -.
DR   SMR; B2AU25; -.
DR   STRING; 515849.B2AU25; -.
DR   EnsemblFungi; CAP67898; CAP67898; PODANS_1_17740.
DR   GeneID; 6191430; -.
DR   KEGG; pan:PODANSg4260; -.
DR   VEuPathDB; FungiDB:PODANS_1_17740; -.
DR   eggNOG; ENOG502S1U4; Eukaryota.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   OrthoDB; 1333771at2759; -.
DR   Proteomes; UP000001197; 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..277
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408679"
FT   TRANSMEM        39..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          77..239
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         131
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   277 AA;  31226 MW;  61011A2A32BE7B91 CRC64;
     MPWSPGSSSA PSGDKDDIKS KLSSWTKPIR DHLSEGGNWI APIIAAGATM GFWSFYKTYL
     RRIPNSAHVS PRYFHRRSLF GKVTSVGDGD GFHLYHTPGG RLAGWGWLRT VPKLKKELKG
     QTIPIRIAGV DAPEGGHFGR TAQPFAAEAQ KFLDSHILNR RVRAYVWRRD QYDRIVATVY
     VRRPPFFQRK DVSMELLKQG FATTYEAKTG AEFGGPSKEI EYKVAEEVAR QKGKGMWSLE
     KGGGFFHPSK KARAIESPMA YKRRVKLAEE PQRKLDS