ID   LCL3_ASPTN              Reviewed;         295 AA.
AC   Q0CUT8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Probable endonuclease lcl3;
DE            EC=3.1.-.-;
GN   Name=lcl3; ORFNames=ATEG_02546;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37508.1; -; Genomic_DNA.
DR   RefSeq; XP_001211724.1; XM_001211724.1.
DR   AlphaFoldDB; Q0CUT8; -.
DR   SMR; Q0CUT8; -.
DR   STRING; 341663.Q0CUT8; -.
DR   EnsemblFungi; EAU37508; EAU37508; ATEG_02546.
DR   GeneID; 4316848; -.
DR   VEuPathDB; FungiDB:ATEG_02546; -.
DR   eggNOG; ENOG502S1U4; Eukaryota.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   OMA; IYHTPGG; -.
DR   OrthoDB; 1333771at2759; -.
DR   Proteomes; UP000007963; 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..295
FT                   /note="Probable endonuclease lcl3"
FT                   /id="PRO_0000408648"
FT   TRANSMEM        60..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          98..265
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         154
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   295 AA;  34200 MW;  9596D61398C50DF6 CRC64;
     MRWPPWGSES QQADTPSPST EQQAQQPPTA PAARPSRPNK DWNQSVNAFD WAAFTELRTI
     IPTAILTTAI LGIVHIHRRY LRRFPDAVSI APSYFRQRSI LGQVTSVGDG DNFRLFHTPG
     GRLAGWGWLP WKKVPTSKKE LRDKTVHVRL AGIDAPELAH FGRPAQPFAR EAHQWLTAYL
     MTRRVRAYVH RQDQYQRVVA SVYVRRALDF PPFRRRDVSY EMLRRGLATV YEAKAGAEFG
     GPGMERKYRR AEWWAKFRGL GLWKGFRRNK EWESPREFKT RMGLEDQTQG RENKS