ID LCL3_YARLI Reviewed; 226 AA.
AC Q6C427;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; OrderedLocusNames=YALI0E30305g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382131; CAG80189.1; -; Genomic_DNA.
DR RefSeq; XP_504585.1; XM_504585.1.
DR AlphaFoldDB; Q6C427; -.
DR SMR; Q6C427; -.
DR STRING; 284591.Q6C427; -.
DR EnsemblFungi; CAG80189; CAG80189; YALI0_E30305g.
DR GeneID; 2911940; -.
DR KEGG; yli:YALI0E30305g; -.
DR VEuPathDB; FungiDB:YALI0_E30305g; -.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; Q6C427; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 208975at2759; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR PANTHER; PTHR12302:SF3; ENDONUCLEASE LCL3-RELATED; 1.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 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..226
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408687"
FT TRANSMEM 15..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 53..212
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 226 AA; 25830 MW; 321F13E2D5E9010B CRC64;
MPEDSNKASN TARVVFYTSI LTGGILSSFY VYSRYFRRFT CTAEVPKKIY RGRTLFGRVT
SVGDGDNFHF YHTPGGRLAG WGWLRPYPET NKRGLGKETL HIRLYGVDAP ERPHFGRQGQ
PYGDEALEWL RSYILGRNVR VKLFSPDQYG RIVGGAKVWK LTGRKDVSTE MLKNGWGVKY
EGKMGAEFNG KGKLFQKLED HARKKKIGMF QQKGKIVTPG QYKKDE
//
