LCL3_DEBHA
ID LCL3_DEBHA Reviewed; 235 AA.
AC Q6BSY9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; OrderedLocusNames=DEHA2D04950g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG86820.2; -; Genomic_DNA.
DR RefSeq; XP_458681.2; XM_458681.1.
DR AlphaFoldDB; Q6BSY9; -.
DR SMR; Q6BSY9; -.
DR STRING; 4959.XP_458681.2; -.
DR PRIDE; Q6BSY9; -.
DR EnsemblFungi; CAG86820; CAG86820; DEHA2D04950g.
DR GeneID; 2901123; -.
DR KEGG; dha:DEHA2D04950g; -.
DR VEuPathDB; FungiDB:DEHA2D04950g; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; Q6BSY9; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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..235
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408659"
FT TRANSMEM 11..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 58..216
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 235 AA; 27210 MW; 3227A5106386C8BB CRC64;
MPPIPSEPEN ISLIHPKVLL LSAGVTTSLF LSYKFYKRYV RRIRNYLDLT PEILDRQTPL
YGRVTRVGDG DNFRFYHTPG GILFGWGWLR HVPTKRQELK DETLMVRLCG VDAPERAHWG
KPAQPYSEEA LAWLKNYIFG RNVVVTPYSI DQYKRLVGRA QVWKWTGKKD ISAEMLRNGL
GVVYEGKIGA EFGDNESWYR KLEARAKWLR RGLWSLGSSM TTPGEFKKVH YRGDS