LCL3_KLULA
ID LCL3_KLULA Reviewed; 270 AA.
AC Q6CMM1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; OrderedLocusNames=KLLA0E19163g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99905.1; -; Genomic_DNA.
DR RefSeq; XP_454818.1; XM_454818.1.
DR AlphaFoldDB; Q6CMM1; -.
DR STRING; 28985.XP_454818.1; -.
DR EnsemblFungi; CAG99905; CAG99905; KLLA0_E19163g.
DR GeneID; 2893956; -.
DR KEGG; kla:KLLA0_E19163g; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; Q6CMM1; -.
DR OMA; IYHTPGG; -.
DR Proteomes; UP000000598; Chromosome E.
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..270
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408662"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 58..257
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 270 AA; 31165 MW; 4E4912589CD578A9 CRC64;
MTEQRTVTNN ATHYFYPTVL LFSILLTGGV LTATSFYNKH LRQYKSAKDI PEAIFKKQWL
YGKVTSVGDG DNFHFFHTPS GIFGGWGWLR SIPELQTVAF DASVEVPQSV RWWNKLFSAK
VANYKSHFMS LHVPYKGRRN LPTISVRLCG VDAPERSHFG KTAQPFSDEA LNWLRYKILG
QYVWVKPLAV DQYGRCVARV ELWSWLKGWQ NISIEMLKEG VGVVYEGKVG AEFDNQEDIY
LYEELNSKKA KRGLWSQRKF ETPGAYKKRT