LCL3_PICGU
ID LCL3_PICGU Reviewed; 228 AA.
AC A5DNZ8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=PGUG_04999;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408160; EDK40901.1; -; Genomic_DNA.
DR RefSeq; XP_001483044.1; XM_001482994.1.
DR AlphaFoldDB; A5DNZ8; -.
DR SMR; A5DNZ8; -.
DR STRING; 4929.XP_001483044.1; -.
DR EnsemblFungi; EDK40901; EDK40901; PGUG_04999.
DR GeneID; 5125052; -.
DR KEGG; pgu:PGUG_04999; -.
DR VEuPathDB; FungiDB:PGUG_04999; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; A5DNZ8; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000001997; 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..228
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408676"
FT TRANSMEM 13..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 52..210
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 228 AA; 26393 MW; E1DEDB4EE8BA9269 CRC64;
MGDSVSVLHP KVLLVSAGFT TSLFVGFNLY RRYCRRIRTY LDLTPSILDN QRQLYGKVTR
VGDGDNFRFY HTPGGIFLGW GWLRKVPETR SALKDETLMI RLCGVDAPER SHWGKPAQPF
SEEALQWLRN YVMGRYVTIT PYSIDQYKRV VARAQVWKWT GRKDVSAEMI RTGIGVVYES
KVGAEFGDNE SWYRSLQNRA KLLRRGVWSL GKKMTTPGQF KKTYYRGE
