LCL3_CANAW
ID LCL3_CANAW Reviewed; 235 AA.
AC C4YFU9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=CAWG_00075;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
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; CH672346; EEQ41888.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YFU9; -.
DR SMR; C4YFU9; -.
DR STRING; 5476.C4YFU9; -.
DR EnsemblFungi; EEQ41888; EEQ41888; CAWG_00075.
DR VEuPathDB; FungiDB:CAWG_00075; -.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..235
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408651"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 59..217
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 235 AA; 27374 MW; 9900B28BDD053ED7 CRC64;
MPPIPAEPTE NISIFHPKVL LLSAGVTTSL FFGYKFYKRY IKRIRTYLDL TPSIIENNTK
LYGYVTRVGD GDNFRFYHTP GGWFFGWGWL RKIPTTRKDL KDETLMIRLC GVDAPEGAHF
GKPAQPYSKE ALYWLREYVD GKYVTITPYS IDQYKRVVAR AQIWKWTGRK DVSAEMLKVG
YAIVYEGKAE AEFGDNEDWY RKLESRAKLL RKGVWSLGKN LTTPGEFKRI HYRGE
