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LCL3_CANTT
ID   LCL3_CANTT              Reviewed;         235 AA.
AC   C5MC60;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; ORFNames=CTRG_03652;
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1;
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; GG692398; EER33227.1; -; Genomic_DNA.
DR   RefSeq; XP_002549355.1; XM_002549309.1.
DR   AlphaFoldDB; C5MC60; -.
DR   SMR; C5MC60; -.
DR   STRING; 5482.XP_002549355.1; -.
DR   EnsemblFungi; EER33227; EER33227; CTRG_03652.
DR   GeneID; 8297786; -.
DR   KEGG; ctp:CTRG_03652; -.
DR   VEuPathDB; FungiDB:CTRG_03652; -.
DR   eggNOG; ENOG502S1U4; Eukaryota.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   OrthoDB; 1333771at2759; -.
DR   Proteomes; UP000002037; 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..235
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408654"
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;  27012 MW;  917682B36C5CB8A3 CRC64;
     MAPIPPTPAQ DISILHPKVL LLSAGITTSL FLGYRFYTRY VRRVRTYLDL TPSIIENNKK
     LYGYVTRVGD GDNFRFYHTP GGLLMGWGWL RKIPTTRKEL KDETLMIRLC GIDAPEGAHF
     GKPAQPFADD ALNWLRGYVD GKYVTITPYS IDQYKRVVAR AQIWKWTGKK DVSAEMLKTG
     YAIVYEGKAE AEFGDNEDWY RKLEAHSKRL RKGVWSLGKK LTTPGEFKRV HYRGE
 
 
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