LCL3_CANDC
ID LCL3_CANDC Reviewed; 235 AA.
AC B9W9Z5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=CD36_12760;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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; FM992688; CAX45633.1; -; Genomic_DNA.
DR RefSeq; XP_002417915.1; XM_002417870.1.
DR AlphaFoldDB; B9W9Z5; -.
DR SMR; B9W9Z5; -.
DR STRING; 42374.XP_002417915.1; -.
DR EnsemblFungi; CAX45633; CAX45633; CD36_12760.
DR GeneID; 8045466; -.
DR KEGG; cdu:CD36_12760; -.
DR CGD; CAL0000167676; Cd36_12760.
DR VEuPathDB; FungiDB:CD36_12760; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000002605; Chromosome 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_0000408652"
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; 27282 MW; B4B19676689DBED6 CRC64;
MPPIPPDPTE SISIFHPKVI LLSAGVTTSL FFGYKFYKRY IRRIKTYLDL TPTIIENNTK
LYGYVTRVGD GDNFRFYHTP GGWIFGWGWL RKIPTTRKDL KDETLMIRLC GVDAPEGAHF
GKPAQPFSKE ALHWLREYVD GKYVTITPYS IDQYKRVVAR AQIWKWTGKK DISAEMLKVG
YAIVYEGKAE AEFGDNEDWY RKLESRAKLL RKGVWSLGKN LTTPGEFKRI HYRGE
