LCL3_LODEL
ID LCL3_LODEL Reviewed; 238 AA.
AC A5E1Q5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=LELG_03542;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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; CH981527; EDK45363.1; -; Genomic_DNA.
DR RefSeq; XP_001525614.1; XM_001525564.1.
DR AlphaFoldDB; A5E1Q5; -.
DR SMR; A5E1Q5; -.
DR STRING; 379508.A5E1Q5; -.
DR EnsemblFungi; EDK45363; EDK45363; LELG_03542.
DR GeneID; 5232862; -.
DR KEGG; lel:LELG_03542; -.
DR VEuPathDB; FungiDB:LELG_03542; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; A5E1Q5; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000001996; 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..238
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408666"
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 61..220
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 238 AA; 27782 MW; 6524073A08F5ECBC CRC64;
MPPVPVNSTS QDYYGVLEPR VWLLSAGLAA SAIFSYKIYR RYFRRIRSIL DFTPEALEKN
HKLYGYVTRV GDGDNFRFYH TPGGWLLGWG WLRKVPLDNR RIMKDETLMI RLCGVDAPER
AHFGKPAQPF SEDALLWLKN YLLGRYVTVT PYSIDQYKRI VGRCQVWKWN GKKDVSAEML
KNGVAIVYEG KVGAEFGDNE DRYRSLEKRA KWLKRGVWSI GKKMMTPGEY KKVYYRGE