LCL3_SCHJY
ID LCL3_SCHJY Reviewed; 233 AA.
AC B6JYT1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=SJAG_01749;
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936;
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; KE651168; EEB06699.1; -; Genomic_DNA.
DR RefSeq; XP_002172992.1; XM_002172956.2.
DR AlphaFoldDB; B6JYT1; -.
DR SMR; B6JYT1; -.
DR STRING; 4897.EEB06699; -.
DR PRIDE; B6JYT1; -.
DR EnsemblFungi; EEB06699; EEB06699; SJAG_01749.
DR GeneID; 7048181; -.
DR VEuPathDB; FungiDB:SJAG_01749; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; LLGWHWL; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000001744; 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..233
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408682"
FT TRANSMEM 10..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 57..218
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 233 AA; 27138 MW; BD8919A9899911C7 CRC64;
MQNQRNEYSI SLRNLSYIIL TISTGIVIHR KFRRIKDIED LSSRFFRGQQ KSLTKLNSLY
GYVTSVGDGD NFRFYHTPGG RLLGWHWLRK VPSNRNALKN ETLSIRLSGI DAPESGYFGK
LGQPFSLEAK QFLARKLEHR SVRVYPLHRD QYNRAVCGVT YYPIRWLFFK RDIGPQLVSR
GLAVVYEGAN SSYYPTEKSV LMKIQETARK RKLGMHSLGN KLELPKDYKK RNK