LCL3_ASHGO
ID LCL3_ASHGO Reviewed; 276 AA.
AC Q754Z2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; OrderedLocusNames=AFL066C; ORFNames=AGOS_AFL066C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53306.1; -; Genomic_DNA.
DR RefSeq; NP_985482.1; NM_210836.1.
DR AlphaFoldDB; Q754Z2; -.
DR STRING; 33169.AAS53306; -.
DR EnsemblFungi; AAS53306; AAS53306; AGOS_AFL066C.
DR GeneID; 4621712; -.
DR KEGG; ago:AGOS_AFL066C; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; Q754Z2; -.
DR OMA; IYHTPGG; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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..276
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408641"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 56..260
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 276 AA; 31336 MW; 2E32DE013B6A5155 CRC64;
MSDNSVATPA HLLQAKVIFL SFLLTGGFVA TYSAFNRHLR QITSVHDIPT NVFRRKYLYG
KVTSVGDGDN FLFFHTPGGV LGGWHWLRKV PTLQRKGILP RRAQKATGNA LSTLSPLNLF
RGLVGLRSEG GGRDQFALYR GRRKLPTLSI RLCGVDAPER AHFGNSSQPL SEEAYKWLNK
TLLGRFVWVK PLSTDQYGRC VAKVEYWSWF RWKNVSIELL KQGLGVVYES KSGAEFDGQD
TLYRYHESKA KKSKRGVWGL RHFETPGAYK KRINKQ
