LCL3_MAGO7
ID LCL3_MAGO7 Reviewed; 257 AA.
AC A4RMK0; G4MTD2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=MGG_04702;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LCL3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001232; EHA53878.1; -; Genomic_DNA.
DR RefSeq; XP_003713685.1; XM_003713637.1.
DR AlphaFoldDB; A4RMK0; -.
DR SMR; A4RMK0; -.
DR STRING; 318829.MGG_04702T0; -.
DR EnsemblFungi; MGG_04702T0; MGG_04702T0; MGG_04702.
DR GeneID; 2678200; -.
DR KEGG; mgr:MGG_04702; -.
DR VEuPathDB; FungiDB:MGG_04702; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; A4RMK0; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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..257
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408667"
FT TRANSMEM 39..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 76..234
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 236..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 257 AA; 29548 MW; 19FFD7A1393C8024 CRC64;
MMRWPWSSDS SDGPKPARHW NESLNKTDWE HYKEPRNWVP TAIATTTILA AVQFYRSYLR
RIPGTNYIHP GFFRRRSLFG RVTSVGDGDN FHLFHTPGGR LAGWSWLRSI PTERKALKGK
TIPVRIAGVD APEAAHFGRE AQPFSAEALE FLKSYILGRD VRTYIYRRDQ YERVVGTVWV
RRWLLRKDVG LEMIKRGLAT VYDAKIGAEF GGLEEKYRAA EAKAKLKKLG MWGAKGKFES
PRDYKNRHAA TSESKLS