LCL3_PHANO
ID LCL3_PHANO Reviewed; 296 AA.
AC Q0UVH1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=SNOG_04243;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445330; EAT88003.2; -; Genomic_DNA.
DR RefSeq; XP_001794663.1; XM_001794611.1.
DR AlphaFoldDB; Q0UVH1; -.
DR SMR; Q0UVH1; -.
DR STRING; 321614.Q0UVH1; -.
DR EnsemblFungi; SNOT_04243; SNOT_04243; SNOG_04243.
DR GeneID; 5971531; -.
DR KEGG; pno:SNOG_04243; -.
DR eggNOG; ENOG502RZZQ; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; Q0UVH1; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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..296
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408675"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 77..262
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 270..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 296 AA; 33679 MW; C33BAAF7C626067C CRC64;
MRWFGSGDDE KKKKQVGETW ADSLRADSWG QSLTNPRTLI PTFAFTITTV TALRLYKTFL
RRIPTVNHVK PHYFRRKGIF GKVTTVGDAD NFRLYHTPGG RIAGWGWLPW KMVPTKREGL
SNQTVGLPCH LGLLSIVSDS PSLVANNFQL HIRLAGVDAP ELAHWGREEQ PYAKEAQEWL
INLIHNRRVR AYIYRRDQYD RIVAQVYVRR WLFRKDVGLE MLKAGLATIY EAKSGAEFGT
SEAKYRAAEE KAKAQKVGMW AKPTLLQKLG GASTKAPESP REYKARHAAA DKLKKT