LCL3_LEPMJ
ID LCL3_LEPMJ Reviewed; 298 AA.
AC E4ZVE5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=Lema_P027230.1;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(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; FP929127; CBX95571.1; -; Genomic_DNA.
DR RefSeq; XP_003839050.1; XM_003839002.1.
DR AlphaFoldDB; E4ZVE5; -.
DR STRING; 5022.CBX95571; -.
DR EnsemblFungi; CBX95571; CBX95571; LEMA_P027230.1.
DR GeneID; 13281101; -.
DR eggNOG; ENOG502RZZQ; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; E4ZVE5; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000002668; Genome.
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..298
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408665"
FT TRANSMEM 39..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 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..298
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 298 AA; 34585 MW; 7ED3293F2E979400 CRC64;
MRWPWSGHDE EKKRNAATRS KRAETANSWT GTLLESRTLV PSVALTVSTV LGLRLYKAYF
RRIPTVNHIK PDYFRRRTLF GQVTSVGDAD NFRLYHTPGG RLAGWGWLPW KTVPTKREAL
VKQTVGPVLI LWRLRPRRIS SDWMLKAIQL HIRIAGVDAP ELAHWGREAQ PYSKEALDWL
TQLILHQRVR VRLYRRDQYD RVVAQVYYRR WFFRQDVGLE MLKMGLATVY EAKSGAEFGD
VEQQYRAAEE KAKESRAGMW AKPNLLQRLG GAGTKAPESP REYKSRHTAA EKQKKAAW