ID A0A194VVZ5_9PEZI Unreviewed; 292 AA.
AC A0A194VVZ5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Probable endonuclease LCL3 {ECO:0000256|ARBA:ARBA00013404};
DE AltName: Full=Probable endonuclease lcl3 {ECO:0000256|ARBA:ARBA00014651};
GN ORFNames=VM1G_02809 {ECO:0000313|EMBL:KUI68063.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI68063.1};
RN [1] {ECO:0000313|EMBL:KUI68063.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI68063.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the LCL3 family.
CC {ECO:0000256|ARBA:ARBA00005435}.
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; CM003100; KUI68063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VVZ5; -.
DR OrthoDB; 208975at2759; -.
DR Proteomes; UP000078559; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; 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 PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR PANTHER; PTHR12302:SF3; ENDONUCLEASE LCL3-RELATED; 1.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:KUI68063.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:KUI68063.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..246
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
SQ SEQUENCE 292 AA; 33623 MW; D1278A243BD8D19E CRC64;
MPWPWQSGSS SPSNKGDDDK SFIVRSLSWN ESLCVKDWDH YRDPRSWIPA LVITTVLFGS
VKFYRTYLRR IPNVDYIFPH YYRKRTLFGK VTSVGDGDGF HLFHTPGGRL AGWGWLRQVP
TTRKKLKGGT IPIRIAGIDA PESAHFGRPS QPHASEALQW LSASILHRYV HAQIYRRDQY
DRVVATVYVR RFLFFRRDVG LEMLRRGLAT TYEAKSGVEF GGETMEKKYR EVEAEARRKN
LGLWGALAKT GKSTGWFGLG KVETKSKEPF ETPREFKDRM KLVDKAEKGE TK
//