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Database: UniProt
Entry: L7JXM4_TRAHO
LinkDB: L7JXM4_TRAHO
Original site: L7JXM4_TRAHO 
ID   L7JXM4_TRAHO            Unreviewed;       204 AA.
AC   L7JXM4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative SNase-like domain protein {ECO:0000313|EMBL:ELQ75801.1};
DE            EC=3.1.31.1 {ECO:0000313|EMBL:ELQ75801.1};
GN   ORFNames=THOM_1262 {ECO:0000313|EMBL:ELQ75801.1};
OS   Trachipleistophora hominis (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC   Trachipleistophora.
OX   NCBI_TaxID=72359 {ECO:0000313|EMBL:ELQ75801.1, ECO:0000313|Proteomes:UP000011185};
RN   [1] {ECO:0000313|EMBL:ELQ75801.1, ECO:0000313|Proteomes:UP000011185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA   Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA   Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA   Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA   Embley T.M.;
RT   "The genome of the obligate intracellular parasite Trachipleistophora
RT   hominis: new insights into microsporidian genome dynamics and reductive
RT   evolution.";
RL   PLoS Pathog. 8:E1002979-E1002979(2012).
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}.
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DR   EMBL; JH993925; ELQ75801.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7JXM4; -.
DR   STRING; 72359.L7JXM4; -.
DR   VEuPathDB; MicrosporidiaDB:THOM_1262; -.
DR   HOGENOM; CLU_046484_0_0_1; -.
DR   InParanoid; L7JXM4; -.
DR   OMA; PWLANGD; -.
DR   Proteomes; UP000011185; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016894; F:endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:ELQ75801.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011185}.
FT   DOMAIN          42..182
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
SQ   SEQUENCE   204 AA;  23770 MW;  337D50F1DA7CCCDC CRC64;
     MYTLLLIAFI ALPLLIAISA LAKLLHKRFR PIQTNKQFKL NHTIHAIVTK VCDGDTIRVR
     HRPTWSCMRT TKRTILVRLY GIDAPECAHF GMPAQPYSKE STALLRKYVM GKKVYVTKLG
     TDRYDRCIGR VVVDGVDVSV MMVRMGMACV YVGYNAIYGR WYDKLVRCEK RAKKRALGMW
     KEGVELPMDY KRRMRNRNRR RVVL
//
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