ID A0A1W0E847_9MICR Unreviewed; 209 AA.
AC A0A1W0E847;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Lcl3 {ECO:0000313|EMBL:OQS55596.1};
GN Name=lcl3 {ECO:0000313|EMBL:OQS55596.1};
GN ORFNames=EHP00_2556 {ECO:0000313|EMBL:OQS55425.1}, EHP00_665
GN {ECO:0000313|EMBL:OQS55596.1};
OS Ecytonucleospora hepatopenaei.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Ecytonucleospora.
OX NCBI_TaxID=646526 {ECO:0000313|EMBL:OQS55425.1, ECO:0000313|Proteomes:UP000192758};
RN [1] {ECO:0000313|EMBL:OQS55425.1, ECO:0000313|Proteomes:UP000192758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH1 {ECO:0000313|EMBL:OQS55425.1,
RC ECO:0000313|Proteomes:UP000192758};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQS55425.1}.
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DR EMBL; MNPJ01000009; OQS55425.1; -; Genomic_DNA.
DR EMBL; MNPJ01000007; OQS55596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0E847; -.
DR STRING; 646526.A0A1W0E847; -.
DR VEuPathDB; MicrosporidiaDB:EHP00_2556; -.
DR VEuPathDB; MicrosporidiaDB:EHP00_665; -.
DR Proteomes; UP000192758; Unassembled WGS sequence.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000192758};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..195
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
SQ SEQUENCE 209 AA; 23706 MW; BF73CBA0D6EA7AB1 CRC64;
MTAKEFVFKF WYFGIPIVVL LLVGFWLLVK RYTKEEQISI GKSFSVIVTR VGDGDGFKAM
HTPWFRSKQI FDKKGKVQKN LPLLSFRLAG VDAPEVAAFG KPAQPFAKES TDFLKFLILY
RVVQVKIVGK DMYGRLLAMV YTGGFFNKKN VNDLMLKTGM ACVYVGAHAK YGGRLAQMKA
LEKEAKANRL GMWSSKNVVT PMEHKAKYR
//
